ReviewCurrent protocols in protein science2019
Proteome-Wide Analysis of Cysteine S-Sulfenylation Using a Benzothiazine-Based Probe.
Review in Current protocols in protein science, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
What it found
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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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
36 citing papers in PubMed, 66 citations in OpenAlex.
- Regulation of PDH via cysteine oxidation on DLAT.Nature communications · 2026Article
- Protein thiol alterations drive pathologic liquid-liquid phase separation in the aging brain.Nature structural & molecular biology · 2026Article
- Defining and refining the cysteine redoxome through sulfur chemical biology.Nature chemical biology · 2026Review
- A novel SO2 probe inhibits lysophagy induced by Senecavirus A infection by promoting LAMP1 Cys375 sulfenylation.PLoS pathogens · 2026Article
- CysDBase: a comprehensive database of cysteine post-translational modifications across protein sequence, structure, microenvironment, class, cellular localization, biological pathway, and taxonomy.Database : the journal of biological databases and curation · 2026Article
- Bioorthogonal Probe BTD-Az Enables Sensitive and Rapid In Vivo Profiling of Protein Cysteine Sulfenylation.Bioconjugate chemistry · 2025Article
- Profiling the landscape of cysteine posttranslational modifications in brain aging and neurodegeneration.Neurotherapeutics : the journal of the American Society for Experimental NeuroTherapeutics · 2025Review
- Nitrogen limitation causes a seismic shift in redox state and phosphorylation of proteins implicated in carbon flux and lipidome remodeling in Rhodotorula toruloides.Biotechnology for biofuels and bioproducts · 2025Article
- On the utility of immobilized phenylarsine oxide in the study of redox sensitive cardiac proteins.Scientific reports · 2025Article
- Analysis of Protein Cysteine Acylation Using a Modified Suspension Trap (Acyl-Trap).Journal of proteome research · 2024Article
- Analysis of Protein Cysteine Acylation Using a Modified Suspension Trap (Acyl-Trap).bioRxiv : the preprint server for biology · 2024Article
- Article
- Nucleophilic covalent ligand discovery for the cysteine redoxome.Nature chemical biology · 2023Article
- HPlant, cell & environment · 2023Review
- Sulfur signaling pathway in cardiovascular disease.Frontiers in pharmacology · 2023Review
- Cysteine Oxidation in Proteins: Structure, Biophysics, and Simulation.Biochemistry · 2022Review
- Reaction-based fluorogenic probes for detecting protein cysteine oxidation in living cells.Nature communications · 2022Article
- A modification-centric assessment tool for the performance of chemoproteomic probes.Nature chemical biology · 2022Article
- Thiol-based Oxidative Posttranslational Modifications (OxiPTMs) of Plant Proteins.Plant & cell physiology · 2022Review
- Hsp70 in Redox Homeostasis.Cells · 2022Review
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
Oxidation of a protein cysteinyl thiol (Cys-SH) to S-sulfenic acid (Cys-SOH) by a reactive oxygen species (e.g., hydrogen peroxide), which is termed protein S-sulfenylation, is a reversible post-translational modification that plays a crucial role in redox regulation of protein function in various biological processes. Due to its intrinsically labile nature, protein S-sulfenylation cannot be directly detected or analyzed. Chemoselective probing has been the method of choice for analyzing S-sulfenylated proteins either in vitro or in situ, as it allows stabilization and direct detection of this transient oxidative intermediate. However, it remains challenging to globally pinpoint the specific S-sulfenylated cysteine sites on complex proteomes and to quantify their dynamic changes upon oxidative stress. This unit describes how a benzothiazine-based chemoselective probe called BTD and mass spectrometry based chemoproteomics can be used to globally and site-specifically identify and quantify protein S-sulfenylation. © 2018 by John Wiley & Sons, Inc.
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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.