A molecular dynamics approach to explore the structural characterization of cataract causing mutation R58H on human γD crystallin
Author:
Publisher
Springer Science and Business Media LLC
Subject
Cell Biology,Clinical Biochemistry,Molecular Biology,General Medicine
Link
http://link.springer.com/article/10.1007/s11010-018-3342-8/fulltext.html
Reference33 articles.
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2. Zhenzhen L, Allen T, Yizhi L, Mingxing W, Xiaohua G, Fu S (2012) Enhancement of ubiquitin conjugation activity reduces intracellular aggregation of V76D mutant γD-Crystallin. Invest Ophthalmol 53(10):6655–6665
3. Moran SD, Woys AM, Buchanan LE, Bixby E, Decatur SM, Zanni MT (2012) Two-dimensional IR spectroscopy and segmental 13C labeling reveals the domain structure of human γD-crystallin amyloid fibrils. Proc Natl Acad Sci USA 109:3329–3334
4. Moreau KL, King JA (2012) Protein misfolding and aggregation in cataract disease and prospects for prevention. Trends Mol Med 18:273–282
5. Hains PG, Truscott RJ (2007) Post-translational modifications in the nuclear region of young, aged, and cataract human lenses. J Proteome Res 6:3935–3943
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