ArticleJournal of the American Society for Mass Spectrometry2007
The combination of electron capture dissociation and fixed charge derivatization increases sequence coverage for O-glycosylated and O-phosphorylated peptides.
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 17 papers.
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Who cites it
17 citing papers in PubMed.
- Phosphopeptide Fragmentation and Site Localization by Mass Spectrometry: An Update.Analytical chemistry · 2019Review
- Site-specific O-Glycosylation Analysis of Human Blood Plasma Proteins.Molecular & cellular proteomics : MCP · 2016Article
- Chemical derivatization of peptide carboxyl groups for highly efficient electron transfer dissociation.Journal of the American Society for Mass Spectrometry · 2013Article
- Electron transfer dissociation of photolabeled peptides. Backbone cleavages compete with diazirine ring rearrangements.Journal of the American Society for Mass Spectrometry · 2013Article
- Enhanced electron transfer dissociation of peptides modified at C-terminus with fixed charges.Journal of the American Society for Mass Spectrometry · 2012Article
- Photodissociation of charge tagged peptides.Journal of the American Society for Mass Spectrometry · 2012Article
- Tunable charge tags for electron-based methods of peptide sequencing: design and applications.Journal of the American Society for Mass Spectrometry · 2012Article
- Sulfonium ion derivatization, isobaric stable isotope labeling and data dependent CID- and ETD-MS/MS for enhanced phosphopeptide quantitation, identification and phosphorylation site characterization.Journal of the American Society for Mass Spectrometry · 2012Article
- Dissociation channel dependence on peptide size observed in electron capture dissociation of tryptic peptides.Journal of the American Society for Mass Spectrometry · 2011Article
- Formation of peptide radical cations (m+·) in electron capture dissociation of peptides adducted with group IIB metal ions.Journal of the American Society for Mass Spectrometry · 2011Article
- Electron-capture and -transfer dissociation of peptides tagged with tunable fixed-charge groups: structures and dissociation energetics.Journal of the American Society for Mass Spectrometry · 2011Article
- On the charge partitioning between c and z fragments formed after electron-capture induced dissociation of charge-tagged Lys-Lys and Ala-Lys dipeptide dications.Journal of the American Society for Mass Spectrometry · 2009Article
- Probing the mechanism of electron capture and electron transfer dissociation using tags with variable electron affinity.Journal of the American Chemical Society · 2009Article
- Ortho-proteogenomics: multiple proteomes investigation through orthology and a new MS-based protocol.Genome research · 2009Article
- The effect of fixed charge modifications on electron capture dissociation.Journal of the American Society for Mass Spectrometry · 2008Article
- Electron-capture-induced dissociation of protoporphyrin IX ions.Journal of the American Society for Mass Spectrometry · 2008Article
- Electron capture in charge-tagged peptides. Evidence for the role of excited electronic states.Journal of the American Society for Mass Spectrometry · 2007Article
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5 authors.
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Abstract
Electron capture dissociation (ECD) has become an alternative method to collision-activated dissociation (CAD) to avoid gas-phase cleavage of post-translational modifications carried by side chains from the peptide backbone. Nonetheless, as illustrated herein by the study of O-glycosylated and O-phosphorylated peptides, the extent of ECD fragmentations may be insufficient to cover the entire peptide sequence and to localize accurately these modifications. The present work demonstrates that the derivatization of peptides at their N-terminus by a phosphonium group improves dramatically and systematically the sequence coverage deduced from the ECD spectrum for both O-glycosylated and O-phosphorylated peptides compared with their native counterparts. The exclusive presence of N-terminal fragments (c-type ions) in the ECD spectra of doubly charged molecular cations simplifies peptide sequence interpretation. Thus, the combination of ECD and fixed charge derivatization appears as an efficient analytical tool for the extensive sequencing of peptides bearing labile groups.
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