Deletion of 54FLRAPSWF61 Residues Decreases the Oligomeric Size and Enhances the Chaperone Function of αB-Crystallin
Author:
Affiliation:
1. Departments of Ophthalmology
2. Biochemistry
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi900085v
Reference53 articles.
1. Alpha-crystallin
2. αB subunit of lens-specific protein α-crystallin is present in other ocular and non-ocular tissues
3. Small heat-shock proteins and their potential role in human disease
4. α-Crystallin-Type Heat Shock Proteins: Socializing Minichaperones in the Context of a Multichaperone Network
5. Small heat shock proteins: molecular structure and chaperone function
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3. Effect of Structural Changes Induced by Deletion of 54FLRAPSWF61 Sequence in αB-crystallin on Chaperone Function and Anti-Apoptotic Activity;International Journal of Molecular Sciences;2021-10-05
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