: 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
Reactive oxygen species (ROS) and reactive nitrogen species (RNS) play an integral role in the modul...
Reactive oxygen species (ROS) and reactive nitrogen species (RNS) play an integral role in the modul...
Human proteome contains 214.000 cysteine residues. In the subset of protein not-free thiols, these a...
: Originally, small thiols, including glutathione, were viewed as protective antioxidants, acting as...
: Protein cysteines can undergo various forms of oxidation, some of them reversible (disulphide form...
Significance: Secreted proteins are important both as signaling molecules and potential biomarkers. ...
Oxidation is a double-edged sword for cellular processes and its role in normal physiology, cancer a...
: The main function of reduced glutathione (GSH) is to protect from oxidative stress as a reactive o...
Protein S-glutathionylation, the reversible formation of mixed disulfides between glutathione and lo...
Protein S-glutathionylation, the reversible formation of mixed disulfides between glutathione and lo...
Glutathione has traditionally been considered as an antioxidant that protects cells against oxidativ...
Glutathione has traditionally been considered as an antioxidant that protects cells against oxidativ...
Reactive oxygen species (ROS) and reactive nitrogen species (RNS) play an integral role in the modul...
Reactive oxygen species (ROS) and reactive nitrogen species (RNS) play an integral role in the modul...
Human proteome contains 214.000 cysteine residues. In the subset of protein not-free thiols, these a...
: Originally, small thiols, including glutathione, were viewed as protective antioxidants, acting as...
: Protein cysteines can undergo various forms of oxidation, some of them reversible (disulphide form...
Significance: Secreted proteins are important both as signaling molecules and potential biomarkers. ...
Oxidation is a double-edged sword for cellular processes and its role in normal physiology, cancer a...
: The main function of reduced glutathione (GSH) is to protect from oxidative stress as a reactive o...
Protein S-glutathionylation, the reversible formation of mixed disulfides between glutathione and lo...
Protein S-glutathionylation, the reversible formation of mixed disulfides between glutathione and lo...
Glutathione has traditionally been considered as an antioxidant that protects cells against oxidativ...
Glutathione has traditionally been considered as an antioxidant that protects cells against oxidativ...
Reactive oxygen species (ROS) and reactive nitrogen species (RNS) play an integral role in the modul...
Reactive oxygen species (ROS) and reactive nitrogen species (RNS) play an integral role in the modul...
Human proteome contains 214.000 cysteine residues. In the subset of protein not-free thiols, these a...