Abstract：
:Oxidative cysteine modifications have emerged as a central mechanism for dynamic post-translational regulation of all major protein classes and correlate with many disease states. Elucidating the precise roles of cysteine oxidation in physiology and pathology presents a major challenge. This article reviews the current, targeted proteomic strategies that are available to detect and quantify cysteine oxidation. A number of indirect methods have been developed to monitor changes in the redox state of cysteines, with the majority relying on the loss of reactivity with thiol-modifying reagents or restoration of labeling by reducing agents. Recent advances in chemical biology allow for the direct detection of specific cysteine oxoforms based on their distinct chemical attributes. In addition, new chemical reporters of cysteine oxidation have enabled in situ detection of labile modifications and improved proteomic analysis of redox-regulated proteins. Progress in the field of redox proteomics should advance our knowledge of regulatory mechanisms that involve oxidation of cysteine residues and lead to a better understanding of oxidative biochemistry in health and disease.
journal_name
Curr Opin Chem Bioljournal_title
Current opinion in chemical biologyauthors
Leonard SE,Carroll KSdoi
10.1016/j.cbpa.2010.11.012subject
Has Abstractpub_date
2011-02-01 00:00:00pages
88-102issue
1eissn
1367-5931issn
1879-0402pii
S1367-5931(10)00188-2journal_volume
15pub_type
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