Related Experiment Video
Updated: Jun 18, 2026

Resin-Assisted Capture Coupled with Isobaric Tandem Mass Tag Labeling for Multiplexed Quantification of Protein Thiol Oxidation
Published on: June 21, 2021
Orchestrating redox signaling networks through regulatory cysteine switches
Candice E Paulsen1, Kate S Carroll
1Chemical Biology Graduate Program, Department of Chemistry, University of Michigan, Ann Arbor, MI 48109-2216, USA.
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.
More Related Videos
09:37Combining Non-reducing SDS-PAGE Analysis and Chemical Crosslinking to Detect Multimeric Complexes Stabilized by Disulfide Linkages in Mammalian Cells in Culture
Published on: May 2, 2019
05:28Monitoring On-Target Signaling Responses in Larval Zebrafish - Z-REX Unmasks Precise Mechanisms of Electrophilic Drugs and Metabolites
Published on: June 2, 2023
Related Concept Videos
Covalently Linked Protein Regulators
These groups modify specific amino acids in a protein.
Covalently Linked Protein Regulators
These groups modify specific amino acids in a protein.
Redox Reactions
Redox Reactions
Redox Equilibria: Overview
The Supercomplexes in the Crista Membrane