Redox proteomics: Identification and functional role of glutathionylated proteins

Maddalena Fratelli, Elisabetta Gianazza, Pietro Ghezzi

Research output: Contribution to journalArticlepeer-review


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.

Original languageEnglish
Pages (from-to)365-376
Number of pages12
JournalExpert Review of Proteomics
Issue number3
Publication statusPublished - 2004


  • Chaperones
  • Cytoskeletal proteins
  • Glutathione
  • Glycolytic enzymes
  • Oxidative stress
  • Post-translational protein modifications
  • Redox signaling
  • S-glutathiolation
  • S-thiolation

ASJC Scopus subject areas

  • Molecular Biology
  • Genetics
  • Biotechnology


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