Predicted aggregation-prone region (APR) in βB1-crystallin forms the amyloid-like structure and induces aggregation of soluble proteins isolated from human cataractous eye lens-Reference-Cited by-同舟云学术

Predicted aggregation-prone region (APR) in βB1-crystallin forms the amyloid-like structure and induces aggregation of soluble proteins isolated from human cataractous eye lens

Published:2020-11 Issue: Volume:163 Page:702-710
ISSN:0141-8130
Container-title:International Journal of Biological Macromolecules
language:en
Short-container-title:International Journal of Biological Macromolecules

Author:

Harsolia Ram Swaroop,Kanwar Ambika,Gour Shalini,Kumar Vijay,Kumar Vikas,Bansal Rati,Kumar Suman,Singh Manish^ORCID,Yadav Jay Kant

Funder

Science and Engineering Research Board

Publisher

Elsevier BV

Subject

Molecular Biology,General Medicine,Biochemistry,Structural Biology

Reference42 articles.

1. Blindness and Vision Impairment;W.H. Organization,2018

2. Lens aging: effects of crystallins;Sharma;Biochim. Biophys. Acta,2009

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

4. Crystallin proteins and amyloid fibrils;Ecroyd;Cell. Mol. Life Sci.,2009

5. Ageing and vision: structure, stability and function of lens crystallins;Bloemendal;Prog. Biophys. Mol. Biol.,2004

Cited by 5 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. Amyloid Protein Cross-Seeding Provides a New Perspective on Multiple Diseases In Vivo;Biomacromolecules;2022-12-12

2. Recent progress and research trend of anti-cataract pharmacology therapy: A bibliometric analysis and literature review;European Journal of Pharmacology;2022-11

3. A novel cataract-causing mutation Ile82Met of γA crystallin trends to aggregate with unfolding intermediate;International Journal of Biological Macromolecules;2022-06

4. Pathogenic mechanism of congenital cataract caused by the CRYBA1/A3-G91del variant and related intervention strategies;International Journal of Biological Macromolecules;2021-10

5. Trehalose Inhibits the Heat-Induced Formation of the Amyloid-Like Structure of Soluble Proteins Isolated from Human Cataract Lens;The Protein Journal;2020-10