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Updated: Nov 10, 2025

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Resin-Assisted Capture Coupled with Isobaric Tandem Mass Tag Labeling for Multiplexed Quantification of Protein Thiol Oxidation
Published on: June 21, 2021
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Stoichiometric Thiol Redox Proteomics for Quantifying Cellular Responses to Perturbations
Nicholas J Day1, Matthew J Gaffrey1, Wei-Jun Qian1
1Pacific Northwest National Laboratory, Biological Sciences Division, Richland, WA 99352, USA.
Antioxidants (Basel, Switzerland)
|April 3, 2021
Summary
Quantitative redox proteomics uses mass spectrometry to measure oxidative modifications on protein cysteine residues. This technique accurately quantifies thiol modifications, advancing redox biology research.
Area of Science:
- Biochemistry
- Proteomics
- Redox Biology
Background:
- Post-translational modifications regulate protein function and cellular pathways.
- Cysteine residues are sensitive to oxidative environments, undergoing thiol modifications.
- Mass spectrometry is key for identifying protein thiol modifications.
Purpose of the Study:
- To review advancements in mass spectrometry-based redox proteomics.
- To highlight methods for quantifying thiol modifications on cysteine residues.
- To emphasize the importance of quantitative redox proteomics in redox biology.
Main Methods:
- Mass spectrometry-based redox proteomics.
- Quantitative analysis of reversible oxidative modifications.
- Absolute quantitation of protein thiol modifications.
Main Results:
- Mass spectrometry enables accurate quantification of cysteine thiol modifications.
- Methodological advancements allow for absolute quantitation of these modifications.
- Recent studies demonstrate the application of these quantitative approaches.
Conclusions:
- Quantitative redox proteomics is crucial for understanding redox-sensitive pathways.
- Accurate measurements of thiol modifications provide insights into protein function.
- This approach significantly contributes to the field of redox biology.
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