Proteome Screens for Cys Residues Oxidation: The Redoxome

Giovanni Chiappetta, Sega Ndiaye, Aeid Igbaria, Chitranshu Kumar, Joelle Vinh, Michel B. Toledano

Research output: Chapter in Book/Report/Conference proceedingChapterpeer-review

57 Scopus citations

Abstract

The oxidation of the cysteine (Cys) residue to sulfenic (–S–OH), disulfide (–S–S–), or S-nitroso (S–NO) forms are thought to be a posttranslational modifications that regulate protein function. However, despite a few solid examples of its occurrence, thiol-redox regulation of protein function is still debated and often seen as an exotic phenomenon. A systematic and exhaustive characterization of all oxidized Cys residues, an experimental approach called redox proteomics or redoxome analysis, should help establish the physiological scope of Cys residue oxidation and give clues to its mechanisms. Redox proteomics still remains a technical challenge, mainly because of the labile nature of thiol-redox reactions and the lack of tools to directly detect the modified residues. Here we consider recent technical advances in redox proteomics, focusing on a gel-based fluorescent method and on the shotgun OxICAT technique.

Original languageEnglish
Title of host publicationMethods in Enzymology
PublisherAcademic Press Inc.
Pages199-216
Number of pages18
DOIs
StatePublished - 1 Jan 2010
Externally publishedYes

Publication series

NameMethods in Enzymology
Volume473
ISSN (Print)0076-6879
ISSN (Electronic)1557-7988

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology

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