Associated Papers
ATCUN-like Copper Site in βB2-Crystallin Plays a Protective Role in Cataract-Associated Aggregation.
Tovar-Ramírez ME et al.
Inorganic Chemistry, 2023
A novel CRYBB2 mutation causes autosomal dominant cataract: A report from a Chinese family.
Xu LJ et al.
European Journal of Ophthalmology, 2021
Cataract-Associated New Mutants S175G/H181Q of βΒ2-Crystallin and P24S/S31G of γD-Crystallin Are Involved in Protein Aggregation by Structural Changes.
Song IK et al.
International Journal of Molecular Sciences, 2020
Two novel mutations identified in ADCC families impair crystallin protein distribution and induce apoptosis in human lens epithelial cells.
Li L et al.
Scientific Reports, 2017
Cataract-causing mutation S228P promotes βB1-crystallin aggregation and degradation by separating two interacting loops in C-terminal domain.
Qi LB et al.
Protein & Cell, 2016
A Novel CRYBB2 Stopgain Mutation Causing Congenital Autosomal Dominant Cataract in a Chinese Family.
Zhou Y et al.
Journal of Ophthalmology, 2016
The importance of the last strand at the C-terminus in βB2-crystallin stability and assembly.
Zhang K et al.
Biochimica Et Biophysica Acta, 2014
Molecular and structural analysis of genetic variations in congenital cataract.
Kumar M et al.
Molecular Vision, 2013
Identification of a novel CRYBB2 missense mutation causing congenital autosomal dominant cataract.
Weisschuh N et al.
Molecular Vision, 2012
The congenital cataract-linked A2V mutation impairs tetramer formation and promotes aggregation of βB2-crystallin.
Xu J et al.
Plos One, 2012
Characterization of a novel mutation in the CRYBB2 gene associated with autosomal dominant congenital posterior subcapsular cataract in a Chinese family.
Yao K et al.
Molecular Vision, 2011
A novel CRYBB2 missense mutation causing congenital autosomal dominant cataract in an Italian family.
Faletra F et al.
Ophthalmic Genetics, 0
Select a paper to view details