Cataract-causing Y204X mutation of crystallin protein CRYβB1 promotes its C-terminal degradation and higher-order oligomerization

Author:

Jing Xuping,Zhu Mingwei,Lu Xiaoyun,Wei Ping,Shi Lingyu,Zhang Bu-Yu,Xu Yi,Tang Ya-Ping,Xiang Dao-Man,Gong Peng

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference39 articles.

1. Crystal structure of truncated human betaB1-crystallin;Van Montfort;Protein Sci.,2003

2. Increasing susceptibility to oxidative stress by cataract-causing crystallin mutations;Zhao;Int. J. Biol. Macromol.,2018

3. Clinical and experimental advances in congenital and paediatric cataracts;Churchill;Philos. Trans. R. Soc. Lond. B Biol. Sci.,2011

4. A novel truncation mutation in CRYBB1 associated with autosomal dominant congenital cataract with nystagmus;Rao;Mol. Vis.,2017

5. Human betaB2-Crystallin forms a face-en-face dimer in solution: an integrated NMR and SAXS study;Xi;Structure,2017

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