Temperature Effects on Structural and Functional Properties of Rat Lens Phe71 Mutant αA-Crystallins
Author:
Publisher
Wiley
Subject
General Chemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1002/jccs.200800147/fullpdf
Reference45 articles.
1. Correlation Between the Loss of the Chaperone-like Activity and the Oxidation, Isomerization and Racemization of Gamma-irradiated Alpha-crystallin¶
2. Phosphorylation-induced Change of the Oligomerization State of αB-crystallin
3. Deamidation Affects Structural and Functional Properties of Human αA-Crystallin and Its Oligomerization with αB-Crystallin
4. α-Crystallin as a molecular chaperone
5. Decreased Molecular Chaperone Property of α-Crystallins Due to Posttranslational Modifications
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1. H101G Mutation in Rat Lens αB-Crystallin Alters Chaperone Activity and Divalent Metal Ion Binding;Current Pharmaceutical Biotechnology;2022-04
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3. The Chaperone-like Activity and Structure of Mutant H119G of Rat Lens αB-crystallin: A Study of Divalent Metal Ion Binding Site;Journal of the Chinese Chemical Society;2014-05-26
4. Effects of Divalent Metal Ions on the Chaperone Activity and Structure of Rat Lens H18G Mutant αB-Crystallin;Journal of the Chinese Chemical Society;2013-07-03
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