Associated Papers
Characterization of βB2-crystallin tryptophan mutants reveals two different folding states in solution.
Sun J et al.
Protein Science : a Publication of the Protein Society, 2024
Heteromeric formation with βA3 protects the low thermal stability of βB1-L116P.
Xu J et al.
The British Journal of Ophthalmology, 2023
Novel CRYGC Mutation in Conserved Ultraviolet-Protective Tryptophan (p.Trp131Arg) Is Linked to Autosomal Dominant Congenital Cataract.
Delas F et al.
International Journal of Molecular Sciences, 2023
Endoplasmic Reticulum Stress and the Lysosomal Pathway Play Crucial Roles in the Progression of βB2-Crystallin Mutation-Induced Congenital Cataracts in Mice.
Xiao W et al.
Investigative Ophthalmology & Visual Science, 2023
Identification and characterization of six β-crystallin gene mutations associated with congenital cataract in Chinese families.
Yu Y et al.
Molecular Genetics & Genomic Medicine, 2021
Identification of novel mutations causing pediatric cataract in Bhutan, Cambodia, and Sri Lanka.
Javadiyan S et al.
Molecular Genetics & Genomic Medicine, 2018
Effects of cataract-causing mutations W59C and W151C on βB2-crystallin structure, stability and folding.
Zhao WJ et al.
International Journal of Biological Macromolecules, 2017
A Novel CRYBB2 Stopgain Mutation Causing Congenital Autosomal Dominant Cataract in a Chinese Family.
Zhou Y et al.
Journal of Ophthalmology, 2016
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
Molecular analysis of cataract families in India: new mutations in the CRYBB2 and GJA3 genes and rare polymorphisms.
Santhiya ST et al.
Molecular Vision, 2010
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