Structural and functional characterization of a missense mutant of human γS-crystallin associated with dominant infantile cataracts
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry,Biophysics
Reference10 articles.
1. Calcium binding properties of γ-crystallins;Rajini;J. Biol. Chem.,2001
2. Genetics of crystallins: cataract and beyond;Graw;Exp. Eye Res.,2009
3. A novel missense mutation of CRYGS underlies congenital cataract in a Chinese family;Zhang;Gene,2018
4. Evolutionary remodeling of βγ-crystallins for domain stability at cost of Ca2+-binding;Suman;J. Biol. Chem.,2011
5. Sequence specific 1H, 13C and 15N resonance assignments of a cataract-related variant G57W of human γS-crystallin;Bari;Biomol NMR Assign,2018
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1. Chemical Properties Determine Solubility and Stability in βγ‐Crystallins of the Eye Lens;ChemBioChem;2021-02-10
2. The structural biology of crystallin aggregation: challenges and outlook;The FEBS Journal;2021-01-07
3. A Perspective on Biophysical Studies of Crystallin Aggregation and Implications for Cataract Formation;The Journal of Physical Chemistry B;2020-10-14
4. A Molecular Dynamics Perspective To Identify Precursors to Aggregation in Human γS-Crystallin Unravels the Mechanism of Childhood Cataracts;The Journal of Physical Chemistry B;2019-11-18
5. Structural studies on the individual domains of human γS-crystallin and its G57W mutant unfolds mechanistic insights into childhood cataracts;Biochemical and Biophysical Research Communications;2019-09
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