Orchestrating redox signaling networks through regulatory cysteine switches

  • Paulsen C
  • Carroll K
  • 173


    Mendeley users who have this article in their library.
  • 301


    Citations of this article.


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.

Author-supplied keywords

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

Get free article suggestions today

Mendeley saves you time finding and organizing research

Sign up here
Already have an account ?Sign in

Find this document


Cite this document

Choose a citation style from the tabs below

Save time finding and organizing research with Mendeley

Sign up for free