ArticleBioscience reports2010
Electron capture dissociation mass spectrometric analysis of lysine-phosphorylated peptides.
Article in Bioscience reports, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 30 citations in OpenAlex.
- Are you having a LaPh? Diverse roles of Labile Phosphorylation in mammalian cells.Biochemical Society transactions · 2025Review
- Multimodal Tandem Mass Spectrometry Techniques for the Analysis of Phosphopeptides.Journal of the American Society for Mass Spectrometry · 2022Article
- Article
- Immunohistochemistry (IHC): Chromogenic Detection of 3-Phosphohistidine Proteins in Formaldehyde-Fixed, Frozen Mouse Liver Tissue Sections.Methods in molecular biology (Clifton, N.J.) · 2020Article
- Electron Transfer/Higher Energy Collisional Dissociation of Doubly Charged Peptide Ions: Identification of Labile Protein Phosphorylations.Journal of the American Society for Mass Spectrometry · 2019Article
- Phosphopeptide Fragmentation and Site Localization by Mass Spectrometry: An Update.Analytical chemistry · 2019Review
- Electron transfer dissociation mass spectrometry of acidic phosphorylated peptides cationized with trivalent praseodymium.Journal of mass spectrometry : JMS · 2018Article
- Activity-Based Profiling Reveals a Regulatory Link between Oxidative Stress and Protein Arginine Phosphorylation.Cell chemical biology · 2016Article
- Phosphohistidine phosphatase 1 (PHPT1) also dephosphorylates phospholysine of chemically phosphorylated histone H1 and polylysine.Upsala journal of medical sciences · 2015Article
- Hydrogen-deuterium exchange in imidazole as a tool for studying histidine phosphorylation.Analytical and bioanalytical chemistry · 2014Article
- Gas-phase intermolecular phosphate transfer within a phosphohistidine phosphopeptide dimer.International journal of mass spectrometry · 2014Article
- A screening method for phosphohistidine phosphatase 1 activity.Upsala journal of medical sciences · 2011Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Phosphorylation of proteins is an essential signalling mechanism in eukaryotic and prokaryotic cells. Although N-phosphorylation of basic amino acid is known for its importance in biological systems, it is still poorly explored in terms of products and mechanisms. In the present study, two MS fragmentation methods, ECD (electron-capture dissociation) and CID (collision-induced dissociation), were tested as tools for analysis of N-phosphorylation of three model peptides, RKRSRAE, RKRARKE and PLSRTLSVAAKK. The peptides were phosphorylated by reaction with monopotassium phosphoramidate. The results were confirmed by 1H NMR and 31P NMR studies. The ECD method was found useful for the localization of phosphorylation sites in unstable lysine-phosphorylated peptides. Its main advantage is a significant reduction of the neutral losses related to the phosphoramidate moiety. Moreover, the results indicate that the ECD-MS may be useful for analysis of regioselectivity of the N-phosphorylation reaction. Stabilities of the obtained lysine-phosphorylated peptides under various conditions were also tested.
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