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Congenital cataract-causing mutation βB1-L116P is prone to amyloid fibrils aggregation and protease degradation with low structural stability

  • Published:2022-01 Issue: Volume:195 Page:475-482
  • ISSN:0141-8130
  • Container-title:International Journal of Biological Macromolecules
  • language:en
  • Short-container-title:International Journal of Biological Macromolecules

Author:

Liu Jian,Xu Wanyue,Wang Kaijie,Chen Fanrui,Ren Ling,Xu Jingjie,Yao Ke,Chen Xiangjun

Funder

Tsinghua University

Natural Science Foundation of Zhejiang Province

Zhejiang University

National Natural Science Foundation of China

Publisher

Elsevier BV

Subject

Molecular Biology,General Medicine,Biochemistry,Structural Biology

Reference47 articles.

1. Molecular genetic basis of inherited cataract and associated phenotypes;Reddy;Surv. Ophthalmol.,2004

2. Cat-map: putting cataract on the map;Shiels;Mol. Vis.,2010

3. Congenital hereditary cataracts;Graw;Int. J. Dev. Biol.,2004

4. Protein misfolding and aggregation in cataract disease and prospects for prevention;Moreau;Trends Mol. Med.,2012

5. Alpha-crystallin can function as a molecular chaperone;Horwitz;Proc. Natl. Acad. Sci. U. S. A.,1992

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