Results 241 to 250 of about 554,348 (295)
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Degradation of glutathione and glutathione conjugates in plants
Journal of Experimental Botany, 2023Abstract Glutathione (GSH) is a ubiquitous, abundant, and indispensable thiol for plants that participates in various biological processes, such as scavenging reactive oxygen species, redox signaling, storage and transport of sulfur, detoxification of harmful substances, and metabolism of several compounds.
Takehiro Ito, Naoko Ohkama-Ohtsu
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ANZ Journal of Surgery, 2003
Glutathione (GSH) is an ubiquitous thiol‐containing tripeptide that plays a key role in cell biology. It modulates cell response to redox changes associated with the reactive oxygen species, detoxifies the metabolites of drugs; regulates gene expression and apoptosis, and is involved in the transmembrane transport of organic solutes.
Heather, Jefferies +5 more
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Glutathione (GSH) is an ubiquitous thiol‐containing tripeptide that plays a key role in cell biology. It modulates cell response to redox changes associated with the reactive oxygen species, detoxifies the metabolites of drugs; regulates gene expression and apoptosis, and is involved in the transmembrane transport of organic solutes.
Heather, Jefferies +5 more
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Glutathione and glutathione derivatives in immunotherapy
Biological Chemistry, 2016Abstract Reduced glutathione (GSH) is the most prevalent non-protein thiol in animal cells. Its de novo and salvage synthesis serves to maintain a reduced cellular environment, which is important for several cellular functions. Altered intracellular GSH levels are observed in a wide range of pathologies, including several viral ...
FRATERNALE, ALESSANDRA +2 more
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Annual Review of Pharmacology and Toxicology, 2005
▪ Abstract This review describes the three mammalian glutathione transferase (GST) families, namely cytosolic, mitochondrial, and microsomal GST, the latter now designated MAPEG. Besides detoxifying electrophilic xenobiotics, such as chemical carcinogens, environmental pollutants, and antitumor agents, these transferases inactivate endogenous α,β ...
John Hayes, Jack U Flanagan
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▪ Abstract This review describes the three mammalian glutathione transferase (GST) families, namely cytosolic, mitochondrial, and microsomal GST, the latter now designated MAPEG. Besides detoxifying electrophilic xenobiotics, such as chemical carcinogens, environmental pollutants, and antitumor agents, these transferases inactivate endogenous α,β ...
John Hayes, Jack U Flanagan
exaly +4 more sources
2015
Glutathione is an endogenous peptide with antioxidant and other metabolic functions. The nomenclature, formulae, elemental composition, and appearance and uses of the drug are included. The methods used for the synthesis and biosynthesis of glutathione are described.
Amer M, Alanazi +2 more
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Glutathione is an endogenous peptide with antioxidant and other metabolic functions. The nomenclature, formulae, elemental composition, and appearance and uses of the drug are included. The methods used for the synthesis and biosynthesis of glutathione are described.
Amer M, Alanazi +2 more
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Inhibition of glutathione disulfide reductase by glutathione
Archives of Biochemistry and Biophysics, 1991Rat-liver glutathione disulfide reductase is significantly inhibited by physiological concentrations of the product, glutathione. GSH is a noncompetitive inhibitor against GSSG and an uncompetitive inhibitor against NADPH at saturating concentrations of the fixed substrate.
P M, Chung, R E, Cappel, H F, Gilbert
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Transport of glutathione and glutathione conjugates by MRP1
Trends in Pharmacological Sciences, 2006Glutathione (GSH)-conjugated xenobiotics and GSH-conjugated metabolites (e.g. the cysteinyl leukotriene C4) must be exported from the cells in which they are formed before they can be eliminated from the body or act on their cellular targets. This efflux is often mediated by the multidrug resistance protein 1 (MRP1) transporter, which also confers drug
Susan P C, Cole, Roger G, Deeley
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Reactions of glutathione and glutathione radicals with benzoquinones
Free Radical Biology and Medicine, 1992The reactions of glutathione (GSH) and glutathione radicals with a series of methyl-substituted 1,4-benzoquinones and 1,4-benzoquinone have been studied. It was found that by mixing excess benzoquinone with glutathione at pH above 6.5, the products formed were complex and unstable. All of the other experiments were carried out at pH 6.0, where the main
J, Butler, B M, Hoey
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Glutathione and glutathione metabolizing enzymes in yeasts
Antonie van Leeuwenhoek, 1988Total glutathione content, glutathione peroxidase, glutathione transferase and glutathione reductase activities have been measured in 12 species of yeasts. All the strains tested contained glutathione, though in different amounts, as well as the above mentioned enzymes.
CASALONE, ENRICO +3 more
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Measurement of Glutathione and Glutathione Disulfide
Current Protocols in Toxicology, 1999AbstractMeasurements of glutathione should include quantification of both the reduced and oxidized forms. HPLC‐based assays for glutathione and other cellular thiols and disulfides utilize a variety of detection methods, including ultraviolet, fluorescence, and electrochemical methods.
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