Cellular glutathione and thiols metabolism.

By D. Dickinson, H. Forman. Biochemical Pharmacology, 2002

845 citations recorded by the source corpus.

Subfields: Molecular Biology

View Paper: https://www.semanticscholar.org/paper/45b4b0826a40f10ef5a62a36cbc6340394e995a7

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In Molecular Biology

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Citations in the corpus

• The changing faces of glutathione, a cellular protagonist. (2003, background): “Moreover, more recently a family of proteins called peroxiredoxins has been recognized as catalyzing the reduction of H2O2 by GSH and/or other thiols, but with cysteine in its thiolate form, in their active sites rather than selenium-cysteine (Dickinson and Forman, 2002).”
• Cadmium stress: an oxidative challenge (2010, neutral): “Its antioxidant properties are attributed to the thiol (SH-) group on the cysteine residue (Dickinson and Forman 2002; Noctor and Foyer 1998).”
• Glutathione: new roles in redox signaling for an old antioxidant (2014, background): “Such alterations were also associated with inhibition of cytochrome c oxidase (CcOX) activity and microtubule network disassembly, which are considered hallmarks of nitric oxide (NO) toxicity, indicating that NO, rather than the depletion of GSH per se, is the primary mediator of cell damage.”
• The role of glutathione in cancer (2004, background): “The ability of many cells to transport GSH into the extracellular compartment may help in the transfer of cysteine, a limiting amino acid in glutathione synthesis de novo, between cells via the -glutamyl cycle.(12) In addition, GSH may protect the cell membrane by reducing harmful compounds such as ”
• Oxidative stress in angiogenesis and vascular disease. (2014, background): “One of the early implications of ROS in angiogenesis resulted from the studies using thiol-containing compounds, which were shown to inhibit macrophage-derived proangiogenic activity, as the conditioned medium from gold sodium thiomalate-treated macrophages potently reduced angiogenesis in rat corne”
• Endothelial cell superoxide generation: regulation and relevance for cardiovascular pathophysiology. (2004, background): “Alternatively, the reversible covalent addition of GSH to cysteine residues (or S-glutathiolation) may be involved in activating tyrosine kinases (79).”