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- W3095259335 endingPage "8113" @default.
- W3095259335 startingPage "8113" @default.
- W3095259335 abstract "S-glutathionylation, the post-translational modification forming mixed disulfides between protein reactive thiols and glutathione, regulates redox-based signaling events in the cell and serves as a protective mechanism against oxidative damage. S-glutathionylation alters protein function, interactions, and localization across physiological processes, and its aberrant function is implicated in various human diseases. In this review, we discuss the current understanding of the molecular mechanisms of S-glutathionylation and describe the changing levels of expression of S-glutathionylation in the context of aging, cancer, cardiovascular, and liver diseases." @default.
- W3095259335 created "2020-11-09" @default.
- W3095259335 creator A5058952641 @default.
- W3095259335 creator A5089518472 @default.
- W3095259335 date "2020-10-30" @default.
- W3095259335 modified "2023-10-02" @default.
- W3095259335 title "Redox Regulation by Protein S-Glutathionylation: From Molecular Mechanisms to Implications in Health and Disease" @default.
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