Size of Human Lens β-Crystallin Aggregates Are Distinguished by N-terminal Truncation of βB1
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference28 articles.
1. The Eye;Harding,1984
2. Short-range order of crystallin proteins accounts for eye lens transparency
3. The amino acid sequence of the A chain of human α-crystallin
4. The primary structure of the B2 chain of human α-crystallin
5. Sequence Analysis of βA3, βB3, and βA4 Crystallins Completes the Identification of the Major Proteins in Young Human Lens
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1. Cataract-causing Y204X mutation of crystallin protein CRYβB1 promotes its C-terminal degradation and higher-order oligomerization;Journal of Biological Chemistry;2023-08
2. Cataract-causing variant Q70P damages structural stability of βB1-crystallin and increases its tendency to form insoluble aggregates;International Journal of Biological Macromolecules;2023-07
3. A cataract-causing Y204X mutation of CRYßB1 promotes C-terminal degradation and higher-order oligomerization;2023-02-25
4. Congenital cataract-causing mutation βB1-L116P is prone to amyloid fibrils aggregation and protease degradation with low structural stability;International Journal of Biological Macromolecules;2022-01
5. Eye Lens Crystallins: Remarkable Long‐Lived Proteins;Long‐lived Proteins in Human Aging and Disease;2021-02-05
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