INSERT INTO `gmcropdatabase_events_fsafeties` (`id`, `eventId`, `description`, `status`, `created`, `updated`) VALUES
(82, 139, '<p style="text-align: justify;"><b>Food and Feed Use</b></p>\n\n<p style="text-align: justify;">The primary use of commodity soybeans is for soybean meal that is consumed by animals. Raw soybeans contain several antinutritional factors (trypsin inhibitors, urease, and hemagglutinins). Heat treatment is the most common processing method used to minimize the activity of such factors. Soybean oil is the major soybean fraction consumed by humans. Soybean oil accounts for 80% of total United States consumption of oils and fats.</p>\n\n<p style="text-align: justify;">Pioneer states that the 305423 soybean variety is intended to be used for the production of high oleic soybean oil. The oil is intended to be a highly stable vegetable oil suitable for frying applications without the need for hydrogenation which produces trans fatty acids and &quot;hydrogenated flavor.&quot; Pioneer states that it is aware of no food or feed uses of current soybean varieties for which the 305423 soybean variety would not be equally suitable.</p>\n\n<p style="text-align: justify;"><b>Compositional Analysis</b></p>\n\n<p style="text-align: justify;">Pioneer assessed the composition of grain and forage from the 305423 soybean and a null segregant (non-transgenic isoline) control. Pioneer states that the null segregant plants are an appropriate control because they are almost genetically identical to the corresponding 305423 soybean plants with the exception that they do not carry the transgenic DNA. Both the transgenic and control soybeans were grown at six field locations in soybean-growing areas of North America using a randomized complete block design with three replicates at each location. Pioneer also analyzed grain and forage from four different commercial soybean varieties.</p>\n\n<p style="text-align: justify;">Pioneer measured 52 components in grain and 5 in forage. Composition data obtained from the commercial varieties were used to calculate 99% tolerance intervals with 95% confidence for all measured components. To interpret the composition results for 305423 soybeans, Pioneer used the confidence intervals and established a combined literature range using data from published literature and databases on soybean composition. Grain samples were analyzed for proximates (protein, fat, and ash), acid detergent fiber (ADF), neutral detergent fiber (NDF), fatty acids, amino acids, isoflavones, and antinutrients. Compositional analysis of forage samples included proximates, ADF, and NDF.</p>\n\n<p style="text-align: justify;"><b>Grain Analysis:</b> Analysis of the levels of 14 fatty acids confirmed the expected high oleic acid phenotype as shown by a substantial increase in the mean level of oleic acid to 76.5% in 305423 soybean as compared to a mean level of 21% in the control soybean. As expected, the increase in the level of oleic acid was accompanied by a decrease in the level of linoleic acid. The mean level of linoleic acid in the control soybean was 52.5% and that in the 305423 soybean was 3.6%. The level of linolenic acid also decreased since linolenic acid is formed in soybeans directly from linoleic acid. Levels of two minor fatty acids, heptadecanoic and heptadecenoic, increased in the 305423 soybean to 0.8% and 1.2% of the total fatty acids, respectively. This increase in the levels of heptadecanoic and heptadecenoic fatty acids is not unexpected because the GM-HRA enzyme most likely results in the increased concentration of 2-ketobutyrate, which is the substrate in the biosynthesis of hepta fatty acids in soybeans.</p>\n\n<p style="text-align: justify;">Mean levels of protein and fiber in grain from the 305423 and control soybean were not statistically significantly different. While the mean level of fat was statistically significantly lower in the 305423 soybean than in the control using the unadjusted P-value, no statistical difference was detected using the false discovery rate (FDR)-adjusted P-value. The mean level of ash was statistically significantly lower in the 305423 soybean as compared to the control soybean. Mean levels of the proximates and fiber in grain from 305423 and control soybean lines were within the 99% tolerance intervals for the reference varieties and within the combined literature range.</p>\n\n<p style="text-align: justify;">There were no statistically significant differences observed in the mean levels of amino acids between 305423 and control soybean grain with the exception of threonine and glutamic acid. The mean levels of these two amino acids were statistically significantly increased in 305423 soybean when the unadjusted P-values were used, but not when the FDR-adjusted P-values were used. All these levels were within the 99% tolerance intervals.</p>\n\n<p style="text-align: justify;">Mean levels of nine isoflavones were quantified in grain samples. The mean levels for daidzin, malonylgenistin, and malonyldaidzin were statistically significantly increased in the 305423 versus the control soybean. Mean genestin levels were only shown to be statistically significantly increased when the unadjusted P-value was used. Mean values for all the measured isoflavones were within the 99% tolerance intervals. In both the control and 305423 soybean the mean levels of genistin, glycitin, malonylgenistin, malonylglycitin, and malonyldaidzin were above the combined literature range. Daidzin levels were only above the combined literature range in the 305423 soybean. No literature data were available for the level of glycitein. The values for the other two isoflavones (genistein and daidzein) were within the combined literature range.</p>\n\n<p style="text-align: justify;">Concentrations of several antinutrients were measured in soybean grain including non-digestible oligosaccharides stachyose and raffinose, lectins, phytic acid, and trypsin inhibitor. No statistically significant differences were observed between the 305423 and control soybean in mean values for raffinose, lectins, and phytic acid. The mean value for trypsin inhibitor was statistically significantly lower for 305423 soybean as compared to the control soybean. The reduction in the mean value of trypsin inhibitor in 305423 soybean was expected as Pioneer reported that the promoter used to drive expression of the <i>FAD2-1</i> gene, the Kunitz trypsin inhibitor promoter, has been shown to silence the KTi3 gene which encodes the Kunitz trypsin inhibitor. The mean value for stachyose was statistically significantly increased when the unadjusted P-value was used, but not when the FDR-adjusted P-value was used. Mean values for all the measured antinutrients were within the 99% tolerance intervals and within the combined literature ranges.</p>\n\n<p style="text-align: justify;"><b>Forage Analysis:</b> Pioneer analyzed forage for protein, fat, ash, ADF, and NDF. No statistically significant differences were observed between the mean levels of these components in forage from the 305423 and control soybeans with the exception of the level of fat. The mean level of fat was statistically significantly decreased in 305423 using the unadjusted P-value, but not when using the FDR-adjusted P-value. All mean levels were within the 99% tolerance intervals and combined literature ranges, with the exception of NDF. The mean level of NDF in both the control and 305423 soybean was above the combined literature range.</p>\n\n<p style="text-align: justify;"><b>Endogenous Allergens:</b> A study was conducted to assess whether the transformation process may have increased the overall allergenicity of 305423 soybean compared to conventional soybean. Using sera from clinically reactive soy allergic patients, Pioneer conducted IgE immunoblot and ELISA studies using protein extracts from 305423 soybean and conventional soybean. The SDS-PAGE Coomassie blue-stained protein profiles for 305423 and control soybean extracts appeared to be the same; they are similar in their IgE binding profile, and showed the same IgE binding capacity for 305423 and control soy extracts. It was concluded that the levels of endogenous allergens in and the allergic potential of 305423 soybean are comparable to those in nontransgenic control soybean.</p>\n\n<p style="text-align: justify;"><b>Nutritional Quality</b></p>\n\n<p style="text-align: justify;">A poultry feeding study over a period of 42 days has been carried out with diets containing 305423 soybean, non-GM control soybean with comparable genetic background and three commercial non-GM soybeans. The mortality, body weight gain, feed efficiency, organ yield, carcass yield, breast, thigh, wing and leg yield and abdominal fat of the chickens fed with 305423 soybean were compared to chickens fed non-GM control soybean diets. The results from this 42-day poultry study confirm the safety of 305423 soybean and that 305423 soybean is nutritionally equivalent to non-GM control soybean with a comparable genetic background and to commercial soybeans.</p>\n\n<p style="text-align: justify;"><b>Potential Toxicity and Allergenicity</b></p>\n\n<p style="text-align: justify;">The only newly expressed protein in 305423 soybean is the GM-HRA protein. Based on amino acid sequence similarity searches against the National Center for Biotechnology Information (NCBI) Protein dataset, there were no significant similarities with known protein toxins. Pioneer conducted an acute oral toxicity study in mice in which a single dose of 582 mg per kilogram of body weight (mg/kg bw) of GM-HRA protein was administered by oral gavage to five male and five female mice. No clinical symptoms of toxicity, body weight loss, gross organ lesions or mortality were observed. The result of this study shows that the GM-HRA protein does not cause acute toxicity.</p>\n\n<p style="text-align: justify;">While soybean is one of the major food allergens, none of the identified allergens is a member of the ALS family and the ALS protein from soybean has not been characterized as a soy allergen. Comparisons of the amino acid sequence of the GM-HRA protein to the amino acid sequences of known allergens in the Food Allergy Research and Resource Program (FARRP, version 6.0) database using the FASTA34 sequence alignment program showed that none of the identified alignments met or exceeded the threshold of greater than or equal to 35% identity over 80 amino acids and no contiguous stretches of 8 or greater amino acids were shared between the GM-HRA protein and the proteins in the allergen database. Additionally, the GM-HRA protein is not glycosylated.</p>\n\n<p style="text-align: justify;">The GM-HRA protein is rapidly (&lt; 30 seconds) hydrolyzed in simulated gastric fluid (SGF) to fragments of &lt; 3 kDa; and when subjected to simulated intestinal fluid (SIF), the GM-HRA protein, including the low weight molecular fragments seen in SGF, is completely and rapidly (&lt; 2 minutes) hydrolyzed.</p>\n\n<p style="text-align: justify;">Based on this weight of evidence assessment, it was concluded that the GM-HRA protein is unlikely to be a toxin and is not a potential allergen.</p>\n', 'Enabled', NULL, '2013-08-30 01:06:54'),
(83, 141, '<p style="text-align: justify;"><b>Compositional Analysis</b></p>\n\n<p style="text-align: justify;">The main purpose of compositional studies is to determine if any unexpected changes in composition have occurred to the food and to establish its nutritional adequacy. In the case of cottonseed, the key components that should be considered in the comparison include protein, fat, carbohydrate, amino acids, fatty acids, vitamins, minerals and the antinutrients, gossypol and cyclopropenoid fatty acids. Compositional analyses were done on fuzzy seed collected from GHB614 cotton and the non-GM counterpart, Coker 312, grown in field trials typical of commercial agricultural production.</p>\n\n<p style="text-align: justify;">Nine field trials were conducted in 2005 at sites representing primary cotton-growing regions of the south-eastern United States. At each test site, six plots of transgenic event GHB614 cotton and three non-transgenic plots of Coker 312 were planted. Three of the six plots containing GHB614 cotton were sprayed three times with glyphosate herbicide (0.75 pounds active ingredient/acre). Compositional analysis of the cottonseed samples included proximates (protein, fat, ash and moisture), acid detergent fibre (ADF), neutral detergent fibre (NDF), minerals (calcium, iron, magnesium, phosphorus, potassium and zinc), amino acids, fatty acids, vitamin E (alpha tocopherol) and carbohydrates by calculation. In addition, three known anti-nutrients found in cotton (gossypol, cyclopropenoid fatty acids and phytic acid) were analysed. Methods of analysis were based on internationally recognised procedures (e.g. AOAC International methods) or other published methods.</p>\n\n<p style="text-align: justify;">No differences of biological significance were observed between GHB614 cotton and its conventional counterpart. Statistically significant differences in some of the key constituents were noted, however the differences observed were minor, and in each case the levels observed were within the range of literature values reported for conventional cotton varieties. The composition of cotton is known to vary significantly with the site, agricultural conditions and season of production, and differences reported here most likely reflect normal biological variability. Food from GHB614 cotton is therefore considered to be compositionally equivalent to food from conventional cotton varieties.</p>\n\n<p style="text-align: justify;"><b>Potential Toxicity and Allergenicity</b></p>\n\n<p style="text-align: justify;">In terms of its potential toxicity and allergenicity, it is worth noting that the 2mEPSPS protein has been evaluated previously as the novel protein present in glyphosate-tolerant corn line GA21 which has been approved for food and feed use in numerous countries. It is therefore likely to have been widely distributed in corn based foods. This modified enzyme is derived from the native EPSPS enzyme in maize (99.5% amino acid homology), and is closely related to other EPSPS enzymes from plants and microorganisms which are natural constituents of human diets.<br />\nBioinformatic studies with the 2mEPSPS protein sequence has confirmed the absence of any significant amino acid sequence similarity to known protein toxins or allergens.</p>\n\n<p style="text-align: justify;">Two independent acute oral toxicity studies using purified 2mEPSPS protein have been conducted by different applicants. In the study conducted by Monsanto for GA21 maize, the modified EPSPS (2mEPSPS) protein was administered by a single oral gavage dose to ten male and ten female CD-1 mice, at target doses of 5, 15 and 50 mg/kg bodyweight. In this study, this corresponded to actual doses of 3.7, 11.8 and 45.6 mg/kg respectively. The results of the study showed no statistically significant differences between test and control treatment groups in mean body weights, cumulative weight gains or food consumption in either males or females at any treatment level. The study concluded that there was no evidence of toxicity in mice following a single oral dose of 45.6 mg/kg modified EPSPS (2mEPSPS) protein. In the study conducted by Bayer for GHB614 cotton, the 2mEPSPS protein was administered by a single oral gavage dose of 2000 mg protein/kg bodyweight to 5 female OF1 mice. A second group of female mice received the same dose of bovine serum albumin as a negative control. All animals were observed for clinical signs daily for fifteen days and body weights were measured weekly. At termination, all animals were subjected to necropsy including macroscopic examination. There were no clinical signs, mortalities or treatment related effects on bodyweight in female OF1 mice observed during this study. Based on these findings, it was concluded that no oral toxicity was demonstrated in mice at a very high dose of 2000 mg/kg bodyweight.</p>\n\n<p style="text-align: justify;">One of the criteria for assessing potential allergenicity is to determine the stability of novel proteins in conditions that simulate human digestion. Proteins that are rapidly degraded in such conditions are considered less likely to be involved in eliciting an allergic response. The 2mEPSPS protein was subjected to digestibility studies using simulated human gastric fluid (SGF) containing pepsin and simulated intestinal fluid (SIF) containing porcine pancreatin, which is a mixture of enzymes including amylase, trypsin, lipase, ribonuclease and protease. In SGF (with pepsin), there was no full length or partially degraded 2mEPSPS protein observed at 30 seconds and at subsequent time points. In SIF, the 2mEPSPS protein band was only faintly visible after scanning the gel even at time zero. At all subsequent incubation times, there was no full length or partially degraded 2mEPSPS protein observed.</p>\n\n<p style="text-align: justify;">The weight of evidence shows that the 2mEPSPS protein is not toxic and unlikely to be allergenic in humans.</p>\n', 'Enabled', NULL, '2013-08-30 01:10:55'),
(84, 142, '<p style="text-align: justify;"><b>Compositional Analysis</b></p>\n\n<p style="text-align: justify;">Mature fruits from four different specimens of line X17-2 were subjected to compositional analysis. Published information on other transgenic papaya lines (Hawaiian cultivars 55-1 and 63-1) and nontransgenic varieties was used for comparison. The range of analytes included proximates (moisture, ash, total dietary fiber, calories, total fat, carbohydrate, and protein), minerals (sodium, calcium, iron), total sugar, fats (saturated, mono- and poly-unsaturated), benzyl isothiocyanate (BITC), and vitamins (beta-carotene, vitamin A, and vitamin C).</p>\n\n<p style="text-align: justify;">It was concluded that compositional values of the X17-2 line were not meaningfully different from those given for the other varieties. Vitamin C values were comparable to the literature values of other varieties cited by the developer. Although Vitamin A values were somewhat higher on average, the range overlapped with the value reported in the United States Department of Agriculture&#39;s National Nutrient Database.</p>\n\n<p style="text-align: justify;"><b>Endogenous Toxicants</b></p>\n\n<p style="text-align: justify;">The presence of benzyl isothiocyanate (BITC) in the latex of green papaya tissues has been linked to incidents of spontaneous abortions in pregnant women and with a higher incidence of prostate cancer in Japanese men over the age of 70. Because ripe papaya fruits have no latex they also have virtually no BITC content, and, therefore, the consumption of ripe fruit would not be expected to be linked to any abortifactant effects. BITC was assayed in green fruits of seven different X17-2 breeding lines with concentrations ranging from 0.2 milligrams (mg) to 4.8 mg per 100 mg of green fruit. Similar or greater ranges were found with the same assay in three conventional cultivars.</p>\n\n<p style="text-align: justify;"><b>Potential Toxicity and Allergenicity</b></p>\n\n<p style="text-align: justify;">There is a history of safe consumption of PRSV CP derived from virus-infected papaya fruit, and there is no indication that the form of the CP expressed in transgenic X17-2 papaya is materially different in any way that would affect its potential for toxic or allergenic effect. Additionally, the PRSV CP does not possess any of the physiochemical properties normally associated with protein allergens or toxins, such as heat stability and resistance to digestion by simulated gastric fluids. Also, there were no regions of homology when the deduced amino acid sequence of PRSV CP was compared to the amino acid sequences of known protein allergens or toxins.</p>\n', 'Enabled', NULL, '2013-08-30 01:12:58'),
(85, 143, '<p style="text-align: justify;">The composition of cottonseed and oil from Bt cotton hybrids (Event-1) was compared to that of non-Bt cotton hybrids and other conventional cotton varieties. The nutrients measured in the cottonseed included protein, fat, fiber, moisture, ash, carbohydrate, and the anti-nutrients gossypol, fatty acids and aflatoxins. All these analysis revealed that Bt cotton hybrids are equivalent and as safe and nutritious as non-Bt hybrids and other conventional cotton varieties. Also the nutritional studies in cows revealed that no difference on feed intake, milk yield and composition between Bt and non-Bt cotton seed feed groups of cow as well the safety studies confirmed the food and feed safety of Bt cotton to cows</p>\n\n<p style="text-align: justify;">Feeding experiments conducted with Bt cotton seed meal on fish chicken, goat and cows indicated that Bt cotton seed meal is nutritionally equivalent and safe as the non-Bt cottonseed meal.</p>\n\n<p style="text-align: justify;">The feeding experiments were conducted from different institutes in India in which Central Avian Research Institute (CARI), Izatnagar (UP) ICAR conducted studies on Bird; IVRI, Izatnagar on goat and cow; Central Institute of Fisheries Education (Deemed University, ICAR), Mumbai on fish.</p>\n\n<p style="text-align: justify;">The mammalian acute oral toxicity of Bt protein was studied in rat and the specificity and safety of the Cry1Ac protein was recorded. No toxic effects were observed even at extremely high dose levels (5000 mg/kg of body weight), when the Cry1Ac protein was administered orally to rats. Also the sub-chronic oral toxicity study on rat revealed the Cry1Ac protein found safe to animal health. The Cry1Ac protein expressed in the cotton plant is not expected to present a risk of dermal or inhalation toxicity. The proteins that are non-toxic by the oral route are not expected to be toxic by the dermal or pulmonary route. This was confirmed by the study conducted on irritation test to skin and mucous membrane in rabbits and dermal sensitization study in guinea pigs. All these oral toxicity and irritation tests were conducted at Shriram Institute for Industrial Research, New Delhi Feeding studies on ruminants (goat) showed that Bt cottonseed when fed, it was as nutritious as non Bt cotton seeds and did not cause any deleterious effect on the ruminants in comparision to non-Bt cotton seeds. Nutritional studies on lactating cows conducted in IVRI, Izatnagar reconfirm these conclusions.</p>\n\n<p style="text-align: justify;">The toxicological studies on chicken and fish under Indian conditions confirmed the safety of cottonseed meal derived from Bt cotton.</p>\n\n<p style="text-align: justify;">Studies conducted to determine the presence of Cry1Ac protein in refined oil and lint obtained from Bt cotton showed absence of Cry1Ac protein at the detection standard of the experiment. Similarly studies conducted to determine the presence of Cry1Ac gene in cottonseed oil obtained from Bt cotton by using forward and reverse primers specific for internal sequence of the Cry1Ac gene, reveal no DNA amplification in the oil samples.</p>\n\n<p style="text-align: justify;"><i>Source: India Biosafety Clearing House<br />\n(<a class="sbar" href="http://www.indbch.nic.in/risk_assessment_jk.asp" target="_blank">http://www.indbch.nic.in/risk_assessment_jk.asp</a>). Last accessed 26 February 2009.</i></p>\n', 'Enabled', NULL, '2013-08-30 01:15:07'),
(86, 133, '<p style="text-align: justify;"><strong>Dietary Exposure</strong></p>\n\n<p style="text-align: justify;">Although commercialization of soybean 356043 could potentially increase dietary exposure to the acetylated amino acids NAGlu and NAAsp, acetylated amino acids are readily metabolized in humans and raise no safety issues. In addition, neither NAGlu nor NAAsp are detectable in soybean oil, which accounts for 94% of soybean consumption.</p>\n\n<p style="text-align: justify;"><strong>Nutritional Data</strong></p>\n\n<p style="text-align: justify;">Compositional analyses were done to establish the nutritional adequacy of soybean event 356043, and to compare it to a non-transgenic conventional soybean under typical cultivation conditions. The components analyzed were protein, fat, carbohydrate, amino acids, fatty acids, vitamins, minerals, isoflavones, and the anti-nutrients stachyose, faffinose, lectins, phytic acid, and trypsin inhibitor.</p>\n\n<p style="text-align: justify;">The compositional analyses of key components in soybean 356043 indicate that, for the majority of components, there are no compositional differences of biological significance in forage or grain from transgenic soybean 356043, compared to the non-GM control. Several minor differences in key nutrients and other constituents were noted, but the mean levels observed were within the range of values observed for the non transgenic comparator and within the range of natural variation.</p>\n\n<p style="text-align: justify;">Increased levels of two fatty acids, heptadecanoic acid (C17:0) and heptadecenoic acid (C17:1) were observed. C17:0 and C17:1 in soybean 356043 together constitute approximately 0.5% of the total fatty acid content, compared to 0.2% in the conventional counterpart. C17:0 and C17:1 are present in vegetable oils and other commonly consumed foods. As these fatty acids are typical constituents of the human diet and readily metabolized, the increased levels raise no safety or nutritional concerns.</p>\n\n<p style="text-align: justify;">The introduction of dual herbicide-tolerant soybean 356043 into the food supply would be expected to have negligible nutritional impact. This was supported by the results of a feeding study in animals, where no differences in health and growth performance were found between broiler chickens fed diets containing soybean 356043 meal and those fed conventional soybean meal diets.</p>\n\n<p style="text-align: justify;">No potential public health and safety concerns have been identified in the assessment of dual herbicide-tolerant soybean 356043. On the basis of the data provided, and other available information, food derived from soybean 356043 is considered as safe for human consumption as food derived from conventional soybean varieties.</p>\n\n<p style="text-align: justify;">To date, all approved GM plants with modified agronomic production traits (e.g., herbicide tolerance) have been shown to be compositionally equivalent to their conventional counterparts. In the case of soybean 356043, there are unintended changes in the levels of two fatty acids (C17.0 and C17.1) and two-acetylated amino acids (NAGlu and NAAsp), that are outside the range of natural variation for soybean. All of these components are typical constituents of the human diet, and are readily metabolizable, and thus raise no safety issues resulting from their presence in food derived from soybean 356043.</p>\n\n<p style="text-align: justify;"><strong>Potential Toxicity</strong></p>\n\n<p style="text-align: justify;">Bioinformatics studies with the GAT4601 and GM-HRA proteins confirmed the absence of any biologically significant amino acid sequence similarity to known protein toxins or allergens and digestibility studies demonstrated that both proteins would be rapidly degraded following ingestion, similarly to other dietary proteins. Acute oral toxicity studies in mice with both proteins also confirmed the absence of toxicity. Taken together, the evidence indicated that neither protein is toxic or likely to be allergenic in humans.</p>\n\n<p style="text-align: justify;">The metabolite residues generated by glyphosate-treated soybean 356043 plants are considered less toxic than glyphosate, which itself is considered of very low potential toxicity in animals. Hence, there is no increase in overall toxicity arising from the presence of glyphosate residues on soybean 356043, and the current acceptable daily intake (ADI) for glyphosate is considered to be protective of public health and safety.</p>\n\n<p style="text-align: justify;"><strong>Potential Allergenicity</strong></p>\n\n<p style="text-align: justify;">Soybean naturally contains allergenic proteins and is one of a group of known allergens, including milk, eggs, fish, shellfish, wheat, peanuts, tree nuts, and sesame. This group of foods accounts for approximately 90% of all food allergies. The presence of allergenic proteins in the diets of hypersensitive individuals can cause severe adverse reactions. The allergenic effect of soybeans is attributed to the globulin fraction of soybean proteins that comprises about 85% of total protein. Soybean-allergic individuals will also be allergic to soybean 356043.</p>\n\n<p style="text-align: justify;">In order to assess whether soybean 356043 has altered endogenous allergenic potential, a study was conducted to determine binding levels of IgE antibody to protein extracts prepared from soybean 356043 and the parental soybean line &ldquo;Jack.&rdquo; The data indicate that soybean 356043 and control Jack had similar protein/allergen profiles when tested with soy-allergic material. Thus, soybean 356043 appears to be equivalent to the non-transgenic counterpart in terms of its endogenous allergenicity.</p>\n', 'Enabled', NULL, '2013-08-30 00:58:43'),
(87, 146, '<p style="text-align: justify;"><b>Dietary exposure</b></p>\n\n<p style="text-align: justify;">EH92-527-1 is not intended for food use. For this reason, a far-reaching quality assurance system has been established for keeping EH92-527-1 separate from other potatoes. This system, in combination with the innate characteristics of the potato, makes it very unlikely that EH92-527-1 will get into the food chain. However, the possibility cannot be completely ruled out.</p>\n\n<p style="text-align: justify;">Starch rich in amylopectin does not constitute a health risk to normal healthy individuals. However, the branched starch molecule (amylopectin) is digested more quickly than the non-branched starch molecule (amylose), and this could result in undesirable effects for diabetics. It is therefore important that EH92-527-1 be kept well separated from other potatoes so as to avoid confusion with food potatoes. The observed difference in starch composition (from 85% amylopectin and 15 % amylose in Prevalent to 98% amylopectin and 2% amylose in EH92-527-1) is believed to be of no importance in cases of low or temporary intake.</p>\n\n<p style="text-align: justify;">EH92-527-1 produces only one new protein, NPTII, which has not been shown to be either toxic or allergenic.</p>\n\n<p style="text-align: justify;">The byproduct EH92-527-1 pulp, which is the material that remains after the starch has been extracted, will be used as bovine feed. As noted below, statistically significant differences in nutrient composition exist between EH92-527-1 and its parental cultivar Prevalent&mdash;in particular, with respect to higher levels of mono- and disaccharides, higher levels of vitamin C, and lower levels of glycoalkaloids. The measured differences fall within the natural variation interval for potatoes and are deemed to be of little significance. The feed product is considered to be substantially equivalent to the corresponding non-GM product and consequently no health risk is believed to exist.</p>\n\n<p style="text-align: justify;"><b>Nutritional data</b></p>\n\n<p style="text-align: justify;">The analyzed compounds with regard to composition included dry matter, protein, fat, ash, carbohydrates, fiber, digestive fiber, fructose, glucose, sucrose, starch, chlorogenic acid, solanine, chaconine, nitrate, vitamin C, and minerals (Na, K, Ca, Mg, P, Fe, Zn, Cu, Mn, Cd). Composition data were obtained from field trials performed in 1996-1998. In addition to the intended differences in starch composition, some statistically significant differences were observed each year between EH92-527-1 and its parental cultivar Prevalent. These differences included decreases in yield and dry matter and increases in sucrose content and vitamin C content. Additional data on potato EH92-527-1 tested during starch production trials in 1998-2000 showed similar values for yield compared with equivalent potato cultivars. Although additional differences were noted during single years, these were not consistently noted through three years. These differences included decreases in glycoalkaloid levels (solanine and chaconine) in potato EH92-527-1 during two years. The changes in vitamin C and glycoalkaloids were within the background ranges reported in the literature. The change in sucrose content was considered as being related to the intended alteration of starch biosynthesis. It should be noted that nitrates are found in the entire plant and are considered anti-nutritional. It was concluded that the observed differences are unlikely to cause adverse health effects. In addition, analyses of the gross and mineral compounds of pulp and juice derived from potato EH92-527-1 and the non-transgenic cultivar Prevalent showed that their compositions were similar. Taken together, the characteristics of the EH92-527-1 potato, its compositional characteristics due to the introduced trait, the anticipated intake and exposure and the presence and safe use of the starch component amylopectin in the food supply, the EH92-527-1 event is considered to pose negligible risk to human health.</p>\n\n<p style="text-align: justify;"><b>Toxicity</b></p>\n\n<p style="text-align: justify;">The main toxic or anti-nutritional substances in potatoes are glycoalkaloids and nitrates. Glycoalkaloids, which are toxic in high concentrations, are found in harmful amounts chiefly in the above-ground parts of the plant (e.g., stems, leaves, and fruits). Nitrates are found in the entire plant and are considered anti-nutrients.</p>\n\n<p style="text-align: justify;">As noted earlier, statistically significant changes in nutrient composition exist between EH92-527-1 and its parental cultivar Prevalent&mdash;in particular, with respect to higher levels of mono- and disaccharides, higher levels of vitamin C, and lower levels of glycoalkaloids. The measured differences fall within the natural variation interval for potatoes and are deemed to be of little significance.</p>\n\n<p style="text-align: justify;">A total of eighteen open reading frames (ORFs) have been identified in the insert sequence of the potato EH92-527-1. Eleven of these have no sequence homology with known coding regions. Bioinformatic analysis has shown that, for all ORFs identified, there are no homologies with known toxins or allergens.</p>\n\n<p style="text-align: justify;">The only ORF having a complete coding region for a known protein is the nptII gene. Bioinformatic analysis indicates that ORF4 could be transcribed due to its association with ORF1 (nptII). However, a translation start in the correct reading frame is absent and a stop codon is present before ORF4. The hypothetical ORF4 protein showed a high degree of similarity with two proteins that are not known to be toxic or allergenic. Furthermore, extensive studies indicated that, while OR4 transcript is detectable in the GM potato, there is no corresponding translation into protein. It is therefore concluded to be unlikely that the presence of ORF4 in EH92-527-1 would constitute a risk. No toxicity of the NPTII protein has been observed and in simulated digestive fluids this protein is rapidly degraded. In addition, two animal studies have indicated no adverse effects on animal health. A subchronic 90-day feeding study in rats with freeze-dried potatoes derived from EH92-527-1 and its parental line failed to reveal any effects that would raise concern about the transgenic potato. An eight-week nutritional animal feeding study with pulp derived from EH92-527-1 and conventional pulp fed to heifers provided evidence of nutritional equivalence and revealed no detrimental effects on animal health.</p>\n\n<p style="text-align: justify;">The gene sequences introduced to suppress GBSS expression have no homology with known toxins.</p>\n\n<p style="text-align: justify;">The weight of evidence from these studies, taken together, indicates that EH92-527-1 and derived products are no more likely to cause adverse effects on human and animal health than conventional potatoes in the context of the proposed uses.</p>\n\n<p style="text-align: justify;">The application and approval do not include food use, therefore no complete food evaluation has been performed. It is therefore very important that the EH92-527-1 potato be kept out of the food chain. A sophisticated quality-assurance system has been developed for keeping EH92-527-1 separate from other potatoes. It is believed that the combination of this program with the characteristics of the potato will make it extremely unlikely that EH92-527-1 will get into the food chain.</p>\n\n<p style="text-align: justify;"><b>Allergenicity</b></p>\n\n<p style="text-align: justify;">EH92-527-1 produces only one new protein, NPTII, which has been shown not to be allergenic.</p>\n\n<p style="text-align: justify;">The hypothetical ORF4 protein showed a high degree of similarity with two proteins that are not known to be toxic or allergenic. In addition, when screened against a database of sequences of allergenic proteins, the ORF4 protein sequence does not show any similarities that are believed to be relevant or to raise concerns about potential allergenic risk.</p>\n\n<p style="text-align: justify;">Allergenicity of the whole crop could be increased as an unintended effect of the random insertion of the transgene in the genome of Prevalent, for example through qualitative or quantitative modifications of the pattern of expression of endogenous proteins. This issue does not appear relevant because potato is not considered a major allergenic food, and possible over-expression of any endogenous protein that is not known to be allergenic would be unlikely to alter the overall allergenicity of the whole plant. The same considerations also apply to exposure by inhalation during processing. Should the high amylopectin potato be inadvertently consumed, the data supporting its equivalence to the non-modified parent variety would indicate that it is no more of a potential allergen than the non-modified parent.</p>\n', 'Enabled', NULL, '2013-08-30 01:18:13'),
(103, 98, '', 'Enabled', '2013-08-23 12:52:24', '2013-09-03 13:10:52'),
(100, 166, '<p><span style="color: rgb(89, 89, 89); font-family: Verdana, Helvetica, Arial, ''Sans Serif''; font-size: 11px; line-height: 14px; text-align: justify;">For new varieties without purposefully altered nutritional properties, such as 4114 maize, the compositional assessment is part of the weight-of-evidence approach for evaluating whether there were any unanticipated consequences of the genetic modification.&nbsp;</span><br style="color: rgb(89, 89, 89); font-family: Verdana, Helvetica, Arial, ''Sans Serif''; font-size: 11px; line-height: 14px; text-align: justify;" /><br><span style="color: rgb(89, 89, 89); font-family: Verdana, Helvetica, Arial, ''Sans Serif''; font-size: 11px; line-height: 14px; text-align: justify;">Compositional analyses were performed on samples of maize forage and kernels (grain) obtained from hybrid plants of 4114 and near-isogenic control maize grown in side-by-side trials across six locations in the United States and Canada in 2010. The near-isogenic control plants had a genetic background that was&nbsp;</span><i style="color: rgb(89, 89, 89); font-family: Verdana, Helvetica, Arial, ''Sans Serif''; font-size: 11px; line-height: 14px; text-align: justify;">ca</i><span style="color: rgb(89, 89, 89); font-family: Verdana, Helvetica, Arial, ''Sans Serif''; font-size: 11px; line-height: 14px; text-align: justify;">. 98 percent similar to that of the 4114 maize generation used, but did not go through the transformation process.&nbsp;</span><br><span style="color: rgb(89, 89, 89); font-family: Verdana, Helvetica, Arial, ''Sans Serif''; font-size: 11px; line-height: 14px; text-align: justify;">Among the 82 compositional components that were analyzed in samples of 4114 and near-isogenic control maize grain, and nine components that were analyzed in forage samples, the only statistically significant differences observed were in concentrations of ash, phosphorus, potassium, and eicosenoic acid in grain samples. This number of statistically significant differences is within the range that would be expected purely by chance. The magnitudes of the differences in mean concentrations were small, less than 15 percent, and in every case the mean values from 4114 maize grain samples were within the ranges of natural variation as reported in the literature. Overall, no consistent patterns emerged to suggest that biologically meaningful changes in composition or nutritive value of the grain had occurred as a consequence of the genetic modification, or expression of the Cry1F, Cry34Ab1, Cry35Ab1, and PAT proteins in 4114 maize.</span><br><span style="color: rgb(89, 89, 89); font-family: Verdana, Helvetica, Arial, ''Sans Serif''; font-size: 11px; line-height: 14px; text-align: justify;">The conclusion based on these data was that grain and forage from 4114 maize were compositionally equivalent to these same products from unmodified near-isogenic control maize, and to other commercial maize hybrids. Processing is unlikely to alter the compositional components of maize grain, thus, products derived from 4114 grain will also be compositionally equivalent to their conventional counterparts.</span></p><br>', 'Enabled', '2013-08-09 12:49:40', '2013-08-23 00:19:19'),
(105, 107, '', 'Enabled', '2013-08-30 16:46:53', '2013-08-30 16:46:53'),
(106, 108, '', 'Enabled', '2013-09-02 13:10:02', '2013-09-02 13:13:42'),
(107, 119, '', 'Enabled', '2013-09-02 13:41:41', '2013-09-02 13:41:41'),
(108, 11, '', 'Enabled', '2013-09-03 11:25:26', '2013-09-03 11:25:26'),
(110, 169, '', 'Enabled', '2013-09-26 12:43:37', '2013-09-26 12:43:37');



-- -----------------------------------------------------------------------------
INSERT INTO `gmcropdatabase_events_genes` (`id`, `eventId`, `code`, `abbrCode`, `name`, `type`, `lType`, `source`, `promoter`, `effector`, `terminator`, `copies`, `form`, `srcCode`, `eCLink`, `description`, `status`, `created`, `updated`) VALUES
(1, 59, 'PG', 'PG', 'polygalacturonase', 'DR', 'Ripening delayed', 'Tomato', 'CaMV 35S', NULL, '<I>A. tumefaciens</I> nopaline synthase (<I>nos</I>) 3''-untranslated region', NULL, 'Truncated, sense and/or antisense', NULL, NULL, NULL, 'Enabled', NULL, NULL),
(2, 59, 'nptII', 'NPTII', 'neomycin phosphotransferase II', 'SM', 'Selectable marker', 'Escherichia coli', 'nopaline synthase (<I>nos</I>) from <I>A. tumefaciens</I>', NULL, 'octopine synthase', NULL, 'Native', NULL, NULL, NULL, 'Enabled', NULL, NULL),
(3, 43, 'ACC', 'ACC', 'aminocyclopropane cyclase synthase', 'DR', 'Ripening delayed', 'Tomato', 'CaMV 35S', NULL, '<I>A. tumefaciens</I> nopaline synthase (<I>nos</I>) 3''-untranslated region', '3', 'Truncated, sense orientation', NULL, NULL, NULL, 'Enabled', NULL, '2013-11-18 17:26:26'),
(5, 43, 'nptII', 'NPTII', 'neomycin phosphotransferase II', 'SM', 'Selectable marker', 'Escherichia coli', 'nopaline synthase (<I>nos</I>) from <I>A. tumefaciens</I>', NULL, 'octopine synthase', '3', 'Native', NULL, NULL, NULL, 'Enabled', NULL, '2013-11-18 17:26:27'),
(7, 57, 'sam-k', 'SAMase', 'S-adenosylmethionine hydrolase', 'DR', 'Ripening delayed', 'E. coli bacteriophage T3', NULL, NULL, NULL, NULL, '5'' modified with Kozak consensus sequence', NULL, NULL, NULL, 'Enabled', NULL, NULL),
(8, 57, 'nptII', 'NPTII', 'neomycin phosphotransferase II', 'SM', 'Selectable marker', 'Escherichia coli', 'nopaline synthase (<I>nos</I>) from <I>A. tumefaciens</I>', NULL, 'octopine synthase', NULL, 'Native', NULL, NULL, NULL, 'Enabled', NULL, NULL),
(9, 58, 'ACCd', 'ACCd', '1-amino-cyclopropane-1-carboxylic acid deaminase', 'DR', 'Ripening delayed', 'Pseudomonas chlororaphis', 'figwort mosaic virus (FMV) 35S', '5'' leader: petuniaHSP70 gene', 'pea ribulose-1,5-bisphosphate carboxylase small subunit', NULL, 'Native', NULL, NULL, NULL, 'Enabled', NULL, NULL),
(10, 58, 'nptII', 'NPTII', 'neomycin phosphotransferase II', 'SM', 'Selectable marker', 'Escherichia coli', 'CaMV 35S', NULL, 'octopine synthase', NULL, 'Native', NULL, NULL, NULL, 'Enabled', NULL, NULL),
(11, 56, 'cry1Ac', 'cry1Ac', 'Cry1Ac delta-endotoxin', 'IR', 'Insect resistance', 'Bacillus thuringiensis subsp. kurstaki (Btk)', 'CaMV 35S', NULL, '3'' non-translated region of soybean alpha subunit of beta-conglycinin gene', NULL, 'NULL', 'BTKC', NULL, NULL, 'Enabled', NULL, NULL),
(12, 2, 'als', 'ALS', 'acetolactate synthase', 'MUT', 'Mutations', 'Triticum aestivum', 'native AHAS', NULL, NULL, NULL, 'Selected following chemical mutagenesis with NaN3', NULL, NULL, NULL, 'Enabled', NULL, NULL),
(13, 45, 'pat', 'PAT', 'phosphinothricin N-acetyltransferase', 'HT', 'Herbicide tolerance', 'S. viridochromogenes', 'CaMV 35S', NULL, 'CaMV 35S poly(A) signal', '1', 'Synthetic version of native gene', 'SVIR', NULL, NULL, 'Enabled', NULL, NULL),
(14, 46, 'CP4 epsps', 'EPSPS', '5-enolpyruvyl shikimate-3-phosphate synthase', 'HT', 'Herbicide tolerance', 'Agrobacterium tumefaciens CP4', 'figwort mosaic virus (FMV) 35S', 'chloroplast transit peptide from <I>A. thaliana</I>', 'P. sativum (pea) ribulose-1,5-bisphosphate carboxylase small subunit non-translated region', NULL, 'Native', 'CP4EPS', NULL, NULL, 'Enabled', NULL, NULL),
(15, 46, 'gus', 'gus', 'beta-D-glucuronidase', 'SM', 'Selectable marker', 'Escherichia coli', 'CaMV 35S', NULL, 'pea ribulose-1,5-bisphosphate carboxylase small subunit', NULL, 'Native', NULL, NULL, NULL, 'Enabled', NULL, NULL),
(16, 46, 'goxv247', 'gox', 'glyphosate oxidoreductase', 'HT', 'Herbicide tolerance', 'Ochrobactrum anthropi', 'figwort mosaic virus (FMV) 35S', 'chloroplast transit peptide from <I>A. thaliana</I>', NULL, NULL, 'Truncated', NULL, NULL, NULL, 'Enabled', NULL, NULL),
(17, 38, 'CP', 'CP', 'viral coat protein', 'VR', 'Virus resistance', 'Cucumber mosaic cucumovirus', 'CaMV 35S', NULL, NULL, NULL, 'Native', NULL, NULL, NULL, 'Enabled', NULL, NULL),
(18, 38, 'CP', 'CP', 'viral coat protein', 'VR', 'Virus resistance', 'Zucchini yellow mosaic potyvirus', 'CaMV 35S', NULL, NULL, NULL, 'Native', NULL, NULL, NULL, 'Enabled', NULL, NULL),
(19, 38, 'CP', 'CP', 'viral coat protein', 'VR', 'Virus resistance', 'Watermelon mosaic potyvirus 2', 'CaMV 35S', NULL, NULL, NULL, 'Native', NULL, NULL, NULL, 'Enabled', NULL, NULL),
(20, 30, 'CP', 'CP', 'viral coat protein', 'VR', 'Virus  resistance', 'Zucchini yellow mosaic potyvirus', '<p>CaMV 35S</p>\n', '', '', '', '<p>Native</p>\n', '', '', '', 'Enabled', NULL, '2013-08-23 12:29:46'),
(21, 30, 'CP', 'CP', 'viral coat protein', 'VR', 'Virus resistance', 'Watermelon mosaic potyvirus 2', 'CaMV 35S', NULL, NULL, NULL, 'Native', NULL, NULL, NULL, 'Enabled', NULL, NULL),
(22, 40, 'pat', 'PAT', 'phosphinothricin N-acetyltransferase', 'HT', 'Herbicide tolerance', 'S. viridochromogenes', 'CaMV 35S', NULL, 'CaMV 35S poly(A) signal', '1', 'Native', 'SVIR', NULL, NULL, 'Enabled', NULL, NULL),
(23, 40, 'bla', 'bla', 'beta lactamase', 'SM', 'Selectable marker', NULL, 'bacterial promoter', NULL, NULL, NULL, 'Partial, not expressed', NULL, NULL, NULL, 'Enabled', NULL, NULL),
(24, 42, 'pat', 'PAT', 'phosphinothricin N-acetyltransferase', 'HT', 'Herbicide tolerance', 'S. viridochromogenes', 'CaMV 35S', NULL, 'CaMV 35S poly(A) signal', '2', 'Native', 'SVIR', NULL, NULL, 'Enabled', NULL, NULL),
(25, 42, 'bla', 'bla', 'beta lactamase', 'SM', 'Selectable marker', NULL, 'bacterial promoter', NULL, NULL, NULL, 'Partial, not expressed', NULL, NULL, NULL, 'Enabled', NULL, NULL),
(26, 39, 'bar', 'PAT', 'phosphinothricin N-acetyltransferase', 'HT', 'Herbicide tolerance', 'S. hygroscopicus', 'CaMV 35S', NULL, NULL, NULL, 'NULL', 'SHYG', NULL, NULL, 'Enabled', NULL, NULL),
(27, 39, 'gus', 'gus', 'beta-D-glucuronidase', 'SM', 'Selectable marker', 'Escherichia coli', NULL, NULL, NULL, NULL, 'NULL', NULL, NULL, NULL, 'Enabled', NULL, NULL),
(28, 60, 'pat', 'PAT', 'phosphinothricin N-acetyltransferase', 'HT', 'Herbicide tolerance', 'S. viridochromogenes', 'CaMV 35S', NULL, 'CaMV 35S poly-A signal', NULL, 'Synthetic version of native gene', 'SVIR', NULL, NULL, 'Enabled', NULL, NULL),
(29, 61, 'PG', 'PG', 'polygalacturonase', 'DR', 'Ripening delayed', 'Tomato', 'CaMV 35S', NULL, 'tml gene and the transcript 7gene from the octopine-type Ti plasmid pTiA6', NULL, 'Native, anti-sense orientation', NULL, NULL, NULL, 'Enabled', NULL, NULL),
(30, 61, 'nptII', 'NPTII', 'neomycin phosphotransferase II', 'SM', 'Selectable marker', 'Escherichia coli', 'mannopine synthase from <I>A. tumefaciens</I>', NULL, 'mannopine synthase from <I>A. tumefaciens</I>', NULL, 'Native', NULL, NULL, NULL, 'Enabled', NULL, NULL),
(31, 33, 'pat', 'PAT', 'phosphinothricin N-acetyltransferase', 'HT', 'Herbicide tolerance', 'S. viridochromogenes', 'CaMV 35S', NULL, NULL, NULL, 'Native', 'SVIR', NULL, NULL, 'Enabled', NULL, NULL),
(32, 71, 'als', 'ALS', 'acetolactate synthase', 'MUT', 'Mutations', 'Z. mays', NULL, NULL, NULL, NULL, 'In vitro selection of imidazolinone tolerant mutants', NULL, NULL, NULL, 'Enabled', NULL, NULL),
(33, 22, 'pat', 'PAT', 'phosphinothricin N-acetyltransferase', 'HT', 'Herbicide tolerance', 'S. viridochromogenes', 'CaMV 35S', NULL, 'CaMV 35S poly(A) signal', '1', 'Native', 'SVIR', NULL, NULL, 'Enabled', NULL, NULL),
(34, 32, 'pat', 'PAT', 'phosphinothricin N-acetyltransferase', 'HT', 'Herbicide tolerance', 'S. viridochromogenes', 'CaMV 35S', NULL, NULL, '1', 'Native', 'SVIR', NULL, NULL, 'Enabled', NULL, NULL),
(35, 19, 'CP4 epsps', 'EPSPS', '5-enolpyruvyl shikimate-3-phosphate synthase', 'HT', 'Herbicide tolerance', 'Agrobacterium tumefaciens CP4', NULL, 'chloroplast transit peptide from <I>A. thaliana</I>', NULL, '1', 'Native', 'CP4EPS', NULL, NULL, 'Enabled', NULL, NULL),
(36, 19, 'goxv247', 'gox', 'glyphosate oxidoreductase', 'HT', 'Herbicide tolerance', 'Ochrobactrum anthropi', NULL, 'chloroplast transit peptide from <I>A. thaliana</I>', NULL, '1', 'Native', NULL, NULL, NULL, 'Enabled', NULL, NULL),
(37, 23, 'CP4 epsps', 'EPSPS', '5-enolpyruvyl shikimate-3-phosphate synthase', 'HT', 'Herbicide tolerance', 'Agrobacterium tumefaciens CP4', 'figwort mosaic virus (FMV) 35S', 'chloroplast transit peptide from <I>A. thaliana</I> EPSPS gene (CTP2)', NULL, '1', 'Native', 'CP4EPS', NULL, NULL, 'Enabled', NULL, NULL),
(38, 23, 'goxv247', 'gox', 'glyphosate oxidoreductase', 'HT', 'Herbicide tolerance', 'Ochrobactrum anthropi', 'figwort mosaic virus (FMV) 35S', 'chloroplast transit peptide from <I>A. thaliana</I> SSU1A gene (CTP1)', NULL, '1', NULL, NULL, NULL, NULL, 'Enabled', NULL, NULL),
(39, 24, 'als', 'ALS', 'acetolactate synthase', 'MUT', 'Mutations', 'Brassica napus', NULL, NULL, NULL, NULL, 'Selected following chemical mutagenesis.', NULL, NULL, NULL, 'Enabled', NULL, NULL),
(40, 26, 'barnase', 'barnase', 'barnase ribonuclease', 'MS', 'Male sterility', 'Bacillus amyloliquefaciens', 'pTa 29 pollen specific promoter from <I>Nicotiana tabacum</I>', NULL, NULL, '1', 'Introduced into MS1', NULL, NULL, NULL, 'Enabled', NULL, NULL),
(41, 26, 'barstar', 'barstar', 'barnase ribonuclease inhibitor', 'RF', 'Fertility restoration', 'Bacillus amyloliquefaciens', 'anther-specific promoter', NULL, NULL, '1', 'Introduced into RF1', NULL, NULL, NULL, 'Enabled', NULL, NULL),
(42, 26, 'bar', 'PAT', 'phosphinothricin N-acetyltransferase', 'HT', 'Herbicide tolerance', 'S. hygroscopicus', 'PSsuAra from <I>Arabidopsis thaliana</I>', 'chloroplast transit peptide from <I>A. thaliana</I>', NULL, '1', 'Introduced into both MS1 and RF1', 'SHYG', NULL, NULL, 'Enabled', NULL, NULL),
(43, 26, 'nptII', 'NPTII', 'neomycin phosphotransferase II', 'SM', 'Selectable marker', 'Escherichia coli', 'nopaline synthase (<I>nos</I>) from <I>A. tumefaciens</I>', NULL, 'octopine synthase', NULL, 'Native; both MS1 and RF1', NULL, NULL, NULL, 'Enabled', NULL, NULL),
(44, 27, 'barnase', 'barnase', 'barnase ribonuclease', 'MS', 'Male sterility', 'Bacillus amyloliquefaciens', 'pTa 29 pollen specific promoter from <I>Nicotiana tabacum</I>', NULL, NULL, '1', 'Introduced into MS8', NULL, NULL, NULL, 'Enabled', NULL, NULL),
(45, 27, 'barstar', 'barstar', 'barnase ribonuclease inhibitor', 'RF', 'Fertility restoration', 'Bacillus amyloliquefaciens', 'anther-specific promoter', NULL, NULL, '1', 'Introduced into RF3', NULL, NULL, NULL, 'Enabled', NULL, NULL),
(46, 27, 'bar', 'PAT', 'phosphinothricin N-acetyltransferase', 'HT', 'Herbicide tolerance', 'S. hygroscopicus', 'PSsuAra from <I>Arabidopsis thaliana</I>', 'chloroplast transit peptide from <I>A. thaliana</I>', NULL, '1', 'Introduced into MS8 and RF3', 'SHYG', NULL, NULL, 'Enabled', NULL, NULL),
(47, 37, 'bar', 'PAT', 'phosphinothricin N-acetyltransferase', 'HT', 'Herbicide tolerance', 'S. hygroscopicus', 'PSsuAra from <I>Arabidopsis thaliana</I>', 'chloroplast transit peptide from <I>A. thaliana</I>', NULL, NULL, 'NULL', 'SHYG', NULL, NULL, 'Enabled', NULL, NULL),
(48, 37, 'barnase', 'barnase', 'barnase ribonuclease', 'MS', 'Male sterility', 'Bacillus amyloliquefaciens', 'pTa 29 pollen specific promoter from <I>Nicotiana tabacum</I>', NULL, NULL, NULL, 'NULL', NULL, NULL, NULL, 'Enabled', NULL, NULL),
(49, 37, 'barstar', 'barstar', 'barnase ribonuclease inhibitor', 'RF', 'Fertility restoration', 'Bacillus amyloliquefaciens', 'anther-specific promoter', NULL, NULL, NULL, 'NULL', NULL, NULL, NULL, 'Enabled', NULL, NULL),
(50, 36, 'bar', 'PAT', 'phosphinothricin N-acetyltransferase', 'HT', 'Herbicide tolerance', 'S. hygroscopicus', 'PSsuAra from <I>Arabidopsis thaliana</I>', 'chloroplast transit peptide from <I>A. thaliana</I>', NULL, NULL, 'NULL', 'SHYG', NULL, NULL, 'Enabled', NULL, NULL),
(51, 36, 'barnase', 'barnase', 'barnase ribonuclease', 'MS', 'Male sterility', 'Bacillus amyloliquefaciens', 'pTa 29 pollen specific promoter from <I>Nicotiana tabacum</I>', NULL, NULL, NULL, 'NULL', NULL, NULL, NULL, 'Enabled', NULL, NULL),
(52, 36, 'barstar', 'barstar', 'barnase ribonuclease inhibitor', 'RF', 'Fertility restoration', 'Bacillus amyloliquefaciens', 'anther-specific promoter', NULL, NULL, NULL, 'NULL', NULL, NULL, NULL, 'Enabled', NULL, NULL),
(53, 18, 'Bay TE', 'TE', 'thioesterase', 'FA', 'Fatty acid composition', 'Umbellularia californica', '<p>seed-specific promoter</p>\n', NULL, '', '15 copies at 5 loci (original transformant)', '<p>Native</p>\n', '', '', '', 'Enabled', NULL, '2013-09-03 13:39:25'),
(54, 18, 'nptII', 'NPTII', 'neomycin phosphotransferase II', 'SM', 'Selectable marker', 'Escherichia coli', 'CaMV 35S', NULL, 'tml3''  from <i>Agrobacterium tumefaciens</i>', '', 'Native', NULL, NULL, NULL, 'Enabled', NULL, '2013-09-03 13:39:25'),
(55, 70, 'sam-k', 'SAMase', 'S-adenosylmethionine hydrolase', 'DR', 'Ripening delayed', 'E. coli bacteriophage T3', NULL, NULL, NULL, NULL, 'NULL', NULL, NULL, NULL, 'Enabled', NULL, NULL),
(56, 70, 'nptII', 'NPTII', 'neomycin phosphotransferase II', 'SM', 'Selectable marker', 'Escherichia coli', 'nopaline synthase (<I>nos</I>) from <I>A. tumefaciens</I>', NULL, NULL, NULL, 'Native', NULL, NULL, NULL, 'Enabled', NULL, NULL),
(57, 4, 'bxn', 'nitrilase', 'nitrilase', 'HT', 'Herbicide tolerance', 'Klebsiella pneumoniae subspecies ozanae', 'CaMV 35S', 'Enhancer: non-translated leader of RuBisCO small subunit gene derived from maize', '<I>A. tumefaciens</I> nopaline synthase (<I>nos</I>) 3''-untranslated region', '1', 'Native', 'BXN', NULL, NULL, 'Enabled', NULL, NULL),
(58, 11, 'CP4 epsps', 'EPSPS', '5-enolpyruvyl shikimate-3-phosphate synthase', 'HT', 'Herbicide tolerance', 'Agrobacterium tumefaciens CP4', NULL, 'chloroplast transit peptide from <I>A. thaliana</I>', NULL, '1', 'Native; Introduction through interpsecific cross', 'CP4EPS', NULL, NULL, 'Enabled', NULL, '2013-09-03 11:25:26'),
(59, 11, 'goxv247', 'gox', 'glyphosate oxidoreductase', 'HT', 'Herbicide tolerance', 'Ochrobactrum anthropi', NULL, 'chloroplast transit peptide from <I>A. thaliana</I>', NULL, '1', 'Truncated; Inserted by interspecific cross', NULL, NULL, NULL, 'Enabled', NULL, '2013-09-03 11:25:26'),
(60, 47, 'bar', 'PAT', 'phosphinothricin N-acetyltransferase', 'HT', 'Herbicide tolerance', 'S. hygroscopicus', 'PSsuAra from <I>Arabidopsis thaliana</I>', 'chloroplast transit peptide from <I>A. thaliana</I>', 'TL-DNA gene 7 terminator from <I>Agrobacterium tumefaciens</I>', NULL, 'NULL', 'SHYG', NULL, NULL, 'Enabled', NULL, NULL),
(61, 47, 'barnase', 'barnase', 'barnase ribonuclease', 'MS', 'Male sterility', 'Bacillus amyloliquefaciens', 'pTa 29 pollen specific promoter from <I>Nicotiana tabacum</I>', NULL, '<I>A. tumefaciens</I> nopaline synthase (<I>nos</I>) 3''-untranslated region', NULL, 'NULL', NULL, NULL, NULL, 'Enabled', NULL, NULL),
(62, 47, 'nptII', 'NPTII', 'neomycin phosphotransferase II', 'SM', 'Selectable marker', 'Escherichia coli', 'nopaline synthase (<I>nos</I>) from <I>A. tumefaciens</I>', NULL, 'octopine synthase', NULL, 'Native', NULL, NULL, NULL, 'Enabled', NULL, NULL),
(63, 17, 'ACCase', 'ACCase', 'acetyl-CoA-carboxylase', 'MUT', 'Mutations', 'Z. mays', 'N/A', 'N/A', 'N/A', 'single partially dominant allele', 'No introduced genetic material. Sethoxydim selection.', NULL, NULL, NULL, 'Enabled', NULL, NULL),
(64, 51, 'cry1Ab', 'cry1Ab', 'Cry1Ab delta-endotoxin (Btk HD-1)', 'IR', 'Insect resistance', 'Bacillus thuringiensis subsp. kurstaki (Btk)', 'CaMV 35S', 'HSP70 intron', 'A. tumefaciens nopaline synthase (nos) 3''-untranslated region', '', 'Native', 'BTK', NULL, NULL, 'Enabled', NULL, NULL),
(65, 51, 'CP4 epsps', 'EPSPS', '5-enolpyruvyl shikimate-3-phosphate synthase', 'SM', 'Selectable marker', 'Agrobacterium tumefaciens CP4', 'CaMV 35S', 'chloroplast transit peptide from A. thaliana EPSPS gene (CTP1)', 'A. tumefaciens nopaline synthase (nos) 3''-untranslated region', '', '', 'CP4EPS', NULL, NULL, 'Enabled', NULL, NULL),
(66, 51, 'goxv247', 'gox', 'glyphosate oxidoreductase', 'HT', 'Herbicide tolerance', 'Ochrobactrum anthropi', 'CaMV 35S', 'chloroplast transit peptide from A. thaliana ribulose-1,5-bisphosphate carboxylase gene (CTP2)', 'A. tumefaciens nopaline synthase (nos) 3''-untranslated region', '', 'Expression not detected in plants', NULL, NULL, NULL, 'Enabled', NULL, NULL),
(67, 9, 'cry1Ab', 'cry1Ab', 'Cry1Ab delta-endotoxin (<I>Btk</I> HD-1)', 'IR', 'Insect resistance', 'Bacillus thuringiensis subsp. kurstaki (Btk)', 'enhanced CaMV 35S, maize HSP70 intron', NULL, 'None. Lost through 3'' truncation during integration', '1', 'Truncated', 'BTK', NULL, NULL, 'Enabled', NULL, '2013-09-02 14:27:02'),
(68, 25, 'cry1Ab', 'cry1Ab', 'Cry1Ab delta-endotoxin (<I>Btk</I> HD-1)', 'IR', 'Insect resistance', 'Bacillus thuringiensis subsp. kurstaki (Btk)', 'first copy promoter from the maize phosphoenolpyruvate carboxylase gene and the CaMV 35S terminator, and the second copy under the regulation of a promoter derived from a maize calcium-dependent protein kinase gene and the CaMV 35S terminator', NULL, 'CaMV 35S poly(A) signal', '2', 'Native', 'BTK', NULL, NULL, 'Enabled', NULL, NULL),
(69, 25, 'bar', 'PAT', 'phosphinothricin N-acetyltransferase', 'SM', 'Selectable marker', 'S. hygroscopicus', 'CaMV 35S', NULL, 'CaMV 35S poly(A) signal', NULL, 'NULL', 'SHYG', NULL, NULL, 'Enabled', NULL, NULL),
(70, 49, 'bar', 'PAT', 'phosphinothricin N-acetyltransferase', 'HT', 'Herbicide tolerance', 'S. hygroscopicus', 'CaMV 35S', NULL, '<I>A. tumefaciens</I> nopaline synthase (<I>nos</I>) 3''-untranslated region', '>=4', 'NULL', 'SHYG', NULL, NULL, 'Enabled', NULL, NULL),
(71, 49, 'bla', 'bla', 'beta lactamase', 'SM', 'Selectable marker', NULL, 'bacterial promoter', NULL, NULL, NULL, 'Not expressed in plant tissues', NULL, NULL, NULL, 'Enabled', NULL, NULL),
(72, 7, 'bar', 'PAT', 'phosphinothricin N-acetyltransferase', 'HT', 'Herbicide tolerance', 'S. hygroscopicus', 'CaMV 35S', NULL, 'T-DNA transcript number 7 (Tr7) termination signal', '2', '1 copy rearranged', 'SHYG', NULL, NULL, 'Enabled', NULL, '2013-09-02 14:23:30'),
(73, 7, 'bla', 'bla', 'beta lactamase', 'SM', 'Selectable marker', NULL, 'bacterial promoter', NULL, NULL, '4', 'Not expressed in plant tissues', NULL, NULL, NULL, 'Enabled', NULL, '2013-09-02 14:23:30'),
(74, 5, 'cry1Ab', 'cry1Ab', 'Cry1Ab delta-endotoxin (<I>Btk</I> HD-1)', 'IR', 'Insect resistance', 'Bacillus thuringiensis subsp. kurstaki (Btk)', 'enhanced CaMV 35S', NULL, '<I>A. tumefaciens</I> nopaline synthase (<I>nos</I>) 3''-untranslated region', '1 full length, 2 partial', 'Truncated, modified; Located within first insertion site', 'BTK', NULL, NULL, 'Enabled', NULL, NULL),
(75, 49, 'cry9c', 'cry9c', 'cry9c delta-endotoxin', 'IR', 'Insect resistance', 'Bacillus thuringiensis subsp. Tolworthi', 'CaMV 35S', '; leader sequence of the cab22L gene of Petunia hybridia (chloroplast transit peptide)', 'CaMV 35S poly(A) signal', '>=1', 'Truncated N-,C-terminal', 'CR9C', NULL, NULL, 'Enabled', NULL, NULL),
(76, 7, 'cry1Ac', 'cry1Ac', 'Cry1Ac delta-endotoxin', 'IR', 'Insect resistance', 'Bacillus thuringiensis subsp. kurstaki (Btk)', 'CaMV 35S, octopine synthase double enhancers', '; maize alcohol dehydrogenase (adh1) gene introns I and VI (promote transcript stability)', 'potato <i>pinII</i> termination and poly(A) signal', '2', '', 'BTKC', NULL, NULL, 'Enabled', NULL, '2013-09-02 14:23:30'),
(77, 7, 'pinII', 'pinII', 'protease inhibitor', 'IR', 'Insect resistance', 'S. tuberosum', 'CaMV 35S', '; maize alcohol dehydrogenase (adh1) gene introns I and VI (promote transcript stability)', 'potato pinII and Tr7 termination and poly(A) signal', '1', 'Incomplete, non-functional', NULL, NULL, NULL, 'Enabled', NULL, '2013-09-02 14:23:30'),
(78, 16, 'cry1Ab', 'cry1Ab', 'Cry1Ab delta-endotoxin (<I>Btk</I> HD-1)', 'IR', 'Insect resistance', 'Bacillus thuringiensis subsp. kurstaki (Btk)', 'CaMV 35S', 'IVS 6 intron from the maize alcohol dehydrogenase gene', '<I>A. tumefaciens</I> nopaline synthase (<I>nos</I>) 3''-untranslated region', '1', 'Truncated, modified', 'BTK', NULL, NULL, 'Enabled', NULL, NULL),
(79, 16, 'pat', 'PAT', 'phosphinothricin N-acetyltransferase', 'HT', 'Herbicide tolerance', 'S. viridochromogenes', 'CaMV 35S', 'IVS 2 intron from the maize alcohol dehydrogenase gene', '<I>A. tumefaciens</I> nopaline synthase (<I>nos</I>) 3''-untranslated region', '1', 'Modified for enhanced expression', 'SVIR', NULL, NULL, 'Enabled', NULL, NULL),
(80, 5, 'CP4 epsps', 'EPSPS', '5-enolpyruvyl shikimate-3-phosphate synthase', 'HT', 'Herbicide tolerance', 'Agrobacterium tumefaciens CP4', 'enhanced CaMV 35S, HSP70 intron, gox cassette', 'chloroplast transit peptide from <I>A. thaliana</I> EPSPS gene (CTP2)', NULL, '1', 'Located within first insertion site', 'CP4EPS', NULL, NULL, 'Enabled', NULL, NULL),
(81, 5, 'goxv247', 'gox', 'glyphosate oxidoreductase', 'HT', 'Herbicide tolerance', 'Ochrobactrum anthropi', NULL, 'chloroplast transit peptide from <I>A. thaliana</I> SSU1A gene (CTP1)', NULL, '2+1', '2 full length copies at first insertion site, 1 and second site', NULL, NULL, NULL, 'Enabled', NULL, NULL),
(82, 5, 'nptII', 'NPTII', 'neomycin phosphotransferase II', 'SM', 'Selectable marker', 'Escherichia coli', NULL, NULL, NULL, '2', 'Not expressed in plant tissues; 1 copy at each insertion site', NULL, NULL, NULL, 'Enabled', NULL, NULL),
(83, 12, 'cry1Ab', 'cry1Ab', 'Cry1Ab delta-endotoxin (<I>Btk</I> HD-1)', 'IR', 'Insect resistance', 'Bacillus thuringiensis subsp. kurstaki (Btk)', 'enhanced CaMV 35S', NULL, '<I>A. tumefaciens</I> nopaline synthase (<I>nos</I>) 3''-untranslated region', '1', 'Truncated, modified; second partial copy present', 'BTK', NULL, NULL, 'Enabled', NULL, '2013-05-10 15:06:16'),
(84, 12, 'CP4 epsps', 'EPSPS', '5-enolpyruvyl shikimate-3-phosphate synthase', 'SM', 'Selectable marker', 'Agrobacterium tumefaciens CP4', 'enhanced CaMV 35S', 'chloroplast transit peptide from <I>A. thaliana</I> EPSPS gene (CTP2)', '', '2', '', 'CP4EPS', NULL, NULL, 'Enabled', NULL, '2013-05-10 15:06:16'),
(85, 12, 'goxv247', 'gox', 'glyphosate oxidoreductase', 'HT', 'Herbicide tolerance', 'Ochrobactrum anthropi', '', 'chloroplast transit peptide from <I>A. thaliana</I> SSU1A gene (CTP1)', '', '', 'partial copy, no expression detected', NULL, NULL, NULL, 'Enabled', NULL, '2013-05-10 15:06:16'),
(86, 48, 'bar', 'PAT', 'phosphinothricin N-acetyltransferase', 'HT', 'Herbicide tolerance', 'S. hygroscopicus', 'CaMV 35S', NULL, 'T-DNA transcript number 7 (Tr7) termination signal', '1', 'Modified', 'SHYG', NULL, NULL, 'Enabled', NULL, NULL),
(87, 48, 'bla', 'bla', 'beta lactamase', 'SM', 'Selectable marker', NULL, 'bacterial promoter', NULL, NULL, NULL, 'Not expressed in plant tissues', NULL, NULL, NULL, 'Enabled', NULL, NULL),
(88, 74, 'CP4 epsps', 'EPSPS', '5-enolpyruvyl shikimate-3-phosphate synthase', 'HT', 'Herbicide tolerance', 'Agrobacterium tumefaciens CP4', 'P-ract1/ract1 intron containing rice actin 1 promoter, transcription start site', 'chloroplast transit peptide from A. thaliana EPSPS gene (CTP2)', 'A. tumefaciens nopaline synthase (nos) 3''-untranslated region', '1', 'CP4 EPSPS gene modified for plant-preferred codons', 'CP4EPS', NULL, NULL, 'Enabled', NULL, '2013-09-04 13:46:43'),
(89, 14, 'aad', 'aad', '3"(9)-O-aminoglycoside adenylyltransferase', 'SM', 'Selectable marker', NULL, 'bacterial promoter', NULL, NULL, NULL, 'Not expressed in plant tissues', NULL, NULL, NULL, 'Enabled', NULL, NULL),
(90, 6, 'bla', 'bla', 'beta lactamase', 'SM', 'Selectable marker', NULL, 'bacterial promoter', NULL, NULL, NULL, 'Truncated beta-lactamase gene missing about 25 % of the gene from the 5'' end; not expressed', NULL, NULL, NULL, 'Enabled', NULL, NULL),
(91, 15, 'als', 'ALS', 'acetolactate synthase', 'MUT', 'Mutations', 'Z. mays', NULL, NULL, NULL, NULL, 'Imidazolinone selection of somatic embryos', NULL, NULL, NULL, 'Enabled', NULL, NULL),
(92, 3, 'als', 'ALS', 'acetolactate synthase', 'MUT', 'Mutations', 'Z. mays', NULL, NULL, NULL, NULL, 'Imidazolinone selection following chemical mutagenesis using ethyl methanesulfonate (EMS)', NULL, NULL, NULL, 'Enabled', NULL, NULL),
(93, 6, 'pat', 'PAT', 'phosphinothricin N-acetyltransferase', 'HT', 'Herbicide tolerance', 'S. viridochromogenes', 'CaMV 35S', NULL, 'CaMV 35S poly(A) signal', '3 or 1*', 'Modified for enhanced expression; PEG mediated uptake into plant protoplasts; 3 copies in T14, 1 copy in T25', 'SVIR', NULL, NULL, 'Enabled', NULL, NULL),
(94, 1, 'epsps', 'EPSPS', '5-enolpyruvyl shikimate-3-phosphate synthase', 'HT', 'Herbicide tolerance', 'Z. mays', 'rice actin I promoter and intron sequences', '; ribulose-1,5-bisphosphate carboxylase oxygenase (RuBisCo) derived chloroplast transit peptide squences (from corn & sunflower)', 'A. tumefaciens nopaline synthase (nos) 3\\\\\\''-untranslated region', '3*', 'Modified by in vitro mutagenesis; single insertion site with 3 complete copies of EPSPS cassette plus 3 incomplete copies', NULL, NULL, NULL, 'Enabled', NULL, NULL),
(95, 50, 'dam', 'dam', 'DNA adenine methylase', 'MS', 'Male sterility', 'Escherichia coli', 'Maize 512del anther-specific promoter', NULL, 'Solanum tuberosum proteinase inhibitor II (pinII) transcription termination signal', '1 (676); 3 (678); 1+3 partial (680)', 'Native', NULL, NULL, NULL, 'Enabled', NULL, NULL),
(96, 50, 'pat', 'PAT', 'phosphinothricin N-acetyltransferase', 'HT', 'Herbicide tolerance', 'S. viridochromogenes', 'CaMV 35S', NULL, NULL, '2 (676); 1+1 partial (678); 1 (680)', 'Native', 'SVIR', NULL, NULL, 'Enabled', NULL, NULL),
(97, 13, 'barnase', 'barnase', 'barnase ribonuclease', 'MS', 'Male sterility', 'Bacillus amyloliquefaciens', 'pTa 29 pollen specific promoter from <I>Nicotiana tabacum</I>', NULL, NULL, '3 at 1 insertion site', 'NULL', NULL, NULL, NULL, 'Enabled', NULL, NULL),
(98, 13, 'bar', 'PAT', 'phosphinothricin N-acetyltransferase', 'HT', 'Herbicide tolerance', 'S. hygroscopicus', 'CaMV 35S', NULL, '<I>A. tumefaciens</I> nopaline synthase (<I>nos</I>) 3''-untranslated region', '3 at 1 insertion site', 'Modified', 'SHYG', NULL, NULL, 'Enabled', NULL, NULL),
(99, 13, 'bla', 'bla', 'beta lactamase', 'SM', 'Selectable marker', NULL, 'bacterial promoter', NULL, NULL, NULL, 'Not expressed in plant tissues', NULL, NULL, NULL, 'Enabled', NULL, NULL),
(100, 34, 'cry1Ac', 'cry1Ac', 'Cry1Ac delta-endotoxin', 'IR', 'Insect resistance', 'Bacillus thuringiensis subsp. kurstaki (Btk)', 'CaMV 35S', NULL, NULL, NULL, 'Truncated', 'BTKC', NULL, NULL, 'Enabled', NULL, NULL),
(101, 34, 'bxn', 'nitrilase', 'nitrilase', 'HT', 'Herbicide tolerance', 'Klebsiella pneumoniae subspecies ozanae', 'chimera of the 35S promoter and the promoter from a mannopine synthase gene from <I>A. tumefaciens</I>', NULL, NULL, NULL, 'Native', NULL, NULL, NULL, 'Enabled', NULL, NULL),
(102, 34, 'nptII', 'NPTII', 'neomycin phosphotransferase II', 'SM', 'Selectable marker', 'Escherichia coli', 'bacterial promoter', NULL, NULL, NULL, 'Not expressed in plant tissues', NULL, NULL, NULL, 'Enabled', NULL, NULL),
(103, 52, 'CP4 epsps', 'EPSPS', '5-enolpyruvyl shikimate-3-phosphate synthase', 'HT', 'Herbicide tolerance', 'Agrobacterium tumefaciens CP4', 'CMoVb from modified figwort mosaic virus (FMV)', 'chloroplast transit peptide from <I>A. thaliana</I> EPSPS gene (CTP2)', 'P. sativum (pea) ribulose-1,5-bisphosphate carboxylase small subunit non-translated region', '1 (line 1445)', 'modified for plant-preferred codons; these data refer to line 1445 only', 'CP4EPS', NULL, NULL, 'Enabled', NULL, NULL),
(104, 52, 'nptII', 'NPTII', 'neomycin phosphotransferase II', 'SM', 'Selectable marker', 'Escherichia coli', 'CaMV 35S', NULL, '<I>A. tumefaciens</I> nopaline synthase (<I>nos</I>) 3''-untranslated region', NULL, 'NULL', NULL, NULL, NULL, 'Enabled', NULL, NULL),
(105, 52, 'aad', 'aad', '3"(9)-O-aminoglycoside adenylyltransferase', 'SM', 'Selectable marker', NULL, 'bacterial promoter', NULL, NULL, NULL, 'Not expressed in plant tissues', NULL, NULL, NULL, 'Enabled', NULL, NULL),
(106, 14, 'cry1Ac', 'cry1Ac', 'Cry1Ac delta-endotoxin', 'IR', 'Insect resistance', 'Bacillus thuringiensis subsp. kurstaki (Btk)', 'double enhanced CaMV 35S', NULL, '3'' poly(A) signal from soybean alpha subunit of the beta-conglycinin gene', '>=1', 'Truncated; Line 757: 1 complete T-DNA and 1 paritial T-DNA insertion event', 'BTKC', NULL, NULL, 'Enabled', NULL, NULL),
(107, 14, 'nptII', 'NPTII', 'neomycin phosphotransferase II', 'SM', 'Selectable marker', 'Escherichia coli', 'nopaline synthase (<I>nos</I>) from <I>A. tumefaciens</I>', NULL, NULL, '>=1', 'Native', NULL, NULL, NULL, 'Enabled', NULL, NULL),
(108, 29, 'bxn', 'nitrilase', 'nitrilase', 'HT', 'Herbicide tolerance', 'Klebsiella pneumoniae subspecies ozanae', NULL, NULL, NULL, NULL, 'Native', NULL, NULL, NULL, 'Enabled', NULL, NULL),
(109, 29, 'nptII', 'NPTII', 'neomycin phosphotransferase II', 'SM', 'Selectable marker', 'Escherichia coli', 'nopaline synthase (<I>nos</I>) from <I>A. tumefaciens</I>', NULL, NULL, NULL, 'Native', NULL, NULL, NULL, 'Enabled', NULL, NULL),
(110, 35, 'als', 'ALS', 'acetolactate synthase', 'HT', 'Herbicide tolerance', 'chimera of 2 resistant AHAS genes (S4-Hr4)', NULL, NULL, NULL, '2 at 1-2 loci', 'Site-directed mutagenesis', NULL, NULL, NULL, 'Enabled', NULL, NULL),
(111, 8, 'als', 'ALS', 'acetolactate synthase', 'HT', 'Herbicide tolerance', 'chlorsulfuron tolerant line of <I>A. thaliana</I>', 'native (<I>A. thaliana</I>)', NULL, 'native (A. thaliana)', '>=2', 'One amino acid substitution from native protein', NULL, NULL, NULL, 'Enabled', NULL, NULL),
(112, 8, 'nptII', 'NPTII', 'neomycin phosphotransferase II', 'SM', 'Selectable marker', 'Escherichia coli', 'nopaline synthase (<I>nos</I>) from <I>A. tumefaciens</I>', NULL, NULL, '>=2', 'Native', NULL, NULL, NULL, 'Enabled', NULL, NULL),
(113, 8, 'nos', 'nos', 'nopaline synthase', 'SM', 'Selectable marker', 'Agrobacterium tumefaciens CP4', 'nopaline synthase (nos) from A. tumefaciens', NULL, NULL, '>=2', 'Native', NULL, NULL, NULL, 'Enabled', NULL, NULL),
(114, 31, 'prsv-cp', 'PRSV-CP', 'viral coat protein', 'VR', 'Virus resistance', 'papaya ringspot potyvirus (PRSV)', 'CaMV 35S', NULL, 'CaMV 35S', NULL, 'Native', NULL, NULL, NULL, 'Enabled', NULL, NULL),
(115, 31, 'nptII', 'NPTII', 'neomycin phosphotransferase II', 'SM', 'Selectable marker', 'Escherichia coli', 'nopaline synthase (<I>nos</I>) from <I>A. tumefaciens</I>', NULL, '<I>A. tumefaciens</I> nopaline synthase (<I>nos</I>) 3''-untranslated region', NULL, 'Native', NULL, NULL, NULL, 'Enabled', NULL, NULL),
(116, 31, 'gus', 'gus', 'beta-D-glucuronidase', 'SM', 'Selectable marker', 'Escherichia coli', 'CaMV 35S', NULL, '<I>A. tumefaciens</I> nopaline synthase (<I>nos</I>) 3''-untranslated region', NULL, 'Native; not present in line 63-1', NULL, NULL, NULL, 'Enabled', NULL, NULL),
(117, 10, 'nptII', 'NPTII', 'neomycin phosphotransferase II', 'SM', 'Selectable marker', 'Escherichia coli', 'CaMV 35S', NULL, '<I>A. tumefaciens</I> nopaline synthase (<I>nos</I>) 3''-untranslated region', NULL, 'Native', NULL, NULL, NULL, 'Enabled', NULL, NULL),
(118, 20, 'nptII', 'NPTII', 'neomycin phosphotransferase II', 'SM', 'Selectable marker', 'Escherichia coli', 'CaMV 35S', NULL, '<I>A. tumefaciens</I> nopaline synthase (<I>nos</I>) 3''-untranslated region', '1 for BT6, BT12, BT17, and BT23; 2 for BT10, BT16', 'Native', NULL, NULL, NULL, 'Enabled', NULL, NULL),
(119, 10, 'cry3A', 'cry3A', 'cry3A delta-endotoxin', 'IR', 'Insect resistance', 'Bacillus thuringiensis subsp. Tenebrionis', 'double enhanced CaMV 35S or ats1A promoter of Arabidopsis thaliana ribulose-1,5-bisphosphate carboxylase', NULL, '3'' poly(A) signal from pea ribulose-1,5-bisphosphate carboxylase, small subunit (rbcS) gene', '1-3 loci depending on line', 'Modified to enhance expression (plant preferred codon usage)', 'BT3A', NULL, NULL, 'Enabled', NULL, NULL),
(120, 20, 'cry3A', 'cry3A', 'cry3A delta-endotoxin', 'IR', 'Insect resistance', 'Bacillus thuringiensis subsp. Tenebrionis', 'double enhanced CaMV 35S', NULL, '3'' poly(A) signal from pea ribulose-1,5-bisphosphate carboxylase, small subunit (rbcS) gene', '1 for BT6, BT12, BT17, and BT23; 2 for BT10, BT16', 'Modified to enhance expression (plant preferred codon usage)', 'BT3A', NULL, NULL, 'Enabled', NULL, NULL),
(121, 54, 'cry3A', 'cry3A', 'cry3A delta-endotoxin', 'IR', 'Insect resistance', 'Bacillus thuringiensis subsp. Tenebrionis', 'arabSSU1A: <I>A. thaliana</I> ribulose-1,5-bisphosphate carboxylase (Rubisco) small subunit promoter', NULL, '<I>A. tumefaciens</I> nopaline synthase (<I>nos</I>) 3''-untranslated region', NULL, 'Modified to enhance expression (plant preferred codon usage)', 'BT3A', NULL, NULL, 'Enabled', NULL, NULL),
(122, 54, 'nptII', 'NPTII', 'neomycin phosphotransferase II', 'SM', 'Selectable marker', 'Escherichia coli', 'nopaline synthase (<I>nos</I>) from <I>A. tumefaciens</I>', NULL, '<I>A. tumefaciens</I> nopaline synthase (<I>nos</I>) 3''-untranslated region', NULL, 'Native', NULL, NULL, NULL, 'Enabled', NULL, NULL),
(123, 54, 'CP', 'CP', 'viral coat protein', 'VR', 'Virus resistance', 'potato potyvirus Y (PVY) strain O (common strain)', 'figwort mosaic virus (FMV) 35S', ';leader sequence from the Glycine max heat-shock protein, Hsp 17.9', '3'' poly(A) signal from pea ribulose-1,5-bisphosphate carboxylase, small subunit (rbcS) gene', NULL, 'Native', NULL, NULL, NULL, 'Enabled', NULL, NULL),
(124, 54, 'aad', 'aad', '3"(9)-O-aminoglycoside adenylyltransferase', 'SM', 'Selectable marker', NULL, 'bacterial promoter', NULL, NULL, NULL, 'Not expressed in plant tissues', NULL, NULL, NULL, 'Enabled', NULL, NULL),
(125, 53, 'cry3A', 'cry3A', 'cry3A delta-endotoxin', 'IR', 'Insect resistance', 'Bacillus thuringiensis subsp. Tenebrionis', 'arabSSU1A: <I>A. thaliana</I> ribulose-1,5-bisphosphate carboxylase (Rubisco) small subunit promoter', NULL, '<I>A. tumefaciens</I> nopaline synthase (<I>nos</I>) 3''-untranslated region', '', 'Modified to enhance expression (plant preferred codon usage)', 'BT3A', NULL, NULL, 'Enabled', NULL, '2013-07-31 17:11:00'),
(126, 53, 'Rep', 'Rep', 'replicase (RNA dependent RNA polymerase)', 'VR', 'Virus resistance', 'potato leafroll luteovirus (PLRV) orf 1', 'figwort mosaic virus (FMV) 35S', '77-nucleotide leader sequence from soybean 17.9 kDa HSP', 'P. sativum (pea) ribulose-1,5-bisphosphate carboxylase small subunit E9 gene 3'' non-translated region', '', '', NULL, NULL, NULL, 'Enabled', NULL, '2013-07-31 17:11:00'),
(127, 53, 'Hel', 'Hel', 'helicase', 'VR', 'Virus resistance', 'potato leafroll luteovirus (PLRV) orf 2', 'figwort mosaic virus (FMV) 35S', '77-nucleotide leader sequence from soybean 17.9 kDa HSP', 'P. sativum (pea) ribulose-1,5-bisphosphate carboxylase small subunit E9 gene 3'' non-translated region', '', '', NULL, NULL, NULL, 'Enabled', NULL, '2013-07-31 17:11:00'),
(128, 53, 'nptII', 'NPTII', 'neomycin phosphotransferase II', 'SM', 'Selectable marker', 'Escherichia coli', 'nopaline synthase (<I>nos</I>) from <I>A. tumefaciens</I>', '', '<I>A. tumefaciens</I> nopaline synthase (<I>nos</I>) 3''-untranslated region', '', 'Native', NULL, NULL, NULL, 'Enabled', NULL, '2013-07-31 17:11:00'),
(129, 55, 'bar', 'PAT', 'phosphinothricin N-acetyltransferase', 'HT', 'Herbicide tolerance', 'S. hygroscopicus', 'CaMV 35S', NULL, 'CaMV 35S poly(A) signal', NULL, 'NULL', 'SHYG', NULL, NULL, 'Enabled', NULL, NULL),
(130, 21, 'CP4 epsps', 'EPSPS', '5-enolpyruvyl shikimate-3-phosphate synthase', 'HT', 'Herbicide tolerance', 'Agrobacterium tumefaciens CP4', 'enhanced CaMV 35S', 'chloroplast transit peptide from Petunia hybrida', '<I>A. tumefaciens</I> nopaline synthase (<I>nos</I>) 3''-untranslated region', '1*', 'Native; Also 2 partial gene sequences (250 bp; 72 bp)', 'CP4EPS', NULL, NULL, 'Enabled', NULL, NULL),
(131, 41, 'gus', 'gus', 'beta-D-glucuronidase', 'SM', 'Selectable marker', 'Escherichia coli', 'CaMV 35S', NULL, '<I>A. tumefaciens</I> nopaline synthase (<I>nos</I>) 3''-untranslated region', NULL, 'Silenced in the lines submitted for approval.', NULL, NULL, NULL, 'Enabled', NULL, NULL),
(132, 41, 'bla', 'bla', 'beta lactamase', 'SM', 'Selectable marker', NULL, 'bacterial promoter', NULL, NULL, NULL, 'Not expressed in plant tissues', NULL, NULL, NULL, 'Enabled', NULL, NULL),
(133, 62, 'ACC', 'ACC', '1-amino-cyclopropane -1-carboxylic acid synthase', 'DR', 'Ripening delayed', 'Dianthus caryophyllus L.', 'CaMV 35S', NULL, '<I>A. tumefaciens</I> nopaline synthase (<I>nos</I>) 3''-untranslated region', NULL, 'Truncated, sense orientation', NULL, NULL, NULL, 'Enabled', NULL, NULL),
(134, 62, 'surB', 'ALS', 'acetolactate synthase', 'HT', 'Herbicide tolerance', 'chlorsulfuron tolerant Nicotiana tabacum', 'CaMV 35S', NULL, '<I>surB</I> terminator from <I>N. tabacum</I>', NULL, 'NULL', NULL, NULL, NULL, 'Enabled', NULL, NULL),
(135, 41, 'GmFad2-1', 'GmFad2-1', 'delta(12)-fatty acid dehydrogenase', 'FA', 'Fatty acid composition', 'Glycine max', 'seed specific promoter from the soybean beta-conglycinin gene', NULL, '3'' poly(A) signal from phaseolin gene from Phaseolus vulgaris', '1 locus', 'Native; coordinate suppression', NULL, NULL, NULL, 'Enabled', NULL, NULL),
(136, 63, 'dfr', 'DHFR', 'dihydroflavonol reductase', 'PM', 'Modified color', 'Petunia hybrida', 'native promoter from Petunia', NULL, 'native terminator', NULL, 'NULL', NULL, NULL, NULL, 'Enabled', NULL, NULL),
(137, 63, 'surB', 'ALS', 'acetolactate synthase', 'HT', 'Herbicide tolerance', 'chlorsulfuron tolerant Nicotiana tabacum', 'CaMV 35S', NULL, '<I>surB</I> terminator from <I>N. tabacum</I>', NULL, 'NULL', NULL, NULL, NULL, 'Enabled', NULL, NULL),
(138, 63, 'bp40', 'FH', 'flavonoid 3p, 5p hydroxylase', 'PM', 'Modified color', 'Viola sp.', 'petal specific CHS promoter derived form <i>Petunia hybrida</i>.', NULL, 'D8 terminator derived from <I>Petunia hybrida</I>', NULL, 'NULL', NULL, NULL, NULL, 'Enabled', NULL, NULL),
(139, 64, 'dfr', 'DHFR', 'dihydroflavonol reductase', 'PM', 'Modified color', 'Petunia hybrida', '<i>A. tumefaciens</i> constitutive mac-1 promoter', NULL, '<I>A. tumefaciens mas</I> terminator', NULL, 'NULL', NULL, NULL, NULL, 'Enabled', NULL, NULL),
(140, 64, 'surB', 'ALS', 'acetolactate synthase', 'HT', 'Herbicide tolerance', 'chlorsulfuron tolerant Nicotiana tabacum', 'CaMV 35S', NULL, '<I>surB</I> terminator from <I>N. tabacum</I>', NULL, 'NULL', NULL, NULL, NULL, 'Enabled', NULL, NULL),
(141, 64, 'hfl', 'FH', 'flavonoid 3p, 5p hydroxylase', 'PM', 'Modified color', 'Petunia hybrida', 'petal specific CHS promoter derived form <i>Anthirrhinum majus</i>.', NULL, 'D8 terminator derived from <I>Petunia hybrida</I>', NULL, 'NULL', NULL, NULL, NULL, 'Enabled', NULL, NULL),
(142, 65, 'barnase', 'barnase', 'barnase ribonuclease', 'MS', 'Male sterility', 'Bacillus amyloliquefaciens', 'pTa 29 pollen specific promoter from <I>Nicotiana tabacum</I>', NULL, NULL, '1', 'Introduced into MS1', NULL, NULL, NULL, 'Enabled', NULL, NULL),
(143, 65, 'barstar', 'barstar', 'barnase ribonuclease inhibitor', 'RF', 'Fertility restoration', 'Bacillus amyloliquefaciens', 'anther-specific promoter', NULL, NULL, '1', 'Introduced into RF2', NULL, NULL, NULL, 'Enabled', NULL, NULL),
(144, 65, 'bar', 'PAT', 'phosphinothricin N-acetyltransferase', 'HT', 'Herbicide tolerance', 'S. hygroscopicus', 'PSsuAra from <I>Arabidopsis thaliana</I>', 'chloroplast transit peptide from <I>A. thaliana</I>', NULL, '1', 'Introduced into both MS1 and RF2', 'SHYG', NULL, NULL, 'Enabled', NULL, NULL),
(145, 65, 'nptII', 'NPTII', 'neomycin phosphotransferase II', 'SM', 'Selectable marker', 'Escherichia coli', 'nopaline synthase (<I>nos</I>) from <I>A. tumefaciens</I>', NULL, 'octopine synthase', NULL, 'Native; both MS1 and RF2', NULL, NULL, NULL, 'Enabled', NULL, NULL),
(146, 66, 'barnase', 'barnase', 'barnase ribonuclease', 'MS', 'Male sterility', 'Bacillus amyloliquefaciens', 'pTa 29 pollen specific promoter from <I>Nicotiana tabacum</I>', NULL, NULL, NULL, 'NULL', NULL, NULL, NULL, 'Enabled', NULL, NULL),
(147, 66, 'bar', 'PAT', 'phosphinothricin N-acetyltransferase', 'HT', 'Herbicide tolerance', 'S. hygroscopicus', 'CaMV 35S', NULL, '<I>A. tumefaciens</I> nopaline synthase (<I>nos</I>) 3''-untranslated region', NULL, 'Modified', 'SHYG', NULL, NULL, 'Enabled', NULL, NULL),
(148, 66, 'bla', 'bla', 'beta lactamase', 'SM', 'Selectable marker', NULL, 'bacterial promoter', NULL, NULL, NULL, 'Fragmented copy; not expressible', NULL, NULL, NULL, 'Enabled', NULL, NULL),
(149, 67, 'bxn', 'nitrilase', 'nitrilase', 'HT', 'Herbicide tolerance', 'Klebsiella pneumoniae subspecies ozanae', 'RuBisCo SSU from <I>Helianthus annuus</I>', NULL, 'nopaline synthase gene terminator from <I>Agrobacterium tumefaciens</I> pTiA6', NULL, 'NULL', NULL, NULL, NULL, 'Enabled', NULL, NULL),
(150, 25, 'bla', 'bla', 'beta-lactamase', 'SM', 'Selectable marker', NULL, 'bacterial promoter', NULL, NULL, NULL, 'Not expressed in plant tissues', NULL, NULL, NULL, 'Enabled', NULL, NULL),
(151, 22, 'nptII', 'NPTII', 'neomycin phosphotransferase II', 'SM', 'Selectable marker', 'Escherichia coli', 'nopaline synthase (<I>nos</I>) from <I>A. tumefaciens</I>', NULL, 'octopine synthase', NULL, 'Native', NULL, NULL, NULL, 'Enabled', NULL, NULL),
(152, 38, 'nptII', 'NPTII', 'neomycin phosphotransferase II', 'SM', 'Selectable marker', 'Escherichia coli', 'nopaline synthase (<I>nos</I>) from <I>A. tumefaciens</I>', NULL, NULL, NULL, 'Native', NULL, NULL, NULL, 'Enabled', NULL, NULL),
(153, 8, 'bla', 'bla', 'beta-lactamase', 'SM', 'Selectable marker', NULL, 'bacterial promoter', NULL, NULL, NULL, 'Not expressed in plant tissues', NULL, NULL, NULL, 'Enabled', NULL, NULL),
(154, 8, 'spc', 'spc', 'Spectinomycin/streptomycin resistance', 'SM', 'Selectable marker', NULL, 'bacterial', NULL, NULL, NULL, 'Not expressed in plant tissues.', NULL, NULL, NULL, 'Enabled', NULL, NULL),
(155, 68, 'fad2', 'fad2', 'fatty acid desaturase', 'FA', 'Fatty acid composition', NULL, NULL, NULL, NULL, NULL, 'Mutagenized endogenous gene', NULL, NULL, NULL, 'Enabled', NULL, NULL),
(156, 72, 'goxv247', 'gox', 'glyphosate oxidoreductase', 'HT', 'Herbicide tolerance', 'Ochrobactrum anthropi', 'CaMV 35S', 'chloroplast transit peptide from <I>A. thaliana</I> SSU1A gene (CTP1)', NULL, '3', 'NULL', NULL, NULL, NULL, 'Enabled', NULL, NULL),
(157, 51, 'nptII', 'NPTII', 'neomycin phosphotransferase II', 'SM', 'Selectable marker', 'Escherichia coli', 'bacterial promoter', NULL, NULL, '', 'Not expressed in plant cells.', NULL, NULL, NULL, 'Enabled', NULL, NULL),
(158, 69, 'fad2', 'fad2', 'fatty acid desaturase', 'FA', 'Fatty acid composition', NULL, NULL, NULL, NULL, NULL, 'Mutagenized endogenous gene', NULL, NULL, NULL, 'Enabled', NULL, NULL),
(159, 72, 'CP4 epsps', 'EPSPS', '5-enolpyruvyl shikimate-3-phosphate synthase', 'HT', 'Herbicide tolerance', 'Agrobacterium tumefaciens CP4', 'enhanced CaMV 35S, maize HSP70 intron', 'chloroplast transit peptide from <I>A. thaliana</I> EPSPS gene (CTP2)', '<I>A. tumefaciens</I> nopaline synthase (<I>nos</I>) 3''-untranslated region', '1', 'NULL', 'CP4EPS', NULL, NULL, 'Enabled', NULL, NULL),
(160, 72, 'nptII', 'NPTII', 'neomycin phosphotransferase II', 'SM', 'Selectable marker', 'Escherichia coli', 'bacterial promoter', NULL, NULL, '1 complete, 1 rearranged', 'Not expressed in plant tissues because of bacterial promoter.', NULL, NULL, NULL, 'Enabled', NULL, NULL),
(161, 74, 'CP4 epsps', 'EPSPS', '5-enolpyruvyl shikimate-3-phosphate synthase', 'HT', 'Herbicide tolerance', 'Agrobacterium tumefaciens CP4', 'enhanced CaMV 35S, maize HSP70 intron', 'chloroplast transit peptide from A. thaliana EPSPS gene (CTP2)', 'A. tumefaciens nopaline synthase (nos) 3''-untranslated region', '1', 'CP4 EPSPS gene modified for plant-preferred codons', NULL, NULL, NULL, 'Enabled', NULL, '2013-09-04 13:46:43'),
(162, 53, 'CP4 epsps', 'EPSPS', '5-enolpyruvyl shikimate-3-phosphate synthase', 'SM', 'Selectable marker', 'Agrobacterium tumefaciens CP4', '<p>figwort mosaic virus (FMV) 35S</p>\n', '77-nucleotide leader sequence from soybean 17.9 HSP, chloroplast transit peptide (CTP2) from A. thaliana', '<p>P. sativum (pea) ribulose-1,5-bisphosphate carboxylase small subunit non-translated region</p>\n', '', '<p>present in RBMT22-82 only</p>\n', '', '', '', 'Enabled', NULL, '2013-07-31 17:11:00'),
(163, 56, 'aad', 'aad', '3"(9)-O-aminoglycoside adenylyltransferase', 'SM', 'Selectable marker', NULL, 'bacterial promoter', NULL, NULL, NULL, 'Not expressed in plant tissues', NULL, NULL, NULL, 'Enabled', NULL, NULL),
(164, 56, 'nptII', 'NPTII', 'neomycin phosphotransferase II', 'SM', 'Selectable marker', 'Escherichia coli', 'CaMV 35S', NULL, '<I>A. tumefaciens</I> nopaline synthase (<I>nos</I>) 3''-untranslated region', NULL, 'Native', NULL, NULL, NULL, 'Enabled', NULL, NULL),
(165, 73, 'fan1', 'fan1', '', 'FA', 'Fatty acid composition', NULL, NULL, NULL, NULL, NULL, NULL, NULL, NULL, NULL, 'Enabled', NULL, NULL),
(166, 45, 'nptII', 'NPTII', 'neomycin phosphotransferase II', 'SM', 'Selectable marker', 'Escherichia coli', 'nopaline synthase (<I>nos</I>) from <I>A. tumefaciens</I>', NULL, NULL, NULL, 'Native', NULL, NULL, NULL, 'Enabled', NULL, NULL),
(167, 28, 'cry1Fa2', 'cry1F', 'cry1F delta-endotoxin', 'IR', 'Insect resistance', 'Bacillus thuringiensis var. aizawai', 'ubiquitin (ubi) ZM (<i>Zea mays</i>) promoter and the first exon and intron', NULL, '3'' polyadenylation signal from ORF25 (<I>Agrobacterium tumefaciens</I>)', '1 functional; 1-2 partial;', 'Altered coding sequence for optimal expression in plant cells.', 'BTA', NULL, NULL, 'Enabled', NULL, NULL),
(168, 28, 'pat', 'PAT', 'phosphinothricin N-acetyltransferase', 'HT', 'Herbicide tolerance', 'S. viridochromogenes', 'CaMV 35S', NULL, 'CaMV 35S 3'' polyadenylation signal', '1 functional;', NULL, 'SVIR', NULL, NULL, 'Enabled', NULL, NULL),
(169, 75, 'nptII', 'NPTII', 'neomycin phosphotransferase II', 'SM', 'Selectable marker', 'Escherichia coli', 'CaMV 35S', NULL, '<I>A. tumefaciens</I> nopaline synthase (<I>nos</I>) 3''-untranslated region', '1', 'The <i>nptII</i> cassette also contains 153 bp portion of bleomycin binding protein gene', NULL, NULL, NULL, 'Enabled', NULL, NULL),
(170, 75, 'cry3Bb1', 'cry3Bb1', 'cry3Bb1 delta-endotoxin', 'IR', 'Insect resistance', 'Bacillus thuringiensis subsp. <i>kumamotoensis</i>', '4-AS1 (single CaMV 35S plus four repeats of activating sequence)', '5'' untranslated leader sequence from wheat chlorphyll a/b binding protein, and rice actin intron', '3'' untranslated sequence of wheat heat shock protein 17.3 (<i>tahsp17</i>)', '1', 'Addition of alanine residue at position 2 of protein', 'BT3B', NULL, NULL, 'Enabled', NULL, NULL),
(171, 76, 'als', 'ALS', 'acetolactate synthase', 'MUT', 'Mutations', 'Oryza sativa', 'native', NULL, NULL, NULL, 'Whole plant selection of imidazolinone tolerant mutants, followed by introgression of HT trait into commercial varieties through cross-breeding.', NULL, NULL, NULL, 'Enabled', NULL, NULL),
(172, 77, 'aad', 'aad', '3', 'SM', 'Selectable marker', NULL, 'bacterial promoter', NULL, NULL, NULL, 'Not expressed in plant tissues', '', '', '', 'Enabled', NULL, NULL),
(173, 77, 'cry1Ac', 'cry1Ac', 'Cry1Ac delta-endotoxin', 'IR', 'Insect resistance', 'Bacillus thuringiensis subsp. kurstaki (Btk)', 'double enhanced CaMV 35S', NULL, '3\\'' poly(A) signal from soybean alpha subunit of the beta-conglycinin gene', '>=1', 'Truncated; Line 757: 1 complete T-DNA and 1 paritial T-DNA insertion event', 'BTKC', '', '', 'Enabled', NULL, NULL),
(174, 77, 'nptII', 'NPTII', 'neomycin phosphotransferase II', 'SM', 'Selectable marker', 'Escherichia coli', 'nopaline synthase (<I>nos</I>) from <I>A. tumefaciens</I>', NULL, NULL, '>=1', 'Native', '', '', '', 'Enabled', NULL, NULL),
(175, 77, 'uidA', 'gus', 'beta-D-glucuronidase', 'SM', 'Selectable marker', 'Escherichia coli', 'double enhanced CaMV 35S', '', '<I>A. tumefaciens</I> nopaline synthase (<I>nos</I>) 3\\''-untranslated region', '1', 'Native', '', '', '', 'Enabled', NULL, NULL),
(176, 78, 'bar', 'PAT', 'phosphinothricin N-acetyltransferase', 'HT', 'Selectable marker', 'S. hygroscopicus', 'CaMV 35S', 'ADH1 intron 1', 'potato <i>pinII</i> termination and poly(A) signal', NULL, NULL, 'SHYG', NULL, NULL, 'Enabled', NULL, NULL),
(177, 78, 'mocry1F', 'cry1F', 'cry1F delta-endotoxin', 'IR', 'Lepidopteran resistance', 'Bacillus thuringiensis', 'ubiquitin 1 (Zea mays)', NULL, 'potato <i>pinII</i> termination and poly(A) signal', NULL, NULL, 'BTA', NULL, NULL, 'Enabled', NULL, NULL),
(178, 79, 'CP4 epsps', 'EPSPS', '5-enolpyruvyl shikimate-3-phosphate synthase', 'HT', 'Herbicide tolerance', 'Agrobacterium tumefaciens CP4', 'enhanced CaMV 35S', 'chloroplast transit peptide from <I>A. thaliana</I> EPSPS gene (CTP2)', '<I>A. tumefaciens</I> nopaline synthase (<I>nos</I>) 3''-untranslated region', NULL, NULL, 'CP4EPS', 'http://www.expasy.org/cgi-bin/nicezyme.pl?2.5.1.19', NULL, 'Enabled', NULL, NULL),
(179, 80, 'CP4 epsps', 'EPSPS', '5-enolpyruvyl shikimate-3-phosphate synthase', 'HT', 'Herbicide tolerance', 'Agrobacterium tumefaciens CP4', 'enhanced CaMV 35S, HSP70 intron, gox cassette', 'chloroplast transit peptide from <I>A. thaliana</I> EPSPS gene (CTP2)', '<I>A. tumefaciens</I> nopaline synthase (<I>nos</I>) 3''-untranslated region', NULL, NULL, 'CP4EPS', 'http://www.expasy.org/cgi-bin/nicezyme.pl?2.5.1.19', NULL, 'Enabled', NULL, NULL),
(180, 81, 'pat', 'PAT', 'phosphinothricin N-acetyltransferase', 'HT', 'Herbicide tolerance', 'S. viridochromogenes', 'CaMV 35S', NULL, NULL, '1', 'Native', 'SVIR', NULL, NULL, 'Enabled', NULL, NULL),
(181, 82, 'bar', 'PAT', 'phosphinothricin N-acetyltransferase', 'HT', 'Herbicide tolerance', 'S. hygroscopicus', 'CaMV 35S', NULL, '<I>A. tumefaciens</I> nopaline synthase (<I>nos</I>) 3''-untranslated region', NULL, NULL, 'SHYG', NULL, NULL, 'Enabled', NULL, NULL),
(182, 83, 'EC2.4.2.19', 'QTPASE', 'nicotinate-nucleotide pyrophosphorylase (carboxylating)', 'NR', 'Nicotine reduced', 'Nicotiana tabaccum', 'NtQPT1 promoter', NULL, '<I>A. tumefaciens</I> nopaline synthase (<I>nos</I>) 3''-untranslated region', NULL, NULL, NULL, 'http://www.expasy.org/cgi-bin/nicezyme.pl?2.4.2.19', NULL, 'Enabled', NULL, NULL);
INSERT INTO `gmcropdatabase_events_genes` (`id`, `eventId`, `code`, `abbrCode`, `name`, `type`, `lType`, `source`, `promoter`, `effector`, `terminator`, `copies`, `form`, `srcCode`, `eCLink`, `description`, `status`, `created`, `updated`) VALUES
(183, 83, 'EC2.7.1.95', 'NPTII', 'neomycin phosphotransferase II', 'SM', 'Selectable marker', 'Escherichia coli', NULL, NULL, '<I>A. tumefaciens</I> nopaline synthase (<I>nos</I>) 3''-untranslated region', NULL, NULL, NULL, 'http://ca.expasy.org/cgi-bin/nicezyme.pl?2.7.1.95', NULL, 'Enabled', NULL, NULL),
(184, 86, 'als', 'ALS', 'acetolactate synthase', 'MUT', 'Mutations', 'Helianthus annuus', NULL, NULL, NULL, NULL, 'Imidazolinone selection for a naturally occurring mutant from wild sunflower populations.', NULL, NULL, NULL, 'Enabled', NULL, NULL),
(185, 87, 'als', 'ALS', 'acetolactate synthase', 'MUT', 'Mutations', 'Triticum aestivum', 'Native AHAS', NULL, NULL, NULL, 'Selected following chemical mutagenesis', NULL, NULL, NULL, 'Enabled', NULL, NULL),
(186, 88, 'als', 'ALS', 'acetolactate synthase', 'MUT', 'Mutations', 'Triticum aestivum', 'Native AHAS', NULL, NULL, NULL, 'Selected following chemical mutagenesis', NULL, NULL, NULL, 'Enabled', NULL, NULL),
(187, 89, 'als', 'ALS', 'acetolactate synthase', 'MUT', 'Mutations', 'Lens culinaris', 'Native AHAS', NULL, NULL, NULL, 'Selected following chemical mutagenesis', NULL, NULL, NULL, 'Enabled', NULL, NULL),
(188, 90, 'als', 'ALS', 'acetolactate synthase', 'MUT', 'Mutations', 'Triticum aestivum', 'Native AHAS', NULL, NULL, NULL, 'Selected following chemical mutagenesis', NULL, NULL, NULL, 'Enabled', NULL, NULL),
(189, 91, 'als', 'ALS', 'acetolactate synthase', 'MUT', 'Mutations', 'Oryza sativa', 'native', NULL, NULL, NULL, 'Whole plant selection of imidazolinone tolerant mutants, followed by introgression of HT trait into commercial varieties through cross-breeding.', NULL, NULL, NULL, 'Enabled', NULL, NULL),
(190, 80, 'CP4 epsps', 'EPSPS', '5-enolpyruvyl shikimate-3-phosphate synthase', 'HT', 'Herbicide tolerance', 'Agrobacterium tumefaciens CP4', 'rice actin I promoter and intron sequences', 'chloroplast transit peptide from <I>A. thaliana</I> EPSPS gene (CTP2)', '<I>A. tumefaciens</I> nopaline synthase (<I>nos</I>) 3''-untranslated region', NULL, NULL, NULL, 'http://www.expasy.org/cgi-bin/nicezyme.pl?2.5.1.19', NULL, 'Enabled', NULL, NULL),
(191, 79, 'CP4 epsps', 'EPSPS', '5-enolpyruvyl shikimate-3-phosphate synthase', 'HT', 'Herbicide tolerance', 'Agrobacterium tumefaciens CP4', 'rice actin I promoter and intron sequences', 'chloroplast transit peptide from <I>A. thaliana</I> EPSPS gene (CTP2)', '<I>A. tumefaciens</I> nopaline synthase (<I>nos</I>) 3''-untranslated region', NULL, NULL, NULL, 'http://www.expasy.org/cgi-bin/nicezyme.pl?2.5.1.19', NULL, 'Enabled', NULL, NULL),
(192, 92, 'cry1F', 'cry1F', 'cry1F delta-endotoxin', 'IR', 'Insect resistance', 'Bacillus thuringiensis var. <i>aizawai</i>', 'mannopine synthase (d mas 2'') promoter from pTi15955', 'four copies of the octopine synthase (4OCS) enhancer from pTiAch5', '3'' polyadenylation signal from ORF25 (<I>Agrobacterium tumefaciens</I>)', '1 functional;', 'Cry1F active insecticidal core and non-toxic portions of the Cry1Ab1 and Cry1Ca3 proteins.  Sequence modified for optimal in planta expression.', 'BTA', NULL, NULL, 'Enabled', NULL, NULL),
(193, 93, 'cry1Ac', 'cry1Ac', 'Cry1Ac delta-endotoxin', 'IR', 'Insect resistance', 'Bacillus thuringiensis subsp. <i>kurstaki</i> (Btk)', 'ubiquitin 1 (Zea mays)', NULL, '3'' polyadenylation signal from ORF25 (<I>Agrobacterium tumefaciens</I>)', '1 functional;', 'Cry1Ac active insecticidal core and non-toxic portions of the Cry1Ab1 and Cry1Ca3 proteins.  Sequence modified for optimal <i>in planta</i> expression.', 'BTKC', NULL, NULL, 'Enabled', NULL, NULL),
(194, 92, 'pat', 'PAT', 'phosphinothricin N-acetyltransferase', 'SM', 'Selectable marker', 'S. viridochromogenes', 'ubiquitin (ubi) ZM (<i>Zea mays</i>) promoter and the first exon and intron', NULL, '3'' polyadenylation signal from ORF25 (<I>Agrobacterium tumefaciens</I>)', '1 functional; 1 partial, non-expressed;', 'Altered coding sequence for optimal expression in plant cells.', 'SVIR', NULL, NULL, 'Enabled', NULL, NULL),
(195, 93, 'pat', 'PAT', 'phosphinothricin N-acetyltransferase', 'SM', 'Selectable marker', 'S. viridochromogenes', 'mannopine synthase (d mas 2'') promoter from pTi15955', 'four copies of the octopine synthase (4OCS) enhancer from pTiAch5', '3'' polyadenylation signal from ORF25 (<I>Agrobacterium tumefaciens</I>)', '1 functional;', 'Altered coding sequence for optimal expression in plant cells.', 'SVIR', NULL, NULL, 'Enabled', NULL, NULL),
(196, 94, 'CP4 epsps', 'EPSPS', '5-enolpyruvyl shikimate-3-phosphate synthase', 'HT', 'Herbicide tolerance', 'Agrobacterium tumefaciens CP4', 'figwort mosaic virus (FMV) 35S', 'chloroplast transit peptide from <I>A. thaliana</I>', '<i>P. sativum</i> (pea) ribulose-1,5-bisphosphate carboxylase small subunit non-translated region', '1 functional', 'Native', 'CP4EPS', 'http://www.expasy.org/cgi-bin/nicezyme.pl?2.5.1.19', NULL, 'Enabled', NULL, NULL),
(197, 95, 'cry34Ab1', 'cry34Ab1', 'Cry34Ab1 delta-endotoxin', 'IR', 'Insect resistance', 'Bacillus thuringiensis strain PS149B1', '<i>Zea mays</i> ubiquitin gene promoter, intron and 5'' UTR', NULL, '<i>Solanum tuberosum</i> proteinase inhibitor II (PINII)', '1 functional', 'Altered coding sequence for optimal expression in maize', 'BTPS', NULL, NULL, 'Enabled', NULL, NULL),
(198, 95, 'cry35Ab1', 'cry35Ab1', 'Cry35Ab1 delta-endotoxin', 'IR', 'Insect resistance', 'Bacillus thuringiensis strain PS149B1', '<i>Triticum aestivum</i> peroxidase gene root-preferred promoter', NULL, '<i>Solanum tuberosum</i> proteinase inhibitor II (PINII)', '1 functional', 'Altered coding sequence for optimal expression in maize', 'BTPS', NULL, NULL, 'Enabled', NULL, NULL),
(199, 95, 'pat', 'PAT', 'phosphinothricin N-acetyltransferase', 'SM', 'Selectable marker', 'S. viridochromogenes', 'Cauliflower Mosaic Virus (CaMV) 35S', NULL, 'Cauliflower Mosaic Virus (CaMV) 35S', '1 functional', NULL, 'SVIR', NULL, NULL, 'Enabled', NULL, NULL),
(200, 96, 'cry3Bb1', 'cry3Bb1', 'Cry3Bb1 delta-endotoxin', 'IR', 'Insect resistance', 'Bacillus thuringiensis subsp. <i>kumamotoensis</i> strain EG4691', 'CaMV 35S promoter with duplicated enhancer region', '5'' UTR from wheat chlorophyll a/b-binding protein; rice actin gene first intron', '3'' UTR from wheat heat shock protein (tahsp17 3'')', '1 functional', 'synthetic', 'BT3B', NULL, NULL, 'Enabled', NULL, NULL),
(201, 96, 'CP4 epsps', 'EPSPS', '5-enolpyruvyl shikimate-3-phosphate synthase', 'HT', 'Herbicide tolerance', 'Agrobacterium tumefaciens CP4', 'rice actin I promoter and intron sequences', 'chloroplast transit peptide from <i>A. thaliana</i>', '<I>A. tumefaciens</I> nopaline synthase (<I>nos</I>) 3''-untranslated region', '1 functional', NULL, 'CP4EPS', 'http://www.expasy.org/cgi-bin/nicezyme.pl?2.5.1.19', NULL, 'Enabled', NULL, NULL),
(202, 97, 'CP4 epsps', 'EPSPS', '5-enolpyruvyl shikimate-3-phosphate synthase', 'HT', 'Herbicide tolerance', 'Agrobacterium tumefaciens CP4', 'P-FMV/TSF1: chimeric promoter containing <i>A. thaliana tsf1</i> promoter', 'elongation factor EF-1 alpha; Figwort Mosaic Virus 35S promoter enhancer; <i>A. thaliana tsf1</i> leader and intron; chloroplast transit peptide from <i>A. thaliana</i>', '<i>Pisum sativum</i> T-E9 DNA  containing 3’ UTR of Rubisco small subunit E9 gene', '1 functional', NULL, 'CP4EPS', 'http://www.expasy.org/cgi-bin/nicezyme.pl?2.5.1.19', NULL, 'Enabled', NULL, NULL),
(203, 97, 'CP4 epsps', 'EPSPS', '5-enolpyruvyl shikimate-3-phosphate synthase', 'HT', 'Herbicide tolerance', 'Agrobacterium tumefaciens CP4', 'P-35S/ACT8: chimeric promoter from <i>A. thaliana</i> <i>act8</i> f', 'Cauliflower Mosaic Virus 35S promoter enhancer; <i>A. thaliana</i> <i>act8</i> leader and intron; chloroplast transit peptide from <i>A. thaliana</i>', '<i>Pisum sativum</i> T-E9 DNA  containing 3’ UTR of Rubisco small subunit E9 gene', '1 functional', NULL, 'CP4EPS', 'http://www.expasy.org/cgi-bin/nicezyme.pl?2.5.1.19', NULL, 'Enabled', NULL, NULL),
(204, 100, 'nptII', 'NPTII', 'neomycin phosphotransferase II', 'SM', 'Selectable marker', 'Escherichia coli', 'CaMV 35S', NULL, '<I>A. tumefaciens</I> nopaline synthase (<I>nos</I>) 3''-untranslated region', '1', 'The <i>nptII</i> cassette also contains 153 bp portion of bleomycin binding protein gene', NULL, NULL, NULL, 'Enabled', NULL, NULL),
(205, 100, 'cry3Bb1', 'cry3Bb1', 'cry3Bb1 delta-endotoxin', 'IR', 'Insect resistance', 'Bacillus thuringiensis subsp. <i>kumamotoensis</i>', '4-AS1 (single CaMV 35S plus four repeats of activating sequence)', '5'' untranslated leader sequence from wheat chlorphyll a/b binding protein, and rice actin intron', '3'' untranslated sequence of wheat heat shock protein 17.3 (<i>tahsp17</i>)', '1', 'Addition of alanine residue at position 2 of protein', 'BT3B', NULL, NULL, 'Enabled', NULL, NULL),
(206, 100, 'cry1Ab', 'cry1Ab', 'Cry1Ab delta-endotoxin (<I>Btk</I> HD-1)', 'IR', 'Insect resistance', 'Bacillus thuringiensis subsp. <i>kurstaki</i> (Btk)', 'enhanced CaMV 35S, maize HSP70 intron', NULL, 'None. Lost through 3'' truncation during integration', '1', 'Truncated', 'BTK', NULL, NULL, 'Enabled', NULL, NULL),
(207, 101, 'nptII', 'NPTII', 'neomycin phosphotransferase II', 'SM', 'Selectable marker', 'Escherichia coli', 'CaMV 35S', NULL, '<I>A. tumefaciens</I> nopaline synthase (<I>nos</I>) 3''-untranslated region', '1', 'The <i>nptII</i> cassette also contains 153 bp portion of bleomycin binding protein gene', NULL, NULL, NULL, 'Enabled', NULL, NULL),
(208, 101, 'cry3Bb1', 'cry3Bb1', 'cry3Bb1 delta-endotoxin', 'IR', 'Insect resistance', 'Bacillus thuringiensis subsp. <i>kumamotoensis</i>', '4-AS1 (single CaMV 35S plus four repeats of activating sequence)', '5'' untranslated leader sequence from wheat chlorphyll a/b binding protein, and rice actin intron', '3'' untranslated sequence of wheat heat shock protein 17.3 (<i>tahsp17</i>)', '1', 'Addition of alanine residue at position 2 of protein', 'BT3B', NULL, NULL, 'Enabled', NULL, NULL),
(209, 101, 'CP4 epsps', 'EPSPS', '5-enolpyruvyl shikimate-3-phosphate synthase', 'HT', 'Herbicide tolerance', 'Agrobacterium tumefaciens CP4', 'P-ract1/ract1 intron containing rice actin 1 promoter, transcription start site', 'chloroplast transit peptide from <I>A. thaliana</I> EPSPS gene (CTP2)', '<I>A. tumefaciens</I> nopaline synthase (<I>nos</I>) 3''-untranslated region', '1', 'CP4 EPSPS gene modified for plant-preferred codons', 'CP4EPS', NULL, NULL, 'Enabled', NULL, NULL),
(210, 101, 'CP4 epsps', 'EPSPS', '5-enolpyruvyl shikimate-3-phosphate synthase', 'HT', 'Herbicide tolerance', 'Agrobacterium tumefaciens CP4', 'enhanced CaMV 35S, maize HSP70 intron', 'chloroplast transit peptide from <I>A. thaliana</I> EPSPS gene (CTP2)', '<I>A. tumefaciens</I> nopaline synthase (<I>nos</I>) 3''-untranslated region', '1', 'CP4 EPSPS gene modified for plant-preferred codons', NULL, NULL, NULL, 'Enabled', NULL, NULL),
(211, 102, 'nptII', 'NPTII', 'neomycin phosphotransferase II', 'SM', 'Selectable marker', 'Escherichia coli', 'CaMV 35S', NULL, '<I>A. tumefaciens</I> nopaline synthase (<I>nos</I>) 3''-untranslated region', '1', 'The <i>nptII</i> cassette also contains 153 bp portion of bleomycin binding protein gene', NULL, NULL, NULL, 'Enabled', NULL, NULL),
(212, 102, 'cry3Bb1', 'cry3Bb1', 'cry3Bb1 delta-endotoxin', 'IR', 'Insect resistance', 'Bacillus thuringiensis subsp. <i>kumamotoensis</i>', '4-AS1 (single CaMV 35S plus four repeats of activating sequence)', '5'' untranslated leader sequence from wheat chlorphyll a/b binding protein, and rice actin intron', '3'' untranslated sequence of wheat heat shock protein 17.3 (<i>tahsp17</i>)', '1', 'Addition of alanine residue at position 2 of protein', 'BT3B', NULL, NULL, 'Enabled', NULL, NULL),
(213, 102, 'cry1Ab', 'cry1Ab', 'Cry1Ab delta-endotoxin (<I>Btk</I> HD-1)', 'IR', 'Insect resistance', 'Bacillus thuringiensis subsp. <i>kurstaki </i>(Btk)', 'enhanced CaMV 35S, maize HSP70 intron', NULL, 'None. Lost through 3'' truncation during integration', '1', 'Truncated', 'BTK', NULL, NULL, 'Enabled', NULL, NULL),
(214, 102, 'CP4 epsps', 'EPSPS', '5-enolpyruvyl shikimate-3-phosphate synthase', 'HT', 'Herbicide tolerance', 'Agrobacterium tumefaciens CP4', 'P-ract1/ract1 intron containing rice actin 1 promoter, transcription start site', 'chloroplast transit peptide from <I>A. thaliana</I> EPSPS gene (CTP2)', '<I>A. tumefaciens</I> nopaline synthase (<I>nos</I>) 3''-untranslated region', '1', 'CP4 EPSPS gene modified for plant-preferred codons', 'CP4EPS', NULL, NULL, 'Enabled', NULL, NULL),
(215, 102, 'CP4 epsps', 'EPSPS', '5-enolpyruvyl shikimate-3-phosphate synthase', 'HT', 'Herbicide tolerance', 'Agrobacterium tumefaciens CP4', 'enhanced CaMV 35S, maize HSP70 intron', 'chloroplast transit peptide from <I>A. thaliana</I> EPSPS gene (CTP2)', '<I>A. tumefaciens</I> nopaline synthase (<I>nos</I>) 3''-untranslated region', '1', 'CP4 EPSPS gene modified for plant-preferred codons', NULL, NULL, NULL, 'Enabled', NULL, NULL),
(216, 103, 'CP4 epsps', 'EPSPS', '5-enolpyruvyl shikimate-3-phosphate synthase', 'HT', 'Herbicide tolerance', 'Agrobacterium tumefaciens CP4', 'P-ract1/ract1 intron containing rice actin 1 promoter, transcription start site', 'chloroplast transit peptide from <I>A. thaliana</I> EPSPS gene (CTP2)', '<I>A. tumefaciens</I> nopaline synthase (<I>nos</I>) 3''-untranslated region', '1', 'CP4 EPSPS gene modified for plant-preferred codons', 'CP4EPS', NULL, NULL, 'Enabled', NULL, NULL),
(217, 103, 'CP4 epsps', 'EPSPS', '5-enolpyruvyl shikimate-3-phosphate synthase', 'HT', 'Herbicide tolerance', 'Agrobacterium tumefaciens CP4', 'enhanced CaMV 35S, maize HSP70 intron', 'chloroplast transit peptide from <I>A. thaliana</I> EPSPS gene (CTP2)', '<I>A. tumefaciens</I> nopaline synthase (<I>nos</I>) 3''-untranslated region', '1', 'CP4 EPSPS gene modified for plant-preferred codons', NULL, NULL, NULL, 'Enabled', NULL, NULL),
(218, 103, 'cry1Ab', 'cry1Ab', 'Cry1Ab delta-endotoxin (<I>Btk</I> HD-1)', 'IR', 'Insect resistance', 'Bacillus thuringiensis subsp. <i>kurstaki</i> (Btk)', 'enhanced CaMV 35S, maize HSP70 intron', NULL, 'None. Lost through 3'' truncation during integration', '1', 'Truncated', 'BTK', NULL, NULL, 'Enabled', NULL, NULL),
(219, 104, 'pat', 'PAT', 'phosphinothricin N-acetyltransferase', 'HT', 'Herbicide tolerance', 'S. viridochromogenes', 'CaMV 35S', NULL, 'CaMV 35S poly(A) signal', '3 or 1*', 'Modified for enhanced expression; PEG mediated uptake into plant protoplasts; 3 copies in T14, 1 copy in T25', 'SVIR', NULL, NULL, 'Enabled', NULL, NULL),
(220, 104, 'bla', 'bla', 'beta lactamase', 'SM', 'Selectable marker', NULL, 'bacterial promoter', NULL, NULL, NULL, 'Truncated beta-lactamase gene missing about 25 % of the gene from the 5'' end; not expressed', NULL, NULL, NULL, 'Enabled', NULL, NULL),
(221, 104, 'cry1Ab', 'cry1Ab', 'Cry1Ab delta-endotoxin (<I>Btk</I> HD-1)', 'IR', 'Insect resistance', 'Bacillus thuringiensis subsp.<i>kurstaki </i>(Btk)', 'enhanced CaMV 35S, maize HSP70 intron', NULL, 'None. Lost through 3'' truncation during integration', '1', 'Truncated', 'BTK', NULL, NULL, 'Enabled', NULL, NULL),
(222, 105, 'cry1Fa2', 'cry1F', 'cry1F delta-endotoxin', 'IR', 'Insect resistance', 'Bacillus thuringiensis var. <i>aizawai</i>', 'ubiquitin (ubi) ZM (<i>Zea mays</i>) promoter and the first exon and intron', NULL, '3'' polyadenylation signal from ORF25 (<I>Agrobacterium tumefaciens</I>)', '1 functional; 1-2 partial;', 'Altered coding sequence for optimal expression in plant cells.', 'BTA', NULL, NULL, 'Enabled', NULL, NULL),
(223, 105, 'pat', 'PAT', 'phosphinothricin N-acetyltransferase', 'HT', 'Herbicide tolerance', 'S. viridochromogenes', 'CaMV 35S', NULL, 'CaMV 35S 3'' polyadenylation signal', '1 functional;', NULL, 'SVIR', NULL, NULL, 'Enabled', NULL, NULL),
(224, 105, 'CP4 epsps', 'EPSPS', '5-enolpyruvyl shikimate-3-phosphate synthase', 'HT', 'Herbicide tolerance', 'Agrobacterium tumefaciens CP4', 'P-ract1/ract1 intron containing rice actin 1 promoter, transcription start site', 'chloroplast transit peptide from <I>A. thaliana</I> EPSPS gene (CTP2)', '<I>A. tumefaciens</I> nopaline synthase (<I>nos</I>) 3''-untranslated region', '1', 'CP4 EPSPS gene modified for plant-preferred codons', 'CP4EPS', NULL, NULL, 'Enabled', NULL, NULL),
(225, 105, 'CP4 epsps', 'EPSPS', '5-enolpyruvyl shikimate-3-phosphate synthase', 'HT', 'Herbicide tolerance', 'Agrobacterium tumefaciens CP4', 'enhanced CaMV 35S, maize HSP70 intron', 'chloroplast transit peptide from <I>A. thaliana</I> EPSPS gene (CTP2)', '<I>A. tumefaciens</I> nopaline synthase (<I>nos</I>) 3''-untranslated region', '1', 'CP4 EPSPS gene modified for plant-preferred codons', NULL, NULL, NULL, 'Enabled', NULL, NULL),
(226, 106, 'epsps', 'EPSPS', '5-enolpyruvyl shikimate-3-phosphate synthase', 'HT', 'Herbicide tolerance', 'Z. mays', 'rice actin I promoter and intron sequences', '; ribulose-1,5-bisphosphate carboxylase oxygenase (RuBisCo) derived chloroplast transit peptide squences (from corn & sunflower)', '<I>A. tumefaciens</I> nopaline synthase (<I>nos</I>) 3''-untranslated region', '3*', 'Modified by <I>in vitro</I> mutagenesis; single insertion site with 3 complete copies of EPSPS cassette plus 3 incomplete copies', NULL, NULL, NULL, 'Enabled', NULL, NULL),
(227, 106, 'cry1Ab', 'cry1Ab', 'Cry1Ab delta-endotoxin (<I>Btk</I> HD-1)', 'IR', 'Insect resistance', 'Bacillus thuringiensis subsp.<i>kurstaki</i> (Btk)', 'enhanced CaMV 35S, maize HSP70 intron', NULL, 'None. Lost through 3'' truncation during integration', '1', 'Truncated', 'BTK', NULL, NULL, 'Enabled', NULL, NULL),
(228, 109, 'CP4 epsps', 'EPSPS', '5-enolpyruvyl shikimate-3-phosphate synthase', 'HT', 'Herbicide tolerance', 'Agrobacterium tumefaciens CP4', 'enhanced Figwort Mosaic Virus (FMV) 35S; petunia HSP 70 5'' untranslated leader sequence', 'chloroplast transit peptide from <I>A. thaliana</I> EPSPS gene (CTP2)', '<i>P. sativum</i> (pea) ribulose-1,5-bisphosphate carboxylase small subunit E9 gene', '1 functional', 'Native', 'CP4EPS', 'http://www.expasy.org/cgi-bin/nicezyme.pl?2.5.1.19', NULL, 'Enabled', NULL, NULL),
(229, 110, 'vip3A(a)', 'vip3Aa', 'VIP3A vegetative insecticidal protein', 'IR', 'Insect resistance', 'Bacillus thuringiensis strain AB88', 'modified promoter, first exon and intron of <i>Arabidopsis thaliana</i> <i>actin-2</i> gene', NULL, '<I>A. tumefaciens</I> nopaline synthase (<I>nos</I>) 3''-untranslated region', '1 functional', 'modified for plant-preferred codons', 'BTVIP', NULL, NULL, 'Enabled', NULL, NULL),
(230, 110, 'aph4', 'APH4', 'hygromycin-B phosphotransferase', 'SM', 'Selectable marker', 'Escherichia coli', 'promoter and first intron of <i>A. thaliana</i> <i>ubiquitin-3</i> gene', NULL, '<I>A. tumefaciens</I> nopaline synthase (<I>nos</I>) 3''-untranslated region', '1 functional', NULL, NULL, NULL, NULL, 'Enabled', NULL, NULL),
(231, 111, 'cordapA', 'cDHDPS', 'dihydrodipicolinate synthase', 'AA', 'Amino acid composition', '<i>Corynebacterium glutamicum</i>', 'promoter from <i>globulin 1</i> (Glb1) gene from <i>Zea mays</i>', 'rice actin gene intron (rAct1) and <i>Z. mays</i> chloroplast transit peptide sequence for DHDPS', 'Glb1 gene 3'' non-translated region from <i>Z. mays</i>', '1 functional', NULL, 'CGLU', NULL, NULL, 'Enabled', NULL, NULL),
(232, 112, 'cordapA', 'cDHDPS', 'dihydrodipicolinate synthase', 'AA', 'Amino acid composition', '<i>Corynebacterium glutamicum</i>', 'promoter from <i>globulin 1</i> (Glb1) gene from <i>Zea mays</i>', 'rice actin gene intron (rAct1) and <i>Z. mays</i> chloroplast transit peptide sequence for DHDPS', 'Glb1 gene 3'' non-translated region from <i>Z. mays</i>', '1 functional', NULL, 'CGLU', NULL, NULL, 'Enabled', NULL, NULL),
(233, 112, 'cry1Ab', 'cry1Ab', 'Cry1Ab delta-endotoxin (<I>Btk</I> HD-1)', 'IR', 'Insect resistance', 'Bacillus thuringiensis subsp. kurstaki (Btk)', 'enhanced CaMV 35S, maize HSP70 intron', NULL, 'None. Lost through 3'' truncation during integration', '1', 'Truncated', 'BTK', NULL, NULL, 'Enabled', NULL, NULL),
(234, 114, 'cry1Ab', 'cry1Ab', 'Cry1Ab delta-endotoxin (<I>Btk</I> HD-1)', 'IR', 'Insect resistance', 'Bacillus thuringiensis subsp. kurstaki (Btk)', 'enhanced CaMV 35S, maize HSP70 intron', NULL, 'None. Lost through 3'' truncation during integration', '1', 'Truncated', 'BTK', NULL, NULL, 'Enabled', NULL, NULL),
(235, 114, 'cry3Bb1', 'cry3Bb1\r\ncry3Bb1\r\ncry3Bb1\r\ncry3Bb1\r\ncry3Bb1', 'Cry3Bb1 delta-endotoxin', 'IR', 'Insect resistance', 'Bacillus thuringiensis subsp. <i>kumamotoensis</i> strain EG4691', 'CaMV 35S promoter with duplicated enhancer region', '5'' UTR from wheat chlorophyll a/b-binding protein; rice actin gene first intron', '3'' UTR from wheat heat shock protein (tahsp17 3'')', '1 functional', 'synthetic', 'BT3B', NULL, NULL, 'Enabled', NULL, NULL),
(236, 114, 'CP4 epsps', 'EPSPS', '5-enolpyruvyl shikimate-3-phosphate synthase', 'HT', 'Herbicide tolerance', 'Agrobacterium tumefaciens CP4', 'rice actin I promoter and intron sequences', 'chloroplast transit peptide from <i>A. thaliana</i>', '<I>A. tumefaciens</I> nopaline synthase (<I>nos</I>) 3''-untranslated region', '1 functional', NULL, 'CP4EPS', 'http://www.expasy.org/cgi-bin/nicezyme.pl?2.5.1.19', NULL, 'Enabled', NULL, NULL),
(237, 115, 'CP4 epsps', 'EPSPS', '5-enolpyruvyl shikimate-3-phosphate synthase', 'HT', 'Herbicide tolerance', 'Agrobacterium tumefaciens CP4', 'P-FMV/TSF1: chimeric promoter containing <i>A. thaliana tsf1</i> promoter', 'elongation factor EF-1 alpha; Figwort Mosaic Virus 35S promoter enhancer; <i>A. thaliana tsf1</i> leader and intron; chloroplast transit peptide from <i>A. thaliana</i>', '<i>Pisum sativum</i> T-E9 DNA  containing 3’ UTR of Rubisco small subunit E9 gene', '1 functional', '', 'CP4EPS', 'http://www.expasy.org/cgi-bin/nicezyme.pl?2.5.1.19', NULL, 'Enabled', NULL, NULL),
(238, 115, 'CP4 epsps', 'EPSPS', '5-enolpyruvyl shikimate-3-phosphate synthase', 'HT', 'Herbicide tolerance', 'Agrobacterium tumefaciens CP4', 'P-35S/ACT8: chimeric promoter from <i>A. thaliana</i> <i>act8</i> f', 'Cauliflower Mosaic Virus 35S promoter enhancer; <i>A. thaliana</i> <i>act8</i> leader and intron; chloroplast transit peptide from <i>A. thaliana</i>', '<i>Pisum sativum</i> T-E9 DNA  containing 3’ UTR of Rubisco small subunit E9 gene', '1 functional', '', 'CP4EPS', 'http://www.expasy.org/cgi-bin/nicezyme.pl?2.5.1.19', NULL, 'Enabled', NULL, NULL),
(239, 115, 'aad', 'aad', '3"(9)-O-aminoglycoside adenylyltransferase', 'SM', 'Selectable marker', NULL, 'bacterial promoter', NULL, NULL, NULL, 'Not expressed in plant tissues', '', NULL, NULL, 'Enabled', NULL, NULL),
(240, 115, 'cry1Ac', 'cry1Ac', 'Cry1Ac delta-endotoxin', 'IR', 'Insect resistance', 'Bacillus thuringiensis subsp. kurstaki (Btk)', 'double enhanced CaMV 35S', NULL, '3'' poly(A) signal from soybean alpha subunit of the beta-conglycinin gene', '>=1', 'Truncated; Line 757: 1 complete T-DNA and 1 paritial T-DNA insertion event', 'BTKC', NULL, NULL, 'Enabled', NULL, NULL),
(241, 115, 'nptII', 'NPTII', 'neomycin phosphotransferase II', 'SM', 'Selectable marker', 'Escherichia coli', 'nopaline synthase (<I>nos</I>) from <I>A. tumefaciens</I>', NULL, NULL, '>=1', 'Native', '', NULL, NULL, 'Enabled', NULL, NULL),
(242, 115, 'cry2Ab', 'cry2Ab', 'Cry2Ab delta-endotoxin', 'IR', 'Insect resistance', 'Bacillus thuringiensis', 'double enhanced CaMV 35S', 'PetHSP70 leader sequence and the chloroplast transit peptide leader sequence (CTP2)', '<I>A. tumefaciens</I> nopaline synthase (<I>nos</I>) 3''-untranslated region', '1', 'Modified to enhance in planta expression', 'BTK2', NULL, NULL, 'Enabled', NULL, NULL),
(243, 115, 'uidA', 'gus', 'beta-D-glucuronidase', 'SM', 'Selectable marker', 'Escherichia coli', 'double enhanced CaMV 35S', '', '<I>A. tumefaciens</I> nopaline synthase (<I>nos</I>) 3''-untranslated region', '1', 'Native', '', NULL, NULL, 'Enabled', NULL, NULL),
(244, 113, 'mcry3A', 'mcry3A', 'Cry3A delta-endotoxin', 'IR', 'Insect resistance', 'Bacillus thuringiensis subsp. tenebrionis', 'promoter derived from the metallo-thionein-like gene from <i>Zea mays</i>', NULL, '<I>A. tumefaciens</I> nopaline synthase (<I>nos</I>) 3''-untranslated region', '1', 'Modified to enhance expression in maize', 'MCRY3A', NULL, NULL, 'Enabled', NULL, NULL),
(245, 113, 'pmi', 'PMI', 'mannose-6-phosphate isomerase', 'SM', 'Selectable marker', 'Escherichia coli', 'ZmUbiInt (<i>Zea mays</i> poly-ubiquitin gene promoter and first intron)', '', '<I>A. tumefaciens</I> nopaline synthase (<I>nos</I>) 3''-untranslated region', '1', '', 'PMI', 'http://www.expasy.ch/cgi-bin/nicezyme.pl?5.3.1.8', NULL, 'Enabled', NULL, NULL),
(246, 116, 'cry1Fa2', 'cry1F', 'cry1F delta-endotoxin', 'IR', 'Insect resistance', 'Bacillus thuringiensis var. aizawai', 'ubiquitin (ubi) ZM (<i>Zea mays</i>) promoter and the first exon and intron', '', '3'' polyadenylation signal from ORF25 (<I>Agrobacterium tumefaciens</I>)', '1 functional; 1-2 partial;', 'Altered coding sequence for optimal expression in plant cells.', 'BTA', NULL, NULL, 'Enabled', NULL, NULL),
(247, 116, 'pat', 'PAT', 'phosphinothricin N-acetyltransferase', 'HT', 'Herbicide tolerance', 'S. viridochromogenes', 'CaMV 35S', '', 'CaMV 35S 3'' polyadenylation signal', '1 functional;', '', 'SVIR', NULL, NULL, 'Enabled', NULL, NULL),
(248, 116, 'cry34Ab1', 'cry34Ab1', 'Cry34Ab1 delta-endotoxin', 'IR', 'Insect resistance', 'Bacillus thuringiensis strain PS149B1', '<i>Zea mays</i> ubiquitin gene promoter, intron and 5'' UTR', '', '<i>Solanum tuberosum</i> proteinase inhibitor II (PINII)', '1 functional', 'Altered coding sequence for optimal expression in maize', 'BTPS', NULL, NULL, 'Enabled', NULL, NULL),
(249, 116, 'cry35Ab1', 'cry35Ab1', 'Cry35Ab1 delta-endotoxin', 'IR', 'Insect resistance', 'Bacillus thuringiensis strain PS149B1', '<i>Triticum aestivum</i> peroxidase gene root-preferred promoter', '', '<i>Solanum tuberosum</i> proteinase inhibitor II (PINII)', '1 functional', 'Altered coding sequence for optimal expression in maize', 'BTPS', NULL, NULL, 'Enabled', NULL, NULL),
(250, 116, 'pat', 'PAT', 'phosphinothricin N-acetyltransferase', 'SM', 'Selectable marker', 'S. viridochromogenes', 'Cauliflower Mosaic Virus (CaMV) 35S', '', 'Cauliflower Mosaic Virus (CaMV) 35S', '1 functional', '', 'SVIR', NULL, NULL, 'Enabled', NULL, NULL),
(251, 117, 'cry34Ab1', 'cry34Ab1', 'Cry34Ab1 delta-endotoxin', 'IR', 'Insect resistance', 'Bacillus thuringiensis strain PS149B1', '<i>Zea mays</i> ubiquitin gene promoter, intron and 5'' UTR', '', '<i>Solanum tuberosum</i> proteinase inhibitor II (PINII)', '1 functional', 'Altered coding sequence for optimal expression in maize', 'BTPS', NULL, NULL, 'Enabled', NULL, NULL),
(252, 117, 'cry35Ab1', 'cry35Ab1', 'Cry35Ab1 delta-endotoxin', 'IR', 'Insect resistance', 'Bacillus thuringiensis strain PS149B1', '<i>Triticum aestivum</i> peroxidase gene root-preferred promoter', '', '<i>Solanum tuberosum</i> proteinase inhibitor II (PINII)', '1 functional', 'Altered coding sequence for optimal expression in maize', 'BTPS', NULL, NULL, 'Enabled', NULL, NULL),
(253, 117, 'pat', 'PAT', 'phosphinothricin N-acetyltransferase', 'SM', 'Selectable marker', 'S. viridochromogenes', 'Cauliflower Mosaic Virus (CaMV) 35S', '', 'Cauliflower Mosaic Virus (CaMV) 35S', '1 functional', '', 'SVIR', NULL, NULL, 'Enabled', NULL, NULL),
(254, 117, 'CP4 epsps', 'EPSPS', '5-enolpyruvyl shikimate-3-phosphate synthase', 'HT', 'Herbicide tolerance', 'Agrobacterium tumefaciens CP4', 'P-ract1/ract1 intron containing rice actin 1 promoter, transcription start site', 'chloroplast transit peptide from <I>A. thaliana</I> EPSPS gene (CTP2)', '<I>A. tumefaciens</I> nopaline synthase (<I>nos</I>) 3''-untranslated region', '1', 'CP4 EPSPS gene modified for plant-preferred codons', 'CP4EPS', NULL, NULL, 'Enabled', NULL, NULL),
(255, 117, 'CP4 epsps', 'EPSPS', '5-enolpyruvyl shikimate-3-phosphate synthase', 'HT', 'Herbicide tolerance', 'Agrobacterium tumefaciens CP4', 'enhanced CaMV 35S, maize HSP70 intron', 'chloroplast transit peptide from <I>A. thaliana</I> EPSPS gene (CTP2)', '<I>A. tumefaciens</I> nopaline synthase (<I>nos</I>) 3''-untranslated region', '1', 'CP4 EPSPS gene modified for plant-preferred codons', '', NULL, NULL, 'Enabled', NULL, NULL),
(256, 118, 'cry34Ab1', 'cry34Ab1', 'Cry34Ab1 delta-endotoxin', 'IR', 'Insect resistance', 'Bacillus thuringiensis strain PS149B1', '<i>Zea mays</i> ubiquitin gene promoter, intron and 5'' UTR', '', '<i>Solanum tuberosum</i> proteinase inhibitor II (PINII)', '1 functional', 'Altered coding sequence for optimal expression in maize', 'BTPS', NULL, NULL, 'Enabled', NULL, NULL),
(257, 118, 'cry35Ab1', 'cry35Ab1', 'Cry35Ab1 delta-endotoxin', 'IR', 'Insect resistance', 'Bacillus thuringiensis strain PS149B1', '<i>Triticum aestivum</i> peroxidase gene root-preferred promoter', '', '<i>Solanum tuberosum</i> proteinase inhibitor II (PINII)', '1 functional', 'Altered coding sequence for optimal expression in maize', 'BTPS', NULL, NULL, 'Enabled', NULL, NULL),
(258, 118, 'pat', 'PAT', 'phosphinothricin N-acetyltransferase', 'SM', 'Selectable marker', 'S. viridochromogenes', 'Cauliflower Mosaic Virus (CaMV) 35S', '', 'Cauliflower Mosaic Virus (CaMV) 35S', '1 functional', '', 'SVIR', NULL, NULL, 'Enabled', NULL, NULL),
(259, 118, 'cry1Fa2', 'cry1F', 'cry1F delta-endotoxin', 'IR', 'Insect resistance', 'Bacillus thuringiensis var. aizawai', 'ubiquitin (ubi) ZM (<i>Zea mays</i>) promoter and the first exon and intron', '', '3'' polyadenylation signal from ORF25 (<I>Agrobacterium tumefaciens</I>)', '1 functional; 1-2 partial;', 'Altered coding sequence for optimal expression in plant cells.', 'BTA', NULL, NULL, 'Enabled', NULL, NULL),
(260, 118, 'pat', 'PAT', 'phosphinothricin N-acetyltransferase', 'HT', 'Herbicide tolerance', 'S. viridochromogenes', 'CaMV 35S', '', 'CaMV 35S 3'' polyadenylation signal', '1 functional;', '', 'SVIR', NULL, NULL, 'Enabled', NULL, NULL),
(261, 118, 'CP4 epsps', 'EPSPS', '5-enolpyruvyl shikimate-3-phosphate synthase', 'HT', 'Herbicide tolerance', 'Agrobacterium tumefaciens CP4', 'P-ract1/ract1 intron containing rice actin 1 promoter, transcription start site', 'chloroplast transit peptide from <I>A. thaliana</I> EPSPS gene (CTP2)', '<I>A. tumefaciens</I> nopaline synthase (<I>nos</I>) 3''-untranslated region', '1', 'CP4 EPSPS gene modified for plant-preferred codons', 'CP4EPS', NULL, NULL, 'Enabled', NULL, NULL),
(262, 118, 'CP4 epsps', 'EPSPS', '5-enolpyruvyl shikimate-3-phosphate synthase', 'HT', 'Herbicide tolerance', 'Agrobacterium tumefaciens CP4', 'enhanced CaMV 35S, maize HSP70 intron', 'chloroplast transit peptide from <I>A. thaliana</I> EPSPS gene (CTP2)', '<I>A. tumefaciens</I> nopaline synthase (<I>nos</I>) 3''-untranslated region', '1', 'CP4 EPSPS gene modified for plant-preferred codons', '', NULL, NULL, 'Enabled', NULL, NULL),
(263, 120, 'bar', 'PAT', 'phosphinothricin N-acetyltransferase', 'HT', 'Herbicide tolerance', 'S. hygroscopicus', 'CaMV 35S', NULL, '<I>A. tumefaciens</I> nopaline synthase (<I>nos</I>) 3''-untranslated region', NULL, '', 'SHYG', NULL, NULL, 'Enabled', NULL, NULL),
(264, 120, 'aad', 'aad', '3"(9)-O-aminoglycoside adenylyltransferase', 'SM', 'Selectable marker', NULL, 'bacterial promoter', NULL, NULL, NULL, 'Not expressed in plant tissues', '', NULL, NULL, 'Enabled', NULL, NULL),
(265, 120, 'cry1Ac', 'cry1Ac', 'Cry1Ac delta-endotoxin', 'IR', 'Insect resistance', 'Bacillus thuringiensis subsp. kurstaki (Btk)', 'double enhanced CaMV 35S', NULL, '3'' poly(A) signal from soybean alpha subunit of the beta-conglycinin gene', '>=1', 'Truncated; Line 757: 1 complete T-DNA and 1 paritial T-DNA insertion event', 'BTKC', NULL, NULL, 'Enabled', NULL, NULL),
(266, 120, 'nptII', 'NPTII', 'neomycin phosphotransferase II', 'SM', 'Selectable marker', 'Escherichia coli', 'nopaline synthase (<I>nos</I>) from <I>A. tumefaciens</I>', NULL, NULL, '>=1', 'Native', '', NULL, NULL, 'Enabled', NULL, NULL),
(267, 120, 'cry2Ab', 'cry2Ab', 'Cry2Ab delta-endotoxin', 'IR', 'Insect resistance', 'Bacillus thuringiensis', 'double enhanced CaMV 35S', 'PetHSP70 leader sequence and the chloroplast transit peptide leader sequence (CTP2)', '<I>A. tumefaciens</I> nopaline synthase (<I>nos</I>) 3''-untranslated region', '1', 'Modified to enhance in planta expression', 'BTK2', NULL, NULL, 'Enabled', NULL, NULL),
(268, 120, 'uidA', 'gus', 'beta-D-glucuronidase', 'SM', 'Selectable marker', 'Escherichia coli', 'double enhanced CaMV 35S', '', '<I>A. tumefaciens</I> nopaline synthase (<I>nos</I>) 3''-untranslated region', '1', 'Native', '', NULL, NULL, 'Enabled', NULL, NULL),
(269, 121, 'cry1Ab', 'cry1Ab', 'Cry1Ab delta-endotoxin (<I>Btk</I> HD-1)', 'IR', 'Insect resistance', 'Bacillus thuringiensis subsp. kurstaki (Btk)', 'CaMV 35S', 'IVS 6 intron from the maize alcohol dehydrogenase gene', '<I>A. tumefaciens</I> nopaline synthase (<I>nos</I>) 3''-untranslated region', '1', 'Truncated, modified', 'BTK', NULL, NULL, 'Enabled', NULL, NULL),
(270, 121, 'pat', 'PAT', 'phosphinothricin N-acetyltransferase', 'HT', 'Herbicide tolerance', 'S. viridochromogenes', 'CaMV 35S', 'IVS 2 intron from the maize alcohol dehydrogenase gene', '<I>A. tumefaciens</I> nopaline synthase (<I>nos</I>) 3''-untranslated region', '1', 'Modified for enhanced expression', 'SVIR', NULL, NULL, 'Enabled', NULL, NULL),
(271, 121, 'epsps', 'EPSPS', '5-enolpyruvyl shikimate-3-phosphate synthase', 'HT', 'Herbicide tolerance', 'Z. mays', 'rice actin I promoter and intron sequences', 'ribulose-1,5-bisphosphate carboxylase oxygenase (RuBisCo) derived chloroplast transit peptide squences (from corn & sunflower)', '<I>A. tumefaciens</I> nopaline synthase (<I>nos</I>) 3''-untranslated region', '3*', 'Modified by <I>in vitro</I> mutagenesis; single insertion site with 3 complete copies of EPSPS cassette plus 3 incomplete copies', NULL, NULL, NULL, 'Enabled', NULL, NULL),
(272, 122, 'als', 'ALS', 'acetolactate synthase', 'MUT', 'Mutations', 'Triticum aestivum', 'Native AHAS', NULL, NULL, NULL, 'Selected following chemical mutagenesis', NULL, NULL, NULL, 'Enabled', NULL, NULL),
(273, 123, 'als', 'ALS', 'acetolactate synthase', 'MUT', 'Mutations', 'Oryza sativa', 'native', NULL, NULL, NULL, 'Whole plant selection of imidazolinone tolerant mutants, followed by introgression of HT trait into commercial varieties through cross-breeding.', NULL, NULL, NULL, 'Enabled', NULL, NULL),
(274, 124, 'bar', 'PAT', 'phosphinothricin N-acetyltransferase', 'HT', 'Herbicide tolerance', 'S. hygroscopicus', 'CaMV 35S', NULL, '<I>A. tumefaciens</I> nopaline synthase (<I>nos</I>) 3''-untranslated region', '1', NULL, NULL, NULL, NULL, 'Enabled', NULL, NULL),
(275, 125, 'CP4 epsps', 'EPSPS', '5-enolpyruvyl shikimate-3-phosphate synthase', 'HT', 'Herbicide tolerance', 'Agrobacterium tumefaciens CP4', 'P-FMV/TSF1: chimeric promoter containing <i>A. thaliana tsf1</i> promoter', 'elongation factor EF-1 alpha; Figwort Mosaic Virus 35S promoter enhancer; <i>A. thaliana tsf1</i> leader and intron; chloroplast transit peptide from <i>A. thaliana</i>', '<i>Pisum sativum</i> T-E9 DNA  containing 3’ UTR of Rubisco small subunit E9 gene', '1', NULL, 'CP4EPS', 'http://www.expasy.org/cgi-bin/nicezyme.pl?2.5.1.19', NULL, 'Enabled', NULL, NULL),
(276, 126, 'als1', 'ALS', 'acetolactate synthase', 'MUT', 'Mutations', 'Triticum aestivum', 'Native AHAS', NULL, NULL, NULL, 'Selected at the whole plant level following chemical mutagenesis with soudium azide.', NULL, NULL, NULL, 'Enabled', NULL, NULL),
(277, 127, 'CP', 'CP', 'Coat protein', 'VR', 'Virus resistance', 'Plum pox virus', 'CaMV 35S', NULL, '<I>A. tumefaciens</I> nopaline synthase (<I>nos</I>) 3''-untranslated region', '1 full length, 1 re-arranged', NULL, NULL, NULL, NULL, 'Enabled', NULL, NULL),
(278, 127, 'nptII', 'NPTII', 'neomycin phosphotransferase II', 'SM', 'Selectable marker', 'Escherichia coli', 'nopaline synthase (<I>nos</I>) from <I>A. tumefaciens</I>', NULL, '<I>A. tumefaciens</I> nopaline synthase (<I>nos</I>) 3''-untranslated region', '1 full length, 4 re-arranged', NULL, NULL, NULL, NULL, 'Enabled', NULL, NULL),
(279, 127, 'uidA', 'gus', 'beta-D-glucuronidase', 'SM', 'Selectable marker', 'Escherichia coli', 'CaMV 35S', NULL, '<I>A. tumefaciens</I> nopaline synthase (<I>nos</I>) 3''-untranslated region', '1 full length, 2 re-arranged', NULL, NULL, NULL, NULL, 'Enabled', NULL, NULL),
(280, 128, 'mcry3A', 'mcry3A', 'Cry3A delta-endotoxin', 'IR', 'Insect resistance', 'Bacillus thuringiensis subsp. tenebrionis', 'promoter derived from the metallothionein-like gene from <i>Zea mays</i>', NULL, '<I>A. tumefaciens</I> nopaline synthase (<I>nos</I>) 3''-untranslated region', '1', 'Modified to enhance expression in maize', 'MCRY3A', NULL, NULL, 'Enabled', NULL, NULL),
(281, 128, 'pmi', 'PMI', 'mannose-6-phosphate isomerase', 'SM', 'Selectable marker', 'Escherichia coli', 'ZmUbiInt (<i>Zea mays</i> poly-ubiquitin gene promoter and first intron)', '', '<I>A. tumefaciens</I> nopaline synthase (<I>nos</I>) 3''-untranslated region', '1', '', 'PMI', 'http://www.expasy.ch/cgi-bin/nicezyme.pl?5.3.1.8', NULL, 'Enabled', NULL, NULL),
(282, 128, 'epsps', 'EPSPS', '5-enolpyruvyl shikimate-3-phosphate synthase', 'HT', 'Herbicide tolerance', 'Z. mays', 'rice actin I promoter and intron sequences', 'ribulose-1,5-bisphosphate carboxylase oxygenase (RuBisCo) derived chloroplast transit peptide squences (from corn & sunflower)', '<I>A. tumefaciens</I> nopaline synthase (<I>nos</I>) 3''-untranslated region', '3*', 'Modified by <I>in vitro</I> mutagenesis; single insertion site with 3 complete copies of EPSPS cassette plus 3 incomplete copies', '', NULL, NULL, 'Enabled', NULL, NULL),
(283, 129, 'cry1Ab', 'cry1Ab', 'Cry1Ab delta-endotoxin (<I>Btk</I> HD-1)', 'IR', 'Insect resistance', 'Bacillus thuringiensis subsp. kurstaki (Btk)', 'CaMV 35S', 'IVS 6 intron from the maize alcohol dehydrogenase gene', '<I>A. tumefaciens</I> nopaline synthase (<I>nos</I>) 3''-untranslated region', '1', 'Truncated, modified', 'BTK', NULL, NULL, 'Enabled', NULL, NULL),
(284, 129, 'pat', 'PAT', 'phosphinothricin N-acetyltransferase', 'HT', 'Herbicide tolerance', 'S. viridochromogenes', 'CaMV 35S', 'IVS 2 intron from the maize alcohol dehydrogenase gene', '<I>A. tumefaciens</I> nopaline synthase (<I>nos</I>) 3''-untranslated region', '1', 'Modified for enhanced expression', 'SVIR', NULL, NULL, 'Enabled', NULL, NULL),
(285, 129, 'pmi', 'PMI', 'mannose-6-phosphate isomerase', 'SM', 'Selectable marker', 'Escherichia coli', 'ZmUbiInt (<i>Zea mays</i> poly-ubiquitin gene promoter and first intron)', NULL, '<I>A. tumefaciens</I> nopaline synthase (<I>nos</I>) 3''-untranslated region', '1', NULL, 'PMI', 'http://www.expasy.ch/cgi-bin/nicezyme.pl?5.3.1.8', NULL, 'Enabled', NULL, NULL),
(286, 129, 'mcry3A', 'mcry3A', 'Cry3A delta-endotoxin', 'IR', 'Insect resistance', 'Bacillus thuringiensis subsp. tenebrionis', 'promoter derived from the metallothionein-like gene from <i>Zea mays</i>', NULL, '<I>A. tumefaciens</I> nopaline synthase (<I>nos</I>) 3''-untranslated region', '1', 'Modified to enhance expression in maize', 'MCRY3A', NULL, NULL, 'Enabled', NULL, NULL),
(287, 130, 'cry1Ab', 'cry1Ab', 'Cry1Ab delta-endotoxin (<I>Btk</I> HD-1)', 'IR', 'Insect resistance', 'Bacillus thuringiensis subsp. kurstaki (Btk)', 'CaMV 35S', 'IVS 6 intron from the maize alcohol dehydrogenase gene', '<I>A. tumefaciens</I> nopaline synthase (<I>nos</I>) 3''-untranslated region', '1', 'Truncated, modified', 'BTK', NULL, NULL, 'Enabled', NULL, NULL),
(288, 130, 'pat', 'PAT', 'phosphinothricin N-acetyltransferase', 'HT', 'Herbicide tolerance', 'S. viridochromogenes', 'CaMV 35S', 'IVS 2 intron from the maize alcohol dehydrogenase gene', '<I>A. tumefaciens</I> nopaline synthase (<I>nos</I>) 3''-untranslated region', '1', 'Modified for enhanced expression', 'SVIR', NULL, NULL, 'Enabled', NULL, NULL),
(289, 130, 'pmi', 'PMI', 'mannose-6-phosphate isomerase', 'SM', 'Selectable marker', 'Escherichia coli', 'ZmUbiInt (<i>Zea mays</i> poly-ubiquitin gene promoter and first intron)', '', '<I>A. tumefaciens</I> nopaline synthase (<I>nos</I>) 3''-untranslated region', '1', NULL, 'PMI', 'http://www.expasy.ch/cgi-bin/nicezyme.pl?5.3.1.8', NULL, 'Enabled', NULL, NULL),
(290, 130, 'mcry3A', 'mcry3A', 'Cry3A delta-endotoxin', 'IR', 'Insect resistance', 'Bacillus thuringiensis subsp. tenebrionis', 'promoter derived from the metallothionein-like gene from <i>Zea mays</i>', '', '<I>A. tumefaciens</I> nopaline synthase (<I>nos</I>) 3''-untranslated region', '1', 'Modified to enhance expression in maize', 'MCRY3A', NULL, NULL, 'Enabled', NULL, NULL),
(291, 130, 'epsps', 'EPSPS', '5-enolpyruvyl shikimate-3-phosphate synthase', 'HT', 'Herbicide tolerance', 'Z. mays', 'rice actin I promoter and intron sequences', 'ribulose-1,5-bisphosphate carboxylase oxygenase (RuBisCo) derived chloroplast transit peptide squences (from corn & sunflower)', '<I>A. tumefaciens</I> nopaline synthase (<I>nos</I>) 3''-untranslated region', '3*', 'Modified by <I>in vitro</I> mutagenesis; single insertion site with 3 complete copies of EPSPS cassette plus 3 incomplete copies', NULL, NULL, NULL, 'Enabled', NULL, NULL),
(292, 131, 'pmi', 'PMI', 'mannose-6-phosphate isomerase', 'SM', 'Selectable marker', 'Escherichia coli', 'ZmUbiInt (<i>Zea mays</i> poly-ubiquitin gene promoter and first intron)', NULL, '<I>A. tumefaciens</I> nopaline synthase (<I>nos</I>) 3''-untranslated region', '1', NULL, 'PMI', 'http://www.expasy.ch/cgi-bin/nicezyme.pl?5.3.1.8', NULL, 'Enabled', NULL, NULL),
(293, 131, 'amy797E', 'AMY797E', 'thermostable alpha-amylase', 'PQ', 'Starch hydrolysis', 'Thermococcales spp.', 'GZein promoter - from maize 27-kDa <i>zein</i> gene', 'PEPC9 - intron 9 from maize phospho-enol-pyruvate carboxylase gene', '35S terminator from cauliflower mosaic virus', '1', 'Chimeric alpha-amylase', 'AMY797', 'http://www.expasy.org/cgi-bin/nicezyme.pl?3.2.1.1', NULL, 'Enabled', NULL, NULL),
(294, 132, 'cry1A.105', 'cry1A.105', 'chimeric cry1 delta-endotoxin', 'IR', 'Insect resistance', 'Bacillus thuringiensis', 'CaMV 35S', '5'' untranslated leader from wheat chlorophyll a/b-binding protein\r\nRice actin gene intron', '3'' untranslated region of wheat heat shock protein 17.3', '1', NULL, 'CRY1A.', NULL, NULL, 'Enabled', NULL, NULL),
(295, 132, 'cry2Ab', 'cry2Ab2', 'cry2Ab delta-endotoxin', 'IR', 'Insect resistance', 'Bacillus thuringiensis', 'FMV-35S - promoter from Figwort Mosaic Virus', '<i>Hsp70</i> intron from maize heat shock protein gene.\r\nTransit peptide from maize RBC-small subunit.', '<I>A. tumefaciens</I> nopaline synthase (<I>nos</I>) 3''-untranslated region', '1', NULL, 'BTK2', NULL, NULL, 'Enabled', NULL, NULL),
(296, 133, 'gat4601', 'GAT4601', 'glyphosate N-acetyltransferase', 'HT', 'Herbicide tolerance', 'Bacillus licheniformis', 'SCP1 - constitutive synthetic core promoter', 'TMV omega 5''-UTR', '<i>Solanum tuberosum</i> proteinase inhibitor II (PINII)', '1', NULL, NULL, NULL, NULL, 'Enabled', NULL, NULL),
(297, 133, 'gm-hra', 'GM-HRA', 'acetolactate synthase', 'HT', 'Herbicide tolerance', 'Glycine max', 'S-adenosyl-L-methionine synthetase (SAMS)', NULL, 'native soybean acetolactate synthase terminator', '1', NULL, NULL, NULL, NULL, 'Enabled', NULL, NULL),
(298, 134, 'cry1A.105', 'cry1A.105', 'chimeric cry1 delta-endotoxin', 'IR', 'Insect resistance', 'Bacillus thuringiensis', 'CaMV 35S', '5'' untranslated leader from wheat chlorophyll a/b-binding protein Rice actin gene intron', '3'' untranslated region of wheat heat shock protein 17.3', '1', '', 'CRY1A.', '', NULL, 'Enabled', NULL, NULL),
(299, 134, 'cry2Ab', 'cry2Ab2', 'cry2Ab delta-endotoxin', 'IR', 'Insect resistance', 'Bacillus thuringiensis', 'FMV-35S - promoter from Figwort Mosaic Virus', '<i>Hsp70</i> intron from maize heat shock protein gene. Transit peptide from maize RBC-small subunit.', '<I>A. tumefaciens</I> nopaline synthase (<I>nos</I>) 3''-untranslated region', '1', '', 'BTK2', '', NULL, 'Enabled', NULL, NULL),
(300, 134, 'cry3Bb1', 'cry3Bb1', 'Cry3Bb1 delta-endotoxin', 'IR', 'Insect resistance', 'Bacillus thuringiensis subsp. <i>kumamotoensis</i> strain EG4691', 'CaMV 35S promoter with duplicated enhancer region', '5'' UTR from wheat chlorophyll a/b-binding protein; rice actin gene first intron', '3'' UTR from wheat heat shock protein (tahsp17 3'')', '1 functional', 'synthetic', 'BT3B', '', NULL, 'Enabled', NULL, NULL),
(301, 134, 'CP4 epsps', 'EPSPS', '5-enolpyruvyl shikimate-3-phosphate synthase', 'HT', 'Herbicide tolerance', 'Agrobacterium tumefaciens CP4', 'rice actin I promoter and intron sequences', 'chloroplast transit peptide from <i>A. thaliana</i>', '<I>A. tumefaciens</I> nopaline synthase (<I>nos</I>) 3''-untranslated region', '1 functional', '', 'CP4EPS', 'http://www.expasy.org/cgi-bin/nicezyme.pl?2.5.1.19', NULL, 'Enabled', NULL, NULL),
(302, 135, 'cry1A.105', 'cry1A.105', 'chimeric cry1 delta-endotoxin', 'IR', 'Insect resistance', 'Bacillus thuringiensis', 'CaMV 35S', '5'' untranslated leader from wheat chlorophyll a/b-binding protein Rice actin gene intron', '3'' untranslated region of wheat heat shock protein 17.3', '1', '', 'CRY1A.', '', '', 'Enabled', NULL, NULL),
(303, 135, 'cry2Ab', 'cry2Ab2', 'cry2Ab delta-endotoxin', 'IR', 'Insect resistance', 'Bacillus thuringiensis', 'FMV-35S - promoter from Figwort Mosaic Virus', '<i>Hsp70</i> intron from maize heat shock protein gene. Transit peptide from maize RBC-small subunit.', '<I>A. tumefaciens</I> nopaline synthase (<I>nos</I>) 3''-untranslated region', '1', '', 'BTK2', '', '', 'Enabled', NULL, NULL),
(304, 135, 'CP4 epsps', 'EPSPS', '5-enolpyruvyl shikimate-3-phosphate synthase', 'HT', 'Herbicide tolerance', 'Agrobacterium tumefaciens CP4', 'P-ract1/ract1 intron containing rice actin 1 promoter, transcription start site', 'chloroplast transit peptide from <I>A. thaliana</I> EPSPS gene (CTP2)', '<I>A. tumefaciens</I> nopaline synthase (<I>nos</I>) 3''-untranslated region', '1', 'CP4 EPSPS gene modified for plant-preferred codons', 'CP4EPS', '', '', 'Enabled', NULL, NULL),
(305, 135, 'CP4 epsps', 'EPSPS', '5-enolpyruvyl shikimate-3-phosphate synthase', 'HT', 'Herbicide tolerance', 'Agrobacterium tumefaciens CP4', 'enhanced CaMV 35S, maize HSP70 intron', 'chloroplast transit peptide from <I>A. thaliana</I> EPSPS gene (CTP2)', '<I>A. tumefaciens</I> nopaline synthase (<I>nos</I>) 3''-untranslated region', '1', 'CP4 EPSPS gene modified for plant-preferred codons', '', '', '', 'Enabled', NULL, NULL),
(306, 136, 'gm-hra', 'GM-HRA', 'acetolactate synthase', 'HT', 'Herbicide tolerance', 'Z. mays', '<i>als</i> (<i>Z. mays</i>)', 'CaMV 35S enhancer element', '<i>Solanum tuberosum</i> proteinase inhibitor II (PINII)', '1', NULL, NULL, NULL, NULL, 'Enabled', NULL, NULL),
(307, 136, 'gat4621', 'GAT4621', 'glyphosate N-acetyltransferase', 'HT', 'Herbicide tolerance', 'Bacillus licheniformis', 'ZmUbiInt (<i>Zea mays</i> polyubiquitin gene promoter and first intron).', 'CaMV 35S enhancer element', '<i>Solanum tuberosum</i> proteinase inhibitor II (PINII)', '1', NULL, NULL, NULL, NULL, 'Enabled', NULL, NULL),
(308, 137, 'vip3Aa20', 'vip3Aa', 'vegetative insecticidal protein', 'IR', 'Insect resistance', 'Bacillus thuringiensis strain AB88', 'ZmUbiInt (<i>Zea mays</i> polyubiquitin gene promoter and first intron).', NULL, 'CaMV 35S 3'' polyadenylation signal', '1', 'native', 'BTVIP', NULL, NULL, 'Enabled', NULL, NULL),
(309, 137, 'pmi', 'PMI', 'mannose-6-phosphate isomerase', 'SM', 'Selectable marker', 'Escherichia coli', 'ZmUbiInt (<i>Zea mays</i> poly-ubiquitin gene promoter and first intron)', '', '<I>A. tumefaciens</I> nopaline synthase (<I>nos</I>) 3''-untranslated region', '1', '', 'PMI', 'http://www.expasy.ch/cgi-bin/nicezyme.pl?5.3.1.8', '', 'Enabled', NULL, NULL),
(310, 138, 'cry1Ab', 'cry1Ab', 'Cry1Ab delta-endotoxin (<I>Btk</I> HD-1)', 'IR', 'Insect resistance', 'Bacillus thuringiensis subsp. kurstaki (Btk)', 'CaMV 35S', 'IVS 6 intron from the maize alcohol dehydro-genase gene', '<I>A. tumefaciens</I> nopaline synthase (<I>nos</I>) 3''-untranslated region', '1', 'Truncated, modified', 'BTK', '', '', 'Enabled', NULL, NULL),
(311, 138, 'pat', 'PAT', 'phosphinothricin N-acetyltransferase', 'HT', 'Herbicide tolerance', 'S. viridochromogenes', 'CaMV 35S', 'IVS 2 intron from the maize alcohol dehydro-genase gene', '<I>A. tumefaciens</I> nopaline synthase (<I>nos</I>) 3''-untranslated region', '1', 'Modified for enhanced expression', 'SVIR', '', '', 'Enabled', NULL, NULL),
(312, 138, 'vip3Aa20', 'vip3Aa', 'vegetative insecticidal protein', 'IR', 'Insect resistance', 'Bacillus thuringiensis strain AB88', 'ZmUbiInt (<i>Zea mays</i> polyubiquitin gene promoter and first intron).', '', 'CaMV 35S 3'' polyadenylation signal', '1', 'native', 'BTVIP', '', '', 'Enabled', NULL, NULL),
(313, 138, 'pmi', 'PMI', 'mannose-6-phosphate isomerase', 'SM', 'Selectable marker', 'Escherichia coli', 'ZmUbiInt (<i>Zea mays</i> poly-ubiquitin gene promoter and first intron)', '', '<I>A. tumefaciens</I> nopaline synthase (<I>nos</I>) 3''-untranslated region', '1', NULL, 'PMI', 'http://www.expasy.ch/cgi-bin/nicezyme.pl?5.3.1.8', '', 'Enabled', NULL, NULL),
(314, 139, 'gm-fad2-1', 'gm-FAD2-1', 'delta(12)-fatty acid dehydrogenase', 'FA', 'Fatty acid composition', 'Glycine max', 'Kti3 (<i>Glycine max</i> Kunitz trypsin inhibitor gene promoter)', NULL, '3'' untranslated region of the <i>KTi3</i> gene', '7 copies', '597 bp fragment of <i>FAD2-1</i> gene', 'SOYB', NULL, NULL, 'Enabled', NULL, NULL),
(315, 139, 'gm-hra', 'GM-HRA', 'acetolactate synthase', 'HT', 'Herbicide tolerance', 'Glycine max', 'S-adenosyl-L-methionine synthetase (SAMS)', '', 'native soybean acetolactate synthase terminator', '1', '', 'SOYB', '', '', 'Enabled', NULL, NULL);
INSERT INTO `gmcropdatabase_events_genes` (`id`, `eventId`, `code`, `abbrCode`, `name`, `type`, `lType`, `source`, `promoter`, `effector`, `terminator`, `copies`, `form`, `srcCode`, `eCLink`, `description`, `status`, `created`, `updated`) VALUES
(316, 140, 'aph4', 'APH4', 'hygromycin-B phosphotransferase', 'SM', 'Selectable marker', 'Escherichia coli', 'promoter and first intron of <i>A. thaliana</i> <i>ubiquitin-3</i> gene', '', '<I>A. tumefaciens</I> nopaline synthase (<I>nos</I>) 3''-untranslated region', 'None. Lost through breeding process.', '', '', '', '', 'Enabled', NULL, NULL),
(317, 140, 'flcry1Ab', 'flcry1Ab', 'Cry1Ab delta-endotoxin', 'IR', 'Insect resistance', 'Bacillus thuringiensis', 'Promoter region from the actin-2 gene of Arabidopsis thaliana and its intron.', NULL, '<I>A. tumefaciens</I> nopaline synthase (<I>nos</I>) 3''-untranslated region', '1', NULL, NULL, NULL, NULL, 'Enabled', NULL, NULL),
(318, 141, 'epsps', 'EPSPS', '5-enolpyruvyl shikimate-3-phosphate synthase', 'HT', 'Herbicide tolerance', 'Z. mays', 'Promoter region of the histone H4 gene from <i>A. thaliana</i>.', 'Intron of gene II of the histone H3.III variant from <i>A. thaliana</i>.', '3’ untranslated region of the histone H4 gene from <i>A. thaliana</i>.', '1', 'double-mutated <i>epsps</i> gene from <i>Z. mays</i>', 'ZMAYS', 'http://www.expasy.org/cgi-bin/nicezyme.pl?2.5.1.19', NULL, 'Enabled', NULL, NULL),
(319, 142, 'prsv-cp', 'PRSV-CP', 'viral coat protein', 'VR', 'Virus resistance', 'papaya ringspot potyvirus (PRSV)', 'CaMV 35S', '<i>uidA</i> leader sequence.', '<I>A. tumefaciens</I> nopaline synthase (<I>nos</I>) 3''-untranslated region', '1', 'Frameshift mutant, repaired', NULL, NULL, NULL, 'Enabled', NULL, NULL),
(320, 142, 'nptII', 'NPTII', 'neomycin phosphotransferase II', 'SM', 'Selectable marker', 'Escherichia coli', 'Promoter for transcription of the <i>nptII</i> gene from plasmid pTiT37', NULL, '<I>A. tumefaciens</I> nopaline synthase (<I>nos</I>) 3''-untranslated region', '1', 'Native', '', '', '', 'Enabled', NULL, NULL),
(321, 143, 'cry1Ac', 'cry1Ac', 'Cry1Ac delta-endotoxin', 'IR', 'Insect resistance', 'Bacillus thuringiensis subsp. kurstaki (Btk)', 'double enhanced CaMV 35S', NULL, '<I>A. tumefaciens</I> nopaline synthase (<I>nos</I>) 3''-untranslated region', '1', 'Truncated Cry1Ac protein', 'BTKC', '', '', 'Enabled', NULL, NULL),
(322, 143, 'nptII', 'NPTII', 'neomycin phosphotransferase II', 'SM', 'Selectable marker', 'Escherichia coli', 'CaMV 35S', NULL, '<I>A. tumefaciens</I> nopaline synthase (<I>nos</I>) 3''-untranslated region', '1', 'Native', '', '', '', 'Enabled', NULL, NULL),
(323, 85, 'cry1Fa2', 'cry1F', 'cry1F delta-endotoxin', 'IR', 'Insect resistance', 'Bacillus thuringiensis var. aizawai', 'ubiquitin (ubi) ZM (<i>Zea mays</i>) promoter and the first exon and intron', '', '3'' poly-adenylation signal from ORF25 (<I>Agrobacterium tumefaciens</I>)', '1 functional; 1-2 partial;', 'Altered coding sequence for optimal expression in plant cells.', 'BTA', NULL, NULL, 'Enabled', NULL, NULL),
(324, 85, 'pat', 'PAT', 'phosphinothricin N-acetyltransferase', 'HT', 'Herbicide tolerance', 'S. viridochromogenes', 'CaMV 35S', '', 'CaMV 35S 3'' poly-adenylation signal', '2', '', 'SVIR', NULL, NULL, 'Enabled', NULL, NULL),
(325, 85, 'cry1A.105', 'cry1A.105', 'chimeric cry1 delta-endotoxin', 'IR', 'Insect resistance', 'Bacillus thuringiensis', 'CaMV 35S', '5'' untranslated leader from wheat chlorophyll a/b-binding protein', '3'' untranslated region of wheat heat shock protein 17.3', '1', NULL, 'CRY1A.', NULL, NULL, 'Enabled', NULL, NULL),
(326, 85, 'cry2Ab', 'cry2Ab2', 'cry2Ab delta-endotoxin', 'IR', 'Insect resistance', 'Bacillus thuringiensis', 'FMV-35S - promoter from Figwort Mosaic Virus', '<i>Hsp70</i> intron from maize heat shock protein gene.', '<I>A. tumefaciens</I> nopaline synthase (<I>nos</I>) 3''-untranslated region', '1', NULL, 'BTK2', NULL, NULL, 'Enabled', NULL, NULL),
(327, 85, 'cry3Bb1', 'cry3Bb1', 'Cry3Bb1 delta-endotoxin', 'IR', 'Insect resistance', 'Bacillus thuringiensis subsp. <i>kumamotoensis</i> strain EG4691', 'CaMV 35S promoter with duplicated enhancer region', '5'' UTR from wheat chlorophyll a/b-binding protein; rice actin gene first intron', '3'' UTR from wheat heat shock protein (tahsp17 3'')', '1 functional', 'synthetic', 'BT3B', NULL, NULL, 'Enabled', NULL, NULL),
(328, 85, 'CP4 epsps', 'EPSPS', '5-enolpyruvyl shikimate-3-phosphate synthase', 'HT', 'Herbicide tolerance', 'Agrobacterium tumefaciens CP4', 'rice actin I promoter and intron sequences', 'chloroplast transit peptide from <i>A. thaliana</i>', '<I>A. tumefaciens</I> nopaline synthase (<I>nos</I>) 3''-untranslated region', '1 functional', '', 'CP4EPS', 'http://www.expasy.org/cgi-bin/nicezyme.pl?2.5.1.19', NULL, 'Enabled', NULL, NULL),
(329, 85, 'cry34Ab1', 'cry34Ab1', 'Cry34Ab1 delta-endotoxin', 'IR', 'Insect resistance', 'Bacillus thuringiensis strain PS149B1', '<i>Zea mays</i> ubiquitin gene promoter, intron and 5'' UTR', '', '<i>Solanum tuberosum</i> proteinase inhibitor II (PINII)', '1 functional', 'Altered coding sequence for optimal expression in maize', 'BTPS', '', '', 'Enabled', NULL, NULL),
(330, 85, 'cry35Ab1', 'cry35Ab1', 'Cry35Ab1 delta-endotoxin', 'IR', 'Insect resistance', 'Bacillus thuringiensis strain PS149B1', '<i>Triticum aestivum</i> peroxidase gene root-preferred promoter', '', '<i>Solanum tuberosum</i> proteinase inhibitor II (PINII)', '1 functional', 'Altered coding sequence for optimal expression in maize', 'BTPS', '', '', 'Enabled', NULL, NULL),
(331, 84, 'cry1Ab', 'cry1Ab', 'Cry1Ab delta-endotoxin (<I>Btk</I> HD-1)', 'IR', 'Insect resistance', 'Bacillus thuringiensis subsp. kurstaki (Btk)', 'CaMV 35S', 'IVS 6 intron from the maize alcohol dehydrogenase gene', '<I>A. tumefaciens</I> nopaline synthase (<I>nos</I>) 3''-untranslated region', '1', 'Truncated, modified', 'BTK', '', '', 'Enabled', NULL, NULL),
(332, 84, 'pat', 'PAT', 'phosphinothricin N-acetyltransferase', 'HT', 'Herbicide tolerance', 'S. viridochromogenes', 'CaMV 35S', 'IVS 2 intron from the maize alcohol dehydrogenase gene', '<I>A. tumefaciens</I> nopaline synthase (<I>nos</I>) 3''-untranslated region', '1', 'Modified for enhanced expression', 'SVIR', '', '', 'Enabled', NULL, NULL),
(333, 84, 'vip3Aa20', 'vip3Aa', 'vegetative insecticidal protein', 'IR', 'Insect resistance', 'Bacillus thuringiensis strain AB88', 'ZmUbiInt (<i>Zea mays</i> poly-ubiquitin gene promoter and first intron)', '', 'CaMV 35S 3'' poly-adenylation signal', '1', 'native', 'BTVIP', '', '', 'Enabled', NULL, NULL),
(334, 84, 'pmi', 'PMI', 'mannose-6-phosphate isomerase', 'SM', 'Selectable marker', 'Escherichia coli', 'ZmUbiInt (<i>Zea mays</i> poly-ubiquitin gene promoter and first intron)', '', '<I>A. tumefaciens</I> nopaline synthase (<I>nos</I>) 3''-untranslated region', '2', NULL, 'PMI', 'http://www.expasy.ch/cgi-bin/nicezyme.pl?5.3.1.8', '', 'Enabled', NULL, NULL),
(335, 84, 'mcry3A', 'mcry3A', 'Cry3A delta-endotoxin', 'IR', 'Insect resistance', 'Bacillus thuringiensis subsp. tenebrionis', 'promoter derived from the metallo-thionein-like gene from <i>Zea mays</i>', '', '<I>A. tumefaciens</I> nopaline synthase (<I>nos</I>) 3''-untranslated region', '1', 'Modified to enhance expression in maize', 'MCRY3A', '', '', 'Enabled', NULL, NULL),
(336, 144, 'csr1-2', 'csr1-2', 'acetohydroxyacid synthase large subunit', 'HT', 'Herbicide tolerance', 'Arabidopsis thaliana', 'native 5'' and 3'' untranslated regions', NULL, NULL, '1', NULL, NULL, NULL, NULL, 'Enabled', NULL, NULL),
(337, 145, 'bla', 'bla', 'beta lactamase', 'SM', 'Selectable marker', NULL, 'bacterial promoter', NULL, NULL, NULL, 'Truncated beta-lactamase gene missing about 25 % of the gene from the 5'' end; not expressed', '', '', '', 'Enabled', NULL, NULL),
(338, 145, 'pat', 'PAT', 'phosphinothricin N-acetyltransferase', 'HT', 'Herbicide tolerance', 'S. viridochromogenes', 'CaMV 35S', NULL, 'CaMV 35S poly(A) signal', '3 or 1*', 'Modified for enhanced expression; PEG mediated uptake into plant protoplasts; 3 copies in T14, 1 copy in T25', 'SVIR', '', '', 'Enabled', NULL, NULL),
(339, 145, 'CP4 epsps', 'EPSPS', '5-enolpyruvyl shikimate-3-phosphate synthase', 'HT', 'Herbicide tolerance', 'Agrobacterium tumefaciens CP4', 'P-ract1/ract1 intron containing rice actin 1 promoter, transcription start site', 'chloroplast transit peptide from <I>A. thaliana</I> EPSPS gene (CTP2)', '<I>A. tumefaciens</I> nopaline synthase (<I>nos</I>) 3''-untranslated region', '1', 'CP4 EPSPS gene modified for plant-preferred codons', 'CP4EPS', '', '', 'Enabled', NULL, NULL),
(340, 145, 'CP4 epsps', 'EPSPS', '5-enolpyruvyl shikimate-3-phosphate synthase', 'HT', 'Herbicide tolerance', 'Agrobacterium tumefaciens CP4', 'enhanced CaMV 35S, maize HSP70 intron', 'chloroplast transit peptide from <I>A. thaliana</I> EPSPS gene (CTP2)', '<I>A. tumefaciens</I> nopaline synthase (<I>nos</I>) 3''-untranslated region', '1', 'CP4 EPSPS gene modified for plant-preferred codons', '', '', '', 'Enabled', NULL, NULL),
(341, 77, 'cry2Ab2', 'cry2Ab2', 'Cry2Ab2 delta-endotoxin', 'IR', 'Insect resistance', 'Bacillus thuringiensis', 'double enhanced CaMV 35S', 'PetHSP70 leader sequence and the chloroplast transit peptide leader sequence (CTP2)', '<em>A. tumefaciens</em> nopaline synthase (<em>nos</em>) 3\\''-untranslated region', '1', 'Modified to enhance in planta expression', 'BTK2', '', '', 'Enabled', NULL, NULL),
(342, 146, 'gbss', 'gbss', 'granule-bound starch synthase', 'PQ', 'Plant quality', 'Solanum tuberosum', 'genomic <i>gbss</i> fragment (Pgbss) functional as a promoter in plants', NULL, '<I>A. tumefaciens</I> nopaline synthase (<I>nos</I>) 3''-untranslated region', '2 (partial)', 'Truncated, antisense RNA interference', 'STUB', NULL, NULL, 'Enabled', NULL, NULL),
(343, 146, 'nptII', 'NPTII', 'neomycin phosphotransferase II', 'SM', 'Selectable marker', 'Escherichia coli', 'nopaline synthase (<I>nos</I>) from <I>A. tumefaciens</I>', NULL, '<I>A. tumefaciens</I> nopaline synthase (<I>nos</I>) 3''-untranslated region', '2', 'Native', NULL, NULL, NULL, 'Enabled', NULL, NULL),
(344, 147, 'cspB', 'cspB', 'cold shock protein B', 'AP', 'Agronomic performance', 'Bacillus subtilis', 'rice actin (act1) promoter', 'intron from rice actin gene', '<i>A. tumefaciens</i> transcript 7 3''-nontranslated sequence', '1', 'Native', NULL, NULL, NULL, 'Enabled', NULL, NULL),
(345, 147, 'nptII', 'NPTII', 'neomycin phosphotransferase II', 'SM', 'Selectable marker', 'Escherichia coli', 'CaMV 35S', NULL, '<I>A. tumefaciens</I> nopaline synthase (<I>nos</I>) 3''-untranslated region', '1', 'Native', NULL, NULL, NULL, 'Enabled', NULL, NULL),
(346, 148, 'cry1Ac', 'Cry1Ac', 'Cry1Ac delta-endotoxin', 'IR', 'Insect resistance', 'Bacillus thuringiensis subsp. kurstaki (Btk)', 'promoter and 5'' non-translated region from <i>A. thaliana</i> <i>rbcS4</i> gene (Rubisco)', 'transit peptide of rbcS4 gene to target the protein to the chloroplast', '3'' region of soybean <i>sphas1</i> gene, including 35 nucleotides of carboxyl terminus of beta-conglycinin coding region', '1', NULL, 'BTKC', NULL, NULL, 'Enabled', NULL, NULL),
(347, 149, 'CP4 epsps', 'EPSPS', '5-enolpyruvyl shikimate-3-phosphate synthase', 'HT', 'Herbicide tolerance', 'Agrobacterium tumefaciens CP4', 'P-FMV/TSF1: chimeric promoter containing <i>A. thaliana tsf1</i> promoter', 'elongation factor EF-1 alpha; Figwort Mosaic Virus 35S promoter enhancer; <i>A. thaliana tsf1</i> leader and intron; chloroplast transit peptide from <i>A. thaliana</i>', '<i>Pisum sativum</i> T-E9 DNA  containing 3’ UTR of Rubisco small subunit E9 gene', '1', '', 'CP4EPS', 'http://www.expasy.org/cgi-bin/nicezyme.pl?2.5.1.19', NULL, 'Enabled', NULL, NULL),
(348, 149, 'cry1Ac', 'Cry1Ac', 'Cry1Ac delta-endotoxin', 'IR', 'Insect resistance', 'Bacillus thuringiensis subsp. kurstaki (Btk)', 'promoter and 5'' non-translated region from <i>A. thaliana</i> <i>rbcS4</i> gene (Rubisco)', 'transit peptide of rbcS4 gene to target the protein to the chloroplast', '3'' region of soybean <i>sphas1</i> gene, including 35 nucleotides of carboxyl terminus of beta-conglycinin coding region', '1', '', 'BTKC', NULL, NULL, 'Enabled', NULL, NULL),
(349, 150, 'cry1Ab', 'cry1Ab', 'Cry1Ab delta-endotoxin (<I>Btk</I> HD-1)', 'IR', 'Insect resistance', 'Bacillus thuringiensis subsp. kurstaki (Btk)', 'CaMV 35S', 'IVS 6 intron from the maize alcohol dehydrogenase gene', '<I>A. tumefaciens</I> nopaline synthase (<I>nos</I>) 3''-untranslated region', '1', 'Truncated, modified', 'BTK', NULL, NULL, 'Enabled', NULL, NULL),
(350, 150, 'pat', 'PAT', 'phosphinothricin N-acetyltransferase', 'HT', 'Herbicide tolerance', 'S. viridochromogenes', 'CaMV 35S', 'IVS 2 intron from the maize alcohol dehydrogenase gene', '<I>A. tumefaciens</I> nopaline synthase (<I>nos</I>) 3''-untranslated region', '1', 'Modified for enhanced expression', 'SVIR', NULL, NULL, 'Enabled', NULL, NULL),
(351, 150, 'vip3Aa20', 'vip3Aa', 'vegetative insecticidal protein', 'IR', 'Insect resistance', 'Bacillus thuringiensis strain AB88', 'ZmUbiInt (<i>Zea mays</i> polyubiquitin gene promoter and first intron).', NULL, 'CaMV 35S 3'' polyadenylation signal', '1', 'native', 'BTVIP', NULL, NULL, 'Enabled', NULL, NULL),
(352, 150, 'pmi', 'PMI', 'mannose-6-phosphate isomerase', 'SM', 'Selectable marker', 'Escherichia coli', 'ZmUbiInt (<i>Zea mays</i> poly-ubiquitin gene promoter and first intron)', NULL, '<I>A. tumefaciens</I> nopaline synthase (<I>nos</I>) 3''-untranslated region', '1', NULL, 'PMI', 'http://www.expasy.ch/cgi-bin/nicezyme.pl?5.3.1.8', NULL, 'Enabled', NULL, NULL),
(353, 150, 'mcry3A', 'mcry3A', 'Cry3A delta-endotoxin', 'IR', 'Insect resistance', 'Bacillus thuringiensis subsp. tenebrionis', 'promoter derived from the metallo-thionein-like gene from <i>Zea mays</i>', NULL, '<I>A. tumefaciens</I> nopaline synthase (<I>nos</I>) 3''-untranslated region', '1', 'Modified to enhance expression in maize', 'MCRY3A', NULL, NULL, 'Enabled', NULL, NULL),
(354, 150, 'epsps', 'EPSPS', '5-enolpyruvyl shikimate-3-phosphate synthase', 'HT', 'Herbicide tolerance', 'Z. mays', 'rice actin I promoter and intron sequences', 'ribulose-1,5-bisphosphate carboxylase oxygenase (RuBisCo) derived chloroplast transit peptide squences (from corn & sunflower)', '<I>A. tumefaciens</I> nopaline synthase (<I>nos</I>) 3''-untranslated region', '3*', 'Modified by <I>in vitro</I> mutagenesis; single insertion site with 3 complete copies of EPSPS cassette plus 3 incomplete copies', NULL, NULL, NULL, 'Enabled', NULL, NULL),
(355, 151, 'cry1Fa2', 'cry1F', 'cry1F delta-endotoxin', 'IR', 'Insect resistance', 'Bacillus thuringiensis var. aizawai', 'ubiquitin (ubi) ZM (<i>Zea mays</i>) promoter and the first exon and intron', '', '3'' poly-adenylation signal from ORF25 (<I>Agrobacterium tumefaciens</I>)', '1 functional; 1-2 partial;', 'Altered coding sequence for optimal expression in plant cells.', 'BTA', NULL, NULL, 'Enabled', NULL, NULL),
(356, 151, 'pat', 'PAT', 'phosphinothricin N-acetyltransferase', 'HT', 'Herbicide tolerance', 'S. viridochromogenes', 'CaMV 35S', '', 'CaMV 35S 3'' polyadenylation signal', '1 functional;', '', 'SVIR', NULL, NULL, 'Enabled', NULL, NULL),
(357, 151, 'cry1Ab', 'cry1Ab', 'Cry1Ab delta-endotoxin (<I>Btk</I> HD-1)', 'IR', 'Insect resistance', 'Bacillus thuringiensis subsp. kurstaki (Btk)', 'enhanced CaMV 35S, maize HSP70 intron', NULL, 'None. Lost through 3'' truncation during integration', '1', 'Truncated', 'BTK', NULL, NULL, 'Enabled', NULL, NULL),
(358, 152, 'cry1Fa2', 'cry1F', 'cry1F delta-endotoxin', 'IR', 'Insect resistance', 'Bacillus thuringiensis var. aizawai', 'ubiquitin (ubi) ZM (<i>Zea mays</i>) promoter and the first exon and intron', '', '3'' poly-adenylation signal from ORF25 (<I>Agrobacterium tumefaciens</I>)', '1 functional; 1-2 partial;', 'Altered coding sequence for optimal expression in plant cells.', 'BTA', NULL, NULL, 'Enabled', NULL, NULL),
(359, 152, 'pat', 'PAT', 'phosphinothricin N-acetyltransferase', 'HT', 'Herbicide tolerance', 'S. viridochromogenes', 'CaMV 35S', '', 'CaMV 35S 3'' polyadenylation signal', '1 functional;', '', 'SVIR', NULL, NULL, 'Enabled', NULL, NULL),
(360, 152, 'cry1Ab', 'cry1Ab', 'Cry1Ab delta-endotoxin (<I>Btk</I> HD-1)', 'IR', 'Insect resistance', 'Bacillus thuringiensis subsp. kurstaki (Btk)', 'enhanced CaMV 35S, maize HSP70 intron', NULL, 'None. Lost through 3'' truncation during integration', '1', 'Truncated', 'BTK', NULL, NULL, 'Enabled', NULL, NULL),
(361, 152, 'CP4 epsps', 'EPSPS', '5-enolpyruvyl shikimate-3-phosphate synthase', 'HT', 'Herbicide tolerance', 'Agrobacterium tumefaciens CP4', 'P-ract1/ract1 intron containing rice actin 1 promoter, transcription start site', 'chloroplast transit peptide from <I>A. thaliana</I> EPSPS gene (CTP2)', '<I>A. tumefaciens</I> nopaline synthase (<I>nos</I>) 3''-untranslated region', '1', 'CP4 EPSPS gene modified for plant-preferred codons', 'CP4EPS', NULL, NULL, 'Enabled', NULL, NULL),
(362, 152, 'CP4 epsps', 'EPSPS', '5-enolpyruvyl shikimate-3-phosphate synthase', 'HT', 'Herbicide tolerance', 'Agrobacterium tumefaciens CP4', 'enhanced CaMV 35S, maize HSP70 intron', 'chloroplast transit peptide from <I>A. thaliana</I> EPSPS gene (CTP2)', '<I>A. tumefaciens</I> nopaline synthase (<I>nos</I>) 3''-untranslated region', '1', 'CP4 EPSPS gene modified for plant-preferred codons', '', NULL, NULL, 'Enabled', NULL, NULL),
(363, 153, 'cry1Ab', 'cry1Ab', 'Cry1Ab delta-endotoxin (<I>Btk</I> HD-1)', 'IR', 'Insect resistance', 'Bacillus thuringiensis subsp. kurstaki (Btk)', 'CaMV 35S', 'IVS 6 intron from the maize alcohol dehydrogenase gene', '<I>A. tumefaciens</I> nopaline synthase (<I>nos</I>) 3''-untranslated region', '1', 'Truncated, modified', 'BTK', NULL, NULL, 'Enabled', NULL, NULL),
(364, 153, 'pat', 'PAT', 'phosphinothricin N-acetyltransferase', 'HT', 'Herbicide tolerance', 'S. viridochromogenes', 'CaMV 35S', 'IVS 2 intron from the maize alcohol dehydrogenase gene', '<I>A. tumefaciens</I> nopaline synthase (<I>nos</I>) 3''-untranslated region', '1', 'Modified for enhanced expression', 'SVIR', NULL, NULL, 'Enabled', NULL, NULL),
(365, 153, 'epsps', 'EPSPS', '5-enolpyruvyl shikimate-3-phosphate synthase', 'HT', 'Herbicide tolerance', 'Z. mays', 'rice actin I promoter and intron sequences', '; ribulose-1,5-bisphosphate carboxylase oxygenase (RuBisCo) derived chloroplast transit peptide squences (from corn & sunflower)', '<I>A. tumefaciens</I> nopaline synthase (<I>nos</I>) 3''-untranslated region', '3*', 'Modified by <I>in vitro</I> mutagenesis; single insertion site with 3 complete copies of EPSPS cassette plus 3 incomplete copies', NULL, NULL, NULL, 'Enabled', NULL, NULL),
(366, 153, 'vip3Aa20', 'vip3Aa', 'vegetative insecticidal protein', 'IR', 'Insect resistance', 'Bacillus thuringiensis strain AB88', 'ZmUbiInt (<i>Zea mays</i> polyubiquitin gene promoter and first intron).', '', 'CaMV 35S 3'' polyadenylation signal', '1', 'native', 'BTVIP', NULL, NULL, 'Enabled', NULL, NULL),
(367, 153, 'pmi', 'PMI', 'mannose-6-phosphate isomerase', 'SM', 'Selectable marker', 'Escherichia coli', 'ZmUbiInt (<i>Zea mays</i> poly-ubiquitin gene promoter and first intron)', '', '<I>A. tumefaciens</I> nopaline synthase (<I>nos</I>) 3''-untranslated region', '1', '', 'PMI', 'http://www.expasy.ch/cgi-bin/nicezyme.pl?5.3.1.8', NULL, 'Enabled', NULL, NULL),
(400, 98, 'cry1Ac', 'cry1Ac', 'Cry1Ac delta-endotoxin', 'IR', 'Insect resistance', 'Bacillus thuringiensis subsp. <i>kurstaki</i> (Btk)', 'ubiquitin 1 (Zea mays)', NULL, '3'' polyadenylation signal from ORF25 (<I>Agrobacterium tumefaciens</I>)', '1 functional;', 'Cry1Ac active insecticidal core and non-toxic portions of the Cry1Ab1 and Cry1Ca3 proteins.  Sequence modified for optimal in planta expression.', 'BTKC', NULL, NULL, 'Enabled', '2013-08-29 14:47:09', '2013-09-03 13:10:52'),
(388, 166, 'pat', 'PAT', 'phosphinothricin N-acetyltransferase', 'HT', 'Herbicide tolerance', '<i>S. viridochromogenes</i>', '<p>CaMV 35S</p>\n', '', '<p>CaMV 35S poly(A) signal</p>\n', '1', '<p>Synthetic version of native gene</p>\n', 'SVIR', '', '', 'Enabled', '2013-08-09 12:49:40', '2013-08-23 00:19:19'),
(387, 166, 'cry35Ab1', 'cry35Ab1', 'Cry35Ab1 delta-endotoxin', 'IR', 'Insect resistance', 'Bacillus thuringiensis strain PS149B1', '<p><i>Triticum aestivum</i> peroxidase gene root-preferred promoter</p>\n', '', '<p><i>Solanum tuberosum</i> proteinase inhibitor II (PINII)</p>\n', '1 functional', '<p>Altered coding sequence for optimal expression in maize</p>\n', 'BTKC', '', '', 'Enabled', '2013-08-09 12:49:40', '2013-08-23 00:19:19'),
(386, 166, 'cry34Ab1', 'cry34Ab1', 'Cry34Ab1 delta-endotoxin', 'IR', 'Insect resistance', 'Bacillus thuringiensis strain PS149B1', '<p><i>Zea mays</i> ubiquitin gene promoter, intron and 5&#39; UTR</p>\n', '', '<p><i>Solanum tuberosum</i> proteinase inhibitor II (PINII)</p>\n', '1 functional', '<p>Altered coding sequence for optimal expression in maize</p>\n', 'BTPS', '', '', 'Enabled', '2013-08-09 12:49:40', '2013-08-23 00:19:19'),
(385, 166, 'cry1Fa2', 'cry1F', 'cry1F delta-endotoxin', 'IR', 'Insect resistance', 'Bacillus thuringiensis var. aizawai', '<p>ubiquitin (ubi) ZM (<i>Zea mays</i>) promoter and the first exon and intron</p>\n', '', '<p>3&#39; polyadenylation signal from ORF25 (<i>Agrobacterium tumefaciens</i>)</p>\n', 'One copy', '<p>Altered coding sequence for optimal expression in plant cells.</p>\n', 'BTA', '', '', 'Enabled', '2013-08-09 12:49:40', '2013-08-23 00:19:19'),
(399, 98, 'pat', 'PAT', 'phosphinothricin N-acetyltransferase', 'SM', 'Selectable marker', 'S. viridochromogenes', 'mannopine synthase (d mas 2'') promoter from pTi15955', 'four copies of the octopine synthase (4OCS) enhancer from pTiAch5', '3'' polyadenylation signal from ORF25 (<I>Agrobacterium tumefaciens</I>)', '1 functional;', 'Altered coding sequence for optimal expression in plant cells.', 'SVIR', NULL, NULL, 'Enabled', '2013-08-29 14:47:09', '2013-09-03 13:10:52'),
(392, 99, 'aad', 'aad', '3"(9)-O-aminoglycoside adenylyltransferase', 'SM', 'Selectable marker', NULL, 'bacterial promoter', NULL, NULL, NULL, 'Not expressed in plant tissues', NULL, NULL, NULL, 'Enabled', '2013-08-29 14:03:25', '2013-08-29 19:05:09'),
(393, 99, 'nptII', 'NPTII', 'neomycin phosphotransferase II', 'SM', 'Selectable marker', 'Escherichia coli', 'CaMV 35S', NULL, '<I>A. tumefaciens</I> nopaline synthase (<I>nos</I>) 3''-untranslated region', NULL, NULL, NULL, NULL, NULL, 'Enabled', '2013-08-29 14:03:25', '2013-08-29 19:05:09'),
(394, 99, 'cry1Ac', 'cry1Ac', 'Cry1Ac delta-endotoxin', 'IR', 'Insect resistance', 'Bacillus thuringiensis subsp. <i>kurstaki</i> (Btk)', 'ubiquitin 1 (Zea mays)', NULL, '3'' polyadenylation signal from ORF25 (<I>Agrobacterium tumefaciens</I>)', '1 functional;', 'Cry1Ac active insecticidal core and non-toxic portions of the Cry1Ab1 and Cry1Ca3 proteins.  Sequence modified for optimal in planta expression.', 'BTKC', NULL, NULL, 'Enabled', '2013-08-29 14:03:25', '2013-08-29 19:05:09'),
(395, 99, 'pat', 'PAT', 'phosphinothricin N-acetyltransferase', 'SM', 'Selectable marker', 'S. viridochromogenes', 'mannopine synthase (d mas 2'') promoter from pTi15955', 'four copies of the octopine synthase (4OCS) enhancer from pTiAch5', '3'' polyadenylation signal from ORF25 (<I>Agrobacterium tumefaciens</I>)', '1 functional;', 'Altered coding sequence for optimal expression in plant cells.', 'SVIR', NULL, NULL, 'Enabled', '2013-08-29 14:03:25', '2013-08-29 19:05:09'),
(396, 99, 'cry1F', 'cry1F', 'cry1F delta-endotoxin', 'IR', 'Insect resistance', 'Bacillus thuringiensis var. <i>aizawai</i>', 'mannopine synthase (d mas 2'') promoter from pTi15955', 'four copies of the octopine synthase (4OCS) enhancer from pTiAch5', '3'' polyadenylation signal from ORF25 (<I>Agrobacterium tumefaciens</I>)', '1 functional;', 'Cry1F active insecticidal core and non-toxic portions of the Cry1Ab1 and Cry1Ca3 proteins.  Sequence modified for optimal in planta expression.', 'BTA', NULL, NULL, 'Enabled', '2013-08-29 14:03:25', '2013-08-29 19:05:09'),
(397, 99, 'pat', 'PAT', 'phosphinothricin N-acetyltransferase', 'SM', 'Selectable marker', 'S. viridochromogenes', 'ubiquitin (ubi) ZM (<i>Zea mays</i>) promoter and the first exon and intron', NULL, '3'' polyadenylation signal from ORF25 (<I>Agrobacterium tumefaciens</I>)', '1 functional; 1 partial, non-expressed;', 'Altered coding sequence for optimal expression in plant cells.', 'SVIR', NULL, NULL, 'Enabled', '2013-08-29 14:03:25', '2013-08-29 19:05:09'),
(398, 99, 'CP4 epsps', 'EPSPS', '5-enolpyruvyl shikimate-3-phosphate synthase', 'HT', 'Herbicide tolerance', 'Agrobacterium tumefaciens CP4', 'CMoVb from modified figwort mosaic virus (FMV)', 'chloroplast transit peptide from <I>A. thaliana</I> EPSPS gene (CTP2)', 'P. sativum (pea) ribulose-1,5-bisphosphate carboxylase small subunit non-translated region', '1 (line 1445)', 'modified for plant-preferred codons; these data refer to line 1445 only', 'CP4EPS', NULL, NULL, 'Enabled', '2013-08-29 14:03:25', '2013-08-29 19:05:09'),
(401, 98, 'cry1F', 'cry1F', 'cry1F delta-endotoxin', 'IR', 'Insect resistance', 'Bacillus thuringiensis var. <i>aizawai</i>', 'mannopine synthase (d mas 2'') promoter from pTi15955', 'four copies of the octopine synthase (4OCS) enhancer from pTiAch5', '3'' polyadenylation signal from ORF25 (<I>Agrobacterium tumefaciens</I>)', '1 functional;', 'Cry1F active insecticidal core and non-toxic portions of the Cry1Ab1 and Cry1Ca3 proteins.  Sequence modified for optimal in planta expression.', 'BTA', NULL, NULL, 'Enabled', '2013-08-29 14:47:09', '2013-09-03 13:10:52'),
(402, 98, 'pat', 'PAT', 'phosphinothricin N-acetyltransferase', 'SM', 'Selectable marker', 'S. viridochromogenes', 'ubiquitin (ubi) ZM (<i>Zea mays</i>) promoter and the first exon and intron', NULL, '3'' polyadenylation signal from ORF25 (<I>Agrobacterium tumefaciens</I>)', '1 functional; 1 partial, non-expressed;', 'Altered coding sequence for optimal expression in plant cells.', NULL, NULL, NULL, 'Enabled', '2013-08-29 14:47:09', '2013-09-03 13:10:53'),
(403, 107, 'cry1Ac', 'cry1Ac', 'Cry1Ac delta-endotoxin', 'IR', 'Insect resistance', 'Bacillus thuringiensis subsp. <i>kurstaki </i>(Btk)', 'double enhanced CaMV 35S', 'NULL', '3'' poly(A) signal from soybean alpha subunit of the beta-conglycinin gene', '>=1', 'Truncated; Line 757: 1 complete T-DNA and 1 paritial T-DNA insertion event', 'BTKC', NULL, NULL, 'Enabled', NULL, '2013-08-30 16:46:54'),
(404, 107, 'nptII', 'NPTII', 'neomycin phosphotransferase II', 'SM', 'Selectable marker', 'Escherichia coli', 'nopaline synthase (<I>nos</I>) from <I>A. tumefaciens</I>', 'NULL', '', '>=1', 'Native', NULL, NULL, NULL, 'Enabled', NULL, '2013-08-30 16:46:54'),
(405, 107, 'CP4 epsps', 'EPSPS', '5-enolpyruvyl shikimate-3-phosphate synthase', 'HT', 'Herbicide tolerance', 'Agrobacterium tumefaciens CP4', 'CMoVb from modified figwort mosaic virus (FMV)', 'chloroplast transit peptide from <I>A. thaliana</I> EPSPS gene (CTP2)', 'P. sativum (pea) ribulose-1,5-bisphosphate carboxylase small subunit non-translated region', '1 (line 1445)', 'modified for plant-preferred codons; these data refer to line 1445 only', 'CP4EPS', NULL, NULL, 'Enabled', NULL, '2013-08-30 16:46:54'),
(406, 107, 'nptII', 'NPTII', 'neomycin phosphotransferase II', 'SM', 'Selectable marker', 'Escherichia coli', 'CaMV 35S', 'NULL', '<I>A. tumefaciens</I> nopaline synthase (<I>nos</I>) 3''-untranslated region', '', '', NULL, NULL, NULL, 'Enabled', NULL, '2013-08-30 16:46:54'),
(407, 107, 'aad', 'aad', '3"(9)-O-aminoglycoside adenylyltransferase', 'SM', 'Selectable marker', 'NULL', 'bacterial promoter', 'NULL', '', '', 'Not expressed in plant tissues', NULL, NULL, NULL, 'Enabled', NULL, '2013-08-30 16:46:54'),
(408, 108, 'aad', 'aad', '3"(9)-O-aminoglycoside adenylyltransferase', 'SM', 'Selectable marker', 'NULL', 'bacterial promoter', 'NULL', '', '', 'Not expressed in plant tissues', NULL, NULL, NULL, 'Enabled', NULL, '2013-09-02 13:13:42'),
(409, 108, 'cry1Ac', 'cry1Ac', 'Cry1Ac delta-endotoxin', 'IR', 'Insect resistance', 'Bacillus thuringiensis subsp. <i>kurstaki </i>(Btk)', 'double enhanced CaMV 35S', 'NULL', '3'' poly(A) signal from soybean alpha subunit of the beta-conglycinin gene', '>=1', 'Truncated; Line 757: 1 complete T-DNA and 1 paritial T-DNA insertion event', 'BTKC', NULL, NULL, 'Enabled', NULL, '2013-09-02 13:13:42'),
(410, 108, 'nptII', 'NPTII', 'neomycin phosphotransferase II', 'SM', 'Selectable marker', 'Escherichia coli', 'nopaline synthase (<I>nos</I>) from <I>A. tumefaciens</I>', 'NULL', '', '>=1', 'Native', NULL, NULL, NULL, 'Enabled', NULL, '2013-09-02 13:13:42'),
(411, 108, 'cry2Ab', 'cry2Ab', 'Cry2Ab delta-endotoxin', 'IR', 'Insect resistance', 'Bacillus thuringiensis', 'double enhanced CaMV 35S', 'PetHSP70 leader sequence and the chloroplast transit peptide leader sequence (CTP2)', '<I>A. tumefaciens</I> nopaline synthase (<I>nos</I>) 3''-untranslated region', '1', 'Modified to enhance in planta expression', 'BTK2', NULL, NULL, 'Enabled', NULL, '2013-09-02 13:13:42'),
(412, 108, 'uidA', 'gus', 'beta-D-glucuronidase', 'SM', 'Selectable marker', 'Escherichia coli', 'double enhanced CaMV 35S', NULL, '<I>A. tumefaciens</I> nopaline synthase (<I>nos</I>) 3''-untranslated region', '1', 'Native', NULL, NULL, NULL, 'Enabled', NULL, '2013-09-02 13:13:42'),
(413, 108, 'CP4 epsps', 'EPSPS', '5-enolpyruvyl shikimate-3-phosphate synthase', 'HT', 'Herbicide tolerance', 'Agrobacterium tumefaciens CP4', 'CMoVb from modified figwort mosaic virus (FMV)', 'chloroplast transit peptide from <I>A. thaliana</I> EPSPS gene (CTP2)', 'P. sativum (pea) ribulose-1,5-bisphosphate carboxylase small subunit non-translated region', '1 (line 1445)', 'modified for plant-preferred codons; these data refer to line 1445 only', 'CP4EPS', NULL, NULL, 'Enabled', NULL, '2013-09-02 13:13:42'),
(414, 108, 'nptII', 'NPTII', 'neomycin phosphotransferase II', 'SM', 'Selectable marker', 'Escherichia coli', 'CaMV 35S', 'NULL', '<I>A. tumefaciens</I> nopaline synthase (<I>nos</I>) 3''-untranslated region', '', '', NULL, NULL, NULL, 'Enabled', NULL, '2013-09-02 13:13:42'),
(415, 119, 'cry1Ac', 'cry1Ac', 'Cry1Ac delta-endotoxin', 'IR', 'Insect resistance', 'Bacillus thuringiensis subsp. kurstaki (Btk)', '<p>ubiquitin 1 (Zea mays)</p>\n', '', '<p>3&#39; polyadenylation signal from ORF25 (<em>Agrobacterium tumefaciens</em>)</p>\n', '1 functional;', '<p>Cry1Ac active insecticidal core and non-toxic portions of the Cry1Ab1 and Cry1Ca3 proteins.&nbsp; Sequence modified for optimal <em>in planta</em> expression.</p>\n', 'BTKC', '', '', 'Enabled', '2013-09-02 13:41:41', '2013-09-02 13:41:41'),
(416, 119, 'pat', 'PAT', 'phosphinothricin N-acetyltransferase', 'SM', 'Selectable marker', 'S. viridochromogenes', 'mannopine synthase (d mas 2'') promoter from pTi15955', 'four copies of the octopine synthase (4OCS) enhancer from pTiAch5', '3'' polyadenylation signal from ORF25 (<I>Agrobacterium tumefaciens</I>)', '1 functional;', 'Altered coding sequence for optimal expression in plant cells.', 'SVIR', NULL, NULL, 'Enabled', NULL, NULL),
(417, 119, 'cry1F', 'cry1F', 'cry1F delta-endotoxin', 'IR', 'Insect resistance', 'Bacillus thuringiensis var. <i>aizawai</i>', 'mannopine synthase (d mas 2'') promoter from pTi15955', 'four copies of the octopine synthase (4OCS) enhancer from pTiAch5', '3'' polyadenylation signal from ORF25 (<I>Agrobacterium tumefaciens</I>)', '1 functional;', 'Cry1F active insecticidal core and non-toxic portions of the Cry1Ab1 and Cry1Ca3 proteins.  Sequence modified for optimal in planta expression.', 'BTA', NULL, NULL, 'Enabled', NULL, NULL),
(418, 119, 'pat', 'PAT', 'phosphinothricin N-acetyltransferase', 'SM', 'Selectable marker', 'S. viridochromogenes', 'ubiquitin (ubi) ZM (<i>Zea mays</i>) promoter and the first exon and intron', '', '3'' polyadenylation signal from ORF25 (<I>Agrobacterium tumefaciens</I>)', '1 functional; 1 partial, non-expressed;', 'Altered coding sequence for optimal expression in plant cells.', 'SVIR', NULL, NULL, 'Enabled', NULL, NULL),
(419, 119, 'CP4 epsps', 'EPSPS', '5-enolpyruvyl shikimate-3-phosphate synthase', 'HT', 'Herbicide tolerance', 'Agrobacterium tumefaciens CP4', 'P-FMV/TSF1: chimeric promoter containing <i>A. thaliana tsf1</i> promoter', 'elongation factor EF-1 alpha; Figwort Mosaic Virus 35S promoter enhancer; <i>A. thaliana tsf1</i> leader and intron; chloroplast transit peptide from <i>A. thaliana</i>', '<i>Pisum sativum</i> T-E9 DNA  containing 3’ UTR of Rubisco small subunit E9 gene', '1 functional', '', 'CP4EPS', 'http://www.expasy.org/cgi-bin/nicezyme.pl?2.5.1.19', NULL, 'Enabled', NULL, NULL),
(420, 119, 'CP4 epsps', 'EPSPS', '5-enolpyruvyl shikimate-3-phosphate synthase', 'HT', 'Herbicide tolerance', 'Agrobacterium tumefaciens CP4', 'P-35S/ACT8: chimeric promoter from <i>A. thaliana</i> <i>act8</i> f', 'Cauliflower Mosaic Virus 35S promoter enhancer; <i>A. thaliana</i> <i>act8</i> leader and intron; chloroplast transit peptide from <i>A. thaliana</i>', '<i>Pisum sativum</i> T-E9 DNA  containing 3’ UTR of Rubisco small subunit E9 gene', '1 functional', '', 'CP4EPS', 'http://www.expasy.org/cgi-bin/nicezyme.pl?2.5.1.19', NULL, 'Enabled', NULL, NULL),
(421, 169, 'ACCd', 'ACCd', '1-amino-cyclopropane-1-carboxylic acid deaminase', 'DR', 'Ripening delayed', 'Pseudomonas chlororaphis', '<p>figwort mosaic virus (FMV) 35S</p>\n', '<p>5&#39; leader: petuniaHSP70 gene</p>\n', '<p>pea ribulose-1,5-bisphosphate carboxylase small subunit</p>\n', '', '<p>Native</p>\n', '', '', '', 'Enabled', '2013-09-26 12:43:37', '2013-09-26 12:43:37');



-- -----------------------------------------------------------------------------
INSERT INTO `gmcropdatabase_events_introductions` (`id`, `eventId`, `description`, `status`, `created`, `updated`) VALUES
(1, 16, '<p style="text-align: justify;">Maize line Bt11 was developed through a specific genetic modification to be resistant to attack by European corn borer (ECB; <i>Ostrinia nubilalis</i>), a major insect pest of maize in agriculture. The novel variety produced the insecticidal protein, Cry1Ab, derived from <i>Bacillus thuringiensis</i> subsp. kurstaki (B.t.k.) HD-1 strain. Delta-endotoxins, such as the Cry1Ab protein expressed in Bt11, act by selectively binding to specific sites localized on the brush border midgut epithelium of susceptible insect species. Following binding, cation-specific pores are formed that disrupt midgut ion flow and thereby cause paralysis and death. Cry1Ab is insecticidal only to lepidopteran insects, and its specificity of action is directly attributable to the presence of specific binding sites in the target insects. There are no binding sites for delta-endotoxins of <i>B. thuringiensis</i> on the surface of mammalian intestinal cells, therefore, livestock animals and humans are not susceptible to these proteins.</p>\n\n<p style="text-align: justify;">Bt11 was also genetically modified to express the <i>pat</i> gene cloned from the common aerobic soil actinomycete, <i>Streptomyces viridochromogenes</i> strain Tu494, which encodes a phosphinothricin-N-acetyltransferase (PAT) enzyme. The PAT enzyme was used as a selectable marker enabling identification of transformed plant cells as well as a source of resistance to the herbicide phosphinothricin (also known as glufosinate ammonium, the active ingredient in the herbicides Basta, Rely, Finale, and Liberty). Glufosinate ammounium acts by inhibiting the plant enzyme glutamine synthetase, the only enzyme in plants that detoxifies ammonia by incorporating it into glutamine. Inhibition of this enzyme leads to an accumulation of ammonia in the plant tissues, which kills the plant within hours of application. PAT catalyses the acetylation of the herbicide phosphinothricin and thus detoxifies glufosinate ammonium into an inactive compound. The modified maize line is protected from ECB and permits farmers to use phosphinothricin-containing herbicides for weed control in the cultivation of maize.</p>\n', 'Enabled', NULL, '2013-08-29 22:04:34'),
(2, 9, '<p style="text-align: justify;">Maize line MON 810 (trade name YieldGard) was developed through a specific genetic modification to be resistant to attack by European corn borer (ECB; <i>Ostrinia nubilalis</i>), a major insect pest of maize in agriculture. The novel variety produces a truncated version of the insecticidal protein, Cry1Ab, derived from <i>Bacillus thuringiensis</i>. Delta-endotoxins, such as the Cry1Ab protein expressed in MON 810, act by selectively binding to specific sites localized on the brush border midgut epithelium of susceptible insect species. Following binding, cation-specific pores are formed that disrupt midgut ion flow and thereby cause paralysis and death. Cry1Ab is insecticidal only to lepidopteran insects, and its specificity of action is directly attributable to the presence of specific binding sites in the target insects. There are no binding sites for delta-endotoxins of <i>B. thuringiensis</i> on the surface of mammalian intestinal cells, therefore, livestock animals and humans are not susceptible to these proteins.</p>\r\n', 'Enabled', NULL, '2013-09-02 14:27:02'),
(3, 25, '<p style="text-align: justify;">The Bt-maize Event 176 (tradenames NaturGard&trade; KnockOut&trade;) was developed through a specific genetic modification to be resistant to attack by European corn borer (ECB; <i>Ostrinia nubilalis</i>), a major insect pest of maize in agriculture. These novel plants produce a truncated version of the insecticidal protein, Cry1Ab, derived from <i>Bacillus thuringiensis</i> subp. kurstaki strain HD-1. Event 176 is also genetically modified to express the <i>bar</i> gene cloned from the soil bacterium <i>Streptomyces hygroscopicus</i>, which encodes a phosphinothricin-N-acetyltransferase (PAT) enzyme. The PAT enzyme is useful as a selectable marker enabling identification of transformed plant cells as well as a source of resistance to the herbicide phosphinothricin (also known as glufosinate ammonium, the active ingredient in the herbicides Basta, Rely, Finale, and Liberty ). PAT catalyses the acetylation of phosphinothricin, and thus detoxifies phosphinothricin, eliminating its herbicidal activity. Delta-endotoxins, such as the Cry1Ab protein expressed in Event 176, act by selectively binding to specific sites localized on the brush border midgut epithelium of susceptible insect species. Following binding, cation-specific pores are formed that disrupt midgut ion flow and thereby cause paralysis and death. Cry1Ab is insecticidal only to lepidopteran insects, and its specificity of action is directly attributable to the presence of specific binding sites in the target insects. There are no binding sites for delta-endotoxins of <i>B. thuringiensis</i> on the surface of mammalian intestinal cells, therefore, livestock animals and humans are not susceptible to these proteins.</p>\n', 'Enabled', NULL, '2013-08-29 22:28:55'),
(4, 49, '<p style="text-align: justify;">Maize line CBH-351 (tradename StarLink) was developed through a specific genetic modification to be resistant to attack by European corn borer (ECB; <i>Ostrinia nubilalis</i>), a major insect pest of maize in agriculture. These novel plants contain a modified <i>cry9C</i> gene from <i>Bacillus thuringiensis</i> subsp. tolworthi strain BTS02618A. CBH-351 maize is also genetically modified to express the <i>bar</i> gene cloned from the soil bacterium <i>Streptomyces hygroscopicus</i>, which encodes a phosphinothricin-N-acetyltransferase (PAT) enzyme. The PAT enzyme is useful as a selectable marker enabling identification of transformed plant cells as well as a source of resistance to the herbicide phosphinothricin (also known as glufosinate ammonium, the active ingredient in the herbicides Basta, Rely, Finale, and Liberty). PAT catalyses the acetylation of phosphinothricin and thus detoxifies phosphinothricin, eliminating its herbicidal activity. Delta-endotoxins such as the Cry9C protein expressed by CBH-351, protects the maize plants against feeding damage of larvae of the lepidopteran insect European corn borer by selectively binding to specific sites localized on the brush border midgut epithelium of susceptible insect species. Following binding, cation-specific pores are formed that disrupt midgut ion flow and thereby cause paralysis and death. Cry9C protein is insecticidal only to lepidopteran insects, and its specificity of action is directly attributable to the presence of specific binding sites in the target insects. There are no binding sites for delta-endotoxins of <i>B. thuringiensis</i> on the surface of mammalian intestinal cells, therefore, livestock animals and humans are not susceptible to these proteins.</p>\n', 'Enabled', NULL, '2013-08-29 23:08:55'),
(5, 7, '<p style="text-align: justify;">The maize line DBT418 (tradename Bt Xtra&trade;) was developed through a specific genetic modification to be resistant to attack by European corn borer (ECB; <i>Ostrinia nubilalis</i>), a major insect pest of maize in agriculture. These novel plants produce a truncated version of the insecticidal protein, Cry1Ac, derived from <i>Bacillus thuringiensis</i> subp. kurstaki strain HD-73. Delta-endotoxins, such as the Cry1Ac protein expressed in DBT418, act by selectively binding to specific sites localized on the brush border midgut epithelium of susceptible insect species. Following binding, cation-specific pores are formed that disrupt midgut ion flow and thereby cause paralysis and death. Cry1Ac is insecticidal only to lepidopteran insects, and its specificity of action is directly attributable to the presence of specific binding sites in the target insects. There are no binding sites for delta-endotoxins of <i>B. thuringiensis</i> on the surface of mammalian intestinal cells, therefore, livestock animals and humans are not susceptible to these proteins.</p>\r\n\r\n<p style="text-align: justify;">DBT418 was also genetically modified to express the <i>bar</i> gene cloned from the soil bacterium <i>Streptomyces hygroscopicus</i>, which encodes a phosphinothricin-N-acetyltransferase (PAT) enzyme. The PAT enzyme was used as a selectable marker enabling identification of transformed plant cells as well as a source of resistance to the herbicide phosphinothricin (also known as glufosinate ammonium, the active ingredient in the herbicides Basta, Rely, Finale, and Liberty). PAT catalyses the acetylation of phosphinothricin and thus detoxifies phosphinothricin into an inactive compound, eliminating its herbicidal activity.</p>\r\n', 'Enabled', NULL, '2013-09-02 14:23:29'),
(6, 6, '<p style="text-align: justify;">Maize lines T14 and T25 were developed through a specific genetic modification to allow the use of glufosinate ammonium, the active ingredient in phosphinothricin herbicides (Basta, Rely, Finale, and Liberty), as a weed control option in maize crops. The <i>pat</i> gene, conferring tolerance to glufosinate ammonium, was cloned from the common aerobic soil actinomycete, <i>Streptomyces viridochromogenes</i>, and encodes the enzyme phosphinothricin-N-acetyltransferase (PAT).</p>\n\n<p style="text-align: justify;">The PAT enzyme was used as a selectable marker enabling identification of transformed plant cells as well as a source of resistance to the herbicide phosphinothricin (also known as glufosinate ammonium). Phosphinothricin containing herbicides, such as glufosinate ammonium, act by inhibiting glutamine synthetase resulting in the accumulation of toxic levels of ammonia that kill the plant within hours of application. The PAT enzyme detoxifies phosphinothricin by acetylation into an inactive compound. The modified corn permits farmers to use phosphinothricin-containing herbicides for weed control in the cultivation of corn.</p>\n', 'Enabled', NULL, '2013-08-29 20:44:10'),
(7, 1, '<!-- Generated by XStandard version 3.0.0.0 on 2012-10-23T14:40:19 -->\n<p style="text-align: justify;">The GA21 line of maize (<i>Zea mays</i> L.) was genetically engineered, by particle acceleration (biolistic) transformation, to be tolerant of glyphosate-containing herbicides. The isolated endogenous maize 5-enolpyruvylshikimate-3-phosphate synthase (EPSSP) gene was modified through site-directed mutagenesis, such that its encoded enzyme was insensitive to inactivation by glyphosate, and inserted into the inbred AT maize variety.</p>\n\n<p style="text-align: justify;">Glyphosate specifically binds to and inactivates EPSPS, which is involved in the biosynthesis of the aromatic amino acids tyrosine, phenylalanine and tryptophan. This enzyme is present in all plants, bacteria and fungi, but not in animals, which do not synthesize their own aromatic amino acids. Thus, EPSPS is normally present in food derived from plant and microbial sources. The modified maize line permits farmers to use glyphosate-containing herbicides, such as Roundup herbicide, for weed control in the cultivation of maize.</p>\n', 'Enabled', NULL, '2013-08-29 20:32:13'),
(8, 51, '<p style="text-align: justify;">Maize line MON80100 was developed through a specific genetic modification to be resistant to attack by European corn borer (ECB; <i>Ostrinia nubilalis</i>), a major insect pest of maize in agriculture. The novel variety produced the insecticidal protein, Cry1Ab, derived from <i>Bacillus thuringiensis</i> subsp. kurstaki (B.t.k.). Delta-endotoxins, such as the Cry1Ab protein expressed in MON80100, act by selectively binding to specific sites localized on the brush border midgut epithelium of susceptible insect species. Following binding, cation-specific pores are formed that disrupt midgut ion flow and thereby cause paralysis and death. Cry1Ab is insecticidal only to lepidopteran insects, and its specificity of action is directly attributable to the presence of specific binding sites in the target insects. There are no binding sites for delta-endotoxins of <i>B. thuringiensis</i> on the surface of mammalian intestinal cells, therefore, livestock animals and humans are not susceptible to these proteins.</p>\n', 'Enabled', NULL, '2013-08-29 23:13:29'),
(9, 74, '<p style="text-align: justify;">Maize line NK603 was developed to allow the use of glyphosate containing herbicides as a weed control option for maize crops. The gene encoding a glyphosate tolerant form of the enzyme 5-enolpyruvlyshikimate-3-phosphate synthase (EPSPS) was isolated from the soil bacterium <i>Agrobacterium tumefaciens</i> strain CP4 and introduced into maize using recombinant DNA techniques. Glyphosate specifically binds to and inactivates EPSPS, which is involved in the biosynthesis of the aromatic amino acids tyrosine, phenylalanine and tryptophan. This enzyme is present in all plants, bacteria and fungi, but not in animals, which do not synthesize their own aromatic amino acids. Thus, EPSPS is normally present in food derived from plant and microbial sources.<br />\r\n<br />\r\nFor environmental release in the United States, another glyphosate tolerant maize line, GA21, was designated as the antecedent organism for NK603. Maize line NK603 and the antecedent organism GA21 were genetically engineered using the same transformation method and contain a functionally equivalent enzyme that makes the plants tolerant to the herbicide glyphosate.</p>\r\n', 'Enabled', NULL, '2013-09-04 13:46:42'),
(10, 4, '<p style="text-align: justify;">Canola (<i>Brassica napus</i>) line Oxy-235 (ACS-BN&Oslash;11-5) was developed to allow the use of oxynil herbicides as weed control options in canola. Bromoxynil is very effective on broadleaf weeds that are common in canola fields and the deployment of transgenic bromoxynil-tolerant canola will allow the post-emergence control of these weeds without crop injury.</p>\n\n<p style="text-align: justify;">The herbicides ioxynil (3,5-di-iodo-4-hydroxybenzonitrile) and bromoxynil (3,5-dibromo-4-hydorxybenzonitrile) act on conventional dicotyledenous plants by blocking electron flow during the light reaction of photosynthesis (photosystem II). This causes super oxide production resulting in the destruction of cell membranes and an inhibition of chlorophyll formation, resulting in plant death.</p>\n\n<p style="text-align: justify;">Tolerance to oxynil herbicides in Oxy-235 was achieved by introduction of the <i>bxn</i> gene isolated from the bacterium <i>Klebsiella pneumoniae</i> (sub. sp <i>ozaenae</i>), which encodes a nitrilase enzyme that hydrolyzes oxynil herbicides to non-phytotoxic compounds.</p>\n', 'Enabled', NULL, '2013-08-29 20:37:47'),
(11, 12, '<p style="text-align: justify;">Maize line MON809 was developed through a specific genetic modification to be resistant to attack by European corn borer (ECB; <i>Ostrinia nubilalis</i>), a major insect pest of maize in agriculture. The novel variety produced the insecticidal protein, Cry1Ab, derived from <i>Bacillus thuringiensis</i> subsp. kurstaki (B.t.k.) HD-1 strain. Delta-endotoxins, such as the Cry1Ab protein expressed in MON809, act by selectively binding to specific sites localized on the brush border midgut epithelium of susceptible insect species. Following binding, cation-specific pores are formed that disrupt midgut ion flow and thereby cause paralysis and death. Cry1Ab is insecticidal only to lepidopteran insects, and its specificity of action is directly attributable to the presence of specific binding sites in the target insects. There are no binding sites for delta-endotoxins of <i>B. thuringiensis</i> on the surface of mammalian intestinal cells, therefore, livestock animals and humans are not susceptible to these proteins.</p>\n\n<p>&nbsp;</p>\n', 'Enabled', NULL, '2013-08-29 21:54:42'),
(12, 72, '<p style="text-align: justify;">Maize line MON832 was developed to allow the use of glyphosate, the active ingredient in the herbicide Roundup&reg;, as a weed control option for maize crops. Two novel genes were introduced into maize line MON832, which in combination provide field level tolerance to glyphosate. The novel plants express a glyphosate tolerant version of the enzyme 5-enolpyruvylshikimate-3-phosphate synthase (EPSPS) encoding gene isolated from <i>Agrobacterium tumefaciens</i> strain CP4 (CP4 EPSPS). Glyphosate specifically binds to and inactivates EPSPS, which is involved in the biosythesis of the aromatic amino acids tyrosine, phenylalanine and tryptophan. The EPSPS enzyme is present in all plants, bacteria and fungi, but not in animals, which do not synthesize their own aromatic amino acids. The modified enzyme (CP4 EPSPS) has a reduced binding affinity for glyphosate and allows the plant to function normally in the presence of the herbicide.</p>\n\n<p style="text-align: justify;">The second gene codes for glyphosate oxidase (<i>gox</i> gene), a bacterial enzyme from <i>Ochrobactrum anthropi</i> and is ubiquitous in nature. Glyphosate oxidase (GOX) accelerates the normal degradation of glyphosate into aminomethylphosphonic acid (AMPA) and glyoxylate. AMPA is the principal metabolite of glyphosate and is degraded by several microorganisms while glyoxylate is commonly found in plant cells and is broken down by the glyoxylic pathway for lipid metabolism.</p>\n\n<p style="text-align: justify;">These two enzymes, CP4 EPSPS and glyphosate oxidase, allow MON832 maize to be protected against herbicide damage when glyphosate is used for weed control in the cultivation of maize.</p>\n', 'Enabled', NULL, '2013-08-29 23:42:29'),
(13, 5, '<p style="text-align: justify;">Maize line MON802 was developed through a specific genetic modification to be resistant to attack by European corn borer (ECB; <i>Ostrinia nubilalis</i>), a major insect pest of maize in agriculture. The novel variety produced the insecticidal protein, Cry1Ab, derived from <i>Bacillus thuringiensis</i> subsp. kurstaki (B.t.k.) HD-1 strain. Delta-endotoxins, such as the Cry1Ab protein expressed in MON802, act by selectively binding to specific sites localized on the brush border midgut epithelium of susceptible insect species. Following binding, cation-specific pores are formed that disrupt midgut ion flow and thereby cause gut paralysis and eventual death due to bacterial sepsis. Cry1Ab is insecticidal only to lepidopteran insects, and its specificity of action is directly attributable to the presence of specific binding sites in the target insects. There are no binding sites for delta-endotoxins of <i>B. thuringiensis</i> on the surface of mammalian intestinal cells, therefore, livestock animals and humans are not susceptible to these proteins.</p>\n\n<p style="text-align: justify;">In addition, two novel genes were introduced into maize line MON802, which in combination provide field level tolerance to glyphosate the active ingredient in Roundup&reg; herbicide. The novel plants express a glyphosate tolerant version of the enzyme 5-enolpyruvylshikimate-3-phosphate synthase (EPSPS) encoding gene isolated from <i>Agrobacterium tumefaciens</i> strain CP4 (CP4 EPSPS). Glyphosate specifically binds to and inactivates EPSPS, which is involved in the biosythesis of the aromatic amino acids tyrosine, phenylalanine and tryptophan. The EPSPS enzyme is present in all plants, bacteria and fungi, but not in animals, which do not synthesize their own aromatic amino acids. The modified enzyme (CP4 EPSPS) has a reduced binding affinity for glyphosate and allows the plant to function normally in the presence of the herbicide.</p>\n\n<p style="text-align: justify;">The second gene codes for glyphosate oxidase (<i>gox</i> gene), a bacterial enzyme from <i>Ochrobactrum anthropi</i> and is ubiquitous in nature. Glyphosate oxidase (GOX) accelerates the normal degradation of glyphosate into aminomethylphosphonic acid (AMPA) and glyoxylate. AMPA is the principal metabolite of glyphosate and is degraded by several microorganisms while glyoxylate is commonly found in plant cells and is broken down by the glyoxylic pathway for lipid metabolism.</p>\n', 'Enabled', NULL, '2013-08-29 20:41:06'),
(14, 23, '<p style="text-align: justify;">Canola (<i>Brassica napus</i>) line GT73 (synonym RT73) was developed to allow the use of glyphosate, the active ingredient in the herbicide Roundup&reg;, as a weed control option in canola crops. Two novel genes were introduced into canola line GT73, which in combination provide field level tolerance to glyphosate. The novel plants express a glyphosate tolerant version of the enzyme 5-enolpyruvylshikimate-3-phosphate synthase (EPSPS) encoding gene isolated from <i>Agrobacterium tumefaciens</i> strain CP4 (CP4 EPSPS). Glyphosate specifically binds to and inactivates EPSPS, which is involved in the biosynthesis of the aromatic amino acids tyrosine, phenylalanine and tryptophan. The EPSPS enzyme is present in all plants, bacteria and fungi, but not in animals, which do not synthesize their own aromatic amino acids. The modified enzyme (CP4 EPSPS) has a reduced binding affinity for glyphosate and allows the plant to function normally in the presence of the herbicide.</p>\n\n<p style="text-align: justify;">The second gene codes for a modified version of glyphosate oxidase, a bacterial enzyme from <i>Ochrobactrum anthropi</i> strain LBAA. The gene was modified to improve the affinity of the enzyme for glyphosate and is referred to as the <i>gox</i> variant (<i>goxv247</i>). Glyphosate oxidase (GOX) accelerates the normal degradation of the herbicide glyphosate into aminomethylphosphonic acid (AMPA) and glyoxylate. AMPA is the principal metabolite of glyphosate and is degraded by several microorganisms while glyoxylate is commonly found in plant cells and is broken down by the glyoxylic pathway for lipid metabolism.</p>\n\n<p style="text-align: justify;">These two enzymes, CP4 EPSPS and glyphosate oxidase, allow GT73 canola to be protected against herbicide damage when glyphosate is used for weed control in the cultivation of canola.</p>\n', 'Enabled', NULL, '2013-08-29 22:26:06'),
(15, 46, '<p style="text-align: justify;">Sugar beet line GTSB77 was developed using recombinant DNA techniques to allow the use of glyphosate, the active ingredient in the herbicide Roundup&reg;, as a weed control option in sugar beet crops. The novel plants express an herbicide tolerant form of the enzyme 5-enolpyruvylshikimate-3-phosphate synthase (EPSPS) derived from the common soil bacterium, <i>Agrobacterium tumefaciens</i> strain CP4. Glyphosate specifically binds to and inactivates EPSPS, which is involved in the synthesis of the aromatic amino acids, tyrosine, phenylalanine and tryptophan (shikimate biochemical pathway). EPSPS is present in all plants, bacteria, and fungi but not in animals, which must obtain these essential amino acids from their diet. Because the aromatic amino acid biosynthetic pathway is not present in mammalian, avian or aquatic life forms, glyphosate has little if any toxicity for these organisms (U.S. EPA, 1993; WHO, 1994; Williams <i>et al.</i> 2000). The EPSPS enzyme is normally present in food derived from plant and microbial sources.</p>\n\n<p style="text-align: justify;">The plasmid used during the transformation of this sugar beet line also contained a second gene that encoded the enzyme glyphosate oxidase (GOX) from the bacterium <i>Ochrobactrum anthropi</i>. This enzyme was intended to accelerate the normal degradation of glyphosate into aminomethylphosphonic acid (AMPA) and glyoxylate in plant cells. Upon insertion into the plant genome, the GOX encoding gene was truncated and fused to genomic sugar beet DNA sequences, resulting in a chimeric sequence that did not express a functional protein.<br />\n<br />\nLine GTSB77 expresses a reporter gene (<i>uidA</i>) encoding the enzyme beta-D-glucuronidase (GUS) from <i>E. coli</i>. The expression of GUS activity was used during the development phase to identify transgenic plants containing the introduced gene sequences.</p>\n', 'Enabled', NULL, '2013-08-29 23:04:50'),
(16, 13, '<p style="text-align: justify;">Maize line MS3 (tradename InVigor&reg;) was developed to provide a reliable hybridization system based on nuclear male sterility. The transgenic line was produced by genetically engineering plants to be male sterile and tolerant to the herbicide glufosinate ammonium, where herbicide tolerance was used as a selectable marker to identify the male sterile plants. These transformed maize lines contain the barnase gene for male sterility, isolated from <i>Bacillus amyloliquefaciens</i>, a common soil bacterium that is frequently used as a source for industrial enzymes. The barnase gene encodes for a ribonuclease enzyme (RNAse) that is expressed only in the tapetum cells of the pollen sac during anther development. The RNAse affects RNA production, disrupting normal cell functioning and arresting early anther development, thus leading to male sterility.</p>\n\n<p style="text-align: justify;">The male sterile maize line MS3 also contained the <i>bar</i> gene isolated from the common soil microorganism <i>Streptomyces hygroscopicus</i>, for use as a selectable marker. The <i>bar</i> gene encodes a phosphinothricin acetyl transferase (PAT) enzyme, which, when introduced into a plant cell, confers tolerance to the herbicide glufosinate ammonium. The herbicide tolerance trait was introduced into the maize line as a selectable marker to identify transformed plants during tissue culture regeneration, and as a field selection method to identify the male sterile lines at any growth stage. Under field conditions, plants that were not male-sterile could be eliminated by application of the herbicide glufosinate ammonium. The novel hybrid system provided an efficient and effective way to identify male-sterile plants for use in hybrid seed production.</p>\n\n<p style="text-align: justify;">Glufosinate ammonium is the active ingredient in phosphinothricin herbicides (Basta, Rely, Finale, and Liberty) and acts by inhibiting the plant enzyme glutamine synthetase, a key enzyme in plants that detoxifies ammonia by incorporating it into glutamine. Inhibition of this enzyme leads to an accumulation of ammonia in the plant tissues, which kills the plant within hours of application. PAT catalyses the acetylation of the herbicide phosphinothricin and thus detoxifies glufosinate ammonium into an inactive compound.</p>\n', 'Enabled', NULL, '2013-08-29 21:58:30'),
(17, 27, '<p style="text-align: justify;">The MS8 and RF3 canola lines (<i>Brassica napus</i>) were developed using genetic engineering techniques to provide a pollination control system for production of hybrid oilseed rape (MS8 x RF3). The novel hybridization system involves the use of two parental lines, a male sterile line MS8 and a fertility restorer line RF3. The transgenic MS8 plants do not produce viable pollen grains and cannot self-pollinate. In order to completely restore fertility in the hybrid progeny, line MS8 must be pollinated by a modified plant containing a fertility restorer gene, such as line RF3. The resultant F1 hybrid seed derived from cross between MS8 x RF3, produces hybrid plants that produce pollen and are completely fertile.</p>\n\n<p style="text-align: justify;">The transgenic line MS8 (DBN230-0028) was produced by genetically engineering plants to be male sterile and tolerant to the herbicide glufosinate ammonium (as a selectable marker). The parental line MS8 contains the barnase gene for male sterility, isolated from <i>Bacillus amyloliquefaciens</i>, a common soil bacterium that occurs naturally in the soil and is frequently used as a source for industrial enzymes. The barnase gene encodes for a ribonuclease enzyme (RNAse) that is expressed only in the tapetum cells of the pollen sac during anther development. The RNAse affects RNA production, disrupting normal cell functioning and arresting early anther development, thus leading to male sterility.<br />\nThe transgenic line RF3 (DBN212-0005) was produced by genetically engineering plants to restore fertility in the hybrid line and to be tolerant to the herbicide glufosinate ammonium (as a selectable marker). Transgenic RF3 plants contain the barstar gene isolated from <i>Bacillus amyloliquefaciens</i>. The barstar gene codes for a ribonuclease inhibitor (barstar enzyme) that is expressed only in the tapetum cells of the pollen sac during anther development. The ribonuclease inhibitor specifically inhibits barnase RNAse expressed by the MS8 line. Together, the RNAse and the ribonuclease inhibitor form a very stable one-to-one complex, in which the RNAse is inactivated. As a result, when pollen from the restorer line RF3 is transferred to the male sterile line MS8, the resultant progeny express the RNAse inhibitor in the tapetum cells of the anthers allowing hybrid plants to develop normal anthers and restore fertility.</p>\n\n<p style="text-align: justify;">Both trangenic canola lines MS8 and RF3 contain the <i>bar</i> gene that confers tolerance to the post-emergence, broad-spectrum phosphinothricin herbicides (Basta, Rely, Finale, and Liberty). The <i>bar</i> gene, isolated from the common soil microorganism <i>Streptomyces hygroscopicus</i> encodes a phosphinothricin acetyl transferase (PAT) enzyme. The active ingredient in phosphinothricin herbicides is glufosinate ammonium which acts by inhibiting the plant enzyme glutamine synthetase, leading to the accumulation of phytotoxic levels of ammonia killing the plant within hours of application. PAT detoxifies glufosinate ammonium by acetylation into an inactive compound, eliminating its herbicidal activity. The herbicide tolerance trait was introduced into the canola lines as a selectable marker to identify transformed plants during tissue culture regeneration, and as a field selection method to obtain 100% hybrid seed.</p>\n', 'Enabled', NULL, '2013-08-29 22:33:33'),
(18, 50, '<p style="text-align: justify;">Maize lines 676, 678, and 680 were developed to provide a reliable hybrid system based on nuclear male sterility. The transgenic lines were produced by genetically engineering plants to be male sterile and tolerant to the herbicide glufosinate ammonium, where herbicide tolerance was used as a selectable marker to identify the male sterile plants. These transformed maize lines contain an introduced gene (<i>dam</i>) from <i>Escherichia coli</i> that encodes the enzyme DNA adenine methylase (DAM). Expression of this gene in specific plant tissues results in the inability of the transformed plants to produce anthers or pollen, resulting in a male sterile plant.</p>\n\n<p style="text-align: justify;">The maize lines 676, 678, and 680 also contained the <i>pat</i> gene, isolated from the bacterium <i>Streptomyces viridochromogenes</i>, for use as a selectable marker. The <i>pat</i> gene encodes a phosphinothricin acetyl transferase (PAT) enzyme, which, when introduced into a plant cell, confers tolerance to the herbicide glufosinate ammonium. The <i>pat</i> gene was used as a selectable marker to identify transformed plants during tissue culture regeneration, and as a field selection method to identify the male sterile lines prior to flowering. Under field conditions, plants that were not male-sterile could be eliminated by application of the herbicide glufosinate ammonium. The novel hybrid system provided an efficient and effective way to identify male-sterile plants for use in hybrid seed production.</p>\n\n<p style="text-align: justify;">Glufosinate ammonium is the active ingredient in phosphinothricin herbicides (Basta&reg;, Rely&reg;, Finale&reg;, and Liberty&reg;). Glufosinate chemically resembles the amino acid glutamate and acts to inhibit an enzyme, called glutamine synthetase, which is involved in the synthesis of glutamine. Essentially, glufosinate acts enough like glutamate, the molecule used by glutamine synthetase to make glutamine, that it blocks the enzyme&#39;s usual activity. Glutamine synthetase is also involved in ammonia detoxification. The action of glufosinate results in reduced glutamine levels and a corresponding increase in concentrations of ammonia in plant tissues, leading to cell membrane disruption and cessation of photosynthesis resulting in plant withering and death. The PAT enzyme detoxifies phosphinothricin by acetylation into an inactive compound.</p>\n', 'Enabled', NULL, '2013-08-29 23:12:05'),
(19, 66, '<p style="text-align: justify;">Maize line MS6 (tradename InVigor&reg;) was developed to provide a reliable hybridization system based on nuclear male sterility. The transgenic line was produced by genetically engineering plants to be male sterile and tolerant to the herbicide glufosinate ammonium, where herbicide tolerance was used as a selectable marker to identify the male sterile plants. These transformed maize lines contain the barnase gene for male sterility, isolated from <i>Bacillus amyloliquefaciens</i>, a common soil bacterium that is frequently used as a source for industrial enzymes. The barnase gene encodes for a ribonuclease enzyme (RNAse) that is expressed only in the tapetum cells of the pollen sac during anther development. The RNAse affects RNA production, disrupting normal cell functioning and arresting early anther development, thus leading to male sterility.</p>\n\n<p style="text-align: justify;">The male sterile maize line MS6 also contained the <i>bar</i> gene isolated from the common soil microorganism <i>Streptomyces hygroscopicus</i>, for use as a selectable marker. The <i>bar</i> gene encodes a phosphinothricin acetyl transferase (PAT) enzyme, which, when introduced into a plant cell, confers tolerance to the herbicide glufosinate ammonium. The herbicide tolerance trait was introduced into the maize line as a selectable marker to identify transformed plants during tissue culture regeneration, and as a field selection method to identify the male sterile lines at any growth stage. Under field conditions, plants that were not male-sterile could be eliminated by application of the herbicide glufosinate ammonium. The novel hybrid system provided an efficient and effective way to identify male-sterile plants for use in hybrid seed production.</p>\n\n<p style="text-align: justify;">Glufosinate ammonium is the active ingredient in phosphinothricin herbicides (Basta, Rely, Finale, and Liberty) and acts by inhibiting the plant enzyme glutamine synthetase, a key enzyme in plants that detoxifies ammonia by incorporating it into glutamine. Inhibition of this enzyme leads to an accumulation of ammonia in the plant tissues, which kills the plant within hours of application. PAT catalyses the acetylation of the herbicide phosphinothricin and thus detoxifies glufosinate ammonium into an inactive compound.</p>\n\n<p style="text-align: justify;">In the United States, the male-sterile line MS3 was designated as the antecedent organism for MS6 for the purposes of conducting the environmental safety assessment. Maize lines MS3 and MS6 were genetically modified using the same transformation technique and the same genetic elements. Based on the similarity between MS6 and the antecedent organism MS3, and on an analysis of scientific data and field tests of MS6, the maize line MS6 was judged not to have any characteristics that would pose a greater impact on the environment or non-target organisms.</p>\n\n<p style="text-align: justify;">For additional information related to either the environmental or food safety assessment of the antecedent organism, MS3, the reader is referred to the description for that product.</p>\n', 'Enabled', NULL, '2013-08-29 23:40:59'),
(20, 17, '<p style="text-align: justify;">The maize hybrid DK404SR was developed to allow the use of sethoxydim, the active ingredient in the herbicide Poast&reg;, for the control of annual and perennial grasses in maize crops. DK404SR originated from a somaclonal variant selected from embryo tissue and expresses a modified version of acetyl-CoA-carboxylase (ACCase) enzyme.</p>\n\n<p style="text-align: justify;">ACCase is a key enzyme in the fatty acid biosynthesis pathway, necessary for the synthesis and maintenance of membranes and for the incorporation of fatty acids into triacylglycerides. The enzyme is inhibited by cyclohexanedione herbicides, such as sethoxydim, resulting in a lethal disruption of lipid biosynthesis. The mutant ACCase gene encodes for a modified version of acetyl-CoA-carboxylase enzyme in which the sethoxydim binding site is altered such that the ACCase enzyme is not inhibited by the sethoxydim herbicide, yet still retains its normal catalytic properties in fatty acid synthesis. The modified maize plants also demonstrated some level of cross-tolerance to the related herbicides, aryloxyphenoxypropionates, including haloxyfop (not registered in Canada), fluazifop (Venture) and quizalofop (Assure). These herbicides all have the same mode of action through ACCase inhibition. Natural tolerance to sethoxydim herbicide is found in several broadleaved plants and grasses and includes annual ryegrass, green foxtail and red fescue.</p>\n', 'Enabled', NULL, '2013-08-29 22:08:03'),
(21, 48, '<p style="text-align: justify;">Maize line DLL25 (synonym B16) was developed through a specific genetic modification to allow the use of glufosinate ammonium, the active ingredient in phosphinothricin herbicides (Basta, Rely, Finale, and Liberty), as a weed control option in maize crops. The <i>bar</i> gene, conferring tolerance to glufosinate ammonium, was isolated from the common aerobic soil actinomycete, <i>Streptomyces hygroscopicus</i>, and encodes the enzyme phosphinothricin-N-acetyltransferase (PAT). The PAT enzyme occurs naturally in the soil and acetyltransferases are ubiquitous in nature.</p>\n\n<p style="text-align: justify;">The PAT enzyme was used as a selectable marker enabling identification of transformed plant cells as well as a source of field tolerance to phosphinothricin containing herbicides. Glufosinate ammounium acts by inhibiting the plant enzyme glutamine synthetase, a key enzyme that detoxifies ammonia by incorporating it into glutamine. Inhibition of this enzyme leads to an accumulation of ammonia in the plant tissues, which kills the plant within hours of application. PAT catalyses the acetylation of phosphinothricin detoxifying it into an inactive compound. The modified corn permits farmers to use phosphinothricin-containing herbicides for weed control in the cultivation of corn.</p>\n', 'Enabled', NULL, '2013-08-29 23:07:25'),
(22, 18, '<p style="text-align: justify;">The 23-198 and 23-18-17 lines of canola (Brassica napus) were developed through a specific genetic modification to produce oil that contains significant levels of lauric acid. The novel varieties were developed from the 212/86 canola variety by introduction of a gene from the California bay tree, the leaves of which are an alternative source of the spice &ldquo;bay leaf&rdquo; which is commercially harvested from <i>Laurus nobilis</i>. The introduced gene encodes a thioesterase enzyme that is active in the fatty acid biosynthetic pathway of the developing seed resulting in the accumulation of triacylglycerides containing esterified lauric acid (12:0) and, to a lesser extent, myristic acid (14:0). The processed oil derived from these novel varieties has a level of lauric acid similar to that of coconut ant palm kernel oil.</p>\r\n', 'Enabled', NULL, '2013-09-03 13:39:25'),
(23, 22, '<p style="text-align: justify;">Canola (<i>Brassica napus</i>) line HCN92 (synonyms: Topas19/2, Innovator) was developed through a specific genetic modification to allow the use of glufosinate ammonium, the active ingredient in phosphinothricin herbicides such as Liberty&reg;. The <i>pat</i> gene, which encodes the enzyme phosphinothricin-N-acetyltransferase (PAT) and confers tolerance to glufosinate ammonium, was isolated from the common aerobic soil actinomycete, <i>Streptomyces viridochromogenes</i> strain T&uuml; 494 and introduced into the parent canola line.</p>\n\n<p style="text-align: justify;">The PAT enzyme was used as a selectable marker enabling identification of transformed plant cells as well as a source of field tolerance to phosphinothricin containing herbicides. Glufosinate ammounium acts by inhibiting the plant enzyme glutamine synthetase, a key enzyme that detoxifies ammonia by incorporating it into glutamine. Inhibition of this enzyme leads to an accumulation of ammonia in the plant tissues, which kills the plant within hours of application. PAT catalyses the acetylation of phosphinothricin detoxifying it into an inactive compound. The modified canola permits farmers to use phosphinothricin-containing herbicides for weed control in the cultivation of canola.</p>\n', 'Enabled', NULL, '2013-08-29 22:24:05'),
(24, 19, '<p style="text-align: justify;">Canola (<i>Brassica napus</i>) line GT200 was developed to allow the use of glyphosate, the active ingredient in the herbicide Roundup&reg;, as a weed control option in canola crops. Two novel genes were introduced into canola line GT200, which in combination provide field level tolerance to glyphosate. The novel plants express a glyphosate tolerant version of the enzyme 5-enolpyruvylshikimate-3-phosphate synthase (EPSPS) isolated from <i>Agrobacterium tumefaciens</i> strain CP4 (CP4 EPSPS). Glyphosate containing herbicides act by binding to and inactivating the wild type EPSPS enzyme, which is involved in the synthesis of aromatic amino acids, tyrosine, phenylalanine and tryptophan (shikimate biochemical pathway).</p>\n\n<p style="text-align: justify;">The EPSPS enzyme is present in all plants, bacteria and fungi, but not in animals, which do not synthesize their own aromatic amino acids. The modified enzyme (CP4 EPSPS) has a reduced binding affinity for glyphosate and allows the plant to function normally in the presence of the herbicide.</p>\n\n<p style="text-align: justify;">The second gene, isolated from <i>Ochrobactrum anthropi</i> strain LBAA, encodes the enzyme glyphosate oxidase, which accelerates the normal degradation of the herbicide glyphosate into aminomethylphosphonic acid (AMPA) and glyoxylate. AMPA is the principal metabolite of glyphosate and is degraded by several microorganisms while glyoxylate is commonly found in plant cells and is broken down by the glyoxylic pathway for lipid metabolism.</p>\n\n<p style="text-align: justify;">These two enzymes, CP4 EPSPS and glyphosate oxidase (GOX), allow GT200 canola to be protected against herbicide damage when glyphosate is used for weed control in the cultivation of canola.</p>\n', 'Enabled', NULL, '2013-08-29 22:14:07'),
(25, 32, '<p style="text-align: justify;">Canola (<i>Brassica napus</i>) line T45 (synonym HCN28) was developed using recombinant DNA techniques to allow the use of glufosinate ammonium, the active ingredient in phosphinothricin herbicides such as Basta&reg;, Rely&reg;, Finale&reg;, and Liberty&reg;.</p>\n\n<p style="text-align: justify;">Prior to the novel food safety assessment of T45, Health Canada had approved the glufosinate tolerant canola lines HCN92 (Innovator) and HCN10, both derived form the transformation event Topas 19/2. The primary difference between T45 and Topas 19/2 derived transformants is that the former does not contain an antibiotic resistance marker gene. The phosphinothricin-N-acetyltransferase (<i>pat</i>) gene introduced into T45, which conferred the novel trait of glufosinate herbicide tolerance, was also used as a selectable marker for screening transgenic plants, thereby eliminating the need for an antibiotic resistance marker in the construct.</p>\n\n<p style="text-align: justify;">Glufosinate is a short name for the ammonium salt, glufosinate-ammonium. It is a broad-spectrum contact herbicide and is used to control a wide range of weeds after the crop emerges or for total vegetation control on land not used for cultivation. Glufosinate herbicides are also used to desiccate (dry off) crops before harvest.</p>\n\n<p style="text-align: justify;">Glufosinate is a natural compound isolated from two species of Streptomyces fungi. It inhibits the activity of an enzyme, glutamine synthetase, which is necessary for the production of glutamine and for ammonia detoxification. The application of glufosinate leads to reduced glutamine and increased ammonia levels in the plant tissues. This causes photosynthesis to stop and the plant dies within a few days. Glufosinate also inhibits the same enzyme in animals. Glufosinate ammonium is currently registered in Canada as a non-selective herbicide for both non-crop and crop uses. It is highly biodegradable, has no residual activity, and very low toxicity for humans and wild fauna.</p>\n', 'Enabled', NULL, '2013-08-29 22:46:08'),
(26, 26, '<p style="text-align: justify;">The MS1 and RF1 canola lines (<i>Brassica napus</i>) were developed using genetic engineering techniques to provide a pollination control system for production of hybrid oilseed rape (MS1 x RF1). The novel hybridization system involves the use of two parental lines, a male sterile line MS1 and a fertility restorer line RF1. The transgenic MS1 plants do not produce viable pollen grains and cannot self-pollinate. In order to completely restore fertility in the hybrid progeny, line MS1 must be pollinated by a modified plant containing a fertility restorer gene, such as line RF1. The resultant F1 hybrid seed derived from cross between MS1 x RF1, produces hybrid plants that produce pollen and are completely fertile.</p>\n\n<p style="text-align: justify;">The transgenic line MS1 (B91-4) was produced by genetically engineering plants to be male sterile and tolerant to the herbicide glufosinate ammonium (as a selectable marker). The parental line MS1 contains the <i>barnase</i> gene for male sterility, isolated from <i>Bacillus amyloliquefaciens</i>, a common soil bacterium that occurs naturally in the soil and in various organisms including bacteria and plants, and frequently used as a source for industrial enzymes. The <i>barnase</i> gene encodes for a ribonuclease enzyme (RNAse) expressed only in the tapetum cells of the pollen sac during anther development. The RNAse affects RNA production, disrupting normal cell functioning and arresting early anther development, thus leading to male sterility.</p>\n\n<p style="text-align: justify;">The transgenic line RF1 (B93-101) was produced by genetically engineering plants to restore fertility in the hybrid line and to be tolerant to the herbicide glufosinate ammonium (as a selectable marker). Transgenic RF1 plants contain the <i>barstar</i> gene isolated from <i>Bacillus amyloliquefaciens</i>. The <i>barstar</i> gene codes for a ribonuclease inhibitor (barstar enzyme) expressed only in the tapetum cells of the pollen sac during anther development. The ribonuclease inhibitor (barstar enzyme) specifically inhibits barnase RNAse expressed by the MS1 line. Together, the RNAse and the ribonuclease inhibitor form a very stable one-to-one complex, in which the RNAse is inactivated. As a result, when pollen from the restorer line RF1 is crossed to the male sterile line MS1, the resultant progeny express the RNAse inhibitor in the tapetum cells of the anthers allowing hybrid plants to develop normal anthers and restore fertility.<br />\nBoth trangenic canola lines MS1 and RF1 contain the <i>bar</i> gene that confers tolerance to the post-emergence, broad-spectrum phosphinothricin herbicides (Liberty&reg;). The <i>bar</i> gene, isolated from the common soil microorganism <i>Streptomyces hygroscopicus</i>, encodes a phosphinothricin acetyl transferase (PAT) enzyme. The active ingredient in phosphinothricin herbicides is glufosinate ammounium which acts by inhibiting the plant enzyme glutamine synthetase, leading to the accumulation of phytotoxic levels of ammonia killing the plant within hours of application. PAT detoxifies glufosinate ammonium by acetylation into an inactive compound, eliminating its herbicidal activity. The herbicide tolerance trait was introduced into the canola lines as a selectable marker to identify transformed plants cells in the laboratory, and as a field selection method to obtain 100% hybrid seed.</p>\n', 'Enabled', NULL, '2013-08-29 22:31:33');
INSERT INTO `gmcropdatabase_events_introductions` (`id`, `eventId`, `description`, `status`, `created`, `updated`) VALUES
(27, 65, '<p style="text-align: justify;">The MS1 and RF2 canola lines (<i>Brassica napus</i>) were developed using genetic engineering techniques to provide a pollination control system for production of hybrid oilseed rape (MS1 x RF2). The novel hybridization system involves the use of two parental lines, a male sterile line MS1 and a fertility restorer line RF2. The transgenic MS1 plants do not produce viable pollen grains and cannot self-pollinate. In order to completely restore fertility in the hybrid progeny, line MS1 must be pollinated by a modified plant containing a fertility restorer gene, such as line RF2. The resultant F1 hybrid seed derived from cross between MS1 x RF2, produces hybrid plants that produce pollen and are completely fertile.</p>\n\n<p style="text-align: justify;">The transgenic line MS1 (B91-4) was produced by genetically engineering plants to be male sterile and tolerant to the herbicide glufosinate ammonium (as a selectable marker). The parental line MS1 contains the <i>barnase</i> gene for male sterility, isolated from <i>Bacillus amyloliquefaciens</i>, a common soil bacterium that occurs naturally in the soil and in various organisms including bacteria and plants, and frequently used as a source for industrial enzymes. The <i>barnase</i> gene encodes for a ribonuclease enzyme (RNAse) expressed only in the tapetum cells of the pollen sac during anther development. The RNAse affects RNA production, disrupting normal cell functioning and arresting early anther development, thus leading to male sterility.</p>\n\n<p style="text-align: justify;">The transgenic line RF2 (B94-2) was produced by genetically engineering plants to restore fertility in the hybrid line and to be tolerant to the herbicide glufosinate ammonium (as a selectable marker). Transgenic RF2 plants contain the <i>barstar</i> gene isolated from <i>Bacillus amyloliquefaciens</i>. The <i>barstar</i> gene codes for a ribonuclease inhibitor (barstar enzyme) expressed only in the tapetum cells of the pollen sac during anther development. The ribonuclease inhibitor (barstar enzyme) specifically inhibits barnase RNAse expressed by the MS1 line. Together, the RNAse and the ribonuclease inhibitor form a very stable one-to-one complex, in which the RNAse is inactivated. As a result, when pollen from the restorer line RF2 is crossed to the male sterile line MS1, the resultant progeny express the RNAse inhibitor in the tapetum cells of the anthers allowing hybrid plants to develop normal anthers and restore fertility.</p>\n\n<p style="text-align: justify;">Both transgenic canola lines MS1 and RF2 contain the <i>bar</i> gene that confers tolerance to the post-emergence, broad-spectrum phosphinothricin herbicides (Liberty&reg;). The <i>bar</i> gene, isolated from the common soil microorganism <i>Streptomyces hygroscopicus</i>, encodes a phosphinothricin acetyl transferase (PAT) enzyme. The active ingredient in phosphinothricin herbicides is glufosinate ammonium which acts by inhibiting the plant enzyme glutamine synthetase, leading to the accumulation of phytotoxic levels of ammonia killing the plant within hours of application. PAT detoxifies glufosinate ammonium by acetylation into an inactive compound, eliminating its herbicidal activity. The herbicide tolerance trait was introduced into the canola lines as a selectable marker to identify transformed plants cells in the laboratory, and as a field selection method to obtain 100% hybrid seed.</p>\n', 'Enabled', NULL, '2013-08-29 23:39:16'),
(28, 42, '<p style="text-align: justify;">Soybean line GU262 was developed through a specific genetic modification to allow the use of glufosinate ammonium, the active ingredient in phosphinothricin containing herbicides (Basta, Ignite, Rely, Liberty, Harvest, and Finale), as a weed control option in soybean crops. The <i>pat</i> gene, which encodes the enzyme phosphinothricin-N-acetyltransferase (PAT) and confers tolerance to glufosinate ammonium, was isolated from the common aerobic soil actinomycete, <i>Streptomyces viridochromogenes</i> strain T&uuml; 494 and introduced into the parent soybean line.</p>\n\n<p style="text-align: justify;">Glufosinate is a short name for the ammonium salt, glufosinate-ammonium. It is a broad-spectrum contact herbicide and is used to control a wide range of weeds after the crop emerges or for total vegetation control on land not used for cultivation. Glufosinate is a natural compound isolated from two species of Streptomyces fungi. It inhibits the activity of an enzyme, glutamine synthetase, which is necessary for the production of glutamine and for ammonia detoxification. The application of glufosinate leads to reduced glutamine and increased ammonia levels in the plant tissues. This causes photosynthesis to stop and the plant dies within a few days. Glufosinate also inhibits the same enzyme in animals. It is highly biodegradable, has no residual activity, and very low toxicity for humans and wild fauna. The PAT enzyme detoxifies phosphinothricin by acetylation into an inactive compound.</p>\n\n<p style="text-align: justify;">In the United States, the transgenic soybean lines A2704-12, A2704-21, and A5547-35 were designated as the antecedent organisms for GU262 for the purposes of conducting an environmental safety assessment. The soybean GU262 and its progeny were similar to the antecedent organisms as they were genetically engineered to express the same <i>pat</i> gene, and they all exhibited similar agronomic characteristics. Based on the similarity between between GU262 and the antecedent organisms A2704-12, A2704-21, and A5547-35, and on an analysis of scientific data and field tests, the soybean line GU262 was judged not to have any characteristics that would have a significant impact on any beneficial organisms in the environment or on any threatened or endangered species.</p>\n', 'Enabled', NULL, '2013-08-29 22:58:53'),
(29, 60, '<p style="text-align: justify;">Soybean lines A2704-12, A2704-21, and A5547-35 were developed through a specific genetic modification to allow for the use of glufosinate ammonium, the active ingredient in phosphinothricin herbicides (Basta&reg;, Ignite&reg;, Rely&reg;, Liberty&reg;, Harvest&reg;, and Finale&reg;) as a weed control option in soybean crops. The <i>pat</i> gene, conferring tolerance to glufosinate ammonium, was cloned from the common aerobic soil actinomycete, <i>Streptomyces viridochromogenes</i>, and encodes the enzyme phosphinothricin-N-acetyltransferase (PAT).</p>\n\n<p style="text-align: justify;">Glufosinate is a short name for the ammonium salt, glufosinate-ammonium. It is a broad-spectrum contact herbicide and is used to control a wide range of weeds after the crop emerges or for total vegetation control on land not used for cultivation. Glufosinate is a natural compound isolated from two species of Streptomyces fungi. It inhibits the activity of an enzyme, glutamine synthetase, which is necessary for the production of glutamine and for ammonia detoxification. The application of glufosinate leads to reduced glutamine and increased ammonia levels in the plant tissues. This causes photosynthesis to stop and the plant dies within a few days. Glufosinate also inhibits the same enzyme in animals. It is highly biodegradable, has no residual activity, and very low toxicity for humans and wild fauna. The PAT enzyme detoxifies phosphinothricin via acetylation into an inactive compound.</p>\n', 'Enabled', NULL, '2013-08-29 23:33:16'),
(30, 21, '<p style="text-align: justify;">The soybean line GTS 40-3-2 was developed to allow for the use of glyphosate, the active ingredient in the herbicide Roundup&reg;, as a weed control option for soybean. This genetically engineered soybean variety contains a glyphosate tolerant form of the plant enzyme 5-enolpyruvylshikimate-3-phosphate synthase (EPSPS) isolated from the common soil bacterium, <i>Agrobacterium tumefaciens</i> strain CP4 (CP4 EPSPS).</p>\n\n<p style="text-align: justify;">The EPSPS enzyme is part of the shikimate pathway that is involved in the production of aromatic amino acids and other aromatic compounds in plants (Steinrucken &amp; Amrhein, 1980). When conventional plants are treated with glyphosate, the plants cannot produce the aromatic amino acids needed to survive. This enzyme is present in all plants, bacteria, fungi, but not in animals, which do not synthesize their own aromatic amino acids. Because the aromatic amino acid biosynthetic pathway is not present in mammalian, avian or aquatic life forms, glyphosate has little if any toxicity for these organisms (U.S. EPA, 1993; WHO, 1994; Williams <i>et al</i>. 2000). The EPSPS enzyme is normally present in food derived from plant and microbial sources.</p>\n\n<p style="text-align: justify;">GTS 40-3-2 was developed by introducing the CP4 EPSPS coding sequence into the soybean variety A5403, a commercial soybean variety of Asgrow Seed Company, using particle-acceleration (biolistic) transformation. A5403 is a maturity group V cultivar that combines consistently high yield potential with resistance to races 3 and 4 of the soybean cyst nematode (SCN). It also possesses good standability, excellent emergence and tolerance to many leaf and stem diseases. The glyphosate tolerance trait has since been transferred into more than one thousand commercial soybean varieties by traditional breeding techniques. Globally, glyphosate-tolerant soybeans were planted on more than 50 million hectares in 2007. One of the reasons growers have rapidly adopted the glyphosate-tolerant soybean is the simplicity it offers in weed control. Since glyphosate containing herbicides are highly effective against the vast majority of annual and perennial grasses and broadleaf weeds, growers planting glyphosate tolerant soybeans are able to reduce the number of herbicides used to control the economically destructive weeds that grow in their fields and thereby realize a savings in weed control costs. This reduction in herbicides used has benefited the environment by reducing the number of herbicide applications and also allows growers to implement integrated weed management practices in their fields - practices that are generally not possible when pre-plant or pre-emergent herbicides are used.</p>\n', 'Enabled', NULL, '2013-08-29 22:21:16'),
(31, 41, '<p style="text-align: justify;">Three lines of a new variety of soybean (G94-1, G94-19 and G168), high in the monounsaturated fatty acid oleic acid, were generated by the transfer of a second copy of a soybean fatty acid desaturase gene (GmFad2-1) to a high yielding commercial variety of soybean (line A2396). The fatty acid desaturase is responsible for the synthesis of linoleic acid, which is the major polyunsaturated fatty acid present in soybean oil. The presence of a second copy of the fatty acid desaturase gene causes a phenomenon known as &quot;gene silencing&quot; which results in both copies of the fatty acid desaturase gene being &quot;switched off&quot;, thus preventing linoleic acid from being synthesised and leading to the accumulation of oleic acid in the developing soybean seed.</p>\n\n<p style="text-align: justify;">The genetic modification affects only the seed and endogenous GmFad2-1 gene is still expressed in other plant parts such as the leaves. These changes result in a superior, more heat stable soybean oil with improved nutritional and functional properties. High oleic soybean oil contains oleic acid levels higher than those found in olive oil and rapeseed oil.</p>\n\n<p style="text-align: justify;">Other genes transferred along with the GmFad2-1 gene were the <i>uidA</i> gene and the <i>bla</i> gene. The <i>uidA</i> gene is a colourimetric marker used for selection of transformed plant lines during the soybean transformation procedure. It codes for the enzyme beta-glucuronidase and is derived from the bacterium <i>Escherichia coli</i>. The <i>bla</i> gene is a marker used to select transformed bacteria from non-transformed bacteria during the DNA cloning and recombination steps undertaken in the laboratory prior to transformation of the plant cells. It codes for the enzyme beta-lactamase and confers resistance to some beta-lactam antibiotics, such as penicillin and ampicillin.</p>\n', 'Enabled', NULL, '2013-08-29 22:56:47'),
(32, 40, '<p style="text-align: justify;">Soybean line A5547-127 was developed through a specific genetic modification to allow the use of glufosinate ammonium, the active ingredient in phosphinothricin herbicides (Basta , Ignite , Rely , Liberty , Harvest , and Finale ) as a weed control option in soybean crops. The <i>pat</i> gene, conferring tolerance to glufosinate ammonium, was cloned from the common aerobic soil actinomycete, <i>Streptomyces viridochromogenes</i>, and encodes the enzyme phosphinothricin-N-acetyltransferase (PAT).</p>\n\n<p style="text-align: justify;">Glufosinate is a short name for the ammonium salt, glufosinate-ammonium. It is a broad-spectrum contact herbicide and is used to control a wide range of weeds after the crop emerges or for total vegetation control on land not used for cultivation. Glufosinate is a natural compound isolated from two species of Streptomyces fungi. It inhibits the activity of an enzyme, glutamine synthetase, which is necessary for the production of glutamine and for ammonia detoxification. The application of glufosinate leads to reduced glutamine and increased ammonia levels in the plant tissues. This causes photosynthesis to stop and the plant dies within a few days. Glufosinate also inhibits the same enzyme in animals. It is highly biodegradable, has no residual activity, and very low toxicity for humans and wild fauna. The PAT enzyme detoxifies phosphinothricin by acetylation into an inactive compound.</p>\n\n<p style="text-align: justify;">In the United States, the transgenic soybean lines A2704-12, A2704-21, and A5547-35 were designated as the antecedent organisms for A5547-127 for the purposes of conducting an environmental safety assessment. The soybean A5547-127 and its progeny were similar to the antecedent organisms as all of them were genetically engineered with a gene that confers resistance to the herbicide glufosinate, and they all exhibited similar agronomic characteristics. Based on the similarity between between A5547-127 and the antecedent organisms A2704-12, A2704-21, and A5547-35, and on an analysis of scientific data and field tests, the soybean line A5547-127 was judged not to have any characteristics that would have a significant impact on any beneficial organisms in the environment or on any threatened or endangered species.</p>\n', 'Enabled', NULL, '2013-08-29 22:55:28'),
(33, 39, '<p style="text-align: justify;">Soybean lines W62 and W98 were developed through a specific genetic modification to allow the use of glufosinate ammonium, the active ingredient in phosphinothricin herbicides (Basta , Ignite , Rely , Liberty , Harvest , and Finale ) as a weed control option in soybean crops. The <i>bar</i> gene, conferring tolerance to glufosinate ammonium, was cloned from the common aerobic soil actinomycete, <i>Streptomyces hygroscopicus</i>, and encodes the enzyme phosphinothricin-N-acetyltransferase (PAT).</p>\n\n<p style="text-align: justify;">Glufosinate is a short name for the ammonium salt, glufosinate-ammonium. It is a broad-spectrum contact herbicide and is used to control a wide range of weeds after the crop emerges or for total vegetation control on land not used for cultivation. Glufosinate is a natural compound isolated from two species of Streptomyces fungi. It inhibits the activity of an enzyme, glutamine synthetase, which is necessary for the production of glutamine and for ammonia detoxification. The application of glufosinate leads to reduced glutamine and increased ammonia levels in the plant tissues. This causes photosynthesis to stop and the plant dies within a few days. Glufosinate also inhibits the same enzyme in animals. It is highly biodegradable, has no residual activity, and very low toxicity for humans and wild fauna. The PAT enzyme detoxifies phosphinothricin by acetylation into an inactive compound.</p>\n\n<p style="text-align: justify;">These herbicide tolerant soybean lines also expressed a reporter gene encoding the enzyme beta-D-glucuronidase (GUS), which was used during the development process to select for transformed plants during tissue culture regeneration and multiplication.</p>\n', 'Enabled', NULL, '2013-08-29 22:54:15'),
(34, 54, '<p style="text-align: justify;">The Russet Burbank cultivar, RBMT15-101, and Shepody potato cultivars SEMT15-02 and SEMT15-15 (NewLeaf&reg; Y ) were bioengineered to be resistant to two important potato pests, the Colorado potato beetle (CPB, <i>Leptinotarsa decemlineata</i> Say.) and the ordinary (O) strain of potato potyvirus Y (PVY-O).</p>\n\n<p style="text-align: justify;">Resistance to attack by CPB was accomplished by introducing the <i>cry3A</i> gene from <i>Bacillus thuringiensis</i> subsp. tenebrionis, which encodes an insecticidal crystalline Cry3A delta-endotoxin protein. Insecticidal activity is caused by the selective binding of Cry3A protein to specific sites localized on the brush border midgut epithelium of susceptible insect species. Following binding, cation-specific pores are formed that disrupt midgut ion flow and thereby cause gut paralysis, ultimately leading to bacterial sepsis and death. Delta-endotoxins, such as the Cry3A protein expressed in CPB resistant potato lines, exhibit highly selective insecticidal activity against a narrow range of coleopteran insects such as CPB, elm leaf beetle and yellow mealworm. Their specificity of action is directly attributable to the presence of specific receptors in the target insects. There are no receptors for delta-endotoxins of <i>B. thuringiensis</i> on the surface of mammalian intestinal cells, therefore, livestock animals and humans are not susceptible to these proteins.</p>\n\n<p style="text-align: justify;">PVY is the type member of the potyvirus group and is an aphid-transmissible, rod-shaped, RNA virus that commonly infects potato, causing serious disease and economic loss. Pathogen-derived resistance to PVY was conferred by introducing the coat protein (CP) gene from the ordinary, or O-strain, of this virus. The coat protein forms a protective coat around the RNA genome of the virus and comprises 95% by mass of the virus particle. Although the exact mechanism is not fully understood, these transgenic potato lines exhibit resistance to infection and subsequent disease caused by PVY through a process that is related to viral cross-protection. The introduced viral sequences do not result in the formation of any infectious particles, nor does their expression result in any disease pathology.</p>\n\n<p style="text-align: justify;">An antibiotic resistance marker gene (<i>neo</i>) encoding the enzyme neomycin phosphotransferase II (NPTII), which inactivates aminoglycoside antibiotics such as kanamycin and neomycin, was also introduced into the genome of these plants. This gene was derived from a bacterial transposon (Tn5 transposable element from <i>Escherichia coli</i>) and was included as a selectable marker to identify transformed plants during tissue culture regeneration and multiplication. The expression of the <i>neo</i> gene in these plants has no agronomic significance and the safety of the NPTII enzyme as a food additive was evaluated by the United States Food and Drug Administration in 1994 (US FDA, 1994).</p>\n', 'Enabled', NULL, '2013-08-29 23:25:01'),
(35, 53, '<p style="text-align: justify;">The NewLeaf&reg; Plus potato (<i>Solanum tuberosum</i>) lines RBMT21-129, RBMT21-350 and RBMT22-082 were produced by bioengineering the potato cultivar Russet Burbank to be resistant to the Colorado potato beetle (CPB) (<i>Leptinotarsa decemlineata</i> Say.) and to resist infection by potato leafroll virus (PLRV). These transgenic lines produce a version of the insecticidal protein, Cry3A, derived from <i>Bacillus thuringiensis</i> subsp. Tenebrionis, and the DNA sequences corresponding to open reading frames 1 (ORF-1) and 2 (ORF-2) from PLRV. Delta-endotoxins, such as the Cry3A protein expressed in Russet Burbank NewLeaf&reg; Plus potatoes, act by selectively binding to specific receptors localized on the brush border midgut epithelium of susceptible insect species. Following binding, cation-specific pores are formed that disrupt midgut ion flow and thereby cause gut paralysis, ultimately leading to bacterial sepsis and death. The Cry3A protein expressed in these potato lines exhibits highly selective insecticidal activity against a narrow range of coleopteran insects such as CPB, elm leaf beetle and yellow mealworm.</p>\n\n<p style="text-align: justify;">The specificity of action is directly attributable to the presence of specific receptors in the target insects. There are no receptors for delta-endotoxins of <i>B. thuringiensis</i> on the surface of mammalian intestinal cells, therefore, livestock animals and humans are not susceptible to these proteins. PLRV is a spherical RNA virus belonging to the luteovirus group and is transmitted primarily by the green peach aphid (<i>Myzus persicae</i>). This virus has a worldwide distribution and commonly infects potato, causing serious disease and economic loss. The introduced viral sequences do not result in the formation of any infectious particles, nor does their expression result in any disease pathology. These transgenic potato cultivars exhibit the trait of resistance to infection and subsequent disease caused by PLRV through an incompletely understood process that has been termed &quot;replicase-mediated resistance&quot;, which may involve silencing of viral gene translation. An antibiotic resistance marker gene (<i>neo</i>) encoding the enzyme neomycin phosphotransferase II (NPTII), which inactivates aminoglycoside antibiotics such as kanamycin and neomycin, was also introduced into the genome of lines RBMT21-129 and RBMT21-350. This gene was derived from a bacterial transposon (Tn5 transposable element from <i>Escherichia coli</i>) and was included as a selectable marker to identify transformed plants during tissue culture regeneration and multiplication. The expression of the <i>neo</i> gene in these plants has no agronomic significance and the safety of the NPTII enzyme as a food additive was evaluated by the United States Food and Drug Administration in 1994 (US FDA, 1994). Line RBMT22-082 contained a copy of the 5-enolypyruvylshikimate-3-phosphate synthase (EPSPS) encoding gene from <i>A. tumefaciens</i> strain CP4 as a selectable marker. This gene was used as an alternative to antibiotic resistance selection in order to identify transformed plants during tissue culture regeneration and multiplication.</p>\n', 'Enabled', NULL, '2013-08-29 23:24:28'),
(36, 20, '<p style="text-align: justify;">Transgenic Russet Burbank potato lines BT6, BT10, BT12, BT16, BT17, BT18, and BT23 (trademark NewLeaf&trade; ), were bioengineered to be resistant to attack by Colorado potato beetle (CPB, <i>Leptinotarsa decemlineata</i> Say), a major insect pest of potatoes. These novel potato lines contain a CPB resistance gene (<i>cry3A</i>) that encodes an insecticidal crystalline Cry3A delta-endotoxin protein, derived from the soil bacterium <i>Bacillus thuringiensis</i> subsp. tenebrionis (B.t.t). Insecticidal activity is caused by the selective binding of Cry3A to specific sites localized on the brush border midgut epithelium of susceptible insect species. Following binding, cation-specific pores are formed that disrupt midgut ion flow and thereby cause gut paralysis, ultimately leading to bacterial sepsis and death. Delta-endotoxins, such as the Cry3A protein expressed in CPB resistant potato lines, exhibit highly selective insecticidal activity against a narrow range of coleopteran insects such as CPB, elm leaf beetle and yellow mealworm. Their specificity of action is directly attributable to the presence of specific receptors in the target insects. There are no receptors for delta-endotoxins of <i>B. thuringiensis</i> on the surface of mammalian intestinal cells, therefore, livestock animals and humans are not susceptible to these proteins.</p>\n\n<p style="text-align: justify;">An antibiotic resistance marker gene (<i>neo</i>) encoding the enzyme neomycin phosphotransferase II (NPTII), which inactivates aminoglycoside antibiotics such as kanamycin and neomycin, was also introduced into the genome of these plants. This gene was derived from a bacterial transposon (Tn5 transposable element from <i>Escherichia coli</i>) and was included as a selectable marker to identify transformed plants during tissue culture regeneration and multiplication. The expression of the <i>neo</i> gene in these plants has no agronomic significance and the safety of the NPTII enzyme as a food additive was evaluated by the United States Food and Drug Administration in 1994 (US FDA, 1994).</p>\n', 'Enabled', NULL, '2013-08-29 22:17:15'),
(37, 10, '<p style="text-align: justify;">The transgenic cultivars of &lsquo;Atlantic&rsquo; (ATBT04-6, ATBT04-27, ATBT04-30, ATBT04-31, ATBT04-36) and &lsquo;Superior&rsquo; (SPBT02-5, SPBT02-7) NewLeaf&reg; potatoes were genetically engineered to be resistant to attack by Colorado potato beetle (CPB). These lines were developed by introducing the <i>cry3A</i> gene, isolated from the common soil bacterium <i>Bacillus thuringiensis</i> subspecies <i>tenebrionis</i> (<i>Btt</i>), into the potato genome by <i>Agrobacterium</i>-mediated transformation.</p>\n\n<p style="text-align: justify;">The Cry3A protein expressed in these transgenic potato cultivars is identical to that found in nature and in commercial <i>Bt</i> spray formulations. Cry proteins, of which Cry3A is only one, act by selectively binding to specific sites localized on the lining of the midgut of susceptible insect species. Following binding, pores are formed that disrupt midgut ion flow causing gut paralysis and eventual death due to bacterial sepsis. Cry3A is insecticidal only when eaten by the larvae of coleopteran insects such as CPB, elm leaf beetle and yellow mealworm, and its specificity of action is directly attributable to the presence of specific binding sites in the target insects. There are no binding sites for delta-endotoxins of <i>B. thuringiensis</i> on the surface of mammalian intestinal cells, therefore, livestock animals and humans are not susceptible to these proteins.</p>\n\n<p style="text-align: justify;">An antibiotic resistance marker gene (<i>neo</i>) encoding the enzyme neomycin phosphotransferase II (NPTII), which inactivates aminoglycoside antibiotics such as kanamycin and neomycin, was also introduced into the genome of these plants. This gene was derived from a bacterial transposon (Tn5 transposable element from <i>Escherichia coli</i>) and was included as a selectable marker to identify transformed plants during tissue culture regeneration and multiplication. The expression of the <i>neo</i> gene in these plants has no agronomic significance and the safety of the NPTII enzyme as a food additive was evaluated by the United States Food and Drug Administration in 1994 (US FDA, 1994).</p>\n', 'Enabled', NULL, '2013-08-29 21:51:43'),
(38, 14, '<p style="text-align: justify;">Cotton lines 531, 757, and 1076 (trademark Bollgard&reg;, Ingard&reg;) were developed through specific genetic modifications to be resistant to major caterpillar pests of cotton. The transgenic cotton lines express a modified gene (<i>cry1Ac</i>) that encodes an insecticidal crystalline Cry1Ac delta-endotoxin protein, derived from the soil bacterium <i>Bacillus thuringiensis</i> subsp. <i>kurstaki</i> strain HD73. Insecticidal activity is caused by the selective binding of Cry1Ac protein to specific sites localized on the brush border midgut epithelium of susceptible insect species. Following binding, cation-specific pores are formed that disrupt midgut ion flow and thereby cause gut paralysis and eventual death due to bacterial sepsis. Delta-endotoxins, such as the Cry1Ac protein expressed in cotton lines 531, 757, and 1076, exhibit highly selective insecticidal activity against a narrow range of lepidopteran insects such as cotton bollworm, tobacco budworm and pink bollworm. The specificity of action is directly attributable to the presence of specific receptors in the target insects. There are no receptors for delta-endotoxins of <i>B. thuringiensis</i> on the surface of non-lepidopteran insect guts or mammalian intestinal cells, therefore, livestock animals and humans are not susceptible to these proteins.</p>\n\n<p style="text-align: justify;">An antibiotic resistance marker gene (<i>neo</i>) encoding the enzyme neomycin phosphotransferase II (NPTII), which inactivates aminoglycoside antibiotics such as kanamycin and neomycin, was also introduced into the genome of these plants. This gene was derived from a bacterial transposon (Tn5 transposable element from <i>Escherichia coli</i>) and was included as a selectable marker to identify transformed plants during tissue culture regeneration and multiplication. The expression of the <i>neo</i> gene in these plants has no agronomic significance and the safety of the NPTII enzyme as a food additive was evaluated by the United States Food and Drug Administration in 1994 (US FDA, 1994).<br />\nAnother selectable marker gene, <i>aad</i> (3&quot;(9)-O-aminoglycoside adenylyltransferase (AAD)), was also inserted into the host genome. This gene, which was not expressed in the plants, was used during the development process to select for bacterial colonies that had been transformed with recombinant plasmid DNA.</p>\n\n<p style="text-align: justify;">Unless otherwise indicated, the information presented here is based on documentation pertaining to cotton line 531.</p>\n', 'Enabled', NULL, '2013-08-29 22:00:56'),
(39, 52, '<p style="text-align: justify;">Transgenic cotton lines 1445 and 1698 were produced using recombinant DNA techniques to allow for the use of glyphosate, the active ingredient in the non-selective herbicide Roundup&reg;, as a weed control option in cotton crops. The novel plants express a naturally glyphosate tolerant version of the enzyme 5-enolpyruvylshikimate-3-phosphate synthase (EPSPS) gene isolated from <i>Agrobacterium tumefaciens</i> strain CP4 (CP4 EPSPS). Glyphosate specifically binds to and inactivates EPSPS, which is involved in the synthesis of aromatic amino acids, tyrosine, phenylalanine and tryptophan (shikimate biochemical pathway). EPSPS is present in all plants, bacteria, and fungi but not in animals, which do not synthesize their own aromatic amino acids.</p>\n\n<p style="text-align: justify;">An antibiotic resistance marker gene (<i>neo</i>) encoding the enzyme neomycin phosphotransferase II (NPTII), which inactivates aminoglycoside antibiotics such as kanamycin and neomycin, was also introduced into the genome of these transgenic lines. This gene was derived from a bacterial transposon (Tn5 transposable element from <i>Escherichia coli</i>) and was included as a selectable marker to identify transformed plants during tissue culture regeneration and multiplication. The expression of the <i>neo</i> gene in these plants has no agronomic significance and the safety of the NPTII enzyme as a food additive was evaluated by the United States Food and Drug Administration in 1994 (US FDA, 1994).</p>\n\n<p style="text-align: justify;">Another selectable marker gene, <i>aad</i> (3&quot;(9)-O-aminoglycoside adenylyltransferase (AAD)), was also inserted into the host genome. This gene, which was not expressed in the plants, was used during the development process to select for bacterial colonies that had been transformed with recombinant plasmid DNA.</p>\n\n<p style="text-align: justify;">Unless otherwise indicated, the information presented herein is based on documentation pertaining to cotton line 1445.</p>\n', 'Enabled', NULL, '2013-08-29 23:15:07'),
(40, 34, '<p style="text-align: justify;">Transgenic cotton lines 31807 and 31808 were developed using recombinant DNA techniques to be both resistant to major caterpillar pests of cotton and to herbicides in the oxynil family, principally bromoxynil (tradename Buctril&reg;). These cotton lines express a modified gene (<i>cry1Ac</i>) that encodes an insecticidal crystalline Cry1Ac delta-endotoxin protein, derived from the soil bacterium <i>Bacillus thuringiensis</i> subsp. <i>kurstaki (B.t.k)</i> strain HD73. Insecticidal activity is caused by the selective binding of Cry1Ac protein to specific sites localized on the brush border midgut epithelium of susceptible insect species. Following binding, cation-specific pores are formed that disrupt midgut ion flow and thereby cause gut paralysis and eventual death due to bacterial sepsis. Delta-endotoxins, such as the Cry1Ac protein expressed in cotton lines 31807 and 31808, exhibit highly selective insecticidal activity against a narrow range of lepidopteran insects such as cotton bollworm, tobacco budworm and pink bollworm. The specificity of action is directly attributable to the presence of specific receptors in the target insects. There are no receptors for delta-endotoxins of <i>B. thuringiensis</i> on the surface of mammalian intestinal cells, therefore, livestock animals and humans are not susceptible to these proteins.</p>\n\n<p style="text-align: justify;">These cotton lines contain a second gene (<i>bxn</i>) that encodes for a bacterial enzyme, nitrilase, from <i>Klebsiella pneumoniae</i>. The nitrilase enzyme hydrolyses the herbicides ioxynil and bromoxynil into non-phytotoxic compounds. Specifically, the nitrilase enzyme breaks down bromoxynil into 3,5 dibromo-4-hydroxybenzoic acid (DBHA), eliminating its herbicidal activity.</p>\n\n<p style="text-align: justify;">An antibiotic resistance marker gene (<i>neo</i>) encoding the enzyme neomycin phosphotransferase II (NPTII), which inactivates aminoglycoside antibiotics such as kanamycin and neomycin, was also introduced into the genome of these transgenic lines. This gene was derived from a bacterial transposon (Tn5 transposable element from <i>Escherichia coli</i>) and was included as a selectable marker to identify transformed plants during tissue culture regeneration and multiplication. The expression of the <i>neo</i> gene in these plants has no agronomic significance and the safety of the NPTII enzyme as a food additive was evaluated by the United States Food and Drug Administration in 1994 (US FDA, 1994).</p>\n', 'Enabled', NULL, '2013-08-29 22:49:44'),
(41, 29, '<p style="text-align: justify;">Transgenic cotton (<i>Gossypium hirsutum</i> L.) line BXN&trade; was developed using recombinant DNA techniques to be tolerant of herbicides in the oxynil family, principally bromoxynil (tradename Buctril&reg;). The oxynil family of herbicides is active against dicotyledonous plants by blocking electron flow during the light reaction of photosynthesis. This transgenic line was produced by inserting a gene that encodes for a bacterial enzyme, nitrilase, from <i>Klebsiella pneumoniae</i>. The nitrilase enzyme hydrolyses the herbicides ioxynil and bromoxynil into non-phytotoxic compounds. Specifically the nitrilase enzyme breaks down bromoxynil into 3,5 dibromo-4-hydroxybenzoic acid (DBHA), eliminating its herbicidal activity.</p>\n\n<p style="text-align: justify;">An antibiotic resistance marker gene (<i>neo</i>) encoding the enzyme neomycin phosphotransferase II (NPTII), which inactivates aminoglycoside antibiotics such as kanamycin and neomycin, was also introduced into the genome of these transgenic lines. This gene was derived from a bacterial transposon (Tn5 transposable element from <i>Escherichia coli</i>) and was included as a selectable marker to identify transformed plants during tissue culture regeneration and multiplication. The expression of the <i>neo</i> gene in these plants has no agronomic significance and the safety of the NPTII enzyme as a food additive was evaluated by the United States Food and Drug Administration in 1994 (US FDA, 1994).</p>\n', 'Enabled', NULL, '2013-08-29 22:38:07'),
(42, 61, '<p style="text-align: justify;">FLAVR SAVR&trade; tomatoes were developed using recombinant DNA techniques to express the trait of delayed softening of tomato fruit. The novel variety was developed by insertion of an additional copy of the polygalacturonase (PG) encoding gene in the &ldquo;antisense&rdquo; orientation, resulting in reduced translation of the endogenous PG messenger RNA (mRNA). The antisense PG gene is essentially a reverse copy of part of the native tomato PG gene that suppresses the expression of endogenous PG enzyme prior to the onset of fruit ripening. The mechanism of decreased PG activity in FLAVR SAVR&trade; tomato is likely linked to the hybridization of antisense and sense mRNA transcripts, resulting in a decreased amount of free positive sense mRNA available for protein translation. Reduced PG expression decreases the breakdown of pectin and leads to fruit with slowed cell wall breakdown, better viscosity characteristics and delayed softening. FLAVR SAVR&trade; tomatoes have improved harvest and processing properties that allow the transgenic tomatoes to remain longer on the vine to develop their natural flavour, maintain firmness for shipping and produce a thicker consistency in processing.</p>\n\n<p style="text-align: justify;">An antibiotic resistance marker gene (<i>neo</i>) encoding the enzyme neomycin phosphotransferase II (NPTII), which inactivates aminoglycoside antibiotics such as kanamycin and neomycin, was also introduced into the genome of this transgenic tomato. This gene was derived from a bacterial transposon (Tn5 transposable element from <i>Escherichia coli</i>) and was included as a selectable marker to identify transformed plants during tissue culture regeneration and multiplication. The expression of the <i>neo</i> gene in these plants has no agronomic significance and the safety of the NPTII enzyme as a food additive was evaluated by the United States Food and Drug Administration in 1994 (US FDA, 1994).</p>\n', 'Enabled', NULL, '2013-08-29 23:34:39'),
(43, 43, '<p style="text-align: justify;">Tomato line 1345-4 was developed using recombinant DNA techniques to express the trait of delayed ripening of tomato fruit. The transgenic line contains a truncated version of the tomato 1-aminocyclopropane-1-carboxyllic acid (ACC) synthase gene, normally found in tomato. This endogenous enzyme is responsible for the conversion of s-adenosylmethionine to ACC, which is the immediate precursor of ethylene, a phytohormone known to play a key role in fruit ripening. The presence of the truncated ACC synthase gene suppresses the normal expression of the native ACC synthase gene, and while not completely understood, the mechanism of &ldquo;downregulation&rdquo; is likely linked to the coordinate suppression of transcription of both the endogenous gene and the introduced truncated ACC synthase gene. The <i>in situ</i> accumulation of ethylene in the transgenic tomatoes was only about 1/50 the level found in the unmodified parental line and the fruit does not fully ripen unless an external source of ethylene is applied. An antibiotic resistance marker gene (<i>neo</i>) encoding the enzyme neomycin phosphotransferase II (NPTII), which inactivates aminoglycoside antibiotics such as kanamycin and neomycin, was also introduced into the genome of this transgenic tomato. This gene was derived from a bacterial transposon (Tn5 transposable element from <i>Escherichia coli</i>) and was included as a selectable marker to identify transformed plants during tissue culture regeneration and multiplication. The expression of the <i>neo</i> gene in these plants has no agronomic significance and the safety of the NPTII enzyme as a food additive was evaluated by the United States Food and Drug Administration in 1994 (US FDA, 1994).</p>\r\n', 'Enabled', NULL, '2013-11-18 17:26:26'),
(130, 99, '', 'Enabled', '2013-08-29 19:05:09', '2013-08-29 19:05:09'),
(45, 59, '<p style="text-align: justify;">The tomato lines B, Da and F were developed using recombinant DNA techniques to display the trait of delayed ripening of tomato fruit. These transgenic tomatoes lines contain a partial polygalacturonase (PG) gene that encodes for the PG protein, a pectin degrading enzyme derived from tomato. The lines differ slightly in that Da and F contain the partial PG gene in the sense orientation while line B contains a partial antisense PG gene, essentially a reverse copy. The presence of the partial PG gene, in either sense or antisense orientation, suppresses the expression of endogenous PG enzyme at the onset of fruit ripening.</p>\n\n<p style="text-align: justify;">In the case of line B, the mechanism of action is likely linked to the hybridization of antisense and sense mRNA transcripts, resulting in a decreased amount of free positive sense mRNA available for protein translation. For lines Da and F, which contain the truncated PG gene in the sense orientation, reduced PG expression may be due to coordinate suppression of transcription of both the endogenous gene and the introduced truncated gene.</p>\n\n<p style="text-align: justify;">In any event, reduced PG expression decreases the breakdown of pectin and leads to fruit with slowed cell wall breakdown, better viscosity characteristics and delayed softening. Tomato lines B, Da and F have improved harvest and processing properties that allow the transgenic tomatoes to remain longer on the vine to develop their natural flavour, maintain their firmness for shipping and produce a thicker consistency in processing.</p>\n\n<p style="text-align: justify;">An antibiotic resistance marker gene (<i>neo</i>) encoding the enzyme neomycin phosphotransferase II (NPTII), which inactivates aminoglycoside antibiotics such as kanamycin and neomycin, was also introduced into the genome of these transgenic tomatoes. This gene was derived from a bacterial transposon (Tn5 transposable element from <i>Escherichia coli</i>) and was included as a selectable marker to identify transformed plants during tissue culture regeneration and multiplication. The expression of the <i>neo</i> gene in these plants has no agronomic significance and the safety of the NPTII enzyme as a food additive was evaluated by the United States Food and Drug Administration in 1994 (US FDA, 1994).</p>\n', 'Enabled', NULL, '2013-08-29 23:31:33'),
(46, 30, '<p style="text-align: justify;">The modified yellow crookneck squash (<i>Curcurbita pepo</i> L.), line ZW-20 was developed using recombinant DNA techniques to resist infection by two plant viruses that frequently infect commercial squash varieties, namely zucchini yellow mosaic potyvirus (ZYMV) and watermelon mosaic potyvirus (WMV2). This novel variety was developed by insertion of the coat protein (CP) encoding sequences from ZYMV and WMV2 into the plant genome. The expression of these introduced gene sequences does not result in the formation of infectious virus particles, nor does it result in any disease pathology, but rather enables ZW-20 squash plants to resist infection by these two viruses.</p>\n\n<p style="text-align: justify;">ZYMV and WMV2 are members of the potyvirus group, which is one of the largest groups of plant viruses. ZYMV produces a severe disease consisting of mosaic (patchwork of yellow chlorotic tissues and green uninfected tissues), yellowing, shoestringing, stunting, and fruit and seed deformations on cucurbits, such as zucchini squash, muskmelon, cucumber, and watermelon. WMV2 causes mosaic and mottle diseases of cantaloupe, pumpkin, squash, and watermelon. On a given cucurbit host, ZYMV usually causes more severe symptoms than WMV2.</p>\n\n<p style="text-align: justify;">The squash line ZW-20 exhibits resistance to infection and subsequent disease caused by ZYMV and WMV2 through a process that is related to viral cross-protection. Although the exact mechanism by which the viral protection occurs is unknown, most evidence suggests that expression of viral CP by a plant interferes with one of the first steps in viral replication, uncoating (removal of CP) from the incoming virus (Register &amp; Nelson, 1992). For example, when ZYMV or WMV2 infect a ZW-20 plant or another cross-protected squash plant, replication is blocked. Other modes of action of cross protection have also been suggested (Matthews, 1991).</p>\n', 'Enabled', NULL, '2013-08-29 22:39:56'),
(47, 38, '<p style="text-align: justify;">The yellow crookneck squash (<i>Curcurbita pepo</i> L.), line CZW-3 was developed using recombinant DNA techniques to be resistant to infection by three plant viruses that frequently infect commercial squash varieties, namely cucumber mosaic cucumovirus (CMV), zucchini yellow mosaic potyvirus (ZYMV), and watermelon mosaic potyvirus (WMV2). The novel variety was developed by insertion of the coat protein (CP) encoding sequences from these three single-stranded RNA viruses. The expression of viral CPs in this transgenic squash variety does not result in the formation of any infectious particles, or in the manifestation of any disease pathology, but rather enables the plant to resist infection by CMV, ZYMV and WMV2. These viruses are major pathogens of all cucurbit crops (squash, cucumbers, and their relatives) and are present in most regions where these crops are grown.</p>\n\n<p style="text-align: justify;">ZYMV and WMV2 are members of the potyvirus group, one of the largest groups of plant viruses, while CMV is the type member of the cucumovirus group. ZYMV produces a severe disease consisting of mosaic (patchwork of yellow chlorotic tissues and green uninfected tissues), yellowing, shoestringing, stunting, and fruit and seed deformations on zucchini squash, muskmelon, cucumber, and watermelon. WMV2 causes mosaic and mottle diseases of cantaloupe, pumpkin, squash, and watermelon. On a given cucurbit host, ZYMV usually causes more severe symptoms than WMV2.<br />\nCZW-3 squash exhibits &ldquo;pathogen derived resistance&rdquo; to infection and subsequent disease caused by CMV, ZYMV and WMV2 through a process that is related to viral cross-protection. Although the exact mechanism by which the viral protection occurs is unknown, most evidence suggests that expression of viral CP by a plant interferes with one of the first steps in viral replication, uncoating (removal of CP) from the incoming virus (Register &amp; Nelson, 1992). Other modes of action of cross protection have also been suggested (Matthews, 1991). Transgenic CZW-3 squash displayed a high level of resistance to systemic infection with CMV, ZYMV, and WMV 2, although 64% exhibited localized chlorotic dots that were mainly confined to older leaves. CZW-3 plants had a 50-fold increase in marketable yield compared to non-transgenic control plants.</p>\n\n<p style="text-align: justify;">An antibiotic resistance marker gene (<i>neo</i>) encoding the enzyme neomycin phosphotransferase II (NPTII), which inactivates aminoglycoside antibiotics such as kanamycin and neomycin, was also introduced into the genome of this variety. This gene was derived from a bacterial transposon (Tn5 transposable element from <i>Escherichia coli</i>) and was included as a selectable marker to identify transformed plants during tissue culture regeneration and multiplication. The expression of the <i>neo</i> gene in these plants has no agronomic significance and the safety of the NPTII enzyme as a food additive was evaluated by the United States Food and Drug Administration in 1994 (US FDA, 1994).</p>\n', 'Enabled', NULL, '2013-08-29 22:52:41'),
(48, 56, '<p style="text-align: justify;">Insect-resistant tomato line 5345 was developed using recombinant DNA techniques to express the insecticidal protein, Cry1Ac, encoded by the <i>cry1Ac</i> gene from the soil bacterium <i>Bacillus thuringiensis</i> subsp. kurstaki (B.t.k) strain HD73. Insecticidal activity is caused by the selective binding of Cry1Ac protein to specific sites localized on the brush border midgut epithelium of susceptible lepidopteran species. Following binding, cation-specific pores are formed that disrupt midgut ion flow thereby causing gut paralysis and eventual death from bacterial sepsis. Delta-endotoxins, such as the Cry1Ac protein expressed in tomato line 5345, exhibit highly selective insecticidal activity against a narrow range of lepidopteran pests. The specificity of action is directly attributable to the presence of specific receptors in the target insects. There are no receptors for delta-endotoxins of <i>B. thuringiensis</i> on the surface of mammalian intestinal cells, therefore, livestock animals and humans are not susceptible to these proteins.</p>\n\n<p style="text-align: justify;">An antibiotic resistance marker gene (<i>neo</i>) encoding the enzyme neomycin phosphotransferase II (NPTII), which inactivates aminoglycoside antibiotics such as kanamycin and neomycin, was also introduced into the genome of this transgenic tomato. This gene was derived from a bacterial transposon (Tn5 transposable element from <i>Escherichia coli</i>) and was included as a selectable marker to identify transformed plants during tissue culture regeneration and multiplication. The expression of the <i>neo</i> gene in these plants has no agronomic significance and the safety of the NPTII enzyme as a food additive was evaluated by the United States Food and Drug Administration in 1994 (US FDA, 1994).</p>\n', 'Enabled', NULL, '2013-08-29 23:29:40');
INSERT INTO `gmcropdatabase_events_introductions` (`id`, `eventId`, `description`, `status`, `created`, `updated`) VALUES
(49, 73, '<p style="text-align: justify;">This soybean (<i>Glycine max</i>) line was developed by traditional plant breeding methods using the variety Maple Glen and PI361088B, a cultivar from Romania originating from Mica Ungana, as the source of the low linolenic acid trait. OT96-15 is a Maple Glen back cross derived line originating from the cross Maple Arrow/PI361088B(OAC2-K1)//4*Maple Glen. OAC2-K1 is an F2 line developed by the University of Guelph, selected for the <i>fan1</i>(PI361088B) gene that results in a reduced level of seed linolenic acid. The final backcross to Maple Glen was made in 1990 in Ottawa.</p>\n\n<p style="text-align: justify;">The oil derived from OT96-15 has about one-half the content of linolenic acid compared to conventional soybean varieties, but has higher linolenic acid levels than either corn or olive oils.</p>\n', 'Enabled', NULL, '2013-08-29 23:43:32'),
(50, 55, '<p style="text-align: justify;">Rice lines LLRICE06 and LLRICE62 were developed using recombinant DNA techniques to allow the use of glufosinate ammonium, the active ingredient in phosphinothricin herbicides (Basta&reg;, Ignite&reg;, Rely&reg;, Liberty&reg;, Finale&reg;, RadicaleX&reg;), as a weed control option in rice crops. Currently, rice growers in the United States control weeds through a combination of herbicides, crop rotation, and cultural practices such as flooding and tillage. The <i>bar</i> gene, which encodes the enzyme phosphinothricin N-acetyltransferase (PAT), was isolated from the common aerobic soil actinomycete, <i>Streptomyces hygroscopicus</i> strain HP632, and introduced by direct DNA transfer into the rice genome.</p>\n\n<p style="text-align: justify;">In addition to providing the trait of glufosinate herbicide tolerance, the PAT encoding gene was used as a selectable marker to identify transformed plants during regeneration in tissue culture. Glufosinate is a short name for the ammonium salt, glufosinate-ammonium. It is a broad-spectrum contact herbicide and is used to control a wide range of weeds after the crop emerges or for total vegetation control on land not used for cultivation. Glufosinate is a natural compound isolated from two species of Streptomyces fungi. It inhibits the activity of an enzyme, glutamine synthetase, which is necessary for the production of glutamine and for ammonia detoxification. The application of glufosinate leads to reduced glutamine and increased ammonia levels in the plant tissues. This causes photosynthesis to stop and the plant dies within a few days. Glufosinate also inhibits the same enzyme in animals. It is highly biodegradable, has no residual activity, and very low toxicity for humans and wild fauna. The PAT enzyme detoxifies phosphinothricin by acetylation into an inactive compound.</p>\n', 'Enabled', NULL, '2013-08-29 23:27:25'),
(51, 31, '<p style="text-align: justify;">Papaya lines 55-1 and 63-1 were developed using recombinant DNA techniques to resist infection by papaya ringspot virus (PRSV), a major limiting factor in papaya production. These papaya lines were developed by inserting virus-derived sequences that encode the PRSV coat protein (CP). The introduced viral sequences do not result in the formation of any infectious particles, nor does their expression result in any disease pathology. PRSV belongs to the potyvirus group and is an aphid-transmissible RNA virus that commonly infects papaya, causing serious disease and economic loss.</p>\n\n<p style="text-align: justify;">These transgenic papayas exhibit &ldquo;pathogen-derived resistance&rdquo; to infection and subsequent disease caused by PRSV through a process that is related to viral cross-protection. Although the exact mechanism by which the viral protection occurs is unknown, most evidence suggests that expression of viral CP by a plant interferes with one of the first steps in viral replication, uncoating (removal of CP) from the incoming virus (Register &amp; Nelson, 1992). Other modes of action of cross protection have also been suggested (Matthews, 1991).</p>\n\n<p style="text-align: justify;">An antibiotic resistance marker gene (<i>neo</i>) encoding the enzyme neomycin phosphotransferase II (NPTII), which inactivates aminoglycoside antibiotics such as kanamycin and neomycin, was also introduced into the genome of these varieties. This gene was derived from a bacterial transposon (Tn5 transposable element from <i>Escherichia coli</i>) and was included as a selectable marker to identify transformed plants during tissue culture regeneration and multiplication. The expression of the neo gene in these plants has no agronomic significance and the safety of the NPTII enzyme as a food additive was evaluated by the United States Food and Drug Administration in 1994 (US FDA, 1994).</p>\n\n<p style="text-align: justify;">Line 55-1 expresses a reporter gene (<i>uidA</i>) encoding the enzyme beta-D-glucuronidase (GUS) from <i>E. coli</i>. The expression of GUS activity was used during the development phase to identify transgenic plants containing the introduced gene sequences.</p>\n', 'Enabled', NULL, '2013-08-29 22:42:24'),
(52, 62, '<p style="text-align: justify;">Harvested carnation (<i>Dianthus caryophyllus</i> L.) flowers have a defined &#39;vase life&#39;, or time for which the flowers will stay fresh prior to beginning to shrink, dry out and die. This senescence process is triggered by production of a natural plant hormone, ethylene, by the flower. Flower death can also be triggered by exposure of flowers to external sources of ethylene, such as fruit and exhaust fumes. Typically, flower growers have controlled wilting by treating flowers with chemicals (<i>e.g.</i> silver thiosulfate) that either inhibit ethylene synthesis in the flower, or prevent the flower from responding to ethylene.</p>\n\n<p style="text-align: justify;">The enzyme 1-aminocyclopropane-1-carboxyllic acid (ACC) synthase, normally found in carnations, is responsible for the conversion of s-adenosylmethionine to ACC, which is the immediate precursor of ethylene. The transgenic carnation line 66 was developed using recombinant DNA techniques to display suppressed ACC synthase activity, and thus reduced ethylene synthesis and therefore longer vase life, by inserting an additional truncated copy of the ACC synthase encoding gene. The presence of the truncated ACC synthase gene suppresses the normal expression of the native ACC synthase gene, and while not completely understood, the mechanism of &ldquo;downregulation&rdquo; is likely linked to the coordinate suppression of transcription of both the endogenous gene and the introduced truncated ACC synthase gene.</p>\n\n<p style="text-align: justify;">An additional gene encoding a variant form of the enzyme acetolactate synthase (ALS) was also introduced into this transgenic carnation line in order to confer the trait of tolerance to sulfonylurea type herbicides (<i>e.g.</i>, chlorsulfuron, commonly known as Glean&trade;), which are potent inhibitors of ALS. Acetolactate synthase (also known as acetohydroxy acid synthase; AHAS) is involved in the conversion of threonine to alpha-aceto-alpha-hydroxybutyrate and pyruvate to alpha-acetolactate, which are key precursors in the biosynthesis of the essential branched chain amino acids isoleucine and valine, respectively. Alpha-acetolactate is also a precursor in the synthesis of leucine. The variant form of ALS introduced into this carnation line was isolated from a chlorsulfuron tolerant tobacco (<i>Nicotiana tabacum</i>). This trait was introduced as a means of selecting for transformed plants during tissue culture regeneration as sulfonylurea herbicides are not, and will not be, used in the carnation industry.</p>\n', 'Enabled', NULL, '2013-08-29 23:36:23'),
(53, 45, '<p style="text-align: justify;">Sugar beet line T120-7 was developed using recombinant DNA techniques to allow for the use of glufosinate ammonium, the active ingredient in phosphinothricin herbicides (Basta&reg;, Ignite&reg;, Rely&reg;, Liberty&reg;, Harvest&reg;, and Finale&reg;) as a weed control option. This line was genetically engineered to express a new enzyme, phosphinothricin-N-acetyltransferase (PAT), derived from the common aerobic soil actinomycete, <i>Streptomyces viridochromogenes</i>.</p>\n\n<p style="text-align: justify;">Glufosinate is a short name for the ammonium salt, glufosinate-ammonium. It is a broad-spectrum contact herbicide and is used to control a wide range of weeds after the crop emerges or for total vegetation control on land not used for cultivation. Glufosinate is a natural compound isolated from two species of Streptomyces fungi. It inhibits the activity of an enzyme, glutamine synthetase, which is necessary for the production of glutamine and for ammonia detoxification. The application of glufosinate leads to reduced glutamine and increased ammonia levels in the plant tissues. This causes photosynthesis to stop and the plant dies within a few days. Glufosinate also inhibits the same enzyme in animals. It is highly biodegradable, has no residual activity, and very low toxicity for humans and wild fauna.</p>\n\n<p style="text-align: justify;">The PAT enzyme detoxifies phosphinothricin via acetylation into an inactive compound. An antibiotic resistance marker gene (<i>neo</i>) encoding the enzyme neomycin phosphotransferase II (NPTII), which inactivates aminoglycoside antibiotics such as kanamycin and neomycin, was also introduced into the genome of line T120-7. This gene was derived from a bacterial transposon (Tn5 transposable element from <i>Escherichia coli</i>) and was included as a selectable marker to identify transformed plants during tissue culture regeneration and multiplication. The expression of the <i>neo</i> gene in these plants has no agronomic significance and the safety of the NPTII enzyme as a food additive was evaluated by the United States Food and Drug Administration in 1994 (US FDA, 1994).</p>\n', 'Enabled', NULL, '2013-08-29 23:02:40'),
(54, 64, '<p style="text-align: justify;">Transgenic lines 4, 11, 15, and 16 were developed using recombinant DNA techniques to produce flowers with a unique violet/mauve colour by introducing two genes from petunia (<i>Petunia hybrida</i>) that function together in the biosynthesis of the anthocyanin pigment delphinidin. The transgenic lines were derived from the parent cultivar &lsquo;White Unesco&rsquo;, which is a white coloured carnation that was selected for a mutation in the dihydroflavonol reductase (DFR) encoding gene that did not allow for expression of a functional enzyme, and thus did not produce the anthocyanin type pigments that give rise to blue and red coloured flowers. The two genes introduced into the transgenic carnation lines included a functional dihydroflavonol reductase encoding gene and a gene encoding the enzyme flavonoid 3&rsquo;, 5&rsquo;-hydroxylase (F3&rsquo;, 5&rsquo;H), a member of the NADPH-Cytochrome P450 reductase family. Expression of the F3&rsquo;, 5&rsquo;H encoding gene allows for the production of blue coloured delphinidin anthocyanin pigments, which are not normally found in carnations.</p>\n\n<p style="text-align: justify;">An additional gene encoding a variant form of the enzyme acetolactate synthase (ALS) was also introduced into this transgenic carnation line in order to confer the trait of tolerance to sulfonylurea type herbicides (<i>e.g.</i>, chlorsulfuron, commonly known as Glean&trade;), which are potent inhibitors of ALS. Acetolactate synthase (also known as acetohydroxy acid synthase; AHAS) is involved in the conversion of threonine to alpha-aceto-alpha-hydroxybutyrate and pyruvate to alpha-acetolactate, which are key precursors in the biosynthesis of the essential branched chain amino acids isoleucine and valine, respectively. Alpha-acetolactate is also a precursor in the synthesis of leucine. The variant form of ALS introduced into this carnation line was isolated from a chlorsulfuron tolerant tobacco (<i>Nicotiana tabacum</i>). This trait was introduced as a means of selecting for transformed plants during tissue culture regeneration as sulfonylurea herbicides are not, and will not be, used in the carnation industry.</p>\n', 'Enabled', NULL, '2013-08-29 23:38:11'),
(55, 28, '<p style="text-align: justify;">Maize line TC1507 was genetically modified to contain two novel genes, <i>cry1Fa2</i> and <i>pat</i>, for insect resistance and herbicide tolerance respectively. Both genes were introduced into the parental maize hybrid line Hi-II by particle acceleration (biolistic) transformation.</p>\n\n<p style="text-align: justify;">The <i>cry1Fa2</i> gene, isolated from the common soil bacterium <i>Bacillus thuringiensis</i> (<i>Bt</i>) var. <i>aizawai</i>, produces the insect control protein Cry1F, a delta-endotoxin. Cry proteins, of which Cry1F is only one, act by selectively binding to specific sites localized on the lining of the midgut of susceptible insect species. Following binding, pores are formed that disrupt midgut ion flow, causing gut paralysis and eventual death due to bacterial sepsis. Cry1F is lethal only when eaten by the larvae of lepidopteran insects (moths and butterflies), and its specificity of action is directly attributable to the presence of specific binding sites in the target insects. There are no binding sites for the delta-endotoxins of <i>B. thuringiensis</i> on the surface of mammalian intestinal cells, therefore, livestock animals and humans are not susceptible to these proteins.</p>\n\n<p style="text-align: justify;">The Cry1F protein expressed in TC1507 provides protection against European corn borer (ECB), southwestern corn borer (SWCB), fall armyworm (FAW), black cutworm (BCW), and some control of corn earworm (CEW).</p>\n\n<p style="text-align: justify;">In addition to the <i>cry1Fa2</i> gene, TC1507 was developed to allow for the use of glufosinate ammonium, the active ingredient in phosphinothricin herbicides (Basta&reg;, Rely&reg;, Liberty&reg;, and Finale&reg;), as a weed control option, and as a breeding tool for selecting plants that have the insect-tolerant <i>cry1F</i> gene. Glufosinate chemically resembles the amino acid glutamate and acts to inhibit an enzyme, called glutamine synthetase, which is involved in the synthesis of glutamine. Essentially, glufosinate acts enough like glutamate, the molecule used by glutamine synthetase to make glutamine, that it blocks the enzyme&#39;s usual activity. Glutamine synthetase is also involved in ammonia detoxification. The action of glufosinate results in reduced glutamine levels and a corresponding increase in concentrations of ammonia in plant tissues, leading to cell membrane disruption and cessation of photosynthesis resulting in plant withering and death.</p>\n\n<p style="text-align: justify;">Glufosinate tolerance in TC1507 maize is the result of introducing a gene encoding the enzyme phosphinothricin-N-acetyltransferase (PAT) isolated from the common aerobic soil actinomycete, <i>Streptomyces viridochromogenes</i>, the same organism from which glufosinate was originally isolated. The PAT enzyme catalyzes the acetylation of phosphinothricin, detoxifying it into an inactive compound.</p>\n', 'Enabled', NULL, '2013-08-29 22:36:21'),
(56, 63, '<p style="text-align: justify;">Transgenic lines 959A, 988A, 1226A, 1351A, 1363A, and 1400A were developed using recombinant DNA techniques to produce flowers with a unique deep purple colour by introducing two genes that function together in the biosynthesis of the anthocyanin pigment delphinidin. The transgenic lines were derived from the parent cultivar &lsquo;White Unesco&rsquo;, which is a white coloured carnation that was selected for a mutation in the dihydroflavonol reductase (DFR) encoding gene that did not allow for expression of a functional enzyme, and thus did not produce the anthocyanin type pigments that give rise to blue and red coloured flowers. The two genes introduced into the transgenic carnation lines included a functional dihydroflavonol reductase encoding gene isolated from petunia (<i>Petunia hybrida</i>) and a gene encoding the enzyme flavonoid 3&rsquo;, 5&rsquo;-hydroxylase (F3&rsquo;, 5&rsquo;H), a member of the NADPH-Cytochrome P450 reductase family, isolated from Viola. Expression of the F3&rsquo;, 5&rsquo;H encoding gene (<i>bp40</i>) allows for the production of blue coloured delphinidin anthocyanin pigments, which are not normally found in carnations.</p>\n\n<p style="text-align: justify;">An additional gene encoding a variant form of the enzyme acetolactate synthase (ALS) was also introduced into this transgenic carnation line in order to confer the trait of tolerance to sulfonylurea type herbicides (<i>e.g.</i>, chlorsulfuron, commonly known as Glean&trade;), which are potent inhibitors of ALS. Acetolactate synthase (also known as acetohydroxy acid synthase; AHAS) is involved in the conversion of threonine to alpha-aceto-alpha-hydroxybutyrate and pyruvate to alpha-acetolactate, which are key precursors in the biosynthesis of the essential branched chain amino acids isoleucine and valine, respectively. Alpha-acetolactate is also a precursor in the synthesis of leucine. The variant form of ALS introduced into this carnation line was isolated from a chlorsulfuron tolerant tobacco (<i>Nicotiana tabacum</i>). This trait was introduced as a means of selecting for transformed plants during tissue culture regeneration as sulfonylurea herbicides are not, and will not be, used in the carnation industry.</p>\n', 'Enabled', NULL, '2013-08-29 23:37:18'),
(57, 75, '<p style="text-align: justify;">Maize line MON 863 was produced using recombinant-DNA techniques to express the <i>cry3Bb1</i> gene encoding a Coleopteran-specific insecticidal protein from <i>Bacillus thuringiensis</i> (subsp. <i>kumamotoensis</i>) in order to control infestation with corn root worm (CRW; <i>Diabrotica</i> <i>sp</i>.). This gene was introduced into the publicly available inbred line, A634, by particle acceleration (biolistic) transformation.</p>\n\n<p style="text-align: justify;">The <i>cry3Bb1</i> gene encodes the insect control protein Cry3Bb1, a delta-endotoxin. Cry proteins, of which Cry3Bb1 is only one, act by selectively binding to specific sites localized on the lining of the midgut of susceptible insect species. Following binding, pores are formed that disrupt midgut ion flow, causing gut paralysis and eventual death due to bacterial sepsis. Cry3Bb1 is lethal only when eaten by Coleopteran species, including corn root worm, and its specificity of action is directly attributable to the presence of specific binding sites in the target insects. There are no binding sites for the delta-endotoxins of <i>B. thuringiensis</i> on the surface of mammalian intestinal cells, therefore, livestock animals and humans are not susceptible to these proteins.</p>\n\n<p style="text-align: justify;">An antibiotic resistance marker gene (<i>neo</i>; synonym <i>nptII</i>) encoding the enzyme neomycin phosphotransferase II (NPTII), which inactivates aminoglycoside antibiotics such as kanamycin and neomycin, was also introduced into the genome of this transgenic maize. This gene was derived from a bacterial transposon (Tn5 transposable element from <i>Escherichia coli</i>) and was included as a selectable marker to identify transformed plants during tissue culture regeneration and multiplication. The expression of the <i>nptII</i> gene in these plants has no agronomic significance and the safety of the NPTII enzyme as a food additive was evaluated by the United States Food and Drug Administration in 1994 (US FDA, 1994).</p>\n', 'Enabled', NULL, '2013-08-29 23:44:56'),
(58, 76, '<p style="text-align: justify;">Rice lines CL121, CL141, and CFX51, were developed through a combination of chemically-induced accelerated mutagenesis and traditional cross-breeding to exhibit tolerance to imidazolinone containing herbicides, such as imazethapyr. Imidazolinone herbicides are active against the acetolactate synthase (ALS) enzyme in plants, which catalyzes the first reaction in the biosynthesis of branched-chain amino acids. Imidazolinone inhibits the production of these essential amino acids (valine, leucine and isoleucine), resulting in a decrease in protein synthesis and the eventual death of the plant.</p>\n', 'Enabled', NULL, '2013-08-29 23:45:27'),
(59, 77, '<p style="text-align: justify;">Event MON 15985 (tradename Bollgard II&reg;) was derived from the hybrid cotton variety DP50B, which was a cross between DP50 and transgenic Bollgard&reg; cotton line 531, by biolistic transformation with plasmid DNA containing the <i>cry2Ab2</i> gene originally isolated from <i>Bacillus thuringiensis</i> subsp. <i>kurstaki</i>. As a result, event 15985 expresses both the Cry1Ac and Cry2Ab2 insecticidal proteins and exhibits resistance to a range of lepidopteran pests such as the cotton bollworm, tobacco budworm, pink bollworm, and armyworm.</p>\n\n<p style="text-align: justify;">As with other <i>B. thuringiensis</i>-derived delta-endotoxins, the Cry1Ac and Cry2Ab2 proteins exert their insecticidal activity by binding to specific receptors located on the brush border midgut epithelium of susceptible insect species. Following binding, cation-specific pores are formed that disrupt midgut ionic equilibrium leading to gut paralysis and eventual death due to bacterial sepsis. Cry1Ac and Cry2Ab2 are highly selective and are only active against lepidopteran insects. These proteins do, however, interact with different receptor sites in the target insects and it is expected that &ldquo;stacking&rdquo; these traits will result in increased protection against insect attack and a delay in the development of resistant insect populations.</p>\n\n<p style="text-align: justify;">In addition to the <i>cry</i> genes conferring insect resistance, MON 15985 also contains the <i>nptII</i> and <i>aad</i> selectable marker genes (derived from the parental cotton line containing event 531) and the beta-D-glucuronidase (GUS) encoding <i>uidA</i> gene from <i>Escherichia coli</i>. This latter gene was introduced as a visually scorable marker gene to identify transformed plantlets in tissue culture. The GUS enzyme can be used to catalyze a colorimetric reaction resulting in the production of a blue colour in transformed cells.</p>\n\n<p style="text-align: justify;">This product description will focus on those aspects of the risk assessment pertaining to the <i>cry2Ab2</i> and <i>uidA</i> gene products. For additional information on the safety assessment of <i>cry1Ac</i> and <i>nptII</i> gene products, the reader is directed to the product description for line MON 531.</p>\n', 'Enabled', NULL, '2013-08-30 12:32:10'),
(60, 86, '<p style="text-align: justify;">X81359 (Clearfield&trade;) sunflower hybrid was developed to allow the use of imidazolinone herbicides as a post-emergence weed control option in sunflower production. The tolerance to imidazolinone herbicides in X81359 is due to a naturally occurring mutation in the AHAS gene discovered in a wild population of <i>Helianthus annus</i>. This trait was introduced into X81359 using conventional plant breeding techniques.</p>\n\n<p style="text-align: justify;">AHAS catalyses the first step in the biosynthesis of the branched-chain amino acids isoleucine, leucine, and valine, and is active in the glycolytic pathway of plant metabolism. When conventional sunflower plants are treated with an imidazolinone, the herbicide binds to a specific site on the AHAS enzyme, thereby inhibiting its activity. The result of this enzyme inhibition is a decrease in the synthesis of these amino acids, and an accumulation of toxic levels of alpha-ketoglutarate, all of which results in the eventual death of the plant.</p>\n', 'Enabled', NULL, '2013-08-29 23:56:32'),
(61, 83, '<p style="text-align: justify;">Tobacco line Vector 21-41 was developed to reduce the presence of nicotine in the leaves of commercial tobacco (<i>Nicotiania tabacum</i>). Vector 21-41 delivers nicotine levels around 20 times less than conventional tobacco. Nicotine is commonly regarded as the addictive substance in tobacco and is a precursor of Tobacco Specific Nitrosamines which are mutagenic and carcinogenic substances normally found in tobacco. It is thought that delivering nicotine at levels well below those determined to be addictive can reduce dependency on tobacco products.</p>\n\n<p style="text-align: justify;">The synthesis of nicotine is isolated in the roots of tobacco and subsequently transported via the phloem to the leaves. Nicotine is the product of two enzymatic pathways: the methylpyrroline pathway, which produces the nicotine precursor N-methylpyrrolinium cation; and the pyridine nucleotide cycle, which produces the precursor nicotine acid.</p>\n\n<p style="text-align: justify;">In the methylpyrroline pathway, L-ornithine is converted via ornithine decarboxylase to putrescine which in turn is acted on by putrescine N-methyltransferase (PMTase) to produce 4-methyle putrescine and subsequently N-methylpyrrolinium cation. PMTase is the limiting enzyme in this pathway.</p>\n\n<p style="text-align: justify;">The pyridine nucleotide cycle begins with 3-phosphoglyceraldehyde which condenses with aspartic acid, to form quinolinic acid. Quinolinic acid is subject to the action of quinolinic acid phosphoribosyltransferase (QPTase) and through a series of steps becomes nicotinic acid. In this pathway, QPTase is the limiting enzyme.</p>\n\n<p style="text-align: justify;">In Vector 21-41 the pyridine nucleotide cycle was down-regulated through the insertion of the antisense configuration of the gene coding for QPTase (NtQTP1). The reduction in expression of QPTase resulted in a dramatic decrease in the production of nicotinic acid and thus nicotine.</p>\n', 'Enabled', NULL, '2013-08-29 23:54:04'),
(62, 87, '<p style="text-align: justify;">Imidazolinone herbicides are active against the enzyme acetohydroxyacid synthase (AHAS), also known as acetolactate synthase (ALS) or acetolactate pyruvate- lyase.</p>\n\n<p style="text-align: justify;">This enzyme catalyzes the first step in the biosynthesis of the essential branched chain amino acids isoleucine, leucine and valine. Herbicide induced AHAS inhibition results in a lethal decrease in protein synthesis. Unmodified wheat is not tolerant to imidazolinones, while soybeans, peas, white beans and kidney beans are naturally tolerant to them.<br />\nDepending on the species, plants contain single or multiple copies of the AHAS genes. The genome of <i>T. aestivum</i> is believed to contain an AHAS multigene family.</p>\n\n<p style="text-align: justify;">Modifications of AHAS genes in various plant species can result in herbicide tolerant phenotypes and typically consist of one amino acid substitution, sufficient to alter the binding site for imidazolinones such that the herbicide no longer inhibits the AHAS enzyme. Several modified AHAS plants have been isolated.</p>\n\n<p style="text-align: justify;">AP602CL was selected from a population of <i> T. aestivum </i> derived by chemical-induced mutagenesis of seed of the wheat variety Gunner. One mutant, tolerant to imidazoline was selected and designated AP602CL. Tolerance to imadazoline was demonstrated by comparison of the activity of the AHAS enzyme extracted from AP602CL to that of wild type plants.</p>\n\n<p style="text-align: justify;">The novel tolerance to imadazoline is under control of the native AHAS promoter and is believed to be constitutively expressed. Sequence information for the modified AHAS gene in AP602CL was submitted.</p>\n\n<p style="text-align: justify;">The levels of valine, leucine and isoleucine produced in wheat are regulated by feedback inhibition of AHAS. Modified AHAS shows similar feedback inhibition to that of unmodified AHAS. AHAS is not known to be an allergen and modified AHAS also does not exhibit characteristics associated with allergens. The protein components of AHAS are not altered in comparison with unmodified Gunner wheat.</p>\n', 'Enabled', NULL, '2013-08-29 23:57:44'),
(63, 82, '<p style="text-align: justify;">LLCotton25 was developed to allow the use of glufosinate ammonium as a weed control option in cotton production.&nbsp; This genetically engineered cotton line expresses a protein, phosphinothricin-acetyl-transferase (PAT) that confers tolerance to the active ingredient L-phosphinothricin in glufosinate ammonium. The expression of PAT is due to the introduction of the <i>bar</i> gene. This gene was isolated from <i>Streptomyces hygroscopius</i>, a gram-positive soil bacterium.<br />\nGlufosinate ammonium is a post-emergence, broad-spectrum contact herbicide and plant dessicant.&nbsp; L-Phosphinothricin was first isolated as bialaphos, an antibiotic synthesized during the fermentation of <i>Streptomyces hygroscopicus</i> or <i>S.viridochromogenes.&nbsp; </i>&nbsp;In herbicidal formulations it is a component of glufosinate ammonium, which is chemically synthesized.&nbsp; Glufosinate ammonium is a racemic mixture of L-phosphinothricin, the herbicidal active moiety, and its D-enantiomer.&nbsp; L-Phosphinothricin is structurally similar to glutamate, the substrate of glutamine synthetase (GS), an enzyme that catalyzes the synthesis of glutamine from glutamate and ammonia.&nbsp; L-phosphinothricin inhibits the activity of GS irreversibly by binding to its active sites.&nbsp; The inhibition of GS caused by the application of glufosinate ammonium to plants results in the accumulation of ammonia, the reduction in the levels of glutamine, and the inhibition of photosynthesis, all of which results in the death of the plant.&nbsp; Plants transformed with the <i>bar</i> gene express the enzyme phosphinothricin-acetyl-transferase (PAT) which acetylates L-phosphinothricin into a non- phytotoxic metabolite (N-acetyl-L-glufosinate).</p>\n\n<p style="text-align: justify;">LLCotton25 was developed by introducing the bialaphos resistance (<i>bar</i>) gene into the cotton variety &lsquo;Coker312,&rsquo; using <i>Agrobacterium</i>-mediated plant transformation.&nbsp; The development of LLCotton25 has allowed the use of glufosinate ammonium as an alternative herbicide for weed control in cotton.&nbsp; This may help reduce the incidence of herbicide resistant biotypes by adding an additional class of herbicides in weed management systems.</p>\n', 'Enabled', NULL, '2013-08-29 23:52:17'),
(64, 91, '<p style="text-align: justify;">The rice line PWC16 was developed to allow the use of imazethapyr, an imidazolinone herbicide, as a weed control option in rice production. This trait was developed using chemically induced seed mutagenesis and whole plant selection procedures. This rice line expresses a mutated form of the acetohydroxyacid synthase (AHAS) enzyme, which renders the plant tolerant to levels of imazethapyr used in weed control.</p>\n\n<p style="text-align: justify;">AHAS catalyses the first step in the biosynthesis of the branched-chain amino acids isoleucine, leucine and valine, and is active in the glycolytic pathway of plant metabolism. When conventional plants are treated imazethapyr, the herbicide binds to a specific site on the enzyme, thereby inhibiting its activity. The result of this enzyme inhibition is a decrease in the synthesis of these amino acids, and an accumulation of toxic levels of alpha-ketoglutarate, all of which results in the eventual death of the plant.</p>\n', 'Enabled', NULL, '2013-08-30 00:03:30'),
(65, 90, '<p style="text-align: justify;">AP205CL (Clearfield&trade;) spring wheat was developed to allow the use of imazamox, an imidazolinone herbicide, as a weed control option in spring wheat. This trait was developed using chemically induced seed mutagenesis and whole plant selection procedures. This wheat line expresses a mutated form of the acetohydroxyacid synthase (AHAS) enzyme, which renders the plant tolerant to levels of imazamox used in weed control.</p>\n\n<p style="text-align: justify;">AHAS catalyses the first step in the biosynthesis of the branched-chain amino acids isoleucine, leucine, and valine, and is active in the glycolytic pathway of plant metabolism. When conventional plants (i.e., weeds) are treated with imazamox, the herbicide binds to a specific site on the enzyme, thereby inhibiting its activity. The result of this enzyme inhibition is a decrease in the synthesis of these amino acids, and an accumulation of toxic levels of a-ketoglutarate, all of which results in the eventual death of the plant.</p>\n', 'Enabled', NULL, '2013-08-30 00:02:02'),
(66, 88, '<p style="text-align: justify;">Teal 11A (Clearfield&trade;) spring wheat was developed to allow the use of imazamox and imazethapyr, both imidazolinone herbicides, as weed control options in spring wheat production. This trait was developed using chemically induced seed mutagenesis and whole plant selection procedures. This wheat line expresses a mutated form of the acetohydroxyacid synthase (AHAS) enzyme, which renders the plant tolerant to levels of imazamox and imazethapyr used in weed control.</p>\n\n<p style="text-align: justify;">AHAS catalyses the first step in the biosynthesis of the branched-chain amino acids isoleucine, leucine, and valine, and is active in the glycolytic pathway of plant metabolism. When conventional plants are treated with either imazamox or imazethapyr, the herbicide binds to a specific site on the enzyme, thereby inhibiting its activity. The result of this enzyme inhibition is a decrease in the synthesis of these amino acids, and an accumulation of toxic levels of alpha-ketoglutarate, all of which results in the eventual death of the plant.</p>\n', 'Enabled', NULL, '2013-08-29 23:58:50'),
(67, 79, '<p style="text-align: justify;">The spring wheat variety MON 71800 (Roundup Ready&reg; wheat) was developed to allow the use of glyphosate, the active ingredient in the herbicide Roundup&reg;, as a weed control option in spring wheat. This genetically engineered wheat variety contains a glyphosate-tolerant form of the plant enzyme 5-enolpyruvylshikimate-3-phosphate synthase (EPSPS), isolated from the soil bacterium <i>Agrobacterium tumefaciens</i> strain CP4. The novel form of this enzyme is termed hereafter CP4 EPSPS.</p>\n\n<p style="text-align: justify;">The EPSPS enzyme is part of the shikimate pathway that is involved in the production of aromatic amino acids and other aromatic compounds in plants (Steinrucken and Amrhein, 1980). When conventional plants are treated with glyphosate, the herbicide binds to EPSPS, thereby preventing the synthesis of aromatic amino acids needed for plant growth. The CP4 EPSPS enzyme in MON 71800 spring wheat has a reduced affinity for glyphosate; its enzymatic activity is therefore not hindered by the herbicide.</p>\n\n<p style="text-align: justify;">EPSPS is present in all plants, bacteria, fungi, but not in animals, which do not synthesize their own aromatic amino acids. Because the aromatic amino acid biosynthetic pathway is not present in mammalian, avian or aquatic life forms, glyphosate has little if any toxicity for these organisms (U.S. EPA, 1993; WHO, 1994; Williams et al. 2000). The EPSPS enzyme is normally present in food derived from plant and microbial sources.</p>\n\n<p style="text-align: justify;">MON 71800 was developed by introducing the CP4 EPSPS coding sequences into the spring wheat variety &lsquo;Bobwhite&rsquo; using <i>Agrobacterium</i>-mediated transformation.</p>\n', 'Enabled', NULL, '2013-08-29 23:49:45'),
(68, 93, '<p style="text-align: justify;">The cotton line 3006-210-23 was developed to resist attack by lepidopteran insects pests and has demonstrated resistance to tobacco budworm (<i>Heliothis virescens</i>), pink bollworm (<i>Pectinophora gossypiella</i>), cotton bollworm (<i>Helicoverpa zea</i>), beet armyworm (<i>Spodoptera exigua</i>), and soybean looper (<i>Pseudoplusia includens</i>). This line produces, within its tissues, a synthetic version of the insecticidal protein Cry1Ac, a delta-endotoxin, originally derived from <i>Bacillus thuringiensis</i> var. <i>kurstaki</i>. Cry proteins act by binding to specific sites located in the brush border midgut epithelium of susceptible insect species. Following binding, cation-specific pores are formed that disrupt ion flow in the midgut, thereby causing paralysis and death. Cry1Ac is insecticidal only to lepidopteran insects and the specificity of action is directly attributable to the presence of specific binding sites in these insects. The epithelium of mammalian intestinal cells do not possess binding sites for delta-endotoxins of <i>B. thuringiensis</i>, therefore, humans and livestock animals are not susceptible to the damaging effects of these proteins.</p>\n', 'Enabled', NULL, '2013-08-30 00:06:49'),
(69, 92, '<p style="text-align: justify;">The cotton line 281-24-236 was developed to resist attack by lepidopteran insects pests and has demonstrated resistance to tobacco budworm (<i>Heliothis virescens</i>), beet armyworm (<i>Spodoptera exigua</i>), soybean looper (<i>Pseudoplusia includens</i>), and cotton bollworm (<i>Helicoverpa zea</i>). This line produces, within its tissues, a synthetic version of the insecticidal protein Cry1F, a delta-endotoxin, originally derived from <i>Bacillus thuringiensis</i> var.<i>aizawai</i>. Cry proteins act by binding to specific sites located in the brush border midgut epithelium of susceptible insect species. Following binding, cation-specific pores are formed that disrupt ion flow in the midgut, thereby causing paralysis and death. Cry1F is insecticidal only to lepidopteran insects and the specificity of action is directly attributable to the presence of specific binding sites in these insects. The epithelium of mammalian intestinal cells do not possess binding sites for delta-endotoxins of <i>B. thuringiensis</i>, therefore, humans and livestock animals are not susceptible to the damaging effects of these proteins.</p>\n', 'Enabled', NULL, '2013-08-30 00:04:53'),
(70, 94, '<p style="text-align: justify;">Sugar beet line H7-1 was developed using recombinant DNA techniques to allow the use of glyphosate, the active ingredient in the herbicide Roundup&reg;, as a weed control option in sugar beet crops. The novel plants express an herbicide tolerant form of the enzyme 5-enolpyruvylshikimate-3-phosphate synthase (EPSPS) derived from the common soil bacterium, <i>Agrobacterium tumefaciens</i> strain CP4. Glyphosate specifically binds to and inactivates EPSPS, which is involved in the synthesis of the aromatic amino acids, tyrosine, phenylalanine and tryptophan (shikimate biochemical pathway). EPSPS is present in all plants, bacteria, and fungi but not in animals, which must obtain these essential amino acids from their diet. Because the aromatic amino acid biosynthetic pathway is not present in mammalian, avian or aquatic life forms, glyphosate has little if any toxicity for these organisms (U.S. EPA, 1993; WHO, 1994; Williams et al. 2000). The EPSPS enzyme is normally present in food derived from plant and microbial sources.</p>\n', 'Enabled', NULL, '2013-08-30 00:08:36'),
(71, 78, '<p style="text-align: justify;">The maize line DAS-06275-8 (hereafter referred to as <b>TC-6275</b>) was genetically modified to contain two novel genes, <i>cry</i>1F and <i>bar</i>, for insect resistance and herbicide tolerance respectively. Both genes were introduced into the parental maize hybrid line Hi-II by <i>Agrobacterium</i>-mediated plant transformation.</p>\n\n<p style="text-align: justify;">The <i>cry</i>1F gene, isolated from the common soil bacterium <i>Bacillus thuringiensis</i> (<i>Bt</i>) var. <i>aizawai</i>, produces the insect control protein Cry1F, a delta-endotoxin. Cry proteins, of which Cry1F is only one, act by selectively binding to specific sites localized on the lining of the midgut of susceptible insect species. Following binding, pores are formed that disrupt midgut ion flow, causing gut paralysis and eventual death due to bacterial sepsis. Cry1F is lethal only when eaten by the larvae of lepidopteran insects (moths and butterflies), and its specificity of action is directly attributable to the presence of specific binding sites in the target insects. There are no binding sites for the delta-endotoxins of <i>B. thuringiensis</i> on the surface of mammalian intestinal cells, therefore, livestock animals and humans are not susceptible to these proteins. The Cry1F protein expressed in TC-6275 provides protection against European corn borer (ECB), southwestern corn borer (SWCB), fall armyworm (FAW), black cutworm (BCW), and some control of corn earworm (CEW).</p>\n\n<p style="text-align: justify;">The <i>bar</i> gene in TC-6275 confers tolerance to glufosinate ammonium. This herbicide can therefore be applied to TC-6275 as a weed control option, and can also be used as a selection tool for successful transformants containing the insect-tolerant <i>cry</i>1F gene. The herbicide tolerance of TC-6275 is due to the expression of a protein, phosphinothricin-acetyl-transferase (PAT), which confers tolerance to the active ingredient L-phosphinothricin in glufosinate ammonium. The <i>bar</i> gene was isolated from <i>Streptomyces hygroscopius</i>, a gram-positive soil bacterium.</p>\n\n<p style="text-align: justify;">Glufosinate ammonium is a post-emergence, broad-spectrum contact herbicide and plant dessicant. L-Phosphinothricin was first isolated as bialaphos, an antibiotic synthesized during the fermentation of <i>Streptomyces hygroscopicus</i> or <i>S.viridochromogenes</i>. In herbicidal formulations, L-Phosphinothricin is a component of the glufosinate ammonium, which is chemically-synthesized. Glufosinate ammonium is a racemic mixture of L-phosphinothricin, the herbicidal active moiety, and its D-enantiomer. L-phosphinothricin is structurally similar to glutamate, the substrate of glutamine synthetase (GS), an enzyme that catalyzes the synthesis of glutamine from glutamate and ammonia. L-phosphinothricin inhibits the activity of GS irreversibly by binding to its active sites. The inhibition of GS caused by the application of glufosinate ammonium to plants results in the accumulation of ammonia, the reduction in the levels of glutamine, and the inhibition of photosynthesis, all of which results in the death of the plant. Plants transformed with the <i>bar</i> gene express the enzyme phosphinothricin-acetyl-transferase (PAT) which acetylates L-phosphinothricin into a non-phytotoxic metabolite (N-acetyl-L-glufosinate).</p>\n', 'Enabled', NULL, '2013-08-29 23:47:35'),
(72, 89, '<p style="text-align: justify;">The lentil line RH44 was developed to allow the use of imidazolinone herbicides, as a weed control option in lentil production. This trait was developed using chemically induced seed mutagenesis and whole plant selection procedures. This rice line expresses a mutated form of the acetohydroxyacid synthase (AHAS) enzyme, which renders the plant tolerant to levels of imazethapyr used in weed control.</p>\n\n<p style="text-align: justify;">AHAS catalyses the first step in the biosynthesis of the branched-chain amino acids isoleucine, leucine and valine, and is active in the glycolytic pathway of plant metabolism. When conventional lentil plants are treated imazethapyr, the herbicide binds to a specific site on the enzyme, thereby inhibiting its activity. The result of this enzyme inhibition is a decrease in the synthesis of these amino acids, and an accumulation of toxic levels of alpha-ketoglutarate, all of which results in the eventual death of the plant.</p>\n', 'Enabled', NULL, '2013-08-30 00:00:14'),
(73, 80, '<p style="text-align: justify;">ASR368 creeping bentgrass (Roundup Ready&reg; Creeping bentgrass) was developed to allow the use of glyphosate, the active ingredient in the herbicide Roundup&reg;, as a weed control option in turfgrass production (<i>e.g.</i>, putting greens). This genetically engineered wheat variety contains a glyphosate-tolerant form of the plant enzyme 5-enolpyruvylshikimate-3-phosphate synthase (EPSPS), isolated from the soil bacterium <i>Agrobacterium tumefaciens</i> strain CP4. The novel form of this enzyme is termed hereafter CP4 EPSPS.</p>\n\n<p style="text-align: justify;">The EPSPS enzyme is part of the shikimate pathway that is involved in the production of aromatic amino acids and other aromatic compounds in plants (Steinrucken &amp; Amrhein, 1980). When conventional plants are treated with glyphosate, the herbicide binds to EPSPS, thereby preventing the synthesis of aromatic amino acids needed for plant growth. The CP4 EPSPS enzyme in ASR368 creeping bentgrass has a reduced affinity for glyphosate; its enzymatic activity is therefore not hindered by the herbicide.</p>\n\n<p style="text-align: justify;">EPSPS is present in all plants, bacteria, fungi, but not in animals, which do not synthesize their own aromatic amino acids. Because the aromatic amino acid biosynthetic pathway is not present in mammalian, avian or aquatic life forms, glyphosate has little if any toxicity for these organisms (U.S. EPA, 1993; WHO, 1994; Williams et al. 2000). The EPSPS enzyme is normally present in food derived from plant and microbial sources.</p>\n\n<p style="text-align: justify;">ARS368 was developed by introducing the CP4 EPSPS coding sequences into the creeping bentgrass line B99061R using microprojectile bombardment.</p>\n', 'Enabled', NULL, '2013-08-29 23:50:57'),
(74, 95, '<p style="text-align: justify;">Maize line DAS-59122-7 was genetically modified to contain three novel genes, <i>cry</i>34Ab1 and <i>cry</i>35Ab1 for insect resistance, and <i>pat</i>, for herbicide tolerance used as a selectable marker. All three genes were introduced into the parental maize hybrid line Hi-II by <i>Agrobacterium</i>-mediated plant transformation.</p>\n\n<p style="text-align: justify;">The <i>cry</i>34Ab1 and <i>cry</i>35Ab1 genes, isolated from the common soil bacterium <i>Bacillus thuringiensis</i> (<i>Bt</i>) strain PS149B1, produce the insect control proteins (delta-endotoxins) Cry34Ab1 and Cry35Ab1. Cry proteins, of which Cry34Ab1 and Cry35Ab1 are only two among many, act by selectively binding to specific sites localized on the lining of the midgut of susceptible insect species. Following binding, pores are formed that disrupt midgut ion flow, causing gut paralysis and eventual death due to bacterial sepsis. Cry34Ab1 and Cry35Ab1 are both lethal only when eaten by the larvae of coleopteran insects (<i>i.e.</i>, beetles), and its specificity of action is directly attributable to the presence of specific binding sites in the target insects. There are no binding sites for the delta-endotoxins of <i>B. thuringiensis</i> on the surface of mammalian intestinal cells, therefore, livestock animals and humans are not susceptible to these proteins.<br />\nThe <i>pat</i> gene introduced into DAS-59122-7 maize allows the use of the herbicide glufosinate ammonium as a breeding tool for selecting plants containing the <i>cry</i>34Ab1 and <i>cry</i>35Ab1 genes. The herbicidal mode of action of glufosinate ammonium is related to the activity of glutamine synthetase (GS), the enzyme required for the synthesis of the amino acid glutamine. L-phosphinothricin, the active ingredient of glufosinate ammonium, is a structural analog of glutamate, and acts as a competitive inhibitor. After application of the herbicide, L-phosphinothricin competes with glutamine for its active sites on GS. The results of the inhibition of GS are an accumulation of ammonia in the plant, a reduction in the synthesis of glutamine, and an inhibition of photosynthesis. This causes the death of plant cells, and eventually, the entire plant. The <i>pat</i> gene codes for the production of the enzyme phosphinothricin acetyl-transferase (PAT). This enzyme acetylates L-phosphinothricin rendering it inactive in the plant. The PAT enzyme is not known to have any toxic properties. The <i>pat</i> gene was isolated from the soil bacterium <i>Streptomyces viridochromogenes</i>, the same organism from which L-phosphinothricin was originally isolated.</p>\n', 'Enabled', NULL, '2013-08-30 00:10:12');
INSERT INTO `gmcropdatabase_events_introductions` (`id`, `eventId`, `description`, `status`, `created`, `updated`) VALUES
(75, 96, '<p style="text-align: justify;">Maize line MON88017 was genetically modified to contain two novel genes, <i>cry</i>3Bb1 for insect resistance, and <i>cp4 epsps</i>, which confers tolerance to glyphosate. Both genes were introduced into the parental maize line LH198 by <i> Agrobacterium</i>-mediated plant transformation.</p>\n\n<p style="text-align: justify;">The <i>cry</i>3Bb1 gene, isolated from the soil bacterium <i>Bacillus thuringiensis</i> (Bt) subspecies <i>kumamotoensis</i>, produces the insect control protein Cry3Bb1, a delta-endotoxin. Cry proteins, of which Cry3Bb1 is only one, act by selectively binding to specific sites localized on the lining of the midgut of susceptible insect species. Following binding, pores are formed that disrupt midgut ion flow, causing gut paralysis and eventual death due to bacterial sepsis. Cry3Bb1 is lethal only when eaten by the larvae of coleopteran insects (<i>i.e.</i>, beetles), and its specificity of action is directly attributable to the presence of specific binding sites in the target insects. There are no binding sites for the delta-endotoxins of <i>B. thuringiensis</i> on the surface of mammalian intestinal cells, therefore, livestock animals and humans are not susceptible to these proteins. The Cry3Bb1 protein expressed in MON88017 provides protection against the western corn rootworm (<i>Diabrotica vigifera</i>) and northern corn rootworm (<i>Diabrotica barberi</i>).</p>\n\n<p style="text-align: justify;">MON88017 also was developed to allow the use of glyphosate, the active ingredient in the herbicide Roundup&reg;, as a weed control option. The novel plants express an herbicide tolerant form of the enzyme 5-enolpyruvylshikimate-3-phosphate synthase (EPSPS) derived from the common soil bacterium, <i>Agrobacterium tumefaciens</i> strain CP4. Glyphosate specifically binds to and inactivates EPSPS, which is involved in the synthesis of the aromatic amino acids, tyrosine, phenylalanine and tryptophan (shikimate biochemical pathway). EPSPS is present in all plants, bacteria, and fungi but not in animals, which must obtain these essential amino acids from their diet. Because the aromatic amino acid biosynthetic pathway is not present in mammalian, avian or aquatic life forms, glyphosate has little if any toxicity for these organisms (U.S. EPA, 1993; WHO, 1994; Williams et al. 2000). The EPSPS enzyme is normally present in food derived from plant and microbial sources.</p>\n', 'Enabled', NULL, '2013-08-30 00:13:44'),
(76, 97, '<p style="text-align: justify;">MON 88913 (Roundup Ready&reg; Flex) cotton was developed to allow the use of glyphosate, the active ingredient in the herbicide Roundup&reg;, as a weed control option in cotton production. This genetically engineered cotton variety contains a glyphosate-tolerant form of the plant enzyme 5-enolpyruvylshikimate-3-phosphate synthase (EPSPS), isolated from the soil bacterium <i>Agrobacterium tumefacien</i> strain CP4, hereafter termed CP4 EPSPS. Compared to previously approved glyphosate tolerant lines of cotton, which will tolerate glyphosate applications only to the fifth true leaf stage, MON 88913 was developed to tolerate glyphosate applications beyond the fifth true leaf stage.</p>\n\n<p style="text-align: justify;">The EPSPS enzyme is part of the shikimate pathway that is involved in the production of aromatic amino acids and other aromatic compounds in plants (Steinrucken &amp; Amrhein, 1980). When conventional plants are treated with glyphosate, the herbicide binds to EPSPS, thereby preventing the synthesis of aromatic amino acids needed for plant growth. The CP4 EPSPS enzyme in MON 88913 cotton has a reduced affinity for glyphosate; its enzymatic activity is therefore not hindered by the herbicide.</p>\n\n<p style="text-align: justify;">EPSPS is present in all plants, bacteria, fungi, but not in animals, which do not synthesize their own aromatic amino acids. Because the aromatic amino acid biosynthetic pathway is not present in mammalian, avian or aquatic life forms, glyphosate has little if any toxicity for these organisms (U.S. EPA, 1993; WHO, 1994; Williams et al. 2000). The EPSPS enzyme is normally present in food derived from plant and microbial sources.</p>\n\n<p style="text-align: justify;">MON 88913 cotton was developed by introducing two CP4 EPSPS coding sequences into the cotton variety &lsquo;Coker 312&rsquo; using <i>Agrobacterium</i>-mediated transformation.</p>\n', 'Enabled', NULL, '2013-08-30 00:16:40'),
(77, 109, '<p style="text-align: justify;">Events J101 and J163 were developed to allow the use of glyphosate, the active ingredient in the herbicide Roundup&reg;, as a weed control option in the production of pure stands of alfalfa, either as forage or for seed. These genetically engineered alfalfa populations contain a glyphosate-tolerant form of the plant enzyme 5-enolpyruvylshikimate-3-phosphate synthase (EPSPS), isolated from the soil bacterium <i>Agrobacterium tumefaciens</i> strain CP4. The novel form of this enzyme is termed hereafter CP4 EPSPS.</p>\n\n<p style="text-align: justify;">The EPSPS enzyme is part of the shikimate pathway that is involved in the production of aromatic amino acids and other aromatic compounds in plants (Steinrucken and Amrhein, 1980). When conventional plants are treated with glyphosate, the herbicide binds to EPSPS, thereby preventing the synthesis of aromatic amino acids needed for plant growth. The CP4 EPSPS enzyme in events J101 and J1638 has a reduced affinity for glyphosate; its enzymatic activity is therefore not hindered by the herbicide.</p>\n\n<p style="text-align: justify;">EPSPS is present in all plants, bacteria, fungi, but not in animals, which do not synthesize their own aromatic amino acids. Because the aromatic amino acid biosynthetic pathway is not present in mammalian, avian or aquatic life forms, glyphosate has little if any toxicity for these organisms (U.S. EPA, 1993; WHO, 1994; Williams<i>et al.</i> 2000). The EPSPS enzyme is normally present in food derived from plant and microbial sources.</p>\n\n<p style="text-align: justify;">Events J101 and J163 were each developed by introducing the CP4 EPSPS coding sequences into the alfalfa clone &lsquo;R2336&rsquo; using <i>Agrobacterium</i>-mediated transformation.</p>\n', 'Enabled', NULL, '2013-08-30 00:21:31'),
(78, 110, '<p style="text-align: justify;">The cotton line COT102 was developed to resist attack by lepidopteran insects pests such as cotton bollworm (<i>Helicoverpa zea</i>), tobacco budworm (<i>Heliothis virescens</i>), pink bollworm (<i>Pectinophora gossypiella</i>), fall armyworm (<i>Spodoptera frugiperda</i>), beet armyworm (<i>Spodoptera exigua</i>), soybean looper (<i>Pseudoplusia includens</i>), cabbage looper (<i>Trichoplusia ni</i>), and cotton leaf perforator (<i>Bucculatrix thurberiella</i>). The vegetative insecticidal protein VIP3A, which is a product of a gene originally derived from <i>Bacillus thuringiensis</i> strain AB88, is produced in the tissues of COT102. The VIP3A proteins act by binding to specific sites located in the midgut epithelium of susceptible insect species of the order Lepidoptera. Following binding, cation-specific pores are formed that disrupt ion flow in the midgut, thereby causing paralysis and death. The insecticidal nature of the VIP3A protein is attributable to the presence of specific binding sites in these insects, which are different than those specific to Cry1Ab and Cry1Ac. There are no binding sites in the epithelium of mammalian and avian intestinal sites for the vegetative insecticidal proteins of <i>B. thuringiensis</i>. Humans and livestock animals are therefore not susceptible to the damaging effects of these proteins.</p>\n', 'Enabled', NULL, '2013-08-30 00:23:21'),
(79, 122, '<p style="text-align: justify;">BW255-2 and BW238-3 (Clearfield&trade;) bread wheat was developed to allow the use of imidazolinone herbicides as a weed control option in spring wheat. This trait was developed using chemically induced seed mutagenesis and whole plant selection procedures. This wheat line expresses a mutated form of the acetohydroxyacid synthase (AHAS) enzyme, which renders the plant tolerant to levels of imidazolinone herbicides used in weed control.</p>\n\n<p style="text-align: justify;">AHAS catalyses the first step in the biosynthesis of the branched-chain amino acids isoleucine, leucine, and valine, and is active in the glycolytic pathway of plant metabolism. When conventional plants (<i>i.e.</i>, weeds) are treated with imidazolinone herbicides, the herbicide binds to a specific site on the enzyme, thereby inhibiting its activity. The result of this enzyme inhibition is a decrease in the synthesis of branched-chain amino acids and an accumulation of toxic levels of ?-ketoglutarate, which results in the eventual death of the plant.</p>\n', 'Enabled', NULL, '2013-08-30 00:40:13'),
(80, 123, '<p style="text-align: justify;">Rice lines IMINTA 1 and IMINTA 4 were developed to be tolerant to imidazolinone herbicides to provide an alternative strategy for weed control in rice. Imidazolinone herbicides are active against the acetolactate synthase (ALS) enzyme in plants, which catalyzes the first reaction in the biosynthesis of branched-chain amino acids. Imidazolinone inhibits the production of these essential amino acids (valine, leucine and isoleucine), resulting in a decrease in protein synthesis and the eventual death of the plant.</p>\n\n<p style="text-align: justify;">The development of these events was acomplished by mutagenesis and the herbicide tolerance results from a single point mutation in the ALS gene (also known as acetohydroxyacid synthase or AHAS), such that the resulting enzyme has a single amino acid substitution and is no longer affected by imidazolinone herbicides. Previously authorized rice events CL121, CL141, CFX51 and PWC16 also contain modified ALS genes conferring tolerance to imidazolinone herbicides.</p>\n', 'Enabled', NULL, '2013-08-30 00:41:44'),
(81, 111, '<p style="text-align: justify;">LY038 maize has been genetically modified to express the <i>cordapA</i> gene from <i>Corynebacterium glutamicum</i>. This gene encodes for a lysine &ndash;insensitive dihydropicolinate synthase (cDHDPS) enzyme, a regulatory enzyme in the lysine biosynthetic pathway. The activity of the native maize DHDPS is regulated by lysine feedback inhibition. Since the cDHDPS enzyme is less sensitive to lysine feedback inhibition, its expression in maize LY038 results in elevated levels of free lysine in the grain when compared to conventional maize. The expression of the <i>cordapA</i> gene is under the control of the maize Glb1 promoter, which directs cDHDPS expression predominantly in the germ of the seed, resulting in accumulation of lysine in the grain.</p>\n\n<p style="text-align: justify;">Maize-soybean meal based diets formulated for poultry and swine are characteristically deficient in lysine and require the addition of supplemental lysine for optimal growth and production of these animals. The development of LY038 maize provides an alternative to direct supplementation of poultry and swine diets by increasing the amount of lysine in the maize portion of the feed.</p>\n\n<p style="text-align: justify;">There are no selectable markers present in the final LY038 event as these were removed after the selection of the initial transgenic event using a site-specific recombination system. The recombination-mediated removal of the selectable marker was accomplished by crossing with a second transgenic maize plant expressing a specific recombinase gene, and subsequent crossing and selection resulted in the isolation of lines containing only the <i>cordapA</i> gene as inserted DNA.</p>\n', 'Enabled', NULL, '2013-08-30 00:25:20'),
(82, 112, '<p style="text-align: justify;">MON810 X LY038 (OECD identifier: MON-&Oslash;&Oslash;81&Oslash;-6 X REN-&Oslash;&Oslash;&Oslash;38-3) maize is a stacked event resulting from the hybridization of maize inbred MON 810 (MON-&Oslash;&Oslash;81&Oslash;-6) with LY038 (REN-&Oslash;&Oslash;&Oslash;38-3). This stacked maize hybrid is a product of traditional plant breeding, and therefore is not automatically subject to regulation in all jurisdictions as are transgenic plants resulting from recombinant DNA technologies. Certain jurisdictions may request notification in advance of the release of a stacked hybrid, or may request information to conduct an environmental and food safety assessment. Examples of jurisdictions that require either notification or information about stacked hybrids prior to their release into the environment, and for use in human food and livestock feed are the Philippines and Japan.</p>\n\n<p style="text-align: justify;">The stacked hybrid MON810 X LY038 expresses the novel proteins expressed in the parental lines used to breed this line. The insecticidal delta-endotoxin Cry1Ab, which confers resistance to the European Corn Borer and other lepidopterans, is produced by the <i>cry</i>1Ab gene from MON810. The maize line LY038 contains the <i>cordapA</i> gene from <i>Corynebacterium glutamicum</i> to increase the level of the amino acid lysine in the grain for animal feed, primarily for poultry and swine. The use of LY038 as a feed ingredient is expected to reduce or eliminate the need for lysine supplementation. The novel traits of each parent line have been combined, through traditional plant breeding, to produce this new hybrid. For a full description of each parent line please refer to the individual product descriptions in the crop database for MON810 and LY038.</p>\n\n<p style="text-align: justify;">The inserted genes and their gene products have a history of safe use, and have undergone review and approval by several regulatory agencies. No interactions among the gene products or negative synergistic effects are expected in the stacked hybrid. The Cry1Ab protein is not an enzyme and therefore does not affect plant metabolism. The <i>cordapA</i> gene isolated from <i>Corynebacterium glutamicum</i>, codes for the enzyme dihydrodipicolinate syntase (cDHDPS). This enzyme is active in the lysine metabolic pathway and mediates a critical rate-limiting step, that in maize, is controlled by feedback inhibition. DHDPS catalyzes the condensation of L-aspartate-4-semialdehyde and pyruvate , resultling in the synthesis of 2,3-dihydrodipicolinate, a substrate in the lysine metabolic pathway. The DHDPS encoded by <i>cordapA</i> is less sensitive to feedback inhibition than the native maize DHDPS. The reduction in feedback inhibition results in higher levels of free lysine accumulating in the grain of LY038, at levels higher than those typically found in conventional maize.</p>\n', 'Enabled', NULL, '2013-08-30 00:31:08'),
(83, 125, '<p style="text-align: justify;">The soybean line MON98788 was developed to allow for the use of glyphosate, the active ingredient in the herbicide Roundup&reg;, as a weed control option for soybean. This genetically engineered soybean variety contains a glyphosate tolerant form of the plant enzyme 5-enolpyruvylshikimate-3-phosphate synthase (EPSPS) isolated from the common soil bacterium, <i>Agrobacterium tumefaciens</i> strain CP4 (CP4 EPSPS).</p>\n\n<p style="text-align: justify;">The EPSPS enzyme is part of the shikimate pathway that is involved in the production of aromatic amino acids and other aromatic compounds in plants (Steinrucken &amp; Amrhein, 1980). When conventional plants are treated with glyphosate, the plants cannot produce the aromatic amino acids needed to survive. This enzyme is present in all plants, bacteria, fungi, but not in animals, which do not synthesize their own aromatic amino acids. Because the aromatic amino acid biosynthetic pathway is not present in mammalian, avian or aquatic life forms, glyphosate has little if any toxicity for these organisms (U.S. EPA, 1993; WHO, 1994; Williams <i>et al</i>. 2000). The EPSPS enzyme is normally present in food derived from plant and microbial sources.</p>\n\n<p style="text-align: justify;">MON89788 was developed by introducing the CP4 EPSPS gene into a commercial soybean variety using <i>Agrobacterium tumefaciens</i>-mediated transformation of meristem-derived material from soybean variety A3244. A3244 is an elite maturity group III soybean variety which was developed and selected for transformation based on its superior agronomic performance over other soybean lines.</p>\n\n<p style="text-align: justify;">Glyphosate-tolerant soybeans were planted on less than 5% of the U.S. soybean acreage in 1996. Globally, over 50 million hectares of glyphosate-tolerant soybeans were planted in 2007. One of the reasons growers have rapidly adopted the glyphosate-tolerant soybean is the simplicity it offers in weed control. Since glyphosate containing herbicides are highly effective against the vast majority of annual and perennial grasses and broadleaf weeds, growers planting glyphosate tolerant soybeans are able to reduce the number of herbicides used to control the economically destructive weeds that grow in their fields and thereby realize a savings in weed control costs. This reduction in herbicides used has benefited the environment by reducing the number of herbicide applications and also allows growers to implement integrated weed management practices in their fields - practices that are generally not possible when pre-plant or pre-emergent herbicides are used.</p>\n', 'Enabled', NULL, '2013-08-30 00:43:22'),
(84, 131, '<p style="text-align: justify;">Maize (Zea mays L), otherwise known as corn, is the world&rsquo;s third leading cereal crop, behind wheat and rice, and is grown in over 25 countries worldwide. The majority of grain and forage derived from maize is used as animal feed, however maize also has a long history of safe use as food for human consumption. The grain can be processed into industrial products such as ethanol (by fermentation), and highly refined starch (by wetmilling) and sweetener products. In addition to milling, the maize germ can be processed to obtain corn oil and numerous other products.<br />\nThe majority of maize is grown for animal feed production and human food, however an increasing percentage is being used for the production of ethanol as a biofuel alternative to petroleum products from fossil sources. The hydrolysis of the large starch molecules in maize kernels is the first step in ethanol production from maize and the themostable alpha-amylase in Event 3272 is intended to increase the efficiency of this process by operating at high temperatures.</p>\n\n<p style="text-align: justify;">Maize line 3272 has been genetically modified to express a thermostable alpha-amylase enzyme (AMY797E) for use in dry-grind fuel ethanol production in the United States. Amylase is used to hydrolyse starch into smaller sugar subunits, which is the first step in producing ethanol from plants. Amylases used for ethanol production need to be able to work at high temperatures and low calcium concentrations. Plants such as maize naturally contain amylases, however these are destroyed when corn is subjected to the high processing temperatures necessary for ethanol production, making it necessary to add microbially-produced amylase preparations. The use of Event 3272, expressing a highly thermostable amylase, bypasses this step.</p>\n', 'Enabled', NULL, '2013-08-30 00:51:19'),
(85, 113, '<p style="text-align: justify;">Corn line MIR604 has been genetically modified to be resistant to western corn rootworm (<i>Diabrotica vigifera vigifera</i>), northern corn rootworm (<i>D. berberi</i>), and Mexican corn rootworm (<i>D. vigifera zeae</i>). These species are serious insect pests of dent corn in the major corn-producing states of the north-central United States and Canada. Protection is conferred by the expression in the plant of the bacterially derived protein toxin mCry3A, encoded by the <i>mcry3A</i> gene in the corn plants. A selectable marker gene, <i>pmi</i>, encodes phosphomannose isomerase and allows transformed cells to utilise carbon from phosphomannose media.</p>\n\n<p style="text-align: justify;">Commercial corn lines containing the <i>cry</i> genes from <i>Bacillus thuringiensis</i> can provide growers with effective methods for controlling corn rootworm. Formulations with insecticidal toxins from cultures of <i>B. thuringiensis</i> are widely used as biopesticides on a variety of cereal and vegetable crops grown organically or under conventional agricultural conditions.</p>\n\n<p style="text-align: justify;">Corn, together with rice and wheat, is one of the most important cereal crops in the world. The majority of grain and forage derived from maize is used in animal feed. Maize grain is also used in industrial products, such as ethanol by fermentation and highly refined starch by wet milling. Corn-based products, largely as high-fructose corn syrup, are processed into breakfast cereals, baking products, extruded confectionery and corn chips. Other corn products such as cornstarch are also used by the food industry for the manufacture of dessert mixes and canned foods.&nbsp;</p>\n', 'Enabled', NULL, '2013-08-30 00:31:48'),
(86, 126, '<p style="text-align: justify;">BW7 (Clearfield&trade;) bread wheat was developed to allow the use of imidazolinone herbicides as a weed control option in spring wheat. This trait was developed using chemically induced seed mutagenesis and whole plant selection procedures. This wheat line expresses a mutated form of the acetohydroxyacid synthase (AHAS, sometimes referred to as acetolactate synthase or ALS) enzyme, which renders the plant tolerant to levels of imidazolinone herbicides used in weed control.</p>\n\n<p style="text-align: justify;">AHAS catalyses the first step in the biosynthesis of the branched-chain amino acids isoleucine, leucine, and valine, and is active in the glycolytic pathway of plant metabolism. When conventional plants (<i>i.e.</i>, weeds) are treated with imidazolinone herbicides, the herbicide binds to a specific site on the enzyme, thereby inhibiting its activity. The result of this enzyme inhibition is a decrease in the synthesis of branched-chain amino acids and an accumulation of toxic levels of ?-ketoglutarate, which results in the eventual death of the plant.</p>\n', 'Enabled', NULL, '2013-08-30 00:45:02'),
(87, 121, '<p style="text-align: justify;">BT11 X GA21 10 (OECD identifier: SYN-BT&Oslash;11-1 x MON-&Oslash;&Oslash;&Oslash;21-9) maize is an F1 hybrid resulting from the hybridization of the lepidoteran-resistant and herbicide-tolerant maize line BT11 (SYN-BT&Oslash;11-1) and the herbicide-tolerant maize line GA21 (MON-&Oslash;&Oslash;&Oslash;21-9). This stacked maize hybrid is a product of traditional plant breeding, and therefore is not automatically subject to regulation in all jurisdictions as are transgenic plants resulting from recombinant DNA technologies. Certain jurisdictions may request notification in advance of the release of a stacked hybrid, or may request information to conduct an environmental and food safety assessment. Examples of jurisdictions that require either notification or information about stacked hybrids prior to their release into the environment, and for use in human food and livestock feed are Japan and Korea.</p>\n\n<p style="text-align: justify;">The stacked hybrid BT11 X GA21 expresses three novel proteins: the delta-endotoxin Cry1Ab which confers resistance to the European Corn Borer and other lepidopterans, the PAT protein which confers tolerance to the herbicide glufosinate ammonium, and a modified EPSPS protein which confers tolerance to the herbicide glyphosate. The modified EPSPS protein is produced by the <i>mepsps</i> gene from GA21, the insecticidal protein Cry1Ab is produced by the <i>cry</i>1Ab gene and PAT is produced by the <i>pat</i> gene, both from BT11. The novel traits of each parental line have been combined, through traditional plant breeding, to produce this new hybrid. For a full description of each parental line please refer to the individual product descriptions in the crop database for BT11 and GA21.</p>\n\n<p style="text-align: justify;">The inserted genes and their gene products have a history of safe use, and have undergone review and approval by several regulatory agencies. No interactions among the gene products or negative synergistic effects are expected in the stacked hybrid. The Cry1Ab protein is not an enzyme and therefore does not affect plant metabolism. PAT has a high affinity for L-Phosphinothricin, the active ingredient in glufosinate ammonium. The modified EPSPS has high affinity for its substrates phosphoenolpyruvate (PEP) and shikimate-3-phosphate, which are part of the shikimate metabolic pathway. PAT, EPSPS and Cry1Ab are therefore not expected to interact within, nor affect the metabolism of the stacked hybrid.</p>\n', 'Enabled', NULL, '2013-08-30 00:39:48'),
(88, 119, '<p style="text-align: justify;">WideStrike&trade; x MON88913 (OECD identifier: DAS-21023-5 x DAS-24236-5 x MON-88913-8) was produced by crossing WideStrike&trade; insect resistant cotton with the herbicide-tolerant cotton line MON88913. This stacked cotton line is a product of traditional plant breeding, and therefore is not automatically subject to regulation in all jurisdictions as are transgenic plants resulting from recombinant DNA technologies. Certain jurisdictions may request notification in advance of the release of a stacked hybrid, or may request information to conduct an environmental and food safety assessment. Examples of jurisdictions that require either notification or information about stacked hybrids prior to their release into the environment, and for use in human food and livestock feed are Canada and Japan. The United States Environmental Protection Agency (EPA) reviews stacked events when these are the result of stacking two or more plant-incorporated insecticidal proteins, such as WideStrikeTM cotton.</p>\r\n\r\n<p style="text-align: justify;">The stacked cotton line WideStrike&trade; X MON88913 expresses four novel proteins: the delta-endotoxins Cry1F and Cry1Ac, which confer resistance to the lepidopteran pests of cotton, such as the cotton bollworm, pink bollworm and tobacco budworm, the CP4 EPSPS protein, which confers tolerance to the herbicide glyphosate, and the PAT protein, which confers tolerance to glufosinate ammonium. The insecticidal proteins Cry1F and Cry1Ac are produced by the <i>cry</i>1F gene and <i>cry</i>1Ac genes respectively, both of which are from WideStrike&trade;. The cotton line WideStrike&trade; was produced by crossing line 281-24-236 (OECD identifier: DAS-24236-5) with line 3006-210-23 (OECD identifier: DAS-21023-5). The PAT protein in WideStrike&trade; is produced by the <i>pat</i> gene: this expressed novel protein was intended solely for use as a selectable marker during plant transformation. The CP4 EPSPS protein is from MON88913 which contains two copies of the <i>cp4 epsps</i> gene to confer tolerance to glyphosate later in the growing season, specifically after the fifth true leaf stage. For a full description of each parental line please refer to the individual product descriptions in the crop database for 281-24-236 and 3006-210-23 (the parental lines of WideStrike&trade; cotton) and MON88913.</p>\r\n\r\n<p style="text-align: justify;">The inserted genes and their gene products have a history of safe use, and have undergone prior review and approval by several regulatory agencies. No interactions among the gene products or negative synergistic effects are expected in this stacked line. Since neither Cry1F, nor Cry1Ac are enzymes, these proteins have no effect on plant metabolism. The CP4 EPSPS has a very high affinity for its substrates phosphoenolpyruvate (PEP) and shikimate-3-phosphate, which are part of the shikimate metabolic pathway. The PAT protein has a very high affinity for L-Phosphinothricin, the active ingredient in the herbicide glufosinate ammonium. CP4 EPSPS, Cry1F, Cry1Ac, and PAT are therefore not expected to interact within, nor affect the metabolism of the stacked line.</p>\r\n\r\n<p style="text-align: justify;">The EPA conducted an environmental hazard assessment of WideStrike&trade; cotton. Data on the effects of the Cry1F and Cry1Ac were assessed separately, and in combination to detect possible synergistic effects. No synergistic effects were observed, nor any increase in the host range of non-target organisms, from the stacking of both Cry proteins. No harmful effects to aquatic and terrestrial wildlife were observed, and if was concluded that the cultivation of the stacked line would not be hazardous to non-target terrestrial, aquatic and soil organisms.</p>\r\n', 'Enabled', NULL, '2013-09-02 13:41:41'),
(89, 117, '<p style="text-align: justify;">DAS-59122-7 X NK603 (OECD identifier: DAS-59122-7 x MON-&Oslash;&Oslash;6&Oslash;3-6) maize is an F1 hybrid resulting from the hybridization of the insect-resistant maize inbred line DAS-59122-7 and the herbicide-tolerant maize inbred line NK603 (MON-&Oslash;&Oslash;6&Oslash;3-6). This stacked maize hybrid is a product of traditional plant breeding, and therefore is not automatically subject to regulation in all jurisdictions as are transgenic plants resulting from recombinant DNA technologies. Certain jurisdictions may request notification in advance of the release of a stacked hybrid, or may request information to conduct an environmental and food safety assessment. Examples of jurisdictions that require either notification or information about stacked hybrids prior to their release into the environment, and for use in human food and livestock feed are Japan and the Philippines.</p>\n\n<p style="text-align: justify;">The stacked hybrid DAS-59122-7 X NK603 expresses four novel proteins: the insect control proteins (delta-endotoxins) Cry34Ab1 and Cry35Ab1, which are insecticidal to coleopterans such as the Corn Rootworm, together with phosphinothricin acetyl-transferase (PAT) and CP4 EPSPS which confer tolerance to the herbicides glufosinate ammonium and glyphosate, respectively. The CP4 EPSPS protein is produced by the <i>cp4 epsps</i> gene from NK603, and the insecticidal proteins Cry34Ab1 and Cry35Ab1, by the <i>cry</i>34Ab1 and <i>cry</i>35Ab1 genes from DAS-59122-7. The PAT protein is produced by the <i>pat</i> gene, also from DAS-59122-7. The novel traits of each parent line have therefore been combined, using traditional plant breeding methods, to produce this new hybrid. For a full description of each parent line please refer to the individual product descriptions in the crop database for DAS-59122-7 and NK603.</p>\n\n<p style="text-align: justify;">The inserted genes and their gene products have a history of safe use, and have undergone review and approval by several regulatory agencies. No interactions among the gene products or negative synergistic effects are expected in the stacked hybrid. The Cry34Ab1 and Cry35Ab1 proteins are not enzymes and therefore do not affect plant metabolism. The CP4 EPSPS has high affinity for its substrates phosphoenolpyruvate (PEP) and shikimate-3-phosphate, which are part of the shikimate metabolic pathway. Similarly, the PAT protein has a very high affinity for L-Phosphinothricin, the active ingredient in the herbicide glufosinate ammonium. PAT, CP4 EPSPS, Cry34Ab1 and Cry35Ab1 are therefore not expected to interact within nor affect the metabolism of the stacked hybrid.</p>\n', 'Enabled', NULL, '2013-08-30 00:36:57'),
(90, 118, '<p style="text-align: justify;">DAS-59122-7 X TC1507 X NK603 (OECD identifier: DAS-59122-7 X DAS-&Oslash;15&Oslash;7-1 X MON-00603-6) maize is a hybrid resulting from crossing the coleopteran-resistance maize line DAS-59122-7 with the lepidoteran-resistant maize line TC1507 and the herbicide-tolerant maize line NK603. This stacked maize hybrid is a product of traditional plant breeding, and therefore is not automatically subject to regulation in all jurisdictions as are transgenic plants resulting from recombinant DNA technologies. Certain jurisdictions may request notification in advance of the release of a stacked hybrid, or may request information to conduct an environmental and food safety assessment. Examples of jurisdictions that require either notification or information about stacked hybrids prior to their release into the environment, and for use in human food and livestock feed are Japan and Korea.</p>\n\n<p style="text-align: justify;">The stacked hybrid DAS-59122-7 X TC1507 X NK603 expresses five novel proteins: the insect control proteins (delta-endotoxins) Cry34Ab1 and Cry35Ab1, which are insecticidal to coleopterans such as the Corn Rootworm, and Cry1F which confers resistance to the European Corn Borer and other lepidopterans, together with the PAT protein which confers tolerance to the herbicide glufosinate ammonium, and the CP4 EPSPS protein which confers resistance to the herbicide glyphosate. The insecticidal proteins Cry34Ab1 and Cry35Ab1 are produced by the <i>cry</i>34Ab1 and <i>cry</i>35Ab1 genes from DAS-59122-7. The Cry1F insecticidal protein is produced by the <i>cry</i>1F gene from TC1507 and PAT is produced by the <i>pat</i> gene, contained in both DAS-59122-7 and TC1507. The CP4 EPSPS protein is produced by the <i>cp4 epsps</i> gene from NK603. The novel traits of each parental line have been combined, through traditional plant breeding, to produce this new hybrid. For a full description of each parental line please refer to the individual product descriptions in the crop database for DAS-59122-7, TC1507 and NK603.</p>\n\n<p style="text-align: justify;">The inserted genes and their gene products have a history of safe use, and have undergone review and approval by several regulatory agencies. No interactions among the gene products or negative synergistic effects are expected in the stacked hybrid. The Cry34Ab1, Cry35Ab1 and Cry1F proteins are not enzymes and therefore do not affect plant metabolism. Both the PAT and CP4 EPSPS have high substrate affinities: PAT for L-Phosphinothricin, the active ingredient in glufosinate ammonium, and CP4 EPSPS for phosphoenolpyruvate (PEP) and shikimate-3-phosphate, which are part of the shikimate metabolic pathway. Since both PAT and CP4 EPSPS differ in substrates and in mode of action, these are not expected to interact within, nor affect the metabolism of the stacked hybrid.</p>\n', 'Enabled', NULL, '2013-08-30 00:37:41'),
(91, 120, '<p style="text-align: justify;">LLCotton25 x MON15985 (OECD identifier: ACS- GH&Oslash;&Oslash;1-3 x MON-15985-7) cotton is the product of the cross-breeding of the herbicide-tolerant cotton line LLCotton25 (OECD: ACS-GH&Oslash;&Oslash;1-3) with the insect-resistant cotton line 15985 (MON-15985-7). This stacked cotton line is a product of traditional plant breeding, and therefore is not automatically subject to regulation in all jurisdictions as are transgenic plants resulting from recombinant DNA technologies. Certain jurisdictions may request notification in advance of the release of a stacked hybrid, or may request information to conduct an environmental and food safety assessment. Examples of jurisdictions that require either notification or information about stacked hybrids prior to their release into the environment, and for use in human food and livestock feed are Japan and the Philippines.</p>\n\n<p style="text-align: justify;">The stacked cotton line LLCotton25 x MON15985 expresses three novel proteins: the enzyme phosphinothricin acetyl-transferase (PAT) and the delta-endotoxins Cry1Ac and Cry2Ab, both of which confer resistance to the lepidopteran pests of cotton, such as the cotton bollworm, pink bollworm and tobacco budworm. The insecticidal proteins Cry1Ac and Cry2Ab are produced by the <i>cry</i>1Ac and <i>cry</i>2Ab genes respectively, both of which were originally isolated from <i>Bacillus thuringiensis</i> and are derived from MON15985. The <i>bar</i> gene, which codes for the production of PAT, is derived from LLCotton25. This enzyme acetylates glufosinate ammonium, rendering it inactive in the plant. The expression of the <i>bar</i> gene in LLCotton25 allows it to survive the otherwise lethal application of glufosinate ammonium. The bar gene was isolated from <i>Streptomyces hygroscopius</i>, a gram-positive soil bacterium. The novel traits of each parental line have been combined, through traditional plant breeding, to produce this new cotton line. For a full description of each parental line please refer to the individual product descriptions in the crop database for LLCotton25 and MON15985.</p>\n\n<p style="text-align: justify;">The inserted genes and their gene products have a history of safe use, and have undergone review and approval by several regulatory agencies. No interactions among the gene products or negative synergistic effects are expected in the stacked hybrid. Since neither Cry1Ac, nor Cry2Ab are enzymes, these proteins have no effect on plant metabolism. PAT has high affinity for its substrate L-Phosphinothricin, the active ingredient in glufosinate ammonium. PAT, Cry1Ac and Cry2Ab are therefore not expected to interact within, nor affect the metabolism of the stacked line.</p>\n', 'Enabled', NULL, '2013-08-30 00:39:13'),
(92, 115, '<p style="text-align: justify;">MON15985 x MON88913 (OECD identifier: MON-15985-7 x MON-88913-8) cotton is the product of the cross-breeding of the insect-resistant cotton line 15985 (MON-15985-7) with the herbicide-tolerant cotton line MON88913 (OECD: MON-88913-8). This stacked cotton line is a product of traditional plant breeding, and therefore is not automatically subject to regulation in all jurisdictions as are transgenic plants resulting from recombinant DNA technologies. Certain jurisdictions may request notification in advance of the release of a stacked hybrid, or may request information to conduct an environmental and food safety assessment. Examples of jurisdictions that require either notification or information about stacked hybrids prior to their release into the environment, and for use in human food and livestock feed are Japan and the Philippines.</p>\n\n<p style="text-align: justify;">The stacked cotton line 15985 X MON88913 expresses three novel proteins: the delta-endotoxins Cry1Ac and Cry2Ab, both of which confer resistance to the lepidopteran pests of cotton, such as the cotton bollworm, pink bollworm and tobacco budworm, and the CP4 EPSPS protein which confers tolerance to the herbicide glyphosate. The insecticidal proteins Cry1Ac and Cry2Ab are produced by the <i>cry1Ac</i> gene and <i>cry2Ab</i> genes respectively, both of which are from 15985. The CP4 EPSPS protein is produced by two <i>cp4 epsps</i> genes from MON88913 to confer tolerance to glyphosate later in the growing season, specifically after the fifth true leaf stage. The novel traits of each parental line have been combined, through traditional plant breeding, to produce this new cotton line. For a full description of each parental line please refer to the individual product descriptions in the crop database for 15985 and MON88913.</p>\n\n<p style="text-align: justify;">The inserted genes and their gene products have a history of safe use, and have undergone review and approval by several regulatory agencies. No interactions among the gene products or negative synergistic effects are expected in the stacked hybrid. Since neither Cry1Ac, nor Cry2Ab are enzymes, these proteins have no effect on plant metabolism. The CP4 EPSPS has high affinity for its substrates phosphoenolpyruvate (PEP) and shikimate-3-phosphate, which are part of the shikimate metabolic pathway. CP4 EPSPS, Cry1Ac and Cry2Ab are therefore not expected to interact within, nor affect the metabolism of the stacked line.</p>\n', 'Enabled', NULL, '2013-08-30 00:35:39'),
(93, 114, '<p style="text-align: justify;">MON810 X MON88017 (OECD identifier: MON-&Oslash;&Oslash;81&Oslash;-6 X MON-88&Oslash;17-3) maize is an F1 hybrid resulting from the hybridization of maize inbred MON 810 (MON-&Oslash;&Oslash;81&Oslash;-6) with MON88017 (MON-88&Oslash;17-3). This stacked maize hybrid is a product of traditional plant breeding, and therefore is not automatically subject to regulation in all jurisdictions as are transgenic plants resulting from recombinant DNA technologies. Certain jurisdictions may request notification in advance of the release of a stacked hybrid, or may request information to conduct an environmental and food safety assessment. Examples of jurisdictions that require either notification or information about stacked hybrids prior to their release into the environment, and for use in human food and livestock feed are Canada and Japan.</p>\n\n<p style="text-align: justify;">The stacked hybrid MON810 X MON88017 expresses three novel proteins: CP4 EPSPS which confers tolerance to the herbicide glyphosate, and the delta-endotoxins Cry1Ab, which confers resistance to the European Corn Borer and other lepidopterans, and Cry3Bb1 which confers resistance to Corn Rootworm. The insecticidal protein Cry1Ab, is produced by the <i>cry</i>1Ab gene from MON810. The insecticidal protein Cry3Bb1, is produced by the <i>cry</i>3Bb1 gene and the CP4 EPSPS protein is produced by the <i>cp4 epsps</i> gene both from MON88017. The novel traits of each parent line have been combined, through traditional plant breeding, to produce this new hybrid. For a full description of each parent line please refer to the individual product descriptions in the crop database for MON810 and MON88017.</p>\n\n<p style="text-align: justify;">The inserted genes and their gene products have a history of safe use, and have undergone review and approval by several regulatory agencies. No interactions among the gene products or negative synergistic effects are expected in the stacked hybrid. The Cry1Ab and Cry3Bb1 proteins are not enzymes and therefore do not affect plant metabolism. The CP4 EPSPS has high affinity for its substrates phosphoenolpyruvate (PEP) and shikimate-3-phosphate, which are part of the shikimate metabolic pathway. These proteins are therefore not expected to interact within, nor affect the metabolism of the stacked hybrid</p>\n', 'Enabled', NULL, '2013-08-30 00:35:01'),
(94, 116, '<p style="text-align: justify;">TC1507 X DAS-59122-7(OECD identifier: DAS-&Oslash;15&Oslash;7-1 X DAS-59122-7) maize is an F1 hybrid resulting from the hybridization of the lepidopteran-resistant inbred maize TC1507 with the coleopteran-resistant maize inbred DAS-59122-7 and marketed as Herculex&reg; XTRA. This stacked maize hybrid is a product of traditional plant breeding, and therefore is not automatically subject to regulation in all jurisdictions as are transgenic plants resulting from recombinant DNA technologies. Certain jurisdictions may request notification in advance of the release of a stacked hybrid, or may request information to conduct an environmental and food safety assessment. Examples of jurisdictions that require either notification or information about stacked hybrids prior to their release into the environment, and for use in human food and livestock feed are Japan and Korea.</p>\n\n<p style="text-align: justify;">The stacked hybrid TC1507 X DAS-59122-7 expresses four novel proteins: the delta-endotoxin Cry1F which confers resistance to the European Corn Borer and other lepidopterans, Cry34Ab1 and Cry35Ab1, which are also delta-endotoxins in this case insecticidal to coleopterans such as the Corn Rootworm, and the PAT protein which confers tolerance to the herbicide glufosinate ammonium. The Cry1F protein is produced by the <i>cry</i>1F gene and PAT is produced by the <i>pat</i> gene, both from TC1507. The Cry34Ab1 and Cry35Ab1 insecticidal proteins are produced by the <i>cry</i>34Ab1 and <i>cry</i>35Ab1 genes from DAS-59122-7, which also contains a copy of the <i>pat</i> gene. The novel traits of each parental line have been combined, through traditional plant breeding, to produce this new hybrid. For a full description of each parental line please refer to the individual product descriptions in the crop database for TC1507 and DAS-59122-7.</p>\n\n<p style="text-align: justify;">The inserted genes and their gene products have a history of safe use, and have undergone review and approval by several regulatory agencies. No interactions among the gene products or negative synergistic effects are expected in the stacked hybrid. The Cry1F, Cry34Ab1 and Cry35Ab1 proteins are not enzymes and therefore do not affect plant metabolism. The PAT enzyme has a high substrate affinity for L-Phosphinothricin, the active ingredient in glufosinate ammonium. These proteins are not expected to interact within, nor affect the metabolism of the stacked hybrid.</p>\n', 'Enabled', NULL, '2013-08-30 00:36:19'),
(95, 128, '<p style="text-align: justify;">MIR604 X GA21 (OECD identifier: SYN-IR6&Oslash;4-5 x MON-&Oslash;&Oslash;&Oslash;21-9) maize is an F1 hybrid resulting from the hybridization of the coleopteran-resistant maize line MIR604 (SYN-IR6&Oslash;4-5) and the herbicide-tolerant maize line GA21 (MON-&Oslash;&Oslash;&Oslash;21-9). This stacked maize hybrid is a product of traditional plant breeding, and therefore is not automatically subject to regulation in all jurisdictions as are transgenic plants resulting from recombinant DNA technologies. Certain jurisdictions may request notification in advance of the release of a stacked hybrid, or may request information to conduct an environmental and food safety assessment. Examples of jurisdictions that require either notification or information about stacked hybrids prior to their release into the environment, and for use in human food and livestock feed are Japan and Korea.</p>\n\n<p style="text-align: justify;">The stacked hybrid MIR604 X GA21 expresses three novel proteins: the delta-endotoxin mCry3A which confers resistance to corn rootworm (<i>Diabrotica</i> species), the PMI protein which allows growth on mannose as a carbon source and is used as a selectable marker, and a modified EPSPS protein which confers tolerance to the herbicide glyphosate. The modified EPSPS protein is produced by the <i>mepsps</i> gene from GA21, the insecticidal protein mCry3A is produced by the <i>mcry</i>3A gene and PMI is produced by the <i>pmi</i> gene, both from MIR604. The novel traits of each parental line have been combined, through traditional plant breeding, to produce this new hybrid. For a full description of each parental line please refer to the individual product descriptions in the crop database for MIR604 and GA21.</p>\n\n<p style="text-align: justify;">The inserted genes and their gene products have a history of safe use, and have undergone review and approval by several regulatory agencies. No interactions among the gene products or negative synergistic effects are expected in the stacked hybrid. The mCry3A protein is not an enzyme and therefore does not affect plant metabolism. PMI has a high affinity for mannose-6-phosphate, converting it to fructose-6-phosphate which is directly utilised by the plant. The modified EPSPS has high affinity for its substrates phosphoenolpyruvate (PEP) and shikimate-3-phosphate, which are part of the shikimate metabolic pathway. PMI, EPSPS and mCry3A are therefore not expected to interact within, nor affect the metabolism of the stacked hybrid.</p>\n', 'Enabled', NULL, '2013-08-30 00:49:24');
INSERT INTO `gmcropdatabase_events_introductions` (`id`, `eventId`, `description`, `status`, `created`, `updated`) VALUES
(96, 129, '<p style="text-align: justify;">BT11 x MIR604 (OECD identifier: SYN-BT&Oslash;11-1 x SYN-IR6&Oslash;4-5) maize is an F1 hybrid resulting from the hybridization of the lepidopteran-resistant and glufosinate-tolerant maize line BT11 (SYN-BT&Oslash;11-1) and the coleopteran-resistant maize line MIR604 (SYN-IR6&Oslash;4-5). This stacked maize hybrid is a product of traditional plant breeding, and therefore is not automatically subject to regulation in all jurisdictions as are transgenic plants resulting from recombinant DNA technologies. Certain jurisdictions may request notification in advance of the release of a stacked hybrid, or may request information to conduct an environmental and food safety assessment. Examples of jurisdictions that require either notification or information about stacked hybrids prior to their release into the environment, and for use in human food and livestock feed are Japan and Korea.</p>\n\n<p style="text-align: justify;">The stacked hybrid BT11 x MIR604 expresses four novel proteins: the delta-endotoxin Cry1Ab which confers resistance to the European Corn Borer and other lepidopterans, the PAT protein which confers tolerance to the herbicide glufosinate ammonium, the delta-endotoxin mCry3A which confers resistance to corn rootworm (<i>Diabrotica</i> species), and the PMI protein which allows growth on mannose as a carbon source and is used as a selectable marker. The insecticidal protein Cry1Ab is produced by the <i>cry</i>1Ab gene and PAT is produced by the <i>pat</i> gene, both from BT11, the insecticidal protein mCry3A is produced by the <i>mcry</i>3A gene and PMI is produced by the <i>pmi</i> gene, both from MIR604. The novel traits of each parental line have been combined, through traditional plant breeding, to produce this new hybrid. For a full description of each parental line please refer to the individual product descriptions in the crop database for BT11 and MIR604.</p>\n\n<p style="text-align: justify;">The inserted genes and their gene products have a history of safe use, and have undergone review and approval by several regulatory agencies. No interactions among the gene products or negative synergistic effects are expected in the stacked hybrid. The Cry1Ab and mCry3A proteins are not enzymes and therefore do not affect plant metabolism. PAT has a high affinity for L-Phosphinothricin, the active ingredient in glufosinate ammonium and PMI has a high affinity for mannose-6-phosphate, converting it to fructose-6-phosphate which is directly utilised by the plant. PMI, PAT, Cry1Ab and mCry3A are therefore not expected to interact within, nor affect the metabolism of the stacked hybrid.</p>\n', 'Enabled', NULL, '2013-08-30 00:49:57'),
(97, 130, '<p style="text-align: justify;">BT11 x MIR604 x GA21 (OECD identifier: SYN-BT&Oslash;11-1 x SYN-IR6&Oslash;4-5 x MON-&Oslash;&Oslash;&Oslash;21-9) maize is an F1 hybrid resulting from the hybridization of the lepidopteran-resistant and glufosinate-tolerant maize line BT11 (SYN-BT&Oslash;11-1), the coleopteran-resistant maize line MIR604 (SYN-IR6&Oslash;4-5) and the glyphosate-tolerant maize line GA21 (MON-&Oslash;&Oslash;&Oslash;21-9).. This stacked maize hybrid is a product of traditional plant breeding, and therefore is not automatically subject to regulation in all jurisdictions, as are transgenic plants resulting from recombinant DNA technologies. Certain jurisdictions may request notification in advance of the release of a stacked hybrid, or may request information to conduct an environmental and food safety assessment. Examples of jurisdictions that require either notification or information about stacked hybrids prior to their release into the environment, and for use in human food and livestock feed are Japan and Korea.</p>\n\n<p style="text-align: justify;">The stacked hybrid BT11 x MIR604 x GA21 expresses five novel proteins: the delta-endotoxin Cry1Ab which confers resistance to the European Corn Borer and other lepidopterans, the PAT protein which confers tolerance to the herbicide glufosinate ammonium, the delta-endotoxin mCry3A which confers resistance to corn rootworm (<i>Diabrotica</i> species), the PMI protein which allows growth on mannose as a carbon source and is used as a selectable marker, and a modified EPSPS protein which confers tolerance to the herbicide glyphosate. The insecticidal protein Cry1Ab is produced by the <i>cry</i>1Ab gene and PAT is produced by the <i>pat</i> gene, both from BT11, the insecticidal protein mCry3A is produced by the <i>mcry</i>3A gene and PMI is produced by the <i>pmi</i> gene, both from MIR604. The modified EPSPS protein is produced by the <i>mepsps</i> gene from GA21. The novel traits of each parental line have been combined, through traditional plant breeding, to produce this new hybrid. For a full description of each parental line please refer to the individual product descriptions in the crop database for BT11, MIR604 and GA21.</p>\n\n<p style="text-align: justify;">The inserted genes and their gene products have a history of safe use, and have undergone review and approval by several regulatory agencies. No interactions among the gene products or negative synergistic effects are expected in the stacked hybrid. The Cry1Ab and mCry3A proteins are not enzymes and therefore do not affect plant metabolism. PAT has a high affinity for L-Phosphinothricin, the active ingredient in glufosinate ammonium and PMI has a high affinity for mannose-6-phosphate, converting it to fructose-6-phosphate which is directly utilised by the plant. The modified EPSPS has high affinity for its substrates phosphoenolpyruvate (PEP) and shikimate-3-phosphate, which are part of the shikimate metabolic pathway. PMI, PAT, Cry1Ab, mCry3A and mEPSPS are therefore not expected to interact within, nor affect the metabolism of the stacked hybrid.</p>\n', 'Enabled', NULL, '2013-08-30 00:50:52'),
(98, 127, '<p style="text-align: justify;">Plum pox, also known as sharka, is the most devastating viral disease worldwide of stone fruit including peaches, apricots, plums, nectarines, almonds, and sweet and tart cherries. The disease significantly limits stone fruit production in areas where it is established. More than 100 million stone fruit trees in Europe are infected. First described on plums in Bulgaria in 1915, plum pox has spread to a large part of Europe, the Mediterranean, the Middle East (Egypt and Syria), India, and Chile. In 1999, for the first time in North America, plum pox was detected in a Pennsylvania orchard.</p>\n\n<p style="text-align: justify;">The virus causing the disease is plum pox potyvirus (PPV). PPV infects various members of the genus <i>Prunus</i>, such as the stone fruit trees mentioned above. Wild and ornamental species of this genus may also become infected by some strains of the virus. Some weed hosts identified in the field and numerous hosts tested in laboratory settings have also been known to become infected with PPV.</p>\n\n<p style="text-align: justify;">Plum pox is economically important because it can cause fruit to be unmarketable and can decrease the yield of infected trees. The severity of the disease depends on the strain of the virus present and the susceptibility of <i>Prunus</i> cultivars (cultivated varieties of plants). The presence of PPV can enhance the effects of other endemic viruses infecting various species of the genus <i>Prunus</i>, such as prune dwarf virus, Prunus necrotic ringspot virus (causes browning), and apple chlorotic leaf spot virus (causes yellowing), resulting in still greater economic losses. In southeastern France, a newly identified strain of PPV induces severe necrosis, resulting in early leaf drop and tree decline, even in the absence of endemic <i>Prunus</i> viruses.</p>\n\n<p style="text-align: justify;">Plum pox is spread from plant to plant by several aphid vectors (insects that suck sap from plants then carry the virus to other plants) and is also transmitted in budwood used for grafting. Studies indicate that at least 14 aphid species can transmit PPV. These species include <i>Myzus persicae</i>, <i>Aphis spiraecola</i>, <i>A. gossypii</i>, and <i>A. fabae</i>. Some PPV strains have been identified that are not transmissible by aphids. Control and prevention measures for PPV include field surveys, use of certified nursery materials, use of resistant plants (when available), control of aphids, and elimination of infected trees in nurseries and orchards.</p>\n\n<p style="text-align: justify;">Sources of resistance exist in <i>Prunus</i> but are not abundant and, for this reason, a genetically engineered PPV-resistant plum has been developed using the coat protein gene from the virus itself. Multiple insertions of the gene have been identified in the plant, but no coat protein is produced by these genes. The resistance is due to RNA silencing, where the expression of a transgene induces the plant to degrade RNA of the same sequence, including any RNA from an infecting virus, thus preventing infection.</p>\n\n<p style="text-align: justify;">In addition to the use of the engineered variety for direct production, the resistance can by transferred through hybridization to other plum trees. This provides a unique source of germplasm for future breeding programs worldwide as there are few sources of resistance to this disease in conventional germplasm and they have proved difficult to introgress into cultivated varieties. In the United States, there are no plans at this time (2007) to release the transgenic varieties for commercial use as the disease is being controlled though quarantine practices, however discussions with breeders have initiated to develop plans for the deployment of this trait should the need arise.</p>\n', 'Enabled', NULL, '2013-08-30 00:47:19'),
(99, 132, '<p style="text-align: justify;">Maize (Zea mays L), otherwise known as corn, is the world&rsquo;s third leading cereal crop, behind wheat and rice, and is grown in over 25 countries worldwide. The majority of grain and forage derived from maize is used as animal feed, however maize also has a long history of safe use as food for human consumption. The grain can be processed into industrial products such as ethanol (by fermentation), and highly refined starch (by wetmilling) and sweetener products. In addition to milling, the maize germ can be processed to obtain corn oil and numerous other products. The majority of maize is grown for animal feed production and human food, however an increasing percentage is being used for the production of ethanol as a biofuel alternative to petroleum products from fossil sources.</p>\n\n<p style="text-align: justify;">MON 89034 was developed as a second generation insect-resistant maize product to provide enhanced benefits for the control of lepidopteran insect pests. MON 89034 produces the Cry1A.105 and Cry2Ab2 proteins derived from <i>Bacillus thuringiensis</i>, which are active against lepidopteran insect pests. MON 89034 is intended to serve farmers&#39; needs for controlling a wider spectrum of lepidopteran pests and help assure the durability of insect-resistant maize. MON 89034 provides control of <i>Ostrinia</i> species such as European corn borer (ECB) and Asian corn borer, and <i>Diatraea</i> species such as southwestern corn borer (SWCB) and sugarcane borer. MON 89034 also provides a high level control of fall armyworm (FAW) throughout the season and improved protection from damage caused by corn earworm (CEW). In addition to the wider spectrum of insect control, the combination of the Cry1A.105 and Cry2Ab2 insecticidal proteins in a single plant provides a much more effective insect resistance management (IRM) tool. The results of mathematical modeling indicate that biotechnology-derived plants expressing two Cry proteins will have significantly greater durability than plants producing either of the single proteins if the cross-resistance between the Cry proteins is low and the mortality of susceptible insects caused by each of the individual proteins is at least 90%. Comparative biophysical studies indicate that the Cry1A.105 and Cry2Ab2 proteins have important differences in their mode of action, specifically in the way in which they bind to the lepidopteran midgut. Therefore, the probability of cross-resistance between these two proteins is low. Furthermore, <i>in vitro</i> and <i>in planta</i> studies with Cry1A.105 and Cry2Ab2 demonstrate that both proteins are highly active against the primary lepidopteran pests of corn (ECB, SWCB, CEW, and FAW), particularly ECB, achieving close to or greater than the critical 95% level of control in all cases.</p>\n', 'Enabled', NULL, '2013-08-30 00:54:24'),
(100, 133, '<p style="text-align: justify;">Soybean (<i>Glycine max</i> L. Merr.), is grown primarily for its seed which has many uses in the food and industrial sectors and represents one of the major sources of edible vegetable oil and of proteins for livestock feed use. A major food use of soybean in North America and Europe is as purified oil, used in margarines, shortenings, and cooking and salad oils. It is also a major ingredient in food products such as tofu, tempeh, soya sauce, simulated milk and meat products, and is a minor ingredient in many processed foods. Soybean meal is used as a supplement in feed rations for livestock. The major producers of soybeans are the United States, Brazil, Argentina, China, India, Paraguay and Canada.</p>\n\n<p style="text-align: justify;">Weeds are a major production problem in soybean cultivation. Typically, weeds are managed using a combination of cultural (<i>e.g.</i> seed bed preparation, using clean seed, variety selection, and planting date) and chemical controls. Depending on the production area and the prevalent weed species, herbicides may be applied before planting (<i>e.g.</i> pendimethalin, trifluralin, metribuzin), after planting but before emergence (<i>e.g.</i> pendimethalin, linuron, imazethapyr), and/or after emergence (<i>e.g.</i> bentazon, acifluorfen, fomesafen). Commonly, several different herbicides are required to adequately control weeds in soybean fields.</p>\n\n<p style="text-align: justify;">DP356043 has been transformed to express two novel genes, providing tolerance to two different classes of herbicide. The line contains two genes; <i>gat4601</i> which provides tolerance to glyphosate by detoxifying the compound, while <i>gm-hra</i> encodes for a modified acetolactate synthase (ALS) enzyme which is not affected by the imidazolinone class of ALS inhibiting herbicides. The <i>gat4601</i> gene is based on the sequences of three <i>gat</i> genes from the common soil bacterium <i>Bacillus licheniformis</i>. The GAT4601 protein is 84% homologous to each of the three native GAT proteins from which it was derived. In DP356043, the expression of the <i>gat4601</i> gene is driven by the constitutive synthetic core promoter SCP1. The GM-HRA protein in DP356043 is a modified version of the soybean GM-ALS protein. GM-ALS is involved in branched chain amino acid (leucine, isoleucine and valine) biosynthesis in the plastid. The herbicide tolerant <i>gm-hra</i> gene was made by isolating the herbicide sensitive soybean <i>gm-als</i> gene and introducing two specific amino acid changes, known to confer herbicide tolerance to tobacco ALS. The GM-HRA protein is &gt;99% homologous to the native GM-ALS protein from which it was derived. In DP356043, the expression of the <i>gm-hra</i> gene is driven by the soybean constitutive S-adenosyl-L-methionine synthetase (SAMS) promoter.</p>\n', 'Enabled', NULL, '2013-08-30 00:56:43'),
(101, 134, '<p style="text-align: justify;">MON89034 X MON88017 (OECD identifier: MON-89&Oslash;34-3 X MON-88&Oslash;17-3) maize is an F1 hybrid resulting from the hybridization of maize inbred MON89034 (MON-89&Oslash;34-3) with MON88017 (MON-88&Oslash;17-3). This stacked maize hybrid is a product of traditional plant breeding, and therefore is not automatically subject to regulation in all jurisdictions as are transgenic plants resulting from recombinant DNA technologies. Certain jurisdictions may request notification in advance of the release of a stacked hybrid, or may request information to conduct an environmental and food safety assessment. Examples of jurisdictions that require either notification or information about stacked hybrids prior to their release into the environment, and for use in human food and livestock feed are Canada and Japan.</p>\n\n<p style="text-align: justify;">The stacked hybrid MON89034 X MON88017 expresses three novel insecticidal proteins and a protein providing tolerance to the herbicide glyphosate. MON 89034 produces the Cry1A.105 and Cry2Ab2 proteins, which are active against lepidopteran insect pests and MON88017 produces Cry3Bb1 which confers resistance to Corn Rootworm. All of these proteins are derived from <i>Bacillus thuringiensis</i>. Tolerance to glyphosate is provided by the CP4 EPSPS protein, produced by the <i>cp4 epsps</i> gene from MON88017. The novel traits of each parent line have been combined, through traditional plant breeding, to produce this new hybrid. For a full description of each parent line please refer to the individual product descriptions in the crop database for MON89034 and MON88017.</p>\n\n<p style="text-align: justify;">The inserted genes and their gene products have a history of safe use, and have undergone review and approval by several regulatory agencies. No interactions among the gene products or negative synergistic effects are expected in the stacked hybrid. The Cry1A.105, Cry2Ab2 and Cry3Bb1 proteins are not enzymes and therefore do not affect plant metabolism. The CP4 EPSPS has high affinity for its substrates phosphoenolpyruvate (PEP) and shikimate-3-phosphate, which are part of the shikimate metabolic pathway. These proteins are therefore not expected to interact within, nor affect the metabolism of the stacked hybrid.</p>\n', 'Enabled', NULL, '2013-08-30 00:59:24'),
(102, 135, '<p style="text-align: justify;">MON89034 X NK603 (OECD identifier: MON-89&Oslash;34-3 X MON-&Oslash;&Oslash;6&Oslash;3-6) maize is an F1 hybrid resulting from the hybridization of maize inbred MON89034 (MON-89&Oslash;34-3) with NK603 (MON-&Oslash;&Oslash;6&Oslash;3-6). This stacked maize hybrid is a product of traditional plant breeding, and therefore is not automatically subject to regulation in all jurisdictions as are transgenic plants resulting from recombinant DNA technologies. Certain jurisdictions may request notification in advance of the release of a stacked hybrid, or may request information to conduct an environmental and food safety assessment. Examples of jurisdictions that require either notification or information about stacked hybrids prior to their release into the environment, and for use in human food and livestock feed are Canada and Japan.</p>\n\n<p style="text-align: justify;">The stacked hybrid MON89034 X NK603 expresses two novel insecticidal proteins and a protein providing tolerance to the herbicide glyphosate. MON 89034 produces the Cry1A.105 and Cry2Ab2 proteins derived from <i>Bacillus thuringiensis</i>, which are active against lepidopteran insect pests. Tolerance to glyphosate is provided by the CP4 EPSPS protein, produced by the <i>cp4 epsps</i> gene from NK603. The novel traits of each parent line have been combined, through traditional plant breeding, to produce this new hybrid. For a full description of each parent line please refer to the individual product descriptions in the crop database for MON89034 and NK603.</p>\n\n<p style="text-align: justify;">The inserted genes and their gene products have a history of safe use, and have undergone review and approval by several regulatory agencies. No interactions among the gene products or negative synergistic effects are expected in the stacked hybrid. The Cry1A.105 and Cry2Ab2 proteins are not enzymes and therefore do not affect plant metabolism. The CP4 EPSPS has high affinity for its substrates phosphoenolpyruvate (PEP) and shikimate-3-phosphate, which are part of the shikimate metabolic pathway. These proteins are therefore not expected to interact within, nor affect the metabolism of the stacked hybrid.</p>\n', 'Enabled', NULL, '2013-08-30 01:00:01'),
(103, 136, '<p style="text-align: justify;">Corn line 98140 was genetically engineered to express the GAT4621 (glyphosate acetyltransferase) and ZM-HRA (modified version of a maize acetolactate synthase) proteins. The GAT4621 protein, encoded by the <i>gat4621</i> gene, confers tolerance to glyphosate-containing herbicides by acetylating glyphosate and thereby rendering it non-phytotoxic. The ZM-HRA protein, encoded by the <i>zm-hra</i> gene, confers tolerance to the ALS-inhibiting class of herbicides.</p>\n\n<p style="text-align: justify;">The <i>gat4621</i> gene is based on the sequences of three <i>gat</i> genes from the common soil bacterium <i>Bacillus licheniformis</i>. <i>B. licheniformis</i> is widespread in the environment; therefore, animals and humans are regularly exposed without adverse consequences to this organism and its components, such as the glyphosate acetyltransferase (GAT) protein. GAT proteins are members of the GCN 5-related family of N-acetyltransferases (also known as the GNAT family). The GNAT superfamily is one of the largest enzyme superfamilies recognized to date with over 10,000 representatives from plants, animals and microbes. The GAT4621 protein is 75-78% identical and 90-91% similar at the amino acid level to each of the three native GAT enzymes from which it was derived. In 98140 corn, the expression of the <i>gat4621</i> gene is driven by the maize ubiquitin promoter.</p>\n\n<p style="text-align: justify;">The ZM-HRA protein is a modified version of the maize acetolactate synthase (ALS) enzyme, which is involved in branched chain amino acid (leucine, isoleucine and valine) biosynthesis in the plastid. The herbicide tolerant <i>zm-hra</i> gene was made by isolating the herbicide sensitive maize <i>als</i> gene and introducing two specific amino acid changes known to confer herbicide tolerance to tobacco ALS. In 98140 corn, the expression of the <i>zm-hra</i> gene is driven by the maize ALS promoter.</p>\n\n<p style="text-align: justify;">The dual herbicide tolerance of 98140 corn will enable growers to choose an optimal combination of these herbicides to best manage their individual weed populations. The availability of 98140 corn will enable growers to proactively manage weed populations while delaying adverse population shifts of troublesome weeds or the development of resistance. Herbicide tolerant 98140 corn will be marketed in the U.S. under the brand name Optimum&trade; GAT&trade;.</p>\n', 'Enabled', NULL, '2013-08-30 01:00:27'),
(104, 137, '<p style="text-align: justify;">Maize is susceptible to attack by a variety of insects from the time it is planted until it is consumed as food or feed. The most economically significant insect pests of maize are: <i>Ostrinia nubilalis</i> (European corn borer), <i>Diatraea saccharalis</i> (sugarcane borer), <i>Diatraea grandiosella</i> (southwestern corn borer), <i>Diabrotica</i> spp. (corn rootworm complex), <i>Helicoverpa zea</i> (corn earworm/cotton bollworm), <i>Spodoptera frugiperda</i> (fall armyworm), <i>Agrotis ipsilon</i> (black cutworm), <i>Elasmopalpus lignosellus</i> (lesser cornstalk borer), <i>Rhopalosiphum maidis</i> (corn leaf aphids), and <i>Striacosta albicosta</i> (western bean cutworm). Pests of secondary economic importance in maize include both soil-dwelling insects that feed on roots (e.g., wireworms, billbugs, webworms, white grubs, corn root aphids, the seed corn maggot, grape colaspis and seedcorn beetles) and above-ground insects that attack the stalk, leaf, and ear (e.g., cutworms, chinch bugs, grasshoppers, corn fl ea beetles and Japanese beetles).</p>\n\n<p style="text-align: justify;">While crop losses attributable to <i>O. nubilalis</i> and Diabrotica infestations have been well characterized and are significant, there is not as much quantitative information available on the economic impacts of other major insect pests of maize, specifically <i>H. zea</i>, <i>S. frugiperda</i>, <i>A. ipsilon</i>, and <i>S. albicosta</i>. These pests are not as widespread as corn borers and rootworms; however, crop infestations by these leaf and ear-feeding pests can be very costly to growers, as they have the potential to significantly lower grain yield and quality. Conventional insecticide applications are an option for reducing feeding damage caused by these insects; however, most growers do not treat their crops to control these pests because of cost and limited effectiveness of the chemical agents. Currently available novel varieties are not as efficacious against these lepidopteran insects as they are against <i>O. nubilalis</i>. For example, Bt11 maize containing the Cry1Ab toxin provides only limited or no protection against feeding damage caused by <i>H. zea</i>, <i>S. frugiperda</i>, <i>A. ipsilon</i>, and <i>S. albicosta</i>.</p>\n\n<p style="text-align: justify;">Transformation event MIR162 maize has been developed by Syngenta to provide growers with maize hybrids that are resistant to feeding damage caused by a number of lepidopteran insect pests. MIR162 maize contains a Vip3Aa protein from <i>Bacillus thuringiensis</i> that is highly toxic to <i>H. zea</i>, <i>S. frugiperda</i>,<i> A. ipsilon</i>, and <i>S. albicosta</i> larvae. In combination with an <i>O. nubilalis</i>-protected maize trait, the Vip3Aa protein in MIR162 can provide growers the means of protecting their maize crops from damage caused by a broad range of lepidopteran pests.</p>\n', 'Enabled', NULL, '2013-08-30 01:02:52'),
(105, 139, '<p style="text-align: justify;">The intended effect of the modification in 305423 soybean is to produce soybean seeds with increased levels of monounsaturated fatty acid (oleic) and decreased levels of polyunsaturated fatty acids (linoleic and linolenic). To accomplish this objective, Pioneer inserted a fragment of the soybean microsomal omega-6 desaturase gene (<i>FAD2-1</i>) into soybean. The fragment of the <i>FAD2-1</i> gene does not code for a protein. Transcription of the gene fragment under the control of a seed-preferred KTi3 promoter acts to silence the expression of the endogenous soybean omega-6 desaturase, which results in an increased level of oleic acid and decreased levels of linoleic and linolenic acids in the soybean seed. A gene (<i>gm-hra</i>) encoding a modified version of the soybean acetolactate synthase (<i>als</i> gene) that confers tolerance to a sulfonylurea herbicide was used as a selectable marker for the transformation. The 305423 soybean will be commercialized for the production of TREUS&trade; brand high oleic soybean oil. The food service industry and food processors will benefit from the fact that high oleic soybean oil is a highly stable vegetable oil that is suitable for frying applications without the need for hydrogenation. In the industrial sector, high oleic soybean oil will offer an ingredient that is stable to oxidation for the formulation of cost effective, renewable, environmentally friendly industrial fluids.</p>\n', 'Enabled', NULL, '2013-08-30 01:05:03'),
(106, 138, '<p style="text-align: justify;">BT11 x MIR162 (OECD identifier: SYN-BT&Oslash;11-1 x SYN-IR162-4) maize is an F1 hybrid resulting from the hybridization of the lepidopteran-resistant and glufosinate-tolerant maize line BT11 (SYN-BT&Oslash;11-1) and the lepidopteran-resistant maize line MIR162 (SYN-IR162-4). This stacked maize hybrid is a product of traditional plant breeding, and therefore is not automatically subject to regulation in all jurisdictions as are transgenic plants resulting from recombinant-DNA technologies. Certain jurisdictions may request notification in advance of the release of a stacked hybrid, or may request information to conduct an environmental and food safety assessment.</p>\n\n<p style="text-align: justify;">The stacked hybrid BT11 x MIR162 expresses four novel proteins: the delta-endotoxin Cry1Ab which confers resistance to the European Corn Borer and other lepidopterans, the PAT protein which confers tolerance to the herbicide glufosinate ammonium, the vegitative insecticidal protein (VIP) 3Aa from <i>Bacillus thuringiensis</i> that is highly toxic to <i>H. zea, S. frugiperda, A. ipsilon</i>, and <i>S. albicosta</i> larvae, and the PMI protein which allows growth on mannose as a carbon source and is used as a selectable marker. The insecticidal protein Cry1Ab is produced by the <i>cry</i>1Ab gene and PAT is produced by the <i>pat</i> gene, both from BT11; the VIP3Aa protein is produced by the <i>vip3Aa20</i> gene and PMI is produced by the <i>pmi</i> gene, both from MIR162. The novel traits of each parental line have been combined, through traditional plant breeding, to produce this new hybrid.</p>\n\n<p style="text-align: justify;">While crop losses attributable to <i>O. nubilalis</i> and Diabrotica infestations have been well characterized and are significant, there is not as much quantitative information available on the economic impacts of other major insect pests of maize, specifically <i>H. zea</i>, <i>S. frugiperda</i>, <i>A. ipsilon</i>, and <i>S. albicosta</i>. These pests are not as widespread as corn borers and rootworms; however, crop infestations by these leaf and ear-feeding pests can be very costly to growers, as they have the potential to signifi cantly lower grain yield and quality. Conventional insecticide applications are an option for reducing feeding damage caused by these insects; however, most growers do not treat their crops to control these pests because of cost and limited effectiveness of the chemical agents. Currently available novel varieties are not as efficacious against these lepidopteran insects as they are against <i>O. nubilalis</i>. For example, Bt11 maize containing the Cry1Ab toxin provides only limited or no protection against feeding damage caused by <i>H. zea</i>, <i>S. frugiperda</i>, <i>A. ipsilon</i>, and <i>S. albicosta</i>. The combination of the Cry1Ab protein from BT11 and the Vip3Aa protein from MIR162 can provide growers the means of protecting their maize crops from damage caused by a broad range of lepidopteran pests.</p>\n\n<p style="text-align: justify;">For a full description of each parental line please refer to the individual product descriptions in the crop database for BT11 and MIR162.</p>\n\n<p style="text-align: justify;">The inserted genes and their gene products have a history of safe use, and have undergone review and approval by several regulatory agencies. No interactions among the gene products or negative synergistic effects are expected in the stacked hybrid. The Cry1Ab and VIP3Aa proteins do not affect plant metabolism. PAT has a high affinity for L-Phosphinothricin, the active ingredient in glufosinate ammonium and PMI has a high affinity for mannose-6-phosphate, converting it to fructose-6-phosphate which is directly utilised by the plant. PMI, PAT, Cry1Ab and Vip3Aa are therefore not expected to interact within, nor affect the metabolism of the stacked hybrid.</p>\n', 'Enabled', NULL, '2013-08-30 01:04:42'),
(107, 141, '<p style="text-align: justify;">Cotton is the United States and the worlds leading fiber crop. In the US for the 2006 production year, cotton was grown on 15.3 million acres, the major producing states being Texas (6.4 million acres), Georgia (1.4 million acres), Mississippi (1.2 million acres), Arkansas (1.2 million acres), North Carolina (0.9 million acres) and Tennessee (0.7 million acres). The world total planted area in 2005-2006 was 85 million acres, for a production of 114.1 million bales (24.8 million tons).</p>\n\n<p style="text-align: justify;">Cotton is grown in the United States using mechanized practices for planting and harvesting. Cultural practices, including irrigation and crop rotation, and herbicides are employed to control weeds. Weed management is critical to maximum cotton yield and herbicides are used on most cotton acreage grown in the United States. The grower is interested in applying a broad weed spectrum herbicide for weed control, that does not injure the crop, is cost effective, and has positive environmental attributes.</p>\n\n<p style="text-align: justify;">Glyphosate normally exerts herbicide activity by binding and inactivating EPSPS (5-enolpyruvylshikimate-3-phosphate synthase), an enzyme that is essential for the synthesis of proteins in plants. Cotton line GHB614 has been genetically modified (GM) for tolerance to glyphosate herbicides by expression in the plant of a modified <i>epsps</i> gene from corn (<i>Z. mays</i>), <i>2mepsps</i>, which introduces two amino acid changes in the enzyme. The amino acid changes in the 2mEPSPS protein significantly lower the sensitivity to glyphosate, allowing the enzyme to continue to function in the presence of the herbicide. Glyphosate has been shown to be an efficacious weed control system when utilized with glyphosate-tolerant cotton. Broad spectrum weed control is usually achieved with a single application for pre-plant burndown, and then one in-season application. GlyTol cotton event GHB614 has a broad application window which may be used to apply glyphosate, giving growers increased flexibility in their herbicide programs.</p>\n', 'Enabled', NULL, '2013-08-30 01:07:45'),
(108, 142, '<p style="text-align: justify;">Papaya ringspot virus (PRSV) is the most important papaya pathogen and a major limiting factor in commercial papaya production in the world. All major production areas I the Western Hemisphere [Brazil, the Caribbean region, Mexico, and USA (Florida and Hawaii)] and Eastern Hemisphere (the Philippines, Taiwan, Thailand, and China) are affected. Once introduced to a locality, PRSV becomes established in weeds or perennial plants and has never been successfully eradicated from any region. The aphid vectors involved in dissemination of PRSV are found worldwide. Thus, even if new PRSV-free papaya trees are planted in an area where PRSV occurs, they soon become infected.</p>\n\n<p style="text-align: justify;">Transgenic papaya expressing the coat protein (CP) gene of Hawaiian PRSV isolate HA5-1 (see description of events 55-1/63-1) is highly resistant to PRSV isolates from Hawaii but more susceptible to a number of PRSV isolates from other geographic locations. In general, resistance conferred by the CP gene of a potyvirus (such as PRSV) is RNA-mediated and sequence-specific. Resistance is only effective when the transgene has a high similarity to the CP gene of the infecting virus and appears to be due to post-transcriptional gene silencing (PTGS). PTGS can take place when the antisense RNA, either directly from transcription of an antisense CP transgene or indirectly from sense transgene mRNA via RNA-dependent RNA polymerases, binds to the complementary regions of viral RNA transcripts in the cytoplasm to form duplexes, which are subsequently cleaved by dsRNA-specific nucleases into 21-23 nt RNAs that interfere with transcription of homologous RNAs. This requirement for sequence homology points to a need to utilize local PRSV isolates as sources of the CP gene in order to obtain effective PRSV resistance in transgenic papaya.<br />\nIn addition to translatable CP genes, transgene constructs with non-translatable CP genes (e.g., antisense constructs, or frame-shift mutants, or three-in-frame stop-codon mutations) have been shown to be effective in conferring resistance to potyviruses. Papaya line X17-2 was developed to contain a frame-shift mutant of the CP gene from PRSV isolate H1K (a thymidine residue inserted after the initiation codon to yield a frame-shift). Subsequent analysis of the fifth generation progeny of the original transformant revealed that the mutation was repaired and that the CP transgene was both translatable and expressed in later generations.</p>\n', 'Enabled', NULL, '2013-08-30 01:11:34'),
(109, 143, '<p style="text-align: justify;">Transgenic cotton Event-1 was developed through specific genetic modifications to be resistant to major caterpillar pests of cotton, including <i>Helicoverpa armigera</i> (American Bollworm), <i>Pectinophora gossypiella</i> (Pink Bollworm) and <i>Earis vittella</i> (Spotted Bollworm). Event-1 express a modified gene (<i>cry1Ac</i>) that encodes an insecticidal crystalline Cry1Ac delta-endotoxin protein, derived from the soil bacterium <i>Bacillus thuringiensis</i> subsp. <i>kurstaki</i> strain HD73. Insecticidal activity is caused by the selective binding of Cry1Ac protein to specific sites localized on the brush border midgut epithelium of susceptible insect species. Following binding, cation-specific pores are formed that disrupt midgut ion flow and thereby cause gut paralysis and eventual death due to bacterial sepsis. Delta-endotoxins, such as the Cry1Ac protein expressed in cotton Event-1, exhibit highly selective insecticidal activity against a narrow range of lepidopteran insects. The specificity of action is directly attributable to the presence of specific receptors in the target insects. There are no receptors for delta-endotoxins of <i>B. thuringiensis</i> on the surface of non-lepidopteran insect guts or mammalian intestinal cells, therefore, livestock animals and humans are not susceptible to these proteins.</p>\n\n<p style="text-align: justify;">An antibiotic resistance marker gene (<i>nptII</i>) encoding the enzyme neomycin phosphotransferase II (NPTII), which inactivates aminoglycoside antibiotics such as kanamycin and neomycin, was also introduced into the genome of Event-1. This gene was derived from a bacterial transposon (Tn5 transposable element from <i>Escherichia coli</i>) and was included as a selectable marker to identify transformed plants during tissue culture regeneration and multiplication. The expression of the <i>nptII</i> gene in these plants has no agronomic significance and the safety of the NPTII enzyme as a food additive was evaluated by the United States Food and Drug Administration in 1994.</p>\n', 'Enabled', NULL, '2013-08-30 01:13:16'),
(110, 85, '<p style="text-align: justify;">MON89034 x TC1507 x MON88017 x DAS-59122-7 (OECD identifier: MON-89&Oslash;34-3 x DAS- &Oslash;15&Oslash;7-1 x MON-88&Oslash;17-3 x DAS-59122-7) maize is the result of crossing four individual transgenic events. This stacked maize hybrid is a product of traditional plant breeding, and therefore is not automatically subject to regulation in all jurisdictions, as are transgenic plants resulting from recombinant-DNA technologies. Certain jurisdictions may request notification in advance of the release of a stacked hybrid, or may request information to conduct an environmental and food safety assessment.</p>\n\n<p style="text-align: justify;">MON89034 x TC1507 x MON88017 x DAS-59122-7 (SmartStax&trade;) maize provides above-ground insect control for protection against corn earworm, European corn borer, southwestern corn borer, sugar cane borer, fall armyworm, western bean cutworm and black cutworm; and below-ground insect control for protection against Western, Northern and Mexican corn rootworms. In addition, this hybrid displays tolerance to glyphosate and glufosinate-ammonium containing herbicides, allowing for broad-spectrum weed and grass control.</p>\n\n<p style="text-align: justify;">For a full description of each parental line please refer to the individual product descriptions in the crop database for <a href="dbase.php?action=ShowProd&amp;data=MON89034&amp;frmat=LONG"><b>MON89034</b></a> and <a href="dbase.php?action=ShowProd&amp;data=TC1507&amp;frmat=LONG"><b>TC1507</b></a> and <a href="dbase.php?action=ShowProd&amp;data=MON88017&amp;frmat=LONG"><b>MON88017</b></a> and <a href="dbase.php?action=ShowProd&amp;data=DAS-59122-7&amp;frmat=LONG"><b>DAS-59122-7</b></a>.</p>\n\n<p style="text-align: justify;">The inserted genes and their gene products have a history of safe use, and have undergone review and approval by several regulatory agencies. No interactions among the gene products or negative synergistic effects are expected in the stacked hybrid.</p>\n', 'Enabled', NULL, '2013-08-29 23:55:54'),
(111, 84, '<p style="text-align: justify;">BT11 x MIR162 x MIR604 (Agrisure&trade; 3100) maize is a stacked product of traditional plant breeding, and therefore is not automatically subject to regulation in all jurisdictions as are transgenic plants resulting from recombinant-DNA technologies. Certain jurisdictions may request notification in advance of the release of a stacked hybrid, or may request information to conduct an environmental and food safety assessment.</p>\n\n<p style="text-align: justify;">BT11 x MIR162 x MIR604 provides insect protection against European corn borer (<i>Ostrinia nubilalis</i>), southwestern corn borer (<i>Diatraea grandiosella</i>), southern cornstalk borer (<i>Diatraea crambidoides</i>), corn earworm (<i>Helicoverpa zea</i>), fall armyworm (<i>Spodoptera frugiperda</i>), armyworm (<i>Pseudaletia unipunctata</i>), beet armyworm (<i>Spodoptera exigua</i>), black cutworm (<i>Agrotis ipsilon</i>), western bean cutworm (<i>Striacosta albicosta</i>), sugarcane borer (<i>Diatraea saccharalis</i>), common stalk borer (<i>Papaipema nebris</i>), western corn rootworm (<i>Diabrotica virgifera virgifera</i>), northern corn rootworm (<i>Diabrotica barberi</i>), and Mexican corn rootworm (<i>Diabrotica virgifera zeae</i>). Tolerance to glufosinate-ammonium containing herbicides is conferred through expression of the <i>pat</i> gene derived from BT11.</p>\n\n<p style="text-align: justify;">For a full description of each parental line please refer to the individual product descriptions in the crop database for <a href="dbase.php?action=ShowProd&amp;data=BT11+%28X4334CBR%2C+X4734CBR%29&amp;frmat=LONG"><b>BT11</b></a> and <a href="dbase.php?action=ShowProd&amp;data=MIR162&amp;frmat=LONG"><b>MIR162</b></a> and <a href="dbase.php?action=ShowProd&amp;data=MIR604&amp;frmat=LONG"><b>MIR604</b></a>.</p>\n', 'Enabled', NULL, '2013-08-29 23:55:20'),
(112, 140, '<p style="text-align: justify;">Insect-protected COT67B cotton has been genetically modified for protection against feeding damage caused by larvae of a number of insect pest species, including: <i>Helicoverpa zea</i>, cotton bollworm; and <i>Heliothis virescens</i>, tobacco budworm. Protection against these pests is achieved through expression in the plant of an insecticidal Cry protein, Cry1Ab, encoded by the full-length <i>cry1Ab</i> gene derived from <i>Bacillus thuringiensis</i> subspecies <i>kurstaki</i> HD-1.<br />\nCry proteins exert their effect on the target insect by causing lysis of midgut epithelial cells, which leads to gut paralysis, cessation of feeding and eventual death of the larvae. The lysis of the midgut epithelial cells is mediated by the binding of the activated Cry protein to specialized receptors on these cells.</p>\n', 'Enabled', NULL, '2013-08-30 01:07:17'),
(113, 144, '<p style="text-align: justify;">CV127 soybean has been genetically modified to express an altered AtAHASL protein which is encoded by the <i>csr1-2</i> gene from <i>Arabidopsis thaliana</i> and confers tolerance to imidazolinone herbicides. The AtAHASL protein encoded by <i>csr1-2</i> is structurally and functionally identical to the native AtAHASL, except for substitution of a serine with an asparagine at residue 653 (S653N) which results in tolerance to imidazolinone herbicides. In addition, the <i>csr1-2</i> gene in CV127 contains a second mutation, in which arginine at position 272 is replaced by lysine (R272K).</p>\n', 'Enabled', NULL, '2013-08-30 01:15:27'),
(129, 98, '', 'Enabled', '2013-08-23 12:52:24', '2013-09-03 13:10:52'),
(126, 166, '<p style="text-align: justify;"><span style="font-family:georgia,serif;">DuPont Pioneer has developed maize line 4114 (DP-&Oslash;&Oslash;4114-3) as a &ldquo;molecular stack&rdquo; equivalent of the &ldquo;breeding stack&rdquo; containing the combined traits from maize lines 1507 (DAS-&Oslash;15&Oslash;7-1) and 59122 (DAS-59122-7). Maize line 4114 expresses the same insect-resistance and herbicide-tolerance traits as present in currently commercialized hybrids containing 1507 x 59122, which are marketed under the trade name Herculex&reg; XTRA. Just like Herculex&reg; XTRA hybrids, 4114 maize expresses the Cry1F protein, conferring resistance to certain lepidopteran insect pests (e.g., European corn borer), the Cry34Ab1 and Cry35Ab1 proteins, which together form an active binary insecticidal protein conferring resistance to corn rootworm, and the PAT enzyme, which inactivates glufosinate herbicide via acetylation.<br>><br>Unlike the 1507 x 59122 breeding stack, where the DNA insertions carrying traits derived from events 1507 and 59122, respectively, are located at two unlinked genetic loci, the genes encoding the Cry1F, Cry34Ab1, Cry35Ab1, and PAT proteins in 4114 maize are present at a single locus. This allows event 4114 to be bred more efficiently into new product offerings and to serve as a more efficient platform for the production of larger stack combinations through conventional breeding. Efficient breeding of multiple traits is becoming more important as growers demand more complex products, including multiple modes of action for insect control and herbicide-tolerance.</span></p><br>', 'Enabled', '2013-08-09 12:49:40', '2013-08-23 00:19:19'),
(131, 107, '', 'Enabled', '2013-08-30 16:46:53', '2013-08-30 16:46:53'),
(132, 108, '', 'Enabled', '2013-09-02 13:10:02', '2013-09-02 13:13:42'),
(133, 11, '', 'Enabled', '2013-09-03 11:25:26', '2013-09-03 11:25:26'),
(135, 169, '<p><span class="cm-editable"><span class="text">The Center for Environmental Risk Assessment (CERA) is dedicated to developing and applying sound science to the environmental risk assessment of agricultural biotechnologies&nbsp;so their contributions to the sustainable<a class="lightBox-block" data-element="lightBox" data-text="" href="http://cera.projectstagingserver.com/#"> </a>production of food, fuel and fiber may be safely realized. As part of the<a class="lightBox-block" data-element="lightBox" data-text="%3Cp%3Efhkadsdasfkldasfa%3C/p%3E%0A%0A%3Cp%3Easdfa%3C/p%3E%0A%0A%3Cp%3Easf%3C/p%3E%0A%0A%3Cp%3Ea%3C/p%3E%0A%0A%3Cp%3Esdasf%3C/p%3E%0A%0A%3Cp%3Easdasfadsfaasdfaasdf%3C/p%3E%0A" href="http://cera.projectstagingserver.com/#%2011"> </a>non-profit ILSI Research Foundation, <span class="glossary-word" data-element="glossary">CERA</span> serves as a scientific resource for governments, academic and private sector organisations. Our research projects and outreach activities include international representation from all three of these communities.</span></span></p>\r\n', 'Enabled', '2013-09-26 12:43:36', '2013-09-26 12:43:36');



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