Characteristic negative ion fragmentations of deprotonated peptides containing post-translational modifications: mono-phosphorylated Ser, Thr and Tyr. A joint experimental and theoretical study-Reference-Cited by-同舟云学术

Characteristic negative ion fragmentations of deprotonated peptides containing post-translational modifications: mono-phosphorylated Ser, Thr and Tyr. A joint experimental and theoretical study

Published:2008-09-29 Issue:20 Volume:22 Page:3305-3312
ISSN:0951-4198
Container-title:Rapid Communications in Mass Spectrometry
language:en
Short-container-title:Rapid Commun. Mass Spectrom.

Author:

Andreazza Hayley J.,Fitzgerald Mark,Bilusich Daniel,Hoffmann Ralf,Hoffmann Peter,Eichinger Peter C. H.,Bowie John H.

Funder

Australian Research Council

Publisher

Wiley

Subject

Organic Chemistry,Spectroscopy,Analytical Chemistry

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1002/rcm.3736/fullpdf

Reference25 articles.

1. Analysis of protein phosphorylation on a proteome-scale

2. Mechanistic Insights into the Multistage Gas-Phase Fragmentation Behavior of Phosphoserine- and Phosphothreonine-Containing Peptides

3. Peptide Sequencing and Characterization of Post-Translational Modifications by Enhanced Ion-Charging and Liquid Chromatography Electron-Transfer Dissociation Tandem Mass Spectrometry

4. Identification of single and double sites of phosphorylation by ECD FT-ICR/MS in peptides related to the phosphorylation site domain of the myristoylated alanine-rich c kinase protein

5. Evaluation of the impact of some experimental procedures on different phosphopeptide enrichment techniques

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