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
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
A Gly684Ala substitution in the androgen receptor is the cause for azoospermia in a Chinese family with mild androgen insensitivity syndrome and normal hormone levels.
Yuan Y et al.
Frontiers in Genetics, 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
Clinical utility of genetic testing in 201 preschool children with inherited eye disorders.
Lenassi E et al.
Genetics in Medicine : Official Journal of the American College of Medical Genetics, 2020
Genetic landscape of isolated pediatric cataracts: extreme heterogeneity and variable inheritance patterns within genes.
Reis LM et al.
Human Genetics, 2019
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
Recurrent mutation in the crystallin alpha A gene associated with inherited paediatric cataract.
Javadiyan S et al.
Bmc Research Notes, 2016
Real-time heterogeneous protein-protein interaction between αA-crystallin N-terminal mutants and αB-crystallin using quartz crystal microbalance (QCM).
Ramkumar S et al.
Amino Acids, 2015
Missense Mutations in CRYAB Are Liable for Recessive Congenital Cataracts.
Jiao X et al.
Plos One, 2015
Mutations of small heat shock proteins and human congenital diseases.
Datskevich PN et al.
Biochemistry. Biokhimiia, 2012
Quaternary structural parameters of the congenital cataract causing mutants of αA-crystallin.
Kore R et al.
Molecular and Cellular Biochemistry, 2012
Mutations in human αA-crystallin/sHSP affect subunit exchange interaction with αB-crystallin.
Raju I et al.
Plos One, 2012
Congenital cataract causing mutants of αA-crystallin/sHSP form aggregates and aggresomes degraded through ubiquitin-proteasome pathway.
Raju I et al.
Plos One, 2011
Characterization of a mutant R11H αB-crystallin associated with human inherited cataract.
Chen Q et al.
Biological Chemistry, 2010
Trimethylamine N-oxide alleviates the severe aggregation and ER stress caused by G98R alphaA-crystallin.
Gong B et al.
Molecular Vision, 2009
Congenital cataracts and their molecular genetics.
Hejtmancik JF
Seminars in Cell & Developmental Biology, 2008