ArticleMolecular & cellular proteomics : MCP2010
Targeted quantitation of site-specific cysteine oxidation in endogenous proteins using a differential alkylation and multiple reaction monitoring mass spectrometry approach.
Article in Molecular & cellular proteomics : MCP, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 67 papers, 1 of them a synthesis that pooled it.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
67 citing papers in PubMed, 1 synthesis or guideline pooled it, 137 citations in OpenAlex.
- Differential alkylation-based redox proteomics--Lessons learnt.Redox biology · 2015Pooled it
- A Peptide-Centric DIA-NN Reanalysis Uncovers Structurally Coherent Salivary Signatures of Type 2 Diabetes.International journal of molecular sciences · 2026Article
- Deciphering the safeguarding role of cysteine residues in p53 against HCommunications chemistry · 2025Article
- Combining Native Mass Spectrometry and Proteomics to Differentiate and Map the Metalloform Landscape in Metallothioneins.Journal of proteome research · 2024Article
- Ten "Cheat Codes" for Measuring Oxidative Stress in Humans.Antioxidants (Basel, Switzerland) · 2024Review
- Protein Oxidative Modifications in Neurodegenerative Diseases: From Advances in Detection and Modelling to Their Use as Disease Biomarkers.Antioxidants (Basel, Switzerland) · 2024Review
- Tat-malate dehydrogenase fusion protein protects neurons from oxidative and ischemic damage by reduction of reactive oxygen species and modulation of glutathione redox system.Scientific reports · 2023Article
- Quantitative redox proteomics revealed molecular mechanisms of salt tolerance in the roots of sugar beet monomeric addition line M14.Botanical studies · 2022Article
- RedoxiFluor: A microplate technique to quantify target-specific protein thiol redox state in relative percentage and molar terms.Free radical biology & medicine · 2022Article
- Automating Assignment, Quantitation, and Biological Annotation of Redox Proteomics Datasets with ProteoSushi.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Redox Sensitive Cysteine Residues as Crucial Regulators of Wild-Type and Mutant p53 Isoforms.Cells · 2021Review
- p53 Forms Redox-Dependent Protein-Protein Interactions through Cysteine 277.Antioxidants (Basel, Switzerland) · 2021Article
- Proteomic Approaches to Study Cysteine Oxidation: Applications in Neurodegenerative Diseases.Frontiers in molecular neuroscience · 2021Review
- Metal- and Affinity-Specific Dual Labeling of Cysteine-Rich Proteins for Identification of Metal-Binding Sites.Analytical chemistry · 2020Article
- A clickable probe for versatile characterization of S-nitrosothiols.Redox biology · 2020Article
- Immunological Techniques to Assess Protein Thiol Redox State: Opportunities, Challenges and Solutions.Antioxidants (Basel, Switzerland) · 2020Review
- Redox Systems Biology: Harnessing the Sentinels of the Cysteine Redoxome.Antioxidants & redox signaling · 2020Review
- Redox RegulationAntioxidants & redox signaling · 2020Review
- Spatial and temporal alterations in protein structure by EGF regulate cryptic cysteine oxidation.Science signaling · 2020Article
- oxSWATH: An integrative method for a comprehensive redox-centered analysis combined with a generic differential proteomics screening.Redox biology · 2019Article
7 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
10 authors at 2 institutions in 1 country.
Funding
Abstract
Reactive oxygen species (ROS) are both physiological intermediates in cellular signaling and mediators of oxidative stress. The cysteine-specific redox-sensitivity of proteins can shed light on how ROS are regulated and function, but low sensitivity has limited quantification of the redox state of many fundamental cellular regulators in a cellular context. Here we describe a highly sensitive and reproducible oxidation analysis approach (OxMRM) that combines protein purification, differential alkylation with stable isotopes, and multiple reaction monitoring mass spectrometry that can be applied in a targeted manner to virtually any cysteine or protein. Using this approach, we quantified the site-specific cysteine oxidation status of endogenous p53 for the first time and found that Cys182 at the dimerization interface of the DNA binding domain is particularly susceptible to diamide oxidation intracellularly. OxMRM enables analysis of sulfinic and sulfonic acid oxidation levels, which we validate by assessing the oxidation of the catalytic Cys215 of protein tyrosine phosphatase-1B under numerous oxidant conditions. OxMRM also complements unbiased redox proteomics discovery studies as a verification tool through its high sensitivity, accuracy, precision, and throughput.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.