Evidence of Highly Conserved β-Crystallin Disulfidome that Can be Mimicked by In Vitro Oxidation in Age-related Human Cataract and Glutathione Depleted Mouse Lens*

Author:

Fan Xingjun,Zhou Sheng,Wang Benlian,Hom Grant,Guo Minfei,Li Binbin,Yang Jing,Vaysburg Dennis,Monnier VincentM

Funder

National Institutes of Health

Publisher

Elsevier BV

Subject

Molecular Biology,Biochemistry,Analytical Chemistry

Reference54 articles.

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

2. Lens beta-crystallins: the role of deamidation and related modifications in aging and cataract;Lampi;Prog. Biophys. Mol. Biol,2014

3. Structural and functional roles of deamidation of N146 and/or truncation of NH2- or COOH-termini in human alphaB-crystallin;Asomugha;Mol. Vision,2011

4. Racemization of two proteins over our lifespan: deamidation of asparagine 76 in gammaS crystallin is greater in cataract than in normal lenses across the age range;Hooi;Invest. Ophthalmol. Visual Sci,2012

5. Anaerobic vs aerobic pathways of carbonyl and oxidant stress in human lens and skin during aging and in diabetes: A comparative analysis;Fan;Free Radical Biol. Med,2010

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