ArticleJournal of the American Society for Mass Spectrometry2007
Sulfopeptide fragmentation in electron-capture and electron-transfer dissociation.
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 24 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.
The trial behind it
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
24 citing papers in PubMed.
- Mobility-Assisted Pseudo-MSJournal of the American Society for Mass Spectrometry · 2024Article
- Electron Capture vs Transfer Dissociation for Site Determination of Tryptic Peptide Tyrosine Sulfation: Direct Detection of Fibrinogen Sulfation Sites and Identification of Novel Isobaric Interferences.Journal of proteome research · 2024Article
- Sulfoproteomics Workflow with Precursor Ion Accurate Mass Shift Analysis Reveals Novel Tyrosine Sulfoproteins in the Golgi.Journal of proteome research · 2024Article
- Custom Workflow for the Confident Identification of Sulfotyrosine-Containing Peptides and Their Discrimination from Phosphopeptides.Journal of proteome research · 2023Article
- MSFragger-Labile: A Flexible Method to Improve Labile PTM Analysis in Proteomics.Molecular & cellular proteomics : MCP · 2023Article
- The Key Role of Metal Adducts in the Differentiation of Phosphopeptide from Sulfopeptide Sequences by High-Resolution Mass Spectrometry.Analytical chemistry · 2022Article
- Free Radical Initiated Peptide Sequencing for Direct Site Localization of Sulfation and Phosphorylation with Negative Ion Mode Mass Spectrometry.Analytical chemistry · 2018Article
- Distinguishing Sulfotyrosine Containing Peptides from their Phosphotyrosine Counterparts Using Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2018Article
- Positive Mode LC-MS/MS Analysis of Chondroitin Sulfate Modified Glycopeptides Derived from Light and Heavy Chains of The Human Inter-α-Trypsin Inhibitor Complex.Molecular & cellular proteomics : MCP · 2015Article
- Direct identification of tyrosine sulfation by using ultraviolet photodissociation mass spectrometry.Journal of the American Society for Mass Spectrometry · 2014Article
- Electron capture dissociation of trivalent metal ion-peptide complexes.Journal of the American Society for Mass Spectrometry · 2013Article
- Cysteine oxidative posttranslational modifications: emerging regulation in the cardiovascular system.Circulation research · 2013Review
- Chasing cysteine oxidative modifications: proteomic tools for characterizing cysteine redox status.Circulation. Cardiovascular genetics · 2012Article
- Discrimination between peptide O-sulfo- and O-phosphotyrosine residues by negative ion mode electrospray tandem mass spectrometry.Journal of the American Society for Mass Spectrometry · 2011Article
- Sequential abundant ion fragmentation analysis (SAIFA): an alternative approach for phosphopeptide identification using an ion trap mass spectrometer.Analytical biochemistry · 2011Article
- Metastable atom-activated dissociation mass spectrometry of phosphorylated and sulfonated peptides in negative ion mode.Journal of the American Society for Mass Spectrometry · 2011Article
- Phosphoproteomics for the masses.ACS chemical biology · 2010Review
- Analysis of flagellar phosphoproteins from Chlamydomonas reinhardtii.Eukaryotic cell · 2009Article
- Collisions or electrons? Protein sequence analysis in the 21st century.Analytical chemistry · 2009Article
- Artifactual sulfation of silver-stained proteins: implications for the assignment of phosphorylation and sulfation sites.Molecular & cellular proteomics : MCP · 2009Article
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
Sulfopeptides can be misassigned as phosphopeptides because of the isobaric nature of the sulfo- and the phosphomoieties. Instruments having the ability to measure mass with high accuracy may be employed to distinguish these moieties based on their mass defect (the sulfo-group is 9 mmu lighter than the phosphomoiety). However, the assignment of the exact site(s) of post-translational modification is required to probe biological function. We have reported earlier that peptides with identical sequences containing either O-sulfo- or O-phospho-modifications display different fragmentation behavior (K. F. Medzihradszky et al., Mol. Cell. Proteom.2004, 3, 429-440). We have also established that O-sulfo moieties are susceptible to side-chain fragmentation during collision-induced dissociation. Our present study provides evidence that neutral SO(3) losses can also occur in electron capture dissociation and electron-transfer dissociation experiments. We also report that such neutral losses may be reduced by fragmenting peptide-alkali metal adducts, such as sodiated or potassiated peptides.
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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.