Results 271 to 280 of about 569,398 (304)
Some of the next articles are maybe not open access.
American Journal of Therapeutics, 2002
A growing body of evidence indicates that glutathione (GSH) plays a vitally important role in cellular function. It detoxifies toxic metabolites of drugs and reactive oxygen species and regulates gene expression, apoptosis, and transmembrane transport of organic solutes.
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A growing body of evidence indicates that glutathione (GSH) plays a vitally important role in cellular function. It detoxifies toxic metabolites of drugs and reactive oxygen species and regulates gene expression, apoptosis, and transmembrane transport of organic solutes.
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Cellular and Molecular Life Sciences, 2001
There are several proteins in mammalian cells that can metabolize hydrogen peroxide and lipid hydroperoxides. These proteins include four selenium-containing glutathione peroxidases that are found in different cell fractions and tissues of the body. This review considers the structure and distribution of the selenoperoxidases and how this relates to ...
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There are several proteins in mammalian cells that can metabolize hydrogen peroxide and lipid hydroperoxides. These proteins include four selenium-containing glutathione peroxidases that are found in different cell fractions and tissues of the body. This review considers the structure and distribution of the selenoperoxidases and how this relates to ...
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On the discovery of glutathione
Trends in Biochemical Sciences, 1988Abstract 1988 is the 100th anniversary of de Rey-Pailhade's finding that yeast and other cells contain a substance that reacts spontaneously with elemental sulfur to give hydrogen sulfide. In 1921, Hopkins concluded that this substance is a dipeptide containing cysteine and glutamate.
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Reduced Glutathione and Glutathione Disulfide
2003R W, Browne, D, Armstrong
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2000
Abstract The glutathione transferases (GSTs) are a family of multi-functional proteins which act as enzymes and also as binding proteins in detoxification processes (1-5). GSTs catalyse the nucleophilic attack of the sulfur atom of reduced glutathione by electrophilic groups in a second substrate. Most GSTs are located in the cytosol,
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Abstract The glutathione transferases (GSTs) are a family of multi-functional proteins which act as enzymes and also as binding proteins in detoxification processes (1-5). GSTs catalyse the nucleophilic attack of the sulfur atom of reduced glutathione by electrophilic groups in a second substrate. Most GSTs are located in the cytosol,
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Glutathione Restricts Serine Metabolism to Preserve Regulatory T Cell Function
Cell Metabolism, 2020Tak W Mak, Dirk Brenner, Karsten Hiller
exaly

