ArticleBiochemistry2010
Characterization of surface-exposed reactive cysteine residues in Saccharomyces cerevisiae.
Article in Biochemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 50 citations in OpenAlex.
- Characteristics of Two Saccharomyces cerevisiae Strains and Their Extracellular Vesicles as New Candidates for Probiotics.Probiotics and antimicrobial proteins · 2026Article
- Advanced adhesion and targeting strategies to prolong gut residence time and improve eLBP efficacy in colonic diseases.Advanced drug delivery reviews · 2025Review
- Arsenic binds to nuclear transport factors and disrupts nucleocytoplasmic transport.Journal of cell science · 2025Article
- The interactome of the Bakers' yeast peroxiredoxin Tsa1 implicates it in redox regulation of intermediary metabolism, glycolysis, and zinc homeostasis.Metallomics : integrated biometal science · 2025Article
- Direct binding of arsenicals to nuclear transport factors disrupts nucleocytoplasmic transport.bioRxiv : the preprint server for biology · 2025Article
- Ageing-dependent thiol oxidation reveals early oxidation of proteins with core proteostasis functions.Life science alliance · 2024Article
- Distinguishable short-term effects of tea and water drinking on human saliva redox.NPJ science of food · 2024Article
- Modular Diazo Compound for the Bioreversible Late-Stage Modification of Proteins.Journal of the American Chemical Society · 2023Article
- The Structure of Blood Coagulation Factor XIII Is Adapted to Oxidation.Biomolecules · 2020Article
- Trapping redox partnerships in oxidant-sensitive proteins with a small, thiol-reactive cross-linker.Free radical biology & medicine · 2016Article
- Mechanism-based proteomic screening identifies targets of thioredoxin-like proteins.The Journal of biological chemistry · 2015Article
- Chemical approaches to discovery and study of sources and targets of hydrogen peroxide redox signaling through NADPH oxidase proteins.Annual review of biochemistry · 2015Review
- Global analysis of protein aggregation in yeast during physiological conditions and arsenite stress.Biology open · 2014Article
- Review
- Article
- Biophysical and proteomic characterization strategies for cysteine modifications in Ras GTPases.Methods in molecular biology (Clifton, N.J.) · 2014Article
- Cysteine-mediated redox signaling: chemistry, biology, and tools for discovery.Chemical reviews · 2013Review
- Bifunctional electrophiles cross-link thioredoxins with redox relay partners in cells.Chemical research in toxicology · 2013Article
- Cysteine-based redox regulation and signaling in plants.Frontiers in plant science · 2013Article
- Multimolecular salivary mucin complex is altered in saliva of cigarette smokers: detection of disulfide bridges by Raman spectroscopy.BioMed research international · 2013Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
Numerous cellular processes are subject to redox regulation, and thiol-dependent redox control, acting through reactive cysteine (Cys) residues, is among the major mechanisms of redox regulation. However, information on the sets of proteins that provide thiol-based redox regulation or are affected by it is limited. Here, we describe proteomic approaches to characterize proteins that contain reactive thiols and methods to identify redox Cys in these proteins. Using Saccharomyces cerevisiae as a eukaryotic model organism, we identified 284 proteins with exposed reactive Cys and determined the identities of 185 of these residues. We then characterized subsets of these proteins as in vitro targets of major cellular thiol oxidoreductases, thioredoxin and glutaredoxin, and found that these enzymes can control the redox state of a significant number of thiols in target proteins. We further examined common features of exposed reactive Cys and compared them with an unbiased control set of Cys using computational approaches. This analysis (i) validated the efficacy of targeting exposed Cys in proteins in their native, folded state, (ii) quantified the proportion of targets that can be redox regulated via thiol oxidoreductase systems, and (iii) revealed the theoretical range of the experimental approach with regard to protein abundance and physicochemical properties of reactive Cys. From these analyses, we estimate that approximately one-fourth of exposed Cys in the yeast proteome can be regarded as functional sites, either subject to regulation by thiol oxidoreductases or involved in structural disulfides and metal binding.
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Registered trials
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