Associated Papers
Structural and functional consequences of the cardiomyopathy-associated p.R157C mutation in the C-terminal palindromic motif of human αB-crystallin.
Rezaei Somee L et al.
Febs Letters, 2025
A computational study of the R120G mutation in human αB-crystallin: implications for structural stability and functionality.
Darvazi M et al.
Journal of Biomolecular Structure & Dynamics, 2024
Investigating the role of double mutations R12C/P20R, and R12C/R69C on structure, chaperone-like activity, and amyloidogenic properties of human αB-crystallin.
Khaleghinejad SH et al.
International Journal of Biological Macromolecules, 2023
Myopathy-associated G154S mutation causes important changes in the conformational stability, amyloidogenic properties, and chaperone-like activity of human αB-crystallin.
Khoshaman K et al.
Biophysical Chemistry, 2022
Protein Aggregation and Cataract: Role of Age-Related Modifications and Mutations in α-Crystallins.
Budnar P et al.
Biochemistry. Biokhimiia, 2022
Insights on Human Small Heat Shock Proteins and Their Alterations in Diseases.
Tedesco B et al.
Frontiers in Molecular Biosciences, 2022
Crystalline gene mutations in Turkish children with congenital cataracts.
Karahan M et al.
International Ophthalmology, 2021
A new heterozygous mutation in the stop codon of CRYAB (p.X176Y) is liable for congenital posterior pole cataract in a Chinese family.
Yu Y et al.
Ophthalmic Genetics, 2021
αB-crystallin as a promising target in pathological conditions - A review.
Maksimiuk M et al.
Annals of Agricultural and Environmental Medicine : Aaem, 2020
A novel dominant mutation in CRYAB gene leading to a severe phenotype with childhood onset.
Marcos AT et al.
Molecular Genetics & Genomic Medicine, 2020
The congenital cataract-causing mutations P20R and A171T are associated with important changes in the amyloidogenic feature, structure and chaperone-like activity of human αB-crystallin.
Ghahramani M et al.
Biopolymers, 2020
The novel αB-crystallin (CRYAB) mutation p.D109G causes restrictive cardiomyopathy.
Brodehl A et al.
Human Mutation, 2017
A novel dominant D109A CRYAB mutation in a family with myofibrillar myopathy affects αB-crystallin structure.
Fichna JP et al.
Bba Clinical, 2017
Correlations of single nucleotide polymorphisms of CRYAA and CRYAB genes with the risk and clinicopathological features of children suffering from congenital cataract.
Cui XJ et al.
Medicine, 2017
The P20R mutation of αB-crystallin diminishes its anti-apoptotic activity in human lens epithelial cells.
Zhu P et al.
Biochemical and Biophysical Research Communications, 2017
Missense Mutations in CRYAB Are Liable for Recessive Congenital Cataracts.
Jiao X et al.
Plos One, 2015
A novel P20R mutation in the alpha-B crystallin gene causes autosomal dominant congenital posterior polar cataracts in a Chinese family.
Xia XY et al.
Bmc Ophthalmology, 2014