ArticleProtein science : a publication of the Protein Society2008
Functional site profiling and electrostatic analysis of cysteines modifiable to cysteine sulfenic acid.
Article in Protein science : a publication of the Protein Society, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 68 papers.
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Who cites it
68 citing papers in PubMed, 125 citations in OpenAlex.
- Proteasomal surveillance of exposed cysteines.bioRxiv : the preprint server for biology · 2026Article
- Non-Reducing Proteomics Reveals Disulfide-dependent Proteoform Remodeling Under Oxidative Stress.Molecular & cellular proteomics : MCP · 2026Article
- Effect of pH on the Kinetics of Cysteine-to-Cystine Conversion in Thin Films Formed by ESI Microdroplet Deposition.Journal of the American Society for Mass Spectrometry · 2025Article
- Crystal structures of 40- and 71-substitution variants of hydroxynitrile lyase from rubber tree.Acta crystallographica. Section D, Structural biology · 2025Article
- The role of oxidative post-translational modifications in type 1 diabetes pathogenesis.Frontiers in immunology · 2025Review
- Bioinformatic Analyses of Peroxiredoxins and RF-Prx: A Random Forest-Based Predictor and Classifier for Prxs.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Identification of sulfenylation patterns in trophozoite stage Plasmodium falciparum using a non-dimedone based probe.Molecular and biochemical parasitology · 2021Article
- Activation of Nm23-H1 to suppress breast cancer metastasis via redox regulation.Experimental & molecular medicine · 2021Review
- Cysteine modifications (oxPTM) and protein sulphenylation-mediated sulfenome expression in plants: evolutionary conserved signaling networks?Plant signaling & behavior · 2021Article
- Exercise, redox homeostasis and the epigenetic landscape.Redox biology · 2020Review
- The role of thiols in antioxidant systems.Free radical biology & medicine · 2019Review
- Thioredoxin and glutaredoxin regulate metabolism through different multiplex thiol switches.Redox biology · 2019Article
- Genetic Code Expansion: A Powerful Tool for Understanding the Physiological Consequences of Oxidative Stress Protein Modifications.Oxidative medicine and cellular longevity · 2018Review
- Discovery of Heteroaromatic Sulfones As a New Class of Biologically Compatible Thiol-Selective Reagents.ACS chemical biology · 2017Article
- Prediction of reversible disulfide based on features from local structural signatures.BMC genomics · 2017Article
- Detection of ROS Induced Proteomic Signatures by Mass Spectrometry.Frontiers in physiology · 2017Review
- An oxygen-sensitive toxin-antitoxin system.Nature communications · 2016Article
- Proteomic approaches to quantify cysteine reversible modifications in aging and neurodegenerative diseases.Proteomics. Clinical applications · 2016Review
- Protein S-sulfenylation is a fleeting molecular switch that regulates non-enzymatic oxidative folding.Nature communications · 2016Article
- Light-Mediated Sulfenic Acid Generation from Photocaged Cysteine Sulfoxide.Organic letters · 2015Article
8 more citing papers are in PubMed but not listed here.
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Cysteine sulfenic acid (Cys-SOH), a reversible modification, is a catalytic intermediate at enzyme active sites, a sensor for oxidative stress, a regulator of some transcription factors, and a redox-signaling intermediate. This post-translational modification is not random: specific features near the cysteine control its reactivity. To identify features responsible for the propensity of cysteines to be modified to sulfenic acid, a list of 47 proteins (containing 49 known Cys-SOH sites) was compiled. Modifiable cysteines are found in proteins from most structural classes and many functional classes, but have no propensity for any one type of protein secondary structure. To identify features affecting cysteine reactivity, these sites were analyzed using both functional site profiling and electrostatic analysis. Overall, the solvent exposure of modifiable cysteines is not different from the average cysteine. The combined sequence, structure, and electrostatic approaches reveal mechanistic determinants not obvious from overall sequence comparison, including: (1) pKaS of some modifiable cysteines are affected by backbone features only; (2) charged residues are underrepresented in the structure near modifiable sites; (3) threonine and other polar residues can exert a large influence on the cysteine pKa; and (4) hydrogen bonding patterns are suggested to be important. This compilation of Cys-SOH modification sites and their features provides a quantitative assessment of previous observations and a basis for further analysis and prediction of these sites. Agreement with known experimental data indicates the utility of this combined approach for identifying mechanistic determinants at protein functional sites.
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