Redox proteomics: Identification of oxidatively modified proteins

Pietro Ghezzi, Valentina Bonetto

Research output: Contribution to journalArticlepeer-review


Reactive oxygen and nitrogen species may cause various types of chemical modifications on specific proteins, Such modifications if irreversible are often associated with permanent loss of function and may lead to the elimination or to the accumulation of the damaged proteins. Reversible modifications, particularly at the cysteine residues, may have a dual role of protection from cysteine irreversible oxidation and modulation of protein function (redox regulation). Here we will review the techniques available for identifying proteins based on their redox state. In particular, we will focus on protein carbonylation, tyrosine nitration and thiol-disulfide chemistry of cysteines, with special emphasis on glutathionylation, because these are the fields where the tools of proteome analysis have been applied.

Original languageEnglish
Pages (from-to)1145-1153
Number of pages9
Issue number7
Publication statusPublished - Jul 1 2003


  • Carbonylation
  • Glutathionylation
  • Post-translational modification
  • Protein oxidation
  • Review

ASJC Scopus subject areas

  • Molecular Biology
  • Genetics


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