Î²-strand interactions at the domain interface critical for the stability of human lens Î³D-crystallin-Reference-Cited by-同舟云学术

Î²-strand interactions at the domain interface critical for the stability of human lens Î³D-crystallin

Published:2009 Issue: Volume: Page:NA-NA
ISSN:0961-8368
Container-title:Protein Science
language:en
Short-container-title:Protein Science

Author:

Das Payel,King Jonathan A.,Zhou Ruhong

Publisher

Wiley

Subject

Molecular Biology,Biochemistry

Reference72 articles.

1. Global data on visual impairment in the year 2002;Resnikoff;Bull World Health Organ,2004

2. Posterior capsule opacification: a review of the aetiopathogenesis, experimental and clinical studies and factors for prevention;Pandey;Indian J Ophthalmol,2004

3. Cataract as a protein condensation disease: the Proctor Lecture;Benedek;Invest Ophthalmol Vis Sci,1997

4. Crystallin gene-expression during rat lens development;Aarts;Eur J Biochem,1989

5. Lens proteomics: analysis of rat crystallin sequences and two-dimensional electrophoresis map;Lampi;Invest Ophthalmol Visual Sci,2002

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