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- W2904396117 startingPage "151" @default.
- W2904396117 abstract "Protein S-glutathionylation reactions are a ubiquitous oxidative modification required to control protein function in response to changes in redox buffering capacity. These reactions are rapid and reversible and are, for the most part, enzymatically mediated by glutaredoxins (GRX) and glutathione S-transferases (GST). Protein S-glutathionylation has been found to control a range of cell functions in response to different physiological cues. Although these reactions occur throughout the cell, mitochondrial proteins seem to be highly susceptible to reversible S-glutathionylation, a feature attributed to the unique physical properties of this organelle. Indeed, mitochondria contain a number of S-glutathionylation targets which includes proteins involved in energy metabolism, solute transport, reactive oxygen species (ROS) production, proton leaks, apoptosis, antioxidant defense, and mitochondrial fission and fusion. Moreover, it has been found that conjugation and removal of glutathione from proteins in mitochondria fulfills a number of important physiological roles and defects in these reactions can have some dire pathological consequences. Here, we provide an updated overview on mitochondrial protein S-glutathionylation reactions and their importance in cell functions and physiology." @default.
- W2904396117 created "2018-12-22" @default.
- W2904396117 creator A5003190574 @default.
- W2904396117 creator A5061668188 @default.
- W2904396117 creator A5083479575 @default.
- W2904396117 date "2019-02-01" @default.
- W2904396117 modified "2023-10-17" @default.
- W2904396117 title "Protein S-glutathionylation: The linchpin for the transmission of regulatory information on redox buffering capacity in mitochondria" @default.
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