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. © 2010 American Chemical Society.
CITATION STYLE
Paulsen, C. E., & Carroll, K. S. (2010, January 15). Orchestrating redox signaling networks through regulatory cysteine switches. ACS Chemical Biology. https://doi.org/10.1021/cb900258z
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