Thiol–disulfide balance: from the concept of oxidative stress to that of redox regulation
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 …
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 …
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. Antioxid. Redox Signal. 7, 964–972.
Mary Ann Liebert