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.

Redox proteomics: identification and functional role of glutathionylated proteins / M. Fratelli, E. Gianazza, P. Ghezzi. - In: EXPERT REVIEW OF PROTEOMICS. - ISSN 1478-9450. - 1:3(2004), pp. 365-376.

Redox proteomics: identification and functional role of glutathionylated proteins

E. Gianazza
Secondo
;
2004

Abstract

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.
Chaperones; Cytoskeletal proteins; Glutathione; Glycolytic enzymes; Oxidative stress; Post-translational protein modifications; Redox signaling; S-glutathiolation; S-thiolation
Settore BIO/10 - Biochimica
2004
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/2434/182580
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