ReviewAntioxidants (Basel, Switzerland)2021
Stoichiometric Thiol Redox Proteomics for Quantifying Cellular Responses to Perturbations.
Review in Antioxidants (Basel, Switzerland), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed.
- Aged Mitochondrial DNA Is Associated With Aberrant Acute Exercise-Induced Redox Responses in Human Skeletal Muscle.Aging cell · 2026Article
- Defining and refining the cysteine redoxome through sulfur chemical biology.Nature chemical biology · 2026Review
- Proteoforms as the true units of physiological function.European journal of applied physiology · 2026Review
- Integrating Redox Proteomics and Computational Modeling to Decipher Thiol-Based Oxidative Post-Translational Modifications (oxiPTMs) in Plant Stress Physiology.International journal of molecular sciences · 2025Review
- Comparative Quantitative Proteomic Analysis of High and Low Toxin-ProducingMarine drugs · 2025Article
- Low-input redoxomics facilitates global identification of metabolic regulators of oxidative stress in the gut.Signal transduction and targeted therapy · 2025Article
- Mechanisms and therapeutic potential of disulphidptosis in cancer.Cell proliferation · 2025Review
- Ten "Cheat Codes" for Measuring Oxidative Stress in Humans.Antioxidants (Basel, Switzerland) · 2024Review
- Article
- Thiol redox proteomics: Characterization of thiol-based post-translational modifications.Proteomics · 2023Review
- A deep redox proteome profiling workflow and its application to skeletal muscle of a Duchenne Muscular Dystrophy model.Free radical biology & medicine · 2022Article
- Defining the S-Glutathionylation Proteome by Biochemical and Mass Spectrometric Approaches.Antioxidants (Basel, Switzerland) · 2022Review
- SP3-Enabled Rapid and High Coverage Chemoproteomic Identification of Cell-State-Dependent Redox-Sensitive Cysteines.Molecular & cellular proteomics : MCP · 2022Article
- RedoxiFluor: A microplate technique to quantify target-specific protein thiol redox state in relative percentage and molar terms.Free radical biology & medicine · 2022Article
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
Post-translational modifications regulate the structure and function of proteins that can result in changes to the activity of different pathways. These include modifications altering the redox state of thiol groups on protein cysteine residues, which are sensitive to oxidative environments. While mass spectrometry has advanced the identification of protein thiol modifications and expanded our knowledge of redox-sensitive pathways, the quantitative aspect of this technique is critical for the field of redox proteomics. In this review, we describe how mass spectrometry-based redox proteomics has enabled researchers to accurately quantify the stoichiometry of reversible oxidative modifications on specific cysteine residues of proteins. We will describe advancements in the methodology that allow for the absolute quantitation of thiol modifications, as well as recent reports that have implemented this approach. We will also highlight the significance and application of such measurements and why they are informative for the field of redox biology.
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Registered trials
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