Thiol-disulfide balance: From the concept of oxidative stress to that of redox regulation

Research output: Contribution to journalArticle

Abstract

Originally, small thiols, including glutathione, were viewed as protective antioxidants, acting as free radical scavengers in the context of oxidative damage. Recently, there is a growing literature showing that protein glutathionylation (formation of protein-glutathione mixed disulfides) and other forms of cysteine oxidation may be a means of redox regulation under physiological conditions. This review discusses the importance of protein oxidation in redox regulation in view of the recent data originating from the application of redox proteomics to identify redox-sensitive targets.

Original languageEnglish
Pages (from-to)964-972
Number of pages9
JournalAntioxidants and Redox Signaling
Volume7
Issue number7-8
DOIs
Publication statusPublished - Jul 2005

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Oxidative stress
Sulfhydryl Compounds
Disulfides
Oxidation-Reduction
Oxidative Stress
Glutathione
Oxidation
Free Radical Scavengers
Proteins
Glutathione Disulfide
Proteomics
Cysteine
Antioxidants

ASJC Scopus subject areas

  • Biochemistry

Cite this

Thiol-disulfide balance : From the concept of oxidative stress to that of redox regulation. / Ghezzi, Pietro; Bonetto, Valentina; Fratelli, Maddalena.

In: Antioxidants and Redox Signaling, Vol. 7, No. 7-8, 07.2005, p. 964-972.

Research output: Contribution to journalArticle

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