Associated Papers
Potential role of βB1 crystallin in cataract formation:a systematic review.
Li M et al.
Archives of Biochemistry and Biophysics, 2025
Pervasive mislocalization of pathogenic coding variants underlying human disorders.
Lacoste J et al.
Cell, 2024
Pervasive mislocalization of pathogenic coding variants underlying human disorders.
Lacoste J et al.
Biorxiv : the Preprint Server for Biology, 2023
Cataract-causing Y204X mutation of crystallin protein CRYβB1 promotes its C-terminal degradation and higher-order oligomerization.
Jing X et al.
The Journal of Biological Chemistry, 2023
Congenital cataract-causing mutation βB1-L116P is prone to amyloid fibrils aggregation and protease degradation with low structural stability.
Liu J et al.
International Journal of Biological Macromolecules, 2022
A novel missense mutation of CRYBB1 causes congenital cataract in a Chinese family.
Ji Y et al.
European Journal of Ophthalmology, 2021
A Novel Mutation p.S93R in CRYBB1 Associated with Dominant Congenital Cataract and Microphthalmia.
Jin A et al.
Current Eye Research, 2020
Dissimilarity in the Contributions of the N-Terminal Domain Hydrophobic Core to the Structural Stability of Lens β/γ-Crystallins.
Zhang K et al.
Biochemistry, 2019
A novel truncation mutation in CRYBB1 associated with autosomal dominant congenital cataract with nystagmus.
Rao Y et al.
Molecular Vision, 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
Molecular genetics of congenital nuclear cataract.
Deng H et al.
European Journal of Medical Genetics, 2014
Structural integrity of the Greek key motif in βγ-crystallins is vital for central eye lens transparency.
Vendra VP et al.
Plos One, 2013
Molecular and structural analysis of genetic variations in congenital cataract.
Kumar M et al.
Molecular Vision, 2013
Clinical and molecular analysis of children with central pulverulent cataract from the Arabian Peninsula.
Khan AO et al.
The British Journal of Ophthalmology, 2012
A novel mutation in CRYBB1 associated with congenital cataract-microcornea syndrome: the p.Ser129Arg mutation destabilizes the βB1/βA3-crystallin heteromer but not the βB1-crystallin homomer.
Wang KJ et al.
Human Mutation, 2011
Initiation codon mutation in betaB1-crystallin (CRYBB1) associated with autosomal recessive nuclear pulverulent cataract.
Meyer E et al.
Molecular Vision, 2009
A missense mutation S228P in the CRYBB1 gene causes autosomal dominant congenital cataract.
Wang J et al.
Chinese Medical Journal, 2007
CRYBB1 mutation associated with congenital cataract and microcornea.
Willoughby CE et al.
Molecular Vision, 2005