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Orchestrating redox signaling networks through regulatory cysteine switches

Academic Article
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Overview

authors

  • Paulsen, C. E.
  • Carroll, Kate

publication date

  • 2010

journal

  • ACS Chemical Biology  Journal

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.

subject areas

  • Animals
  • Cysteine
  • Humans
  • Oxidation-Reduction
  • Reactive Oxygen Species
  • Signal Transduction
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Research

keywords

  • Chemoselective/chemospecific probes
  • NADPH oxidases (NOX)
  • Oxidative stress
  • Oxoform
  • Posttranslational modification (PTM)
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Identity

PubMed Central ID

  • PMC4537063

International Standard Serial Number (ISSN)

  • 1554-8929

Digital Object Identifier (DOI)

  • 10.1021/cb900258z

PubMed ID

  • 19957967
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Additional Document Info

start page

  • 47

end page

  • 62

volume

  • 5

issue

  • 1

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