Proteomic approaches to the characterization of protein thiol modification.

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.

journal_name

Curr Opin Chem Biol

authors

Chouchani ET,James AM,Fearnley IM,Lilley KS,Murphy MP

doi

10.1016/j.cbpa.2010.11.003

subject

Has Abstract

pub_date

2011-02-01 00:00:00

pages

120-8

issue

1

eissn

1367-5931

issn

1879-0402

pii

S1367-5931(10)00164-X

journal_volume

15

pub_type

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