Associated Papers
Cataract-Causing Mutant R188C of βB2 Crystallin With Low Structural Stability is Sensitive to Environmental Stresses and Prone to Aggregates Formation.
Yu Y et al.
Exploration (beijing, China), 2025
Case Report: A family of congenital cataract caused by a novel mutation in the CRYGC gene c.52G>A.
Ma S et al.
Frontiers in Medicine, 2025
Novel CRYGC Mutation in Conserved Ultraviolet-Protective Tryptophan (p.Trp131Arg) Is Linked to Autosomal Dominant Congenital Cataract.
Delas F et al.
International Journal of Molecular Sciences, 2023
The Y46D Mutation Destabilizes Dense Packing of the Second Greek Key Pair of Human γC-Crystallin Causing Congenital Nuclear Cataracts.
Vendra VPR et al.
Biochemistry, 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
A Novel Mutation in CRYGC Mutation Associated with Autosomal Dominant Congenital Cataracts and Microcornea.
Zhou Z et al.
Ophthalmology Science, 2022
Effects of Mutating Trp42 Residue on γD-Crystallin Stability.
Aguayo-Ortiz R et al.
Journal of Chemical Information and Modeling, 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
Recurrent PTPRT/JAK2 mutations in lung adenocarcinoma among African Americans.
Mitchell KA et al.
Nature Communications, 2019
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
Novel mutations in CRYGC are associated with congenital cataracts in Chinese families.
Zhong Z et al.
Scientific Reports, 2017
Congenital microcornea-cataract syndrome-causing mutation X253R increases βB1-crystallin hydrophobicity to promote aggregate formation.
Leng XY et al.
The Biochemical Journal, 2016
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
Congenital Cataract-Causing Mutation G129C in γC-Crystallin Promotes the Accumulation of Two Distinct Unfolding Intermediates That Form Highly Toxic Aggregates.
Xi YB et al.
Journal of Molecular Biology, 2015
Molecular genetics of congenital nuclear cataract.
Deng H et al.
European Journal of Medical Genetics, 2014
A CRYGC gene mutation associated with autosomal dominant pulverulent cataract.
González-Huerta LM et al.
Gene, 2013
A novel mutation impairing the tertiary structure and stability of γC-crystallin (CRYGC) leads to cataract formation in humans and zebrafish lens.
Li XQ et al.
Human Mutation, 2012
A nonsense mutation of CRYGC associated with autosomal dominant congenital nuclear cataracts and microcornea in a Chinese pedigree.
Guo Y et al.
Molecular Vision, 2012
A novel nonsense mutation in CRYGC is associated with autosomal dominant congenital nuclear cataracts and microcornea.
Zhang L et al.
Molecular Vision, 2009
A family with autosomal dominant primary congenital cataract associated with a CRYGC mutation: evidence of clinical heterogeneity.
Gonzalez-Huerta LM et al.
Molecular Vision, 2007