ArticleThe FEBS journal2013
Thiol-blocking electrophiles interfere with labeling and detection of protein sulfenic acids.
Article in The FEBS journal, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 71 papers.
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Who cites it
71 citing papers in PubMed, 113 citations in OpenAlex.
- Protein persulfidation in plants: a central regulator of multiple signaling pathways.Plant cell reports · 2026Review
- Protein thiol alterations drive pathologic liquid-liquid phase separation in the aging brain.Nature structural & molecular biology · 2026Article
- A FRET-Based Assay for Assessing Covalent Warhead Reactivity.ACS omega · 2026Article
- Multifaceted roles for persulfide species in redox chemical biology.Nature chemical biology · 2026Review
- Defining and refining the cysteine redoxome through sulfur chemical biology.Nature chemical biology · 2026Review
- A proteomics and redox proteomics approach to understanding ARDS heterogeneity.Scientific reports · 2026Article
- Profiling the landscape of cysteine posttranslational modifications in brain aging and neurodegeneration.Neurotherapeutics : the journal of the American Society for Experimental NeuroTherapeutics · 2025Review
- Redox-driven regulation of UCHL3/Yuh1 influences mitochondrial health via the NEDD8/Rub1 pathway.Redox biology · 2025Article
- Mechanism of glutathionylation of the active site thiols of peroxiredoxin 2.The Journal of biological chemistry · 2025Article
- A Novel Peptide Mapping Method Utilizing Cysteine as a Reducing Agent.Pharmaceutical research · 2025Article
- Quantification of persulfidation on specific proteins: are we nearly there yet?Essays in biochemistry · 2024Review
- Analytical Methods for Assessing Thiol Antioxidants in Biological Fluids: A Review.Molecules (Basel, Switzerland) · 2024Review
- Exploring 2-Sulfonylpyrimidine Warheads as Acrylamide Surrogates for Targeted Covalent Inhibition: A BTK Story.Journal of medicinal chemistry · 2024Article
- Ten "Cheat Codes" for Measuring Oxidative Stress in Humans.Antioxidants (Basel, Switzerland) · 2024Review
- Article
- Nucleophilic covalent ligand discovery for the cysteine redoxome.Nature chemical biology · 2023Article
- Structure-Reactivity Studies of 2-Sulfonylpyrimidines Allow Selective Protein Arylation.Bioconjugate chemistry · 2023Article
- Emerging Chemical Biology of Protein Persulfidation.Antioxidants & redox signaling · 2023Review
- 3-Chloro-5-Substituted-1,2,4-Thiadiazoles (TDZs) as Selective and Efficient Protein Thiol Modifiers.Chembiochem : a European journal of chemical biology · 2022Article
- Peroxisome-Derived Hydrogen Peroxide Modulates the Sulfenylation Profiles of Key Redox Signaling Proteins in Flp-In T-REx 293 Cells.Frontiers in cell and developmental biology · 2022Article
11 more citing papers are in PubMed but not listed here.
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Cellular exposure to reactive oxygen species induces rapid oxidation of DNA, proteins, lipids and other biomolecules. At the proteome level, cysteine thiol oxidation is a prominent post-translational process that is implicated in normal physiology and numerous pathologies. Methods for investigating protein oxidation include direct labeling with selective chemical probes and indirect tag-switch techniques. Common to both approaches is chemical blocking of free thiols using reactive electrophiles to prevent post-lysis oxidation or other thiol-mediated cross-reactions. These reagents are used in large excess, and their reactivity with cysteine sulfenic acid, a critical oxoform in numerous proteins, has not been investigated. Here we report the reactivity of three thiol-blocking electrophiles, iodoacetamide, N-ethylmaleimide and methyl methanethiosulfonate, with protein sulfenic acid and dimedone, the structural core of many sulfenic acid probes. We demonstrate that covalent cysteine -SOR (product) species are partially or fully susceptible to reduction by dithiothreitol, tris(2-carboxyethyl)phosphine and ascorbate, regenerating protein thiols, or, in the case of ascorbate, more highly oxidized species. The implications of this reactivity on detection methods for protein sulfenic acids and S-nitrosothiols are discussed.
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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.