Quantitating the relative abundance of isoaspartyl residues in deamidated proteins by electron capture dissociation
Author:
Affiliation:
1. Department of Chemistry, Boston University, Boston, Massachusetts, USA
2. Department of Biochemistry, Mass Spectrometry Resource, Boston University School of Medicine, 715 Albany Street, 02118, Boston, MA, USA
Publisher
American Chemical Society (ACS)
Subject
Spectroscopy,Structural Biology
Link
https://pubs.acs.org/doi/pdf/10.1016/j.jasms.2006.08.008
Reference50 articles.
1. Propensity for spontaneous succinimide formation from aspartyl and asparaginyl residues in cellular proteins
2. Isoaspartate in peptides and proteins: formation, significance, and analysis
3. The Major in vivo Modifications of the Human Water-insoluble Lens Crystallins are Disulfide Bonds, Deamidation, Methionine Oxidation and Backbone Cleavage
4. Low levels of asparagine deamidation can have a dramatic effect on aggregation of amyloidogenic peptides: Implications for the study of amyloid formation
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