Journal
ACS CHEMICAL BIOLOGY
Volume 5, Issue 1, Pages 47-62Publisher
AMER CHEMICAL SOC
DOI: 10.1021/cb900258z
Keywords
Chemoselective/chemospecific probes; NADPH oxidases (NOX); Oxidative stress; Oxoform; Posttranslational modification (PTM)
Categories
Funding
- CBI [T32-GM-008597-13]
- Life Sciences Institute
- American Heart Association [0835419N]
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM087638, T32GM008597] Funding Source: NIH RePORTER
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Hydrogen peroxide (H2O2) acts as a second messenger that can mediate intracellular signal transduction via chemoselective oxidation of cysteine residues in signaling proteins. This Review presents current mechanistic insights into signal-mediated H2O2 production and highlights recent advances in methods to detect reactive oxygen species (ROS) and cysteine oxidation both in vitro and in cells. Selected examples from the recent literature are used to illustrate the diverse mechanisms by which H2O2 can regulate protein function. The continued development of methods to detect and quantify discrete cysteine oxoforms should further our mechanistic understanding of redox regulation of protein function and may lead to the development of new therapeutic strategies.
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