Dynamical structure of αB-crystallin
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,Biophysics
Reference79 articles.
1. Polydispersity of a mammalian chaperone: mass spectrometry reveals the population of oligomers in αB-crystallin;Aquilina;Proc. Natl. Acad. Sci. USA,2003
2. Subunit exchange of polydisperse proteins, mass spectrometry reveals consequences of αA-crystallin truncation;Aquilina;J. Biol. Chem.,2005
3. Phosphorylation of αB-crystallin alters chaperone function through loss of dimeric substructure;Aquilina;J. Biol. Chem.,2004
4. Structural and functional aspects of hetero-oligomers formed by the small heat shock proteins αB-crystallin and HSP27;Aquilina;J. Biol. Chem.,2013
5. Dissociation is not required for α-crystallin's chaperone function;Augusteyn;Exp. Eye Res.,2004
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1. Insights into the dual nature of αB-crystallin chaperone activity from the p.P39L mutant at the N-terminal region;Scientific Reports;2024-03-28
2. Dynamic fibrillar assembly of αB-crystallin induced by perturbation of the conserved NT-IXI motif resolved by cryo-EM;2024-03-27
3. Chaperone quality control in liquid-phase separated organelles;2024-01-23
4. The Double-Edged Sword of αB-Crystallin Chaperone Activity: Insights from P39L Mutant at N-terminal region;2023-08-21
5. The beauty and complexity of the small heat shock proteins: a report on the proceedings of the fourth workshop on small heat shock proteins;Cell Stress and Chaperones;2023-07-18
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