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- W2014163310 endingPage "963" @default.
- W2014163310 startingPage "951" @default.
- W2014163310 abstract "Protein thiolation is elicited by oxidation by different mechanisms and is involved in a variety of biological processes. Thiols, protein SH (PSH) and non-protein SH groups (NPSH, namely GSH), are in competition in all biological environments in the regulation of oxidant homeostasis because oxidants thiolate proteins, whereas GSH dethiolates them (e.g., GSSG + PSH --> GSSP + GSH). Although poorly investigated, the elimination of disulfides from thiolated proteins to regenerate critical PSH is important. These aspects are poorly known in cells, where glutaredoxin and peroxiredoxin operate as enzymes or potential chaperones to accelerate dethiolation. On the contrary, studies with plasma or albumin have highlighted the importance of protein conformation in dethiolation processes and have clarified the reason why homocysteine (thiol with potential toxicity) is preferentially bound to albumin as protein-thiol mixed disulfide with respect to other NPSH. Here we provide an overview of protein thiolation/dethiolation processes, with an emphasis on recent developments and future perspectives in this field." @default.
- W2014163310 created "2016-06-24" @default.
- W2014163310 creator A5022894248 @default.
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- W2014163310 creator A5069107657 @default.
- W2014163310 creator A5075565550 @default.
- W2014163310 creator A5082806187 @default.
- W2014163310 date "2005-07-01" @default.
- W2014163310 modified "2023-10-17" @default.
- W2014163310 title "Biochemical and Biological Aspects of Protein Thiolation in Cells and Plasma" @default.
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