ArticleJournal of the American Society for Mass Spectrometry2010
Observation of phosphorylation site-specific dissociation of singly protonated phosphopeptides.
Article in Journal of the American Society for Mass Spectrometry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
What it found
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Who cites it
11 citing papers in PubMed.
- Characterization of Phosphorylated Peptides by Electron-Activated and Ultraviolet Dissociation Mass Spectrometry: A Comparative Study with Collision-Induced Dissociation.Journal of the American Society for Mass Spectrometry · 2024Article
- Ultraviolet Photodissociation Mass Spectrometry for Analysis of Biological Molecules.Chemical reviews · 2020Review
- Modulation of Phosphopeptide Fragmentation via Dual Spray Ion/Ion Reactions Using a Sulfonate-Incorporating Reagent.Analytical chemistry · 2016Article
- 193 nm Ultraviolet Photodissociation Mass Spectrometry for Phosphopeptide Characterization in the Positive and Negative Ion Modes.Journal of proteome research · 2016Article
- Comparison of Ultraviolet Photodissociation and Collision Induced Dissociation of Adrenocorticotropic Hormone Peptides.Journal of the American Society for Mass Spectrometry · 2015Article
- Photodissociation mass spectrometry: new tools for characterization of biological molecules.Chemical Society reviews · 2014Review
- Unambiguous phosphosite localization using electron-transfer/higher-energy collision dissociation (EThcD).Journal of proteome research · 2013Article
- Systematic comparison of ultraviolet photodissociation and electron transfer dissociation for peptide anion characterization.Journal of the American Society for Mass Spectrometry · 2012Article
- Shedding light on the frontier of photodissociation.Journal of the American Society for Mass Spectrometry · 2011Article
- Enhanced characterization of singly protonated phosphopeptide ions by femtosecond laser-induced ionization/dissociation tandem mass spectrometry (fs-LID-MS/MS).Journal of the American Society for Mass Spectrometry · 2010Article
- Ultrafast ultraviolet photodissociation at 193 nm and its applicability to proteomic workflows.Journal of proteome research · 2010Article
Corrections and comments
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In ultraviolet photodissociation of phosphopeptide ions with a basic residue (arginine, lysine, or histidine) at the N-terminus, intense a(n) - 97 peaks were observed. These ions were formed by cleavage at phosphorylated residues only. For multiply phosphorylated peptides, this site-specific cleavage occurred at every phosphorylated residue. H/D exchange studies showed that a(n) - 97 was formed by H(3)PO(4) loss from a(n) + 1 radical cations. The site-specificity of phosphate loss observed here is in contrast to the nonspecific phosphate loss from b(n) and y(n) reported previously. Characteristics of the reaction and its potential utility for phosphopeptide analysis are discussed.
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Identifiers
19836972What OpenQuestion holds
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.