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ReviewRegulation of protein function by glutathionylation
Abstract
The main function of reduced glutathione (GSH) is to protect from oxidative stress as a reactive oxygen scavenger. However, in the context of redox regulation, the ratio between GSH and its oxidized form (GSSG) determines the redox state of redox-sensitive cysteines in some proteins and, thus, acts as a signaling system. While GSH/GSSG can catalyze oxido-reduction of intra- and inter-chain disulfides by thiol-disulfide exchange, this review focuses on the formation of mixed disulfides between glutathione and proteins, also known as glutathionylation. The review discusses the regulatory role of this post-translational modification and the role of protein disulfide oxidoreductases (thioredoxin/thioredoxin reductase, glutaredoxin, protein disulfide isomerase) in the reversibility of this process.
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Metadata
- Authors
- Ghezzi, P.
- Venue
- Free Radical Research
- Publisher
- Informa UK Limited
- Published
- 2005-06
- Volume
- 39
- Issue
- 6
- Pages
- 573-580
- ISSN
- 1029-2470 (ISSN-L)
- 1071-5762
- OpenAlex
- W2009745570
- Cited by
- 270
- References
- 50
- FWCI
- 10.03
- Type
- journal article
- Language
- en
- Open access
- closed
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