Associated Papers
Mimicking oxidative damage in γS-crystallin with site-specific incorporation of 5-hydroxytryptophan.
Seo Y et al.
Biophysical Reports, 2026
Mini-αA-crystallin protects a client lens protein from catastrophic aggregation due to heat stress.
Sroge C et al.
Protein Science : a Publication of the Protein Society, 2025
The 18th amino acid glycine plays an essential role in maintaining the structural stabilities of γS-crystallin linking with congenital cataract.
Zhu S et al.
International Journal of Biological Macromolecules, 2023
Human γS-Crystallin Mutation F10_Y11delinsLN in the First Greek Key Pair Destabilizes and Impairs Tight Packing Causing Cortical Lamellar Cataract.
Vendra VPR et al.
International Journal of Molecular Sciences, 2023
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
Cumulative deamidations of the major lens protein γS-crystallin increase its aggregation during unfolding and oxidation.
Vetter CJ et al.
Protein Science : a Publication of the Protein Society, 2020
Human γS-Crystallin-Copper Binding Helps Buffer against Aggregation Caused by Oxidative Damage.
Roskamp KW et al.
Biochemistry, 2020
Function and Aggregation in Structural Eye Lens Crystallins.
Roskamp KW et al.
Accounts of Chemical Research, 2020
Human αB-crystallin discriminates between aggregation-prone and function-preserving variants of a client protein.
Sprague-Piercy MA et al.
Biochimica Et Biophysica Acta. General Subjects, 2020
Two Pathogenic Gene Mutations Identified Associating with Congenital Cataract and Iris Coloboma Respectively in a Chinese Family.
Li B et al.
Journal of Ophthalmology, 2020
Biology of Inherited Cataracts and Opportunities for Treatment.
Shiels A et al.
Annual Review of Vision Science, 2019
Molecular Mechanism of Aggregation of the Cataract-Related γD-Crystallin W42R Variant from Multiscale Atomistic Simulations.
Wong EK et al.
Biochemistry, 2019
Conformational dynamics study on human γS-crystallin as an efficient route to childhood blindness.
Bari KJ et al.
Biochemical and Biophysical Research Communications, 2019
Sequence specific 1H, 13C and 15N resonance assignments of the C-terminal domain of human γS-crystallin.
Bari KJ et al.
Biomolecular Nmr Assignments, 2019
Disruption of protein function by pathogenic mutations: common and uncommon mechanisms 1.
Taipale M
Biochemistry and Cell Biology = Biochimie Et Biologie Cellulaire, 2019
A novel missense mutation of CRYGS underlies congenital cataract in a Chinese family.
Zhang T et al.
Gene, 2018
Sequence specific 1H, 13C and 15N resonance assignments of a cataract-related variant G57W of human γS-crystallin.
Bari KJ et al.
Biomolecular Nmr Assignments, 2018
Cataract-associated P23T γD-crystallin retains a native-like fold in amorphous-looking aggregates formed at physiological pH.
Boatz JC et al.
Nature Communications, 2017
Targeted Exome Sequencing of Congenital Cataracts Related Genes: Broadening the Mutation Spectrum and Genotype-Phenotype Correlations in 27 Chinese Han Families.
Zhai Y et al.
Scientific Reports, 2017
Multiple Aggregation Pathways in Human γS-Crystallin and Its Aggregation-Prone G18V Variant.
Roskamp KW et al.
Investigative Ophthalmology & Visual Science, 2017
Mutations and mechanisms in congenital and age-related cataracts.
Shiels A et al.
Experimental Eye Research, 2017
Gamma crystallins of the human eye lens.
Vendra VP et al.
Biochimica Et Biophysica Acta, 2016
Increased hydrophobic surface exposure in the cataract-related G18V variant of human γS-crystallin.
Khago D et al.
Biochimica Et Biophysica Acta, 2016
Structural study of the G57W mutant of human gamma-S-crystallin, associated with congenital cataract.
Khan I et al.
Molecular Vision, 2016
A G57W Mutation of CRYGS Associated with Autosomal Dominant Pulverulent Cataracts in a Chinese Family.
Yang Z et al.
Ophthalmic Genetics, 2015
Preferential and specific binding of human αB-crystallin to a cataract-related variant of γS-crystallin.
Kingsley CN et al.
Structure (london, England : 1993), 2013
Exploring the aggregation propensity of γS-crystallin protein variants using two-dimensional spectroscopic tools.
Jiang J et al.
The Journal of Physical Chemistry. B, 2013
Structural analysis of the mutant protein D26G of human γS-crystallin, associated with Coppock cataract.
Karri S et al.
Molecular Vision, 2013
sHSP in the eye lens: crystallin mutations, cataract and proteostasis.
Clark AR et al.
The International Journal of Biochemistry & Cell Biology, 2012
¹H, ¹³C, and ¹⁵N assignments of wild-type human γS-crystallin and its cataract-related variant γS-G18V.
Brubaker WD et al.
Biomolecular Nmr Assignments, 2012
The mutation V42M distorts the compact packing of the human gamma-S-crystallin molecule, resulting in congenital cataract.
Vendra VP et al.
Plos One, 2012
Separating instability from aggregation propensity in γS-crystallin variants.
Brubaker WD et al.
Biophysical Journal, 2011
PhenoHM: human-mouse comparative phenome-genome server.
Sardana D et al.
Nucleic Acids Research, 2010
The G18V CRYGS mutation associated with human cataracts increases gammaS-crystallin sensitivity to thermal and chemical stress.
Ma Z et al.
Biochemistry, 2009
Novel mutation in the gamma-S crystallin gene causing autosomal dominant cataract.
Vanita V et al.
Molecular Vision, 2009
Crystallin gene mutations in Indian families with inherited pediatric cataract.
Devi RR et al.
Molecular Vision, 2008
Crystallins and hereditary cataracts: molecular mechanisms and potential for therapy.
Andley UP
Expert Reviews in Molecular Medicine, 2006
Gamma-S crystallin gene (CRYGS) mutation causes dominant progressive cortical cataract in humans.
Sun H et al.
Journal of Medical Genetics, 2005
Molecular characteristics of inherited congenital cataracts.
Huang B et al.
European Journal of Medical Genetics, 0