Proteomic approaches to the characterization of protein thiol modification.

TitleProteomic approaches to the characterization of protein thiol modification.
Publication TypeJournal Article
Year of Publication2011
AuthorsChouchani, ET, James, AM, Fearnley, IM, Lilley, KS, Murphy, MP
JournalCurr Opin Chem Biol
Volume15
Issue1
Pagination120-8
Date Published2011 Feb
ISSN1879-0402
KeywordsCysteine, Humans, Oxidation-Reduction, Proteins, Proteomics, Sulfhydryl Compounds
Abstract

Protein cysteine residues are central to redox signaling and to protection against oxidative damage through their interactions with reactive oxygen and nitrogen species, and electrophiles. Although there is considerable evidence for a functional role for cysteine modifications, the identity and physiological significance of most protein thiol alterations are unknown. One way to identify candidate proteins involved in these processes is to utilize the proteomic methodologies that have been developed in recent years for the identification of proteins that undergo cysteine modification in response to redox signals or oxidative damage. These tools have proven effective in uncovering novel protein targets of redox modification and are important first steps that allow for a better understanding of how reactive molecules may contribute to signaling and damage. Here, we discuss a number of these approaches and their application to the identification of a variety of cysteine-centered redox modifications.

DOI10.1016/j.cbpa.2010.11.003
Alternate JournalCurr Opin Chem Biol
Citation Key10.1016/j.cbpa.2010.11.003
PubMed ID21130020
PubMed Central IDPMC3087609
Grant ListMC_U105663142 / / Medical Research Council / United Kingdom