ArticleJournal of the American Chemical Society2016
Harnessing Redox Cross-Reactivity To Profile Distinct Cysteine Modifications.
Article in Journal of the American Chemical Society, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 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.
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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
20 citing papers in PubMed, 50 citations in OpenAlex.
- Thiol redox proteomics: Characterization of thiol-based post-translational modifications.Proteomics · 2023Review
- Cyclic Thiosulfonates for Thiol-Mediated Uptake: Cascade Exchangers, Transporters, Inhibitors.JACS Au · 2022Article
- Hsp70 in Redox Homeostasis.Cells · 2022Review
- A ratiometric photoelectrochemical microsensor based on a small-molecule organic semiconductor for reliableChemical science · 2021Article
- Oxidation-Induced "One-Pot" Click Chemistry.Chemical reviews · 2021Article
- Contemporary proteomic strategies for cysteine redoxome profiling.Plant physiology · 2021Review
- Introduction to approaches and tools for the evaluation of protein cysteine oxidation.Essays in biochemistry · 2020Review
- Activity-Based Sensing for Site-Specific Proteomic Analysis of Cysteine Oxidation.Accounts of chemical research · 2020Review
- Chemical Probes for Redox Signaling and Oxidative Stress.Antioxidants & redox signaling · 2019Review
- Mass Spectrometry in Advancement of Redox Precision Medicine.Advances in experimental medicine and biology · 2019Review
- n→π* Interactions Modulate the Properties of Cysteine Residues and Disulfide Bonds in Proteins.Journal of the American Chemical Society · 2018Article
- Chemical proteomics reveals new targets of cysteine sulfinic acid reductase.Nature chemical biology · 2018Article
- Redox regulation of cell proliferation: Bioinformatics and redox proteomics approaches to identify redox-sensitive cell cycle regulators.Free radical biology & medicine · 2018Review
- Chemical proteomic profiling of proteinChemical science · 2018Article
- Profiling Protein S-Sulfination with Maleimide-Linked Probes.Chembiochem : a European journal of chemical biology · 2017Article
- Targeted Annotation of S-Sulfonylated Peptides by Selective Infrared Multiphoton Dissociation Mass Spectrometry.Analytical chemistry · 2017Article
- Quantitative proteomic characterization of redox-dependent post-translational modifications on protein cysteines.Molecular bioSystems · 2017Review
- Subcellular Redox Targeting: Bridging in Vitro and in Vivo Chemical Biology.ACS chemical biology · 2017Review
- Activity-based protein profiling for mapping and pharmacologically interrogating proteome-wide ligandable hotspots.Current opinion in biotechnology · 2017Review
- Chemoproteomic Strategy to Quantitatively Monitor Transnitrosation Uncovers Functionally Relevant S-Nitrosation Sites on Cathepsin D and HADH2.Cell chemical biology · 2016Article
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
Cysteine S-nitrosation and S-sulfination are naturally occurring post-translational modifications (PTMs) on proteins induced by physiological signals and redox stress. Here we demonstrate that sulfinic acids and nitrosothiols react to form a stable thiosulfonate bond, and leverage this reactivity using sulfinate-linked probes to enrich and annotate hundreds of endogenous S-nitrosated proteins. In physiological buffers, sulfinic acids do not react with iodoacetamide or disulfides, enabling selective alkylation of free thiols and site-specific analysis of S-nitrosation. In parallel, S-nitrosothiol-linked probes enable enrichment and detection of endogenous S-sulfinated proteins, confirming that a single sulfinic acid can react with a nitrosothiol to form a thiosulfonate linkage. Using this approach, we find that hydrogen peroxide addition increases S-sulfination of human DJ-1 (PARK7) at Cys106, whereas Cys46 and Cys53 are fully oxidized to sulfonic acids. Comparative gel-based analysis of different mouse tissues reveals distinct profiles for both S-nitrosation and S-sulfination. Quantitative proteomic analysis demonstrates that both S-nitrosation and S-sulfination are widespread, yet exhibit enhanced occupancy on select proteins, including thioredoxin, peroxiredoxins, and other validated redox active proteins. Overall, we present a direct, bidirectional method to profile select redox cysteine modifications based on the unique nucleophilicity of sulfinic acids.
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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.