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Letteratura scientifica selezionata sul tema "Transferases"

Autore: Grafiati

Pubblicato: 4 giugno 2021

Ultima modifica: 25 luglio 2025

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Articoli di riviste sul tema "Transferases"

Alin, P., H. Jensson, E. Cederlund, H. Jörnvall, and B. Mannervik. "Cytosolic glutathione transferases from rat liver. Primary structure of class alpha glutathione transferase 8-8 and characterization of low-abundance class Mu glutathione transferases." Biochemical Journal 261, no. 2 (1989): 531–39. http://dx.doi.org/10.1042/bj2610531.

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Six GSH transferases with neutral/acidic isoelectric points were purified from the cytosol fraction of rat liver. Four transferases are class Mu enzymes related to the previously characterized GSH transferases 3-3, 4-4 and 6-6, as judged by structural and enzymic properties. Two additional GSH transferases are distinguished by high specific activities with 4-hydroxyalk-2-enals, toxic products of lipid peroxidation. The most abundant of these two enzymes, GSH transferase 8-8, a class Alpha enzyme, has earlier been identified in rat lung and kidney. The amino acid sequence of subunit 8 was deter

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Stockman, P. K., G. J. Beckett та J. D. Hayes. "Identification of a basic hybrid glutathione S-transferase from human liver. Glutathione S-transferase δ is composed of two distinct subunits (B1 and B2)". Biochemical Journal 227, № 2 (1985): 457–65. http://dx.doi.org/10.1042/bj2270457.

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The purification of a hybrid glutathione S-transferase (B1 B2) from human liver is described. This enzyme has an isoelectric point of 8.75 and the B1 and B2 subunits are distinguishable immunologically and are ionically distinct. Hybridization experiments demonstrated that B1 B1 and B2 B2 could be resolved by CM-cellulose chromatography and have pI values of 8.9 and 8.4 respectively. Transferase B1 B2, and the two homodimers from which it is formed, are electrophoretically and immunochemically distinct from the neutral enzyme (transferase mu) and two acidic enzymes (transferases rho and lambda

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Meyer, D. J., E. Lalor, B. Coles, et al. "Single-step purification and h.p.l.c. analysis of glutathione transferase 8–8 in rat tissues." Biochemical Journal 260, no. 3 (1989): 785–88. http://dx.doi.org/10.1042/bj2600785.

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GSSG selectively elutes two GSH transferases from a mixture of rat GSH transferases bound to a GSH-agarose affinity matrix. One is a form of GSH transferase 1-1 and the other is shown to be GSH transferase 8-8. By using tissues that lack this form of GSH transferase 1-1 (e.g. lung), GSH transferase 8-8 may thus be purified from cytosol in a single step. Quantitative analysis of the tissue distribution of GSH transferase 8-8 was obtained by h.p.l.c.

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Yamamoto, Miyako, Emili Cid, and Fumiichiro Yamamoto. "ABO blood group A transferases catalyze the biosynthesis of FORS blood group FORS1 antigen upon deletion of exon 3 or 4." Blood Advances 1, no. 27 (2017): 2756–66. http://dx.doi.org/10.1182/bloodadvances.2017009795.

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Key PointsABO blood group A transferases possess intrinsic FS activity upon deletion of exon 3 or 4 of A transferase messenger RNAs. Cointroduction of exon 3 or 4 deletion and GlyGlyAla substitution synergistically confers human A transferases with strong FS activity.

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Tan, K. H., D. J. Meyer, N. Gillies, and B. Ketterer. "Detoxification of DNA hydroperoxide by glutathione transferases and the purification and characterization of glutathione transferases of the rat liver nucleus." Biochemical Journal 254, no. 3 (1988): 841–45. http://dx.doi.org/10.1042/bj2540841.

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DNA peroxidized by exposure to ionizing radiation in the presence of oxygen is a substrate for the Se-independent GSH peroxidase activity of several GSH transferases, GSH transferases 5-5, 3-3 and 4-4 being the most active in the rat liver soluble supernatant fraction (500, 35 and 20 nmol/min per mg of protein respectively) and GSH transferases mu and pi the most active, so far found, in the human liver soluble supernatant fraction (80 and 10 nmol/min per mg respectively). Although the GSH transferase content of the rat nucleus was found to be much lower than that of the soluble supernatant, n

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Peters, W. H. M., H. M. J. Roelofs, F. M. Nagengast, and J. H. M. van Tongeren. "Human intestinal glutathione S-transferases." Biochemical Journal 257, no. 2 (1989): 471–76. http://dx.doi.org/10.1042/bj2570471.

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Cytosolic glutathione S-transferases were purified from the epithelial cells of human small and large intestine. These preparations were characterized with regard to specific activities, subunit and isoenzyme composition. Isoenzyme composition and specific activity showed little variation from proximal to distal small intestine. Specific activities of hepatic and intestinal enzymes from the same patient were comparable. Hepatic enzymes were mainly composed of 25 kDa subunits. Transferases from small intestine contained 24 and 25 kDa subunits, in variable amounts. Colon enzymes were composed of

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Danielson, U. H., H. Esterbauer, and B. Mannervik. "Structure-activity relationships of 4-hydroxyalkenals in the conjugation catalysed by mammalian glutathione transferases." Biochemical Journal 247, no. 3 (1987): 707–13. http://dx.doi.org/10.1042/bj2470707.

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The substrate specificities of 15 cytosolic glutathione transferases from rat, mouse and man have been explored by use of a homologous series of 4-hydroxyalkenals, extending from 4-hydroxypentenal to 4-hydroxypentadecenal. Rat glutathione transferase 8-8 is exceptionally active with the whole range of 4-hydroxyalkenals, from C5 to C15. Rat transferase 1-1, although more than 10-fold less efficient than transferase 8-8, is the second most active transferase with the longest chain length substrates. Other enzyme forms showing high activities with these substrates are rat transferase 4-4 and huma

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Kurz, M. A., T. D. Boyer, R. Whalen, T. E. Peterson, and D. G. Harrison. "Nitroglycerin metabolism in vascular tissue: role of glutathione S-transferases and relationship between NO. and NO2– formation." Biochemical Journal 292, no. 2 (1993): 545–50. http://dx.doi.org/10.1042/bj2920545.

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Nitroglycerin is a commonly employed pharmacological agent which produces vasodilatation by release of nitric oxide (NO.). The mechanism by which nitroglycerin releases NO. remains undefined. Recently, glutathione S-transferases have been implicated as important contributors to this process. They are known to release NO2- from nitroglycerin, but have not been shown to release NO.. The present studies were designed to examine the role of endogenous glutathione S-transferases in this metabolic process. Homogenates of dog carotid artery were incubated anaerobically with nitroglycerin, and NO. and

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Wang, Qiang-Qiang, Kai He, Muhammad-Tahir Aleem, and Shaojun Long. "Prenyl Transferases Regulate Secretory Protein Sorting and Parasite Morphology in Toxoplasma gondii." International Journal of Molecular Sciences 24, no. 8 (2023): 7172. http://dx.doi.org/10.3390/ijms24087172.

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Protein prenylation is an important protein modification that is responsible for diverse physiological activities in eukaryotic cells. This modification is generally catalyzed by three types of prenyl transferases, which include farnesyl transferase (FT), geranylgeranyl transferase (GGT-1) and Rab geranylgeranyl transferase (GGT-2). Studies in malaria parasites showed that these parasites contain prenylated proteins, which are proposed to play multiple functions in parasites. However, the prenyl transferases have not been functionally characterized in parasites of subphylum Apicomplexa. Here,

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Charrier, Cédric, Gary J. Duncan, Martin D. Reid, et al. "A novel class of CoA-transferase involved in short-chain fatty acid metabolism in butyrate-producing human colonic bacteria." Microbiology 152, no. 1 (2006): 179–85. http://dx.doi.org/10.1099/mic.0.28412-0.

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Bacterial butyryl-CoA CoA-transferase activity plays a key role in butyrate formation in the human colon, but the enzyme and corresponding gene responsible for this activity have not previously been identified. A novel CoA-transferase gene is described from the colonic bacterium Roseburia sp. A2-183, with similarity to acetyl-CoA hydrolase as well as 4-hydroxybutyrate CoA-transferase sequences. The gene product, overexpressed in an Escherichia coli lysate, showed activity with butyryl-CoA and to a lesser degree propionyl-CoA in the presence of acetate. Butyrate, propionate, isobutyrate and val

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Più fonti

Tesi sul tema "Transferases"

Corrigall, Anne Vint. "Human glutathione S-transferases : characterization, tissue distribution and kinetic studies." Doctoral thesis, University of Cape Town, 1988. http://hdl.handle.net/11427/27205.

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In this study the purification of human basic and near-neutral liver, and human basic and acidic lung glutathione S-transferases (GSH S-T) was undertaken. Purification of the basic and near-neutral GSH S-T was achieved using a combination of affinity chromatography, chromatofocusing and immunoaffinity chromatography. Affinity and ion exchange chromatography were employed in the purification of the basic and acidic lung forms. The purified proteins had similar physicochemical characteristics to the GSH S-T purified by others. The binding of 1-chloro-2,4-dinitrobenzene (CDNB) to the 3 classes of

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Goold, Richard David. "The glutathione S-transferases : kinetics, binding and inhibition." Doctoral thesis, University of Cape Town, 1989. http://hdl.handle.net/11427/27175.

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Abstract (sommario):

The glutathione S-transferases are a group of enzymes which catalyse the conjugation of reduced glutathione with a variety of electrophilic molecules, and they are therefore thought to play a major role in drug biotransformation and the detoxification of xenobiotics. The cytosolic GSH S-transferase isoenzymes of rat, man and mouse have been assigned to three groups, Alpha, Mu and Pi, based on N-terrninal amino acid sequences, substrate specificities, immunological cross-reactivity and sensitivities to inhibitors. The kinetic mechanism of the GSH S-transferases is controversial, due to the obse

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Mosi, Renée M. "Mechanistic studies on Ã-glycosyl transferases." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 1998. http://www.collectionscanada.ca/obj/s4/f2/dsk2/ftp02/NQ34594.pdf.

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Dixon, David Peter. "Glutathione transferases in maize (Zea mays)." Thesis, Durham University, 1998. http://etheses.dur.ac.uk/4788/.

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The glutathione transferases (GSTs) of maize have been the most studied GSTs in plants, however much is still not known about these enzymes. In the course of the current study six GST subunits (Zm GSTs I, II and III, which have been reported previously, and Zm GSTs V, VI and VII, which have not been previously reported) have been identified in the dimers Zm GST I-I, I-II, I-III, V-V, V-VI and V-VII. Maize GSTs are known to be important in herbicide detoxification and the purified maize enzymes were each found to have differing activities toward a number of herbicides, and also a range of other

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Barrozo, Alexandre. "Promiscuity and Selectivity in Phosphoryl Transferases." Doctoral thesis, Uppsala universitet, Struktur- och molekylärbiologi, 2016. http://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-279693.

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Phosphoryl transfers are essential chemical reactions in key life processes, including energy production, signal transduction and protein synthesis. They are known for having extremely low reaction rates in aqueous solution, reaching the scale of millions of years. In order to make life possible, enzymes that catalyse phosphoryl transfer, phosphoryl transferases, have evolved to be tremendously proficient catalysts, increasing reaction rates to the millisecond timescale. Due to the nature of the electronic structure of phosphorus atoms, understanding how hydrolysis of phosphate esters occurs i

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Hayes, Peter C. "Glutathione S-transferases in the pancreas." Thesis, University of Edinburgh, 1993. http://hdl.handle.net/1842/19832.

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Glutathione S-transferase (GST) is an important xenobiotic metabolising enzyme which has been extensively studied in the liver. In the first part of this study immunohistochemistry was used to identify the presence and histological localisation of different GST isoenzymes in various gastrointestinal tract tissues in the human in health and disease. GSTP was found throughout the gastrointestinal and biliary tract whilst the position and quantity of other isoenzymes varied locally. Increased expression of GSTP was observed in cholangiocarcinoma and colonic adenocarcinoma, but not hepatocellular

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DAWOOD, KUTAYBA F. "New physiological roles of glautathione transferases." Doctoral thesis, Università degli Studi di Roma "Tor Vergata", 2009. http://hdl.handle.net/2108/923.

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Glutathione transferases (GSTs) are enzymes able to conjugate GSH to a lot of toxic compounds thereby favoring their excretion. Recently, other protective roles of these enzymes have been discovered. In particular, it has been observed that a peculiar and strong interaction exists between some mammalian GSTs and an endogenous carrier of nitric oxide, the dinitrosyl-diglutathionyl iron complex (DNDGIC). This iron complex is a paramagnetic molecule with a characteristic EPR spectrum centered at g = 2.03, that is spontaneously formed when NO enters the cell. This complex is a strong irreversible

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Dolan, Catherine. "Regulation of mouse hepatic glutathione S-transferases." Thesis, University of Edinburgh, 1991. http://hdl.handle.net/1842/23855.

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The glutathione S-transferases (GST) are a multi-gene family of dimeric proteins which catalyse the conjugation of glutathione to a wide range of electrophilic compounds. Three classes of mouse cytosolic GST have been isolated, alpha, mu and pi, comprising Ya-, Yb- and Yf-type subunits respectively. A marked sexual dimorphism in mouse hepatic GST has been observed. The YfYf GST is the most abundant form in the male, constituting approximately 70% of total hepatic GST content. By contrast, the Yf subunit represents only a minor form in the livers of female mice. The hormonal controls which regu

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Meikle, Ian. "Glutathione S-transferases in the adrenal cortex." Thesis, University of Edinburgh, 1992. http://hdl.handle.net/1842/19139.

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Data available prior to this thesis had shown that, of all bovine organs examined, the adrenal cortex exhibited the second highest level of glutathione S-transferase (GST) expression behind the liver. This finding, along with increasing evidence implicating the importance of GST in endogenous detoxification processes, formed the basis for a further extensive investigation of the GST isoenzymes expressed by the adrenal cortex. Investigation of the GST isoenzymes expressed by a number of different bovine organs using affinity chromatography on S-hexylglutathione-Sepharose 6B (S-hexG-Ag) revealed

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Hill, Alison Elspeth. "Regulation of glutathione S-transferases during stress." Thesis, University of Edinburgh, 1994. http://hdl.handle.net/1842/19846.

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Elevation of glutathione S-transferases (GST) in tumour cells can be responsible for resistance to a variety of chemotherapeutic agents. It has been hypothesised that GSTs may be induced as part of a stress response, similar to that of the prokaryotic adaptive response. To further this investigation I studied the induction of GSTs in a variety of permanent and transient stress models. A chlorambucil resistant CHO cell line which was known to express increased levels of Alpha-class GST was studied to determine the nature of the increase in protein. Northern and Southern blot analysis revealed a

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Più fonti

Libri sul tema "Transferases"

D, Hayes J., Pickett C. B, Mantle T. J, University of Edinburgh. Dept. of Clinical Chemistry., and International GST Conference (3rd : 1989 : Royal College of Physicians of Edinburgh), eds. Glutathione S-transferases and drug resistance. Taylor & Francis, 1990.

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Schomburg, Dietmar, Ida Schomburg, and Antje Chang, eds. Class 2 Transferases. Springer Berlin Heidelberg, 2009. http://dx.doi.org/10.1007/978-3-540-85697-9.

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Schomburg, Dietmar, Ida Schomburg, and Antje Chang, eds. Class 2 Transferases. Springer Berlin Heidelberg, 2009. http://dx.doi.org/10.1007/978-3-540-85699-3.

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D, Tew Kenneth, ed. Structure and function of glutathione transferases. CRC Press, 1993.

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1942-, Sies H., and Packer Lester, eds. Gluthione transferases and gamma-glutamyl transpeptidases. Elsevier Academic Press, 2005.

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Schomburg, Dietmar, Ida Schomburg, and Antje Chang, eds. Class 2 · Transferases I. Springer Berlin Heidelberg, 2006. http://dx.doi.org/10.1007/3-540-37715-8.

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Schomburg, Dietmar, Ida Schomburg, and Antje Chang, eds. Class 2 · Transferases IV. Springer Berlin Heidelberg, 2006. http://dx.doi.org/10.1007/3-540-37718-2.

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Schomburg, Dietmar, Ida Schomburg, and Antje Chang, eds. Class 2 · Transferases VI. Springer Berlin Heidelberg, 2007. http://dx.doi.org/10.1007/978-3-540-49753-0.

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Schomburg, Dietmar, Ida Schomburg, and Antje Chang, eds. Class 2 · Transferases VI. Springer Berlin Heidelberg, 2007. http://dx.doi.org/10.1007/978-3-540-49755-4.

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Schomburg, Dietmar, Ida Schomburg, and Antje Chang, eds. Class 2 Transferases VIII. Springer Berlin Heidelberg, 2007. http://dx.doi.org/10.1007/978-3-540-49756-1.

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Capitoli di libri sul tema "Transferases"

Ferreira, Patricia, Marta Martínez-Júlvez, and Milagros Medina. "Electron Transferases." In Methods in Molecular Biology. Springer New York, 2014. http://dx.doi.org/10.1007/978-1-4939-0452-5_5.

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Althaus, Felix R., and Christoph Richter. "Cellular Transferases." In Molecular Biology Biochemistry and Biophysics. Springer Berlin Heidelberg, 1987. http://dx.doi.org/10.1007/978-3-642-83077-8_14.

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Mannervik, Bengt, and Birgitta Sjödin. "Glutathione Transferases." In Glutathione. CRC Press, 2018. http://dx.doi.org/10.1201/9781351261760-11.

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Dostalek, Miroslav, and Anna-Katarina Stark. "Glutathione S-Transferases." In Metabolism of Drugs and Other Xenobiotics. Wiley-VCH Verlag GmbH & Co. KGaA, 2012. http://dx.doi.org/10.1002/9783527630905.ch5.

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Kedam, Thyaga Raju, Pallavi Chittoor, and Divya Kurumala. "Glutathione-S-Transferases." In Encyclopedia of Signaling Molecules. Springer International Publishing, 2018. http://dx.doi.org/10.1007/978-3-319-67199-4_28.

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Sherratt, Philip J., and John D. Hayes. "Glutathione S-transferases." In Enzyme Systems that Metabolise Drugs and Other Xenobiotics. John Wiley & Sons, Ltd, 2002. http://dx.doi.org/10.1002/0470846305.ch9.

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Ward, Tony Milford. "Glutathione-S-Transferases." In Proteins and Tumour Markers May 1995. Springer Netherlands, 1995. http://dx.doi.org/10.1007/978-94-011-0681-8_38.

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Kedam, Thyaga Raju, Pallavi Chittoor, and Divya Kurumala. "Glutathione-S-Transferases." In Encyclopedia of Signaling Molecules. Springer New York, 2017. http://dx.doi.org/10.1007/978-1-4614-6438-9_28-1.

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Soffer, Richard L. "Aminoacyl-tRNA Transferases." In Advances in Enzymology - and Related Areas of Molecular Biology. John Wiley & Sons, Inc., 2006. http://dx.doi.org/10.1002/9780470122853.ch4.

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Raha, Abhijit, and Kenneth D. Tew. "Glutathione S-Transferases." In Drug Resistance. Springer US, 1996. http://dx.doi.org/10.1007/978-1-4613-1267-3_4.

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Atti di convegni sul tema "Transferases"

Gogić, Anđela D., Marina Ž. Vesović, Miloš V. Nikolić, Andriana M. Bukonjić, Dušan Lj Tomović, and Nikola V. Nedeljković. "Molecular docking study of designed N-myristoyl transferase inhibitors." In 2nd International Conference on Chemo and Bioinformatics. Institute for Information Technologies, University of Kragujevac, 2023. http://dx.doi.org/10.46793/iccbi23.479g.

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N-myristoyl transferase has a key role in the myristoylation of vital proteins and is necessary for the growth and synthesis of material for the survival of various fungi. Due to the difference in the structure of fungal and mammalian N-myristoyl transferase, the crystal structure of the N-myristoyl transferase originating from Candida albicans was used as the target molecule. The present in silico study aims to design compounds, benzofuran derivatives, and simulate the interactions of the compounds and the amino acid sequences of the active center N-myristoyl transferases from Candida albican

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Blanchard, Sophie, Vincent Ferrieres, and Daniel Plusquellec. "STUDY OF GLYCOFURANOSYL TRANSFERASES. A GENERAL SYNTHESIS OF SUITABLE HEXOFURANOSYL DONORS." In XXIst International Carbohydrate Symposium 2002. TheScientificWorld Ltd, 2002. http://dx.doi.org/10.1100/tsw.2002.759.

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Hwa, Kuo-Yuan, Te-Ling Pang, and Mei-Yu Chen. "Classification of LARGE-liked GlcNAc-Transferases of Dictyostelium discoideum by Phylogenetic Analysis." In 2007 Frontiers in the Convergence of Bioscience and Information Technologies. IEEE, 2007. http://dx.doi.org/10.1109/fbit.2007.106.

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Valeeva, L. R., and M. R. Sharipova. "The role of prenyl transferases in the development of multicellular thallus Marchantia polymorpha." In IX Congress of society physiologists of plants of Russia "Plant physiology is the basis for creating plants of the future". Kazan University Press, 2019. http://dx.doi.org/10.26907/978-5-00130-204-9-2019-92.

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Bautista Jimenez, Robin Charlotte. "Diapause regulation in the flesh fly (Sarcophagabullata) by histone acetylase transferases and histone deacetylases." In 2016 International Congress of Entomology. Entomological Society of America, 2016. http://dx.doi.org/10.1603/ice.2016.114622.

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Withers, Stephen G. "ENZYMATIC CLEAVAGE AND FORMATION OF GLYCOSIDIC BONDS: FROM GLYCOSIDASES AND LYASES TO TRANSFERASES AND GLYCOSYNTHASES." In XXIst International Carbohydrate Symposium 2002. TheScientificWorld Ltd, 2002. http://dx.doi.org/10.1100/tsw.2002.355.

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Mailula, Dineo, Magriet Van Der Nest, Almuth Hammerbacher, Nokuthula Mchunu, and Brenda Wingfield. "Catabolism of branched chain and aromatic amino transferases, route to fusel alcohols and acetates by the Ceratocystidaceae." In 1st International Electronic Conference on Microbiology. MDPI, 2020. http://dx.doi.org/10.3390/ecm2020-07097.

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Kakuda, Shinako, Yuki Sato, Kazuaki Ohtsubo, et al. "SUBSTRATE SPECIFICITY AND STRUCTURE-FUNCTION RELATIONSHIP OF THE HNK-1 ASSOCIATED GLUCURONYL TRANSFERASES, GlcAT-P and GlcAT-S." In XXIst International Carbohydrate Symposium 2002. TheScientificWorld Ltd, 2002. http://dx.doi.org/10.1100/tsw.2002.428.

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Yu, AL, K.-H. Liao, C.-H. Chang, et al. "Abstract P1-08-05: Expression levels of sialyl transfereases and fucosyl transferases in breast cancer and their prognostic significance." In Abstracts: Thirty-Eighth Annual CTRC-AACR San Antonio Breast Cancer Symposium; December 8-12, 2015; San Antonio, TX. American Association for Cancer Research, 2016. http://dx.doi.org/10.1158/1538-7445.sabcs15-p1-08-05.

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Abbate, María M., Daiana B. Leonardi, Javier N. Brandani, et al. "Abstract 5021: Glutathione-S-transferases polymorphisms are associated with increased risk of relapse in pediatric patients with acute lymphoblastic leukemia." In Proceedings: AACR 107th Annual Meeting 2016; April 16-20, 2016; New Orleans, LA. American Association for Cancer Research, 2016. http://dx.doi.org/10.1158/1538-7445.am2016-5021.

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Rapporti di organizzazioni sul tema "Transferases"

Haynes, Robin L., and Alan J. Townsend. Glutathione Transferases and the Multidrug Resistance - Associated Protein in Prevention of Potentially Carcinogenic Oxidant Stress in Breast Cancer. Defense Technical Information Center, 2001. http://dx.doi.org/10.21236/ada398035.

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Kun, Ernest. Molecular Cloning of Adenosinediphosphoribosyl Transferase. Defense Technical Information Center, 1987. http://dx.doi.org/10.21236/ada185458.

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Kapoor, T. M. Purification and characterization of the Oligosaccharyl transferase. Office of Scientific and Technical Information (OSTI), 1990. http://dx.doi.org/10.2172/6278276.

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บัวบูชา, ธีรพงษ์, ศุภอรรจ ศิริกันทรมาศ та นุชนาถ วุฒิประดิษฐกุล. การค้นหายีนที่ควบคุมโดยโปรตีนคัลมอดุลินในการตอบสนองต่อสภาวะความเครียดจากสิ่งแวดล้อมของข้าว Oryza sativa L. : รายงานวิจัย. จุฬาลงกรณ์มหาวิทยาลัย, 2015. https://doi.org/10.58837/chula.res.2015.58.

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การวิเคราะห์โปรติโอมิกส์เชิงเปรียบเทียบของข้าว (Oryza sativa L.) ทรานส์เจนิกสายพันธุ์ขาวดอกมะลิ 105 ที่มีการแสดงออกของยีน OsCam1-1 เกินปกติซึ่งแสดงลักษณะทนเค็ม สามารถระบุโปรตีนที่แสดงออกแตกต่างกับข้าว wild-type จำนวน 77 ชนิด ผลการวิเคราะห์ระดับการแสดงออกทรานสคริปของยีน LOC_Os02g11820 ที่สร้าง GTPase-activating protein ซึ่งเป็นหนึ่งในโปรตีนที่แสดงออกแตกต่างกันด้วยวิธี real-time RT-PCR พบว่าข้าวทรานส์เจนิกมีระดับทรานสคริปสูงกว่าข้าว wild-type การวิเคราะห์การแสดงออกร่วมชี้ให้เห็นว่ายีน LOC_Os02g11820 มีการแสดงออกร่วมเชิงบวกกับยีนสร้างเอนไซม์ peroxidase หลายยีน และมีการแสดงออกร่วมเชิงลบกับยีนสร้าง

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Cushing, Donish, and Bomi Joseph. Synthetic cannabinoids severely elevate amino transferase levels. Natural cannabidiol does not. Peak Health Center, 2018. http://dx.doi.org/10.31013/2001e.

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Woldegiorgis, S., R. C. Ahmed, Y. Zhen, C. A. Erdmann, M. L. Russell, and R. Goth-Goldstein. Genetic polymorphism in three glutathione s-transferase genes and breast cancer risk. Office of Scientific and Technical Information (OSTI), 2002. http://dx.doi.org/10.2172/799602.

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Ross, Jeffrey S. Development of an Assay for Prostate Cancer Based on Methylation Status of Glutathione S-Transferase-pi. Defense Technical Information Center, 2000. http://dx.doi.org/10.21236/ada392285.

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Alanyalı, Filiz Susuz. Effects of Sodium Sulphate on Catalase and Glutathione-S-Transferase Enzyme Activities in Tubifex tubifex (Müller, 1774) (Oligochaeta:Tubificidae). "Prof. Marin Drinov" Publishing House of Bulgarian Academy of Sciences, 2021. http://dx.doi.org/10.7546/crabs.2021.11.05.

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