ArticleArchives of biochemistry and biophysics2017
The role of sulfenic acids in cellular redox signaling: Reconciling chemical kinetics and molecular detection strategies.
Article in Archives of biochemistry and biophysics, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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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
23 citing papers in PubMed, 68 citations in OpenAlex.
- Article
- Redox Regulation of Brain Selective Kinases BRSK1/2: Implications for Dynamic Control of the Eukaryotic AMPK family through Cys-based mechanisms.bioRxiv : the preprint server for biology · 2024Article
- Redox-active endosomes mediate α5β1 integrin signaling and promote chondrocyte matrix metalloproteinase production in osteoarthritis.Science signaling · 2023Article
- KRIT1: A Traffic Warden at the Busy Crossroads Between Redox Signaling and the Pathogenesis of Cerebral Cavernous Malformation Disease.Antioxidants & redox signaling · 2023Review
- Development of Dietary Thiol Antioxidant via Reductive Modification of Whey Protein and Its Application in the Treatment of Ischemic Kidney Injury.Antioxidants (Basel, Switzerland) · 2023Article
- Bioinformatic Analyses of Peroxiredoxins and RF-Prx: A Random Forest-Based Predictor and Classifier for Prxs.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Cys-SH based quantitative redox proteomics of salt induced response in sugar beet monosomic addition line M14.Botanical studies · 2021Article
- Characterization of Endogenous and Extruded HACS chemical biology · 2021Article
- Reductively modified albumin attenuates DSS-Induced mouse colitis through rebalancing systemic redox state.Redox biology · 2021Article
- Protein S-glutathionylation reactions as a global inhibitor of cell metabolism for the desensitization of hydrogen peroxide signals.Redox biology · 2020Review
- Redox regulation of tyrosine kinase signalling: more than meets the eye.Journal of biochemistry · 2020Review
- Dual-ReactivityJournal of the American Chemical Society · 2019Article
- Disulfide Bond Formation in the Periplasm ofEcoSal Plus · 2019Review
- Proteomic Methods to Evaluate NOX-Mediated Redox Signaling.Methods in molecular biology (Clifton, N.J.) · 2019Article
- Direct cysteine sulfenylation drives activation of the Src kinase.Nature communications · 2018Article
- Oxidative stress in chronic lung disease: From mitochondrial dysfunction to dysregulated redox signaling.Molecular aspects of medicine · 2018Review
- Redox Signaling by Reactive Electrophiles and Oxidants.Chemical reviews · 2018Review
- Cysteine perthiosulfenic acid (Cys-SSOH): A novel intermediate in thiol-based redox signaling?Redox biology · 2018Article
- Mitochondrial protein sulfenation during aging in the rat brain.Biophysics reports · 2018Article
- Endogenous, regulatory cysteine sulfenylation of ERK kinases in response to proliferative signals.Free radical biology & medicine · 2017Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The reversible oxidation of protein cysteine residues is well recognized as an important regulatory mechanism in redox-dependent cell signaling. Cysteine oxidation is diverse in nature and involves various post-translational modifications (sulfenic acids, disulfides, etc.) and the specific functional or structural impact of these specific oxidative events is still poorly understood. The proximal product of protein cysteine oxidation by biological reactive oxygen species (ROS) is sulfenic acid (Cys-SOH), and experimental evidence is accruing for the formation of Cys-SOH as intermediate in protein cysteine oxidation in various biological settings. However, the plausibility of protein Cys-SH oxidation by ROS has often been put in question because of slow reaction kinetics compared to more favorable reactions with abundant thiol-based reductants such as peroxiredoxins (Prx) or glutathione (GSH). This commentary aims to address this controversy by highlighting the unique physical properties in cells that may restrict ROS diffusion and allow otherwise less favorable cysteine oxidation of proteins. Some limitations of analytical tools to assess Cys-SOH are also discussed. We conclude that formation of Cys-SOH in biological systems cannot always be predicted based on kinetic analyses in homogenous solution, and may be facilitated by unique structural and physical properties of Cys-containing proteins within e.g. signaling complexes.
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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.