Associated Papers
Potential role of βB1 crystallin in cataract formation:a systematic review.
Li M et al.
Archives of Biochemistry and Biophysics, 2025
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
Generation of Lens Progenitor Cells and Lentoid Bodies from Pluripotent Stem Cells: Novel Tools for Human Lens Development and Ocular Disease Etiology.
Cvekl A et al.
Cells, 2022
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
Chemical Properties Determine Solubility and Stability in βγ-Crystallins of the Eye Lens.
Rocha MA et al.
Chembiochem : a European Journal of Chemical Biology, 2021
The impact of different mutations at arginine141 on the structure, subunit exchange dynamics and chaperone activity of Hsp16.3.
Panda AK et al.
Proteins, 2020
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
A novel Cx50 (GJA8) p.H277Y mutation associated with autosomal dominant congenital cataract identified with targeted next-generation sequencing.
Chen C et al.
Graefe's Archive for Clinical and Experimental Ophthalmology = Albrecht Von Graefes Archiv Fur Klinische Und Experimentelle Ophthalmologie, 2015
Cataract-causing mutation R233H affects the stabilities of βB1- and βA3/βB1-crystallins with different pH-dependence.
Xi YB et al.
Biochimica Et Biophysica Acta, 2014
The N-terminal extension of βB1-crystallin chaperones β-crystallin folding and cooperates with αA-crystallin.
Leng XY et al.
Biochemistry, 2014
Molecular genetics of congenital nuclear cataract.
Deng H et al.
European Journal of Medical Genetics, 2014
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
Identification of a novel C-terminal extension mutation in EPHA2 in a family affected with congenital cataract.
Reis LM et al.
Molecular Vision, 2014
Combinational analysis of linkage and exome sequencing identifies the causative mutation in a Chinese family with congenital cataract.
Jia X et al.
Bmc Medical Genetics, 2013
Whole exome sequencing in dominant cataract identifies a new causative factor, CRYBA2, and a variety of novel alleles in known genes.
Reis LM et al.
Human Genetics, 2013
[Mutation analysis of CRYBB1 gene and prenatal diagnosis for a Chinese kindred featuring autosomal dominant congenital nuclear cataract].
Wu Q et al.
Zhonghua Yi Xue Yi Chuan Xue Za Zhi = Zhonghua Yixue Yichuanxue Zazhi = Chinese Journal of Medical Genetics, 2013
Increasing βB1-crystallin sensitivity to proteolysis caused by the congenital cataract-microcornea syndrome mutation S129R.
Wang S et al.
Biochimica Et Biophysica Acta, 2013
Structural integrity of the Greek key motif in βγ-crystallins is vital for central eye lens transparency.
Vendra VP et al.
Plos One, 2013
The congenital cataract-linked A2V mutation impairs tetramer formation and promotes aggregation of βB2-crystallin.
Xu J et al.
Plos One, 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
The congenital cataract-linked G61C mutation destabilizes γD-crystallin and promotes non-native aggregation.
Zhang W et al.
Plos One, 2011
CRYBB1 mutation associated with congenital cataract and microcornea.
Willoughby CE et al.
Molecular Vision, 2005