Associated Papers
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
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
Genetic Restrictive Cardiomyopathy: Causes and Consequences-An Integrative Approach.
Cimiotti D et al.
International Journal of Molecular Sciences, 2021
αB-crystallin as a promising target in pathological conditions - A review.
Maksimiuk M et al.
Annals of Agricultural and Environmental Medicine : Aaem, 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
αB-Crystallin Phosphorylation: Advances and Problems.
Muranova LK et al.
Biochemistry. Biokhimiia, 2018
Some properties of three αB-crystallin mutants carrying point substitutions in the C-terminal domain and associated with congenital diseases.
Gerasimovich ES et al.
Biochimie, 2017
A novel dominant D109A CRYAB mutation in a family with myofibrillar myopathy affects αB-crystallin structure.
Fichna JP et al.
Bba Clinical, 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
αB-Crystallin Interacts with Nav1.5 and Regulates Ubiquitination and Internalization of Cell Surface Nav1.5.
Huang Y et al.
The Journal of Biological Chemistry, 2016
Rescue of αB Crystallin (HSPB5) Mutants Associated Protein Aggregation by Co-Expression of HSPB5 Partners.
Hussein RM 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
Mutants of human αB-crystallin cause enhanced protein aggregation and apoptosis in mammalian cells: influence of co-expression of HspB1.
Raju I et al.
Biochemical and Biophysical Research Communications, 2013
The family of mammalian small heat shock proteins (HSPBs): implications in protein deposit diseases and motor neuropathies.
Boncoraglio A et al.
The International Journal of Biochemistry & Cell Biology, 2012
A novel CRYAB mutation resulting in multisystemic disease.
Sacconi S et al.
Neuromuscular Disorders : Nmd, 2012
Functions of the intermediate filament cytoskeleton in the eye lens.
Song S et al.
The Journal of Clinical Investigation, 2009
Crystallin gene mutations in Indian families with inherited pediatric cataract.
Devi RR et al.
Molecular Vision, 2008