Lanosterol Disrupts Aggregation of Human γD-Crystallin by Binding to the Hydrophobic Dimerization Interface-Reference-Cited by-同舟云学术

Lanosterol Disrupts Aggregation of Human γD-Crystallin by Binding to the Hydrophobic Dimerization Interface

Published:2018-06-19 Issue:27 Volume:140 Page:8479-8486
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Kang Hongsuk¹²,Yang Zaixing³^ORCID,Zhou Ruhong¹²^ORCID

Affiliation:

1. Institute of Quantitative Biology, Department of Physics, Zhejiang University, Hangzhou 310027, China

2. Computational Biology Center, IBM Thomas J. Watson Research Center, Yorktown Heights, New York 10598, United States

3. State Key Laboratory of Radiation Medicine and Protection, School for Radiological and Interdisciplinary Sciences (RAD-X) and Collaborative Innovation Centre of Radiation Medicine of Jiangsu Higher Education Institutions, Soochow University, Suzhou 215123, China

Funder

International Business Machines Corporation

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/jacs.8b03065

Reference39 articles.

1. Global estimates of visual impairment: 2010

2. Lanosterol reverses protein aggregation in cataracts

3. Protein misfolding and aggregation in cataract disease and prospects for prevention