Although radical oxygen and nitrogen species are harmful molecules that destroy cell functions, many operate as mediators of important cell signaling pathways when not in excess. Oxidants can modify protein function through the covalent, reversible addition of glutathione to cysteine. This review addresses different proteomic methods of Identifying glutathionylation targets and emphasizes ways of defining their pattern of modification in response to oxidative stimuli in cells. Finally, the literature on nonproteomic studies that Investigate the functional changes induced by glutathionylation are reviewed and future studies are commented on
Reactive oxygen species (ROS) are formed during normal respiration in the mitochondria through elect...
Protein cysteine residues are central to redox signaling and to protection against oxidative damage ...
: Formation of mixed disulfides between glutathione and the cysteines of some proteins (glutathionyl...
: Although radical oxygen and nitrogen species are harmful molecules that destroy cell functions, ma...
: Reactive oxygen and nitrogen species may cause various types of chemical modifications on specific...
Recent studies indicate that protein glutathionylation is an important regulatory mechanism. The dev...
Reactive oxygen species (ROS) and reactive nitrogen species (RNS) play an integral role in the modul...
Protein S-glutathionylation, the reversible formation of mixed disulfides between glutathione and lo...
Reactive oxygen species (ROS) and reactive nitrogen species (RNS) play an integral role in the modul...
Oxidation is a double-edged sword for cellular processes and its role in normal physiology, cancer a...
Protein S-glutathionylation, the reversible formation of mixed disulfides between glutathione and lo...
ormation of mixed disulfides between glutathione and the cysteines of some proteins (glutathionylati...
Oxidatively modified proteins are characterized by elevations in protein-resident carbonyls or 3-nit...
Glutathione has traditionally been considered as an antioxidant that protects cells against oxidativ...
Reactive oxygen species (ROS) are formed during normal respiration in the mitochondria through elect...
Protein cysteine residues are central to redox signaling and to protection against oxidative damage ...
: Formation of mixed disulfides between glutathione and the cysteines of some proteins (glutathionyl...
: Although radical oxygen and nitrogen species are harmful molecules that destroy cell functions, ma...
: Reactive oxygen and nitrogen species may cause various types of chemical modifications on specific...
Recent studies indicate that protein glutathionylation is an important regulatory mechanism. The dev...
Reactive oxygen species (ROS) and reactive nitrogen species (RNS) play an integral role in the modul...
Protein S-glutathionylation, the reversible formation of mixed disulfides between glutathione and lo...
Reactive oxygen species (ROS) and reactive nitrogen species (RNS) play an integral role in the modul...
Oxidation is a double-edged sword for cellular processes and its role in normal physiology, cancer a...
Protein S-glutathionylation, the reversible formation of mixed disulfides between glutathione and lo...
ormation of mixed disulfides between glutathione and the cysteines of some proteins (glutathionylati...
Oxidatively modified proteins are characterized by elevations in protein-resident carbonyls or 3-nit...
Glutathione has traditionally been considered as an antioxidant that protects cells against oxidativ...
Reactive oxygen species (ROS) are formed during normal respiration in the mitochondria through elect...
Protein cysteine residues are central to redox signaling and to protection against oxidative damage ...
: Formation of mixed disulfides between glutathione and the cysteines of some proteins (glutathionyl...