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Orchestrating Redox Signaling Networks through Regulatory Cysteine Switches

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Paulsen, Candice E., Carroll, Kate S.·2010·ACS Chemical Biology

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Abstract

Hydrogen peroxide (H(2)O(2)) 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 H(2)O(2) 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 H(2)O(2) 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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See all 476

Authors: Paulsen, C. E., & Carroll, K. S.
Venue: ACS Chemical Biology
Publisher: American Chemical Society (ACS)
Published: 2009-12-16
Volume: 5
Issue: 1
Pages: 47-62
ISSN: 1554-8929 (ISSN-L)
1554-8937
DOI: 10.1021/cb900258z
OpenAlex: W2077351642
Cited by: 476
References: 154
FWCI: 15.72
Type: journal article
Language: en
Open access: green

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Orchestrating Redox Signaling Networks through Regulatory Cysteine Switches

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