ArticleNature communications2014
Site-specific mapping and quantification of protein S-sulphenylation in cells.
Article in Nature communications, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 125 papers.
What it found
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Who cites it
125 citing papers in PubMed, 238 citations in OpenAlex.
- Hydrogen peroxide sensing and signaling in physiology and disease: implications for therapy.Signal transduction and targeted therapy · 2026Review
- Crosstalk between cysteine and lysine modifications: Integrating redox and metabolic regulation.Redox biology · 2026Review
- Protein thiol alterations drive pathologic liquid-liquid phase separation in the aging brain.Nature structural & molecular biology · 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
- Profiling the landscape of cysteine posttranslational modifications in brain aging and neurodegeneration.Neurotherapeutics : the journal of the American Society for Experimental NeuroTherapeutics · 2025Review
- Low-input redoxomics facilitates global identification of metabolic regulators of oxidative stress in the gut.Signal transduction and targeted therapy · 2025Article
- BioSemAF-BiLSTM: a protein sequence feature extraction framework based on semantic and evolutionary information.Frontiers in genetics · 2025Article
- Inhibition of Sirtuin Deacylase Activity by Peroxynitrite.Biochemistry · 2024Article
- Ligand discovery by activity-based protein profiling.Cell chemical biology · 2024Review
- Review
- Ascorbate peroxidase in fruits and modulation of its activity by reactive species.Journal of experimental botany · 2024Review
- Nucleophilic covalent ligand discovery for the cysteine redoxome.Nature chemical biology · 2023Article
- Emerging Chemical Biology of Protein Persulfidation.Antioxidants & redox signaling · 2023Review
- Thiol redox proteomics: Characterization of thiol-based post-translational modifications.Proteomics · 2023Review
- Redox proteomics combined with proximity labeling enables monitoring of localized cysteine oxidation in cells.Cell chemical biology · 2023Article
- SIRT6's function in controlling the metabolism of lipids and glucose in diabetic nephropathy.Frontiers in endocrinology · 2023Review
- The role of nitric oxide and hydrogen sulfide in regulation of redox homeostasis at extreme temperatures in plants.Frontiers in plant science · 2023Review
- Emerging chemistry and biology in protein glutathionylation.Current opinion in chemical biology · 2022Review
- CysModDB: a comprehensive platform with the integration of manually curated resources and analysis tools for cysteine posttranslational modifications.Briefings in bioinformatics · 2022Article
- The covalent reactivity of functionalized 5-hydroxy-butyrolactams is the basis for targeting of fatty acid binding protein 5 (FABP5) by the neurotrophic agent MT-21.RSC chemical biology · 2022Article
65 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
4 authors at 2 institutions in 1 country.
Funding
Abstract
Cysteine S-sulphenylation provides redox regulation of protein functions, but the global cellular impact of this transient post-translational modification remains unexplored. We describe a chemoproteomic workflow to map and quantify over 1,000 S-sulphenylation sites on more than 700 proteins in intact cells. Quantitative analysis of human cells stimulated with hydrogen peroxide or epidermal growth factor measured hundreds of site selective redox changes. Different cysteines in the same proteins displayed dramatic differences in susceptibility to S-sulphenylation. Newly discovered S-sulphenylations provided mechanistic support for proposed cysteine redox reactions and suggested novel redox mechanisms, including S-sulphenyl-mediated redox regulation of the transcription factor HIF1A by SIRT6. S-sulphenylation is favored at solvent-exposed protein surfaces and is associated with sequence motifs that are distinct from those for other thiol modifications. S-sulphenylations affect regulators of phosphorylation, acetylation and ubiquitylation, which suggest regulatory crosstalk between redox control and signalling pathways.
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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.