ArticleJournal of the American Society for Mass Spectrometry2007
Characterization by tandem mass spectrometry of stable cysteine sulfenic acid in a cysteine switch peptide of matrix metalloproteinases.
Article in Journal of the American Society for Mass Spectrometry, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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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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Who cites it
16 citing papers in PubMed, 40 citations in OpenAlex.
- Oxidative Stress and Redox Imbalance inInternational journal of molecular sciences · 2026Review
- Oxidative Crosslinking of Peptides and Proteins: Mechanisms of Formation, Detection, Characterization and Quantification.Molecules (Basel, Switzerland) · 2021Review
- Joint Entropy-Assisted Graphene Oxide-Based Multiplexing Biosensing Platform for Simultaneous Detection of Multiple Proteases.Analytical chemistry · 2020Article
- Redox Signaling by Reactive Electrophiles and Oxidants.Chemical reviews · 2018Review
- Mitochondrial protein sulfenation during aging in the rat brain.Biophysics reports · 2018Article
- Inhibitory Effects of Trapping Agents of Sulfur Drug Reactive Intermediates against Major Human Cytochrome P450 Isoforms.International journal of molecular sciences · 2017Article
- Quantitative proteomic characterization of redox-dependent post-translational modifications on protein cysteines.Molecular bioSystems · 2017Review
- Redox Imbalance in the Development of Colorectal Cancer.Journal of Cancer · 2017Review
- The basics of thiols and cysteines in redox biology and chemistry.Free radical biology & medicine · 2015Review
- Thiol-based redox switches.Biochimica et biophysica acta · 2014Review
- Cys34 adducts of reactive oxygen species in human serum albumin.Chemical research in toxicology · 2012Article
- Regulatory control or oxidative damage? Proteomic approaches to interrogate the role of cysteine oxidation status in biological processes.Molecular & cellular proteomics : MCP · 2012Review
- Formation, reactivity, and detection of protein sulfenic acids.Chemical research in toxicology · 2010Review
- Characterization of novel oxidation products of cysteine in an active site motif peptide of PTP1B.Journal of the American Society for Mass Spectrometry · 2009Article
- Aldosterone increases oxidant stress to impair guanylyl cyclase activity by cysteinyl thiol oxidation in vascular smooth muscle cells.The Journal of biological chemistry · 2009Article
- Chemical approaches to detect and analyze protein sulfenic acids.Mass spectrometry reviewsReview
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Cysteine sulfenic acid (Cys-SOH) is an elusive intermediate in reactive oxygen species-induced oxidation reactions of many proteins such as peroxiredoxins and tyrosine phosphatases. Cys-SOH is proposed to play a vital role in catalytic and signaling functions. The formation of cysteine sulfinic acid (Cys-SO(2)H) and cysteine sulfonic acid (Cys-SO(3)H) has been implicated in the activation of matrix metalloproteinase-7 (MMP-7) and oxidation of thiol to cysteine sulfinic acid has been associated with the autolytic cleavage of MMP-7. We have examined the formation of cysteine sulfenic acid in a synthetic peptide PRCGVPDVA, which is a cysteine switch domain of MMP-7 and other matrix metalloproteases. We have prepared the cysteine sulfenic acid containing peptide, PRC(SOH)GVPDVA, by reaction with hydroxyl radicals generated by the Fenton reaction (Fe(+2)/H(2)O(2)). We characterized this modified peptide by tandem mass spectrometry and accurate mass measurement experiments. In addition, we used 7-chloro-4-nitrobenzo-2-oxa-1,3-diazol (NBD-Cl) reagent to form an adduct with PRC(SOH)GVPDVA to provide additional evidence for the viability of PRC(SOH)GVPDVA in solution. We also characterized an intramolecular cysteine sulfinamide cross-link product PRC[S(O)N]GVPDVA based on tandem mass spectrometry and accurate mass measurement experiments. These results contribute to the understanding of a proteolytic cleavage mechanism that is traditionally associated with MMP activation.
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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.