Detection and Characterization of α-Crystallin Intermediate with Maximal Chaperone-like Activity
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry,Biophysics
Reference31 articles.
1. Four small Drosophila heat shock proteins are related to each other and to mammalian alpha-crystallin.
2. Structural and functional similarities of bovine alpha-crystallin and mouse small heat-shock protein. A family of chaperones.
3. Dogfish alpha-crystallin sequences. Comparison with small heat shock proteins and Schistosoma egg antigen.
4. Alpha B-crystallin is a small heat shock protein.
5. Alpha-crystallin can function as a molecular chaperone.
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1. Significant influence of four highly conserved amino-acids in lipochaperon-active sHsps on the structure and functions of the Lo18 protein;Scientific Reports;2023-11-03
2. Structural determinants of multimerization and dissociation in 2-Cys peroxiredoxin chaperone function;Structure;2021-05
3. Protection of ζ-crystallin by α-crystallin under thermal stress;International Journal of Biological Macromolecules;2021-01
4. Functional Amyloid Protection in the Eye Lens: Retention of α-Crystallin Molecular Chaperone Activity after Modification into Amyloid Fibrils;Biomolecules;2017-09-12
5. Structural and functional consequences of chaperone site deletion in αA-crystallin;Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics;2016-11
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