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 Bioljournal_title
Current opinion in chemical biologyauthors
Chouchani ET,James AM,Fearnley IM,Lilley KS,Murphy MPdoi
10.1016/j.cbpa.2010.11.003subject
Has Abstractpub_date
2011-02-01 00:00:00pages
120-8issue
1eissn
1367-5931issn
1879-0402pii
S1367-5931(10)00164-Xjournal_volume
15pub_type
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