Cryogenic Ion Spectroscopy of a Singly Protonated Peptide DYYVVR: Locating Phosphorylation Sites of a Kinase Domain
Author:
Affiliation:
1. Department of Energy Systems Research, Ajou University, Suwon 16499, Korea
2. Department of Chemistry, School of Science, Tokyo Institute of Technology, Tokyo 152-8550, Japan
3. Department of Chemistry, Ajou University, Suwon 16499, Korea
Funder
Ministry of Education, Culture, Sports, Science and Technology
National Research Foundation of Korea
Korea Institute of Energy Technology Evaluation and Planning
Publisher
American Chemical Society (ACS)
Subject
General Materials Science,Physical and Theoretical Chemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/acs.jpclett.0c01802
Reference25 articles.
1. Protein Posttranslational Modifications: The Chemistry of Proteome Diversifications
2. Protein Phosphorylation: A Major Switch Mechanism for Metabolic Regulation
3. Analysis of protein phosphorylation using mass spectrometry: deciphering the phosphoproteome
4. Tandem mass spectrometry strategies for phosphoproteome analysis
5. Determination of Site-Specific Phosphorylation Ratios in Proteins with Targeted Mass Spectrometry
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