Site‐specific rapid deamidation and isomerization in human lens αA‐crystallin in vitro
Author:
Affiliation:
1. Kyoto University Institute for Integrated Radiation and Nuclear Science Osaka Japan
2. Department of Chemistry Graduate School of Science, Kyoto University Kyoto Japan
3. Rexxam Co., Ltd. Osaka Japan
Publisher
Wiley
Subject
Molecular Biology,Biochemistry
Link
https://onlinelibrary.wiley.com/doi/pdf/10.1002/pro.3821
Reference30 articles.
1. Age-Related Changes in Human Crystallins Determined from Comparative Analysis of Post-translational Modifications in Young and Aged Lens: Does Deamidation Contribute to Crystallin Insolubility?
2. A Rapid, Comprehensive Liquid Chromatography-Mass Spectrometry (LC-MS)-based Survey of the Asp Isomers in Crystallins from Human Cataract Lenses
3. Rapid Survey of Four Asp Isomers in Disease-Related Proteins by LC-MS combined with Commercial Enzymes
4. Laser light-scattering evidence for an altered association of B1-crystallin deamidated in the connecting peptide
5. Deamidation in Human Lens βB2-Crystallin Destabilizes the Dimer
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