Results 31 to 40 of about 3,189 (173)
Nature Communications, 2020 Glutaredoxins play a central role in numerous biological processes including cellular redox homeostasis and Fe-S cluster biogenesis. Here the authors establish the molecular basis for glutaredoxin redox catalysis through comprehensive biochemical and ...
Linda Liedgens +7 more
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The Yeast Glutaredoxins Are Active as Glutathione Peroxidases [PDF]
Journal of Biological Chemistry, 2002 The yeast Saccharomyces cerevisiae contains two glutaredoxins, encoded by GRX1 and GRX2, which are active as glutathione-dependent oxidoreductases. Our studies show that changes in the levels of glutaredoxins affect the resistance of yeast cells to oxidative stress induced by hydroperoxides.
Collinson, Emma J. +5 more
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Data in Brief, 2015 This article describes data related to a research article titled “The Busulfan Metabolite EdAG Irreversibly Glutathionylates Glutaredoxins” [1]. EdAG is an electrophilic GSH analog formed in vivo from busulfan, which is used in hematopoietic stem cell ...
Michele Scian, William M. Atkins
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Glutathione-Related Enzymes and Proteins: A Review
Molecules, 2023 The tripeptide glutathione is found in all eukaryotic cells, and due to the compartmentalization of biochemical processes, its synthesis takes place exclusively in the cytosol.
Janka Vašková +3 more
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Glutaredoxins are essential for stress adaptation in the cyanobacterium Synechocystis sp. PCC 6803.
Frontiers in Plant Science, 2013 Glutaredoxin are small redox proteins able to reduce disulfides and mixed disulfides between GSH and proteins. Synechocystis sp. PCC 6803 contains three genes coding for glutaredoxins: ssr2061 (grxA) and slr1562 (grxB) code for dithiolic glutaredoxins ...
Ana M Sánchez-Riego +2 more
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Structural and Functional Diversity of Glutaredoxins in Yeast [PDF]
Current Protein & Peptide Science, 2010 Glutaredoxins are defined as thiol disulfide oxidoreductases that reduce disulfide bonds employing reduced glutathione as electron donor. They constitute a complex family of proteins with a diversity of enzymatic and functional properties. Thus, dithiol glutaredoxins are able to reduce disulfide bonds and deglutathionylate mixed disulfides between ...
Herrero Perpiñán, Enrique +2 more
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Role of GSH and Iron-Sulfur Glutaredoxins in Iron Metabolism—Review
Molecules, 2020 Glutathione (GSH) was initially identified and characterized for its redox properties and later for its contributions to detoxification reactions. Over the past decade, however, the essential contributions of glutathione to cellular iron metabolism have ...
Trnka Daniel +4 more
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Protein-protein interactions in plant antioxidant defense
Frontiers in Plant Science, 2022 The regulation of reactive oxygen species (ROS) levels in plants is ensured by mechanisms preventing their over accumulation, and by diverse antioxidants, including enzymes and nonenzymatic compounds.
Pavol Melicher +3 more
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Thioredoxin and Glutaredoxin Systems [PDF]
, 2019 This Special Issue features recent data concerning thioredoxins and glutaredoxins from various biological systems, including bacteria, mammals, and plants. Four of the sixteen articles are review papers that deal with the regulation of development of the effect of hydrogen peroxide and the interactions between oxidants and reductants, the description ...
Zaffagnini, Mirko, Jacquot, Jean-Pierre
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The Potential Roles of Redox Enzymes in Alzheimer’s Disease: Focus on Thioredoxin
ASN Neuro, 2021 Alzheimer’s disease (AD) is the most common neurodegenerative diseases. Increasing studies have demonstrated the critical importance for redox proteins mediating neuronal protection in models of AD.
Jinjing Jia +3 more
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