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Crystallins are separated into two classes taxon-specific, or enzyme, and ubiquitous. Additionally we are shipping CRYGC Antibodies (40) and and many more products for this protein.
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Study identified eight different mutations in CRYGC associated with autosomal dominant congenital nuclear cataracts (ADCC) in a cohort of Chinese family and shows that CRYGC mutations are responsible for 4.1% of ADCC families in the cohort. The results expand the spectrum of CRYGC mutations as well as their associated phenotypes.
the G129C mutation in gammaC-crystallin, which is associated with autosomal dominant congenital nuclear cataract, perturbed the unfolding process by promoting the accumulation of two distinct aggregation-prone intermediates under mild denaturing conditions.
Exome sequencing in developmental eye disease leads to identification of causal variants in GJA8 (show GJA8 Proteins), CRYGC, PAX6 (show PAX6 Proteins) and CYP1B1 (show CYP1B1 Proteins).
We confirm that congenital cataract is associated with a CRYGC gene mutation.
identified a CRYAA (show CRYAA Proteins) mutation in family A and a CRYGC mutation in family B with congenital cataract
A nonsense mutation c.471G>A in CRYGC is associated with autosomal dominant congenital nuclear cataracts and microcornea in a Chinese pedigree.
Molecular modeling and spectroscopic studies indicated that the mutation impaired the tertiary structure of gamma C crystallin by modifying the H-bonding network in the C-terminal domain.
Two novel nonsynonymous variations and four reported variations in CRYAB (show CRYAB Proteins), CRYGC, CRYGD (show CRYGD Proteins), and GJA8 (show GJA8 Proteins), were observed.
In gammaD-crystallin, methylation is exclusively at Cys (show DNAJC5 Proteins) 110, whereas in gammaC- and gammaB-crystallins, the principal methylation site is Cys (show DNAJC5 Proteins) 22 with minor methylation at Cys (show DNAJC5 Proteins) 79
the loss of interactions of T5P mutant of the gammaC-crystallin with other crystallins may play a larger role than the protection afforded by chaperone-like activity in Coppock-like cataract.
a 1-bp deletion in gammaC-crystallin leads to cataract.
presence of measurable interactions between MIP26 and all crystallins, with the extent of interactions decreasing from alphaA- and alphaB-crystallin (show CRYAB Proteins) to betaB2- and gammaC-crystallin.
Crystallins are separated into two classes taxon-specific, or enzyme, and ubiquitous. The latter class constitutes the major proteins of vertebrate eye lens and maintains the transparency and refractive index of the lens. Since lens central fiber cells lose their nuclei during development, these crystallins are made and then retained throughout life, making them extremely stable proteins. Mammalian lens crystallins are divided into alpha, beta, and gamma families\; beta and gamma crystallins are also considered as a superfamily. Alpha and beta families are further divided into acidic and basic groups. Seven protein regions exist in crystallins: four homologous motifs, a connecting peptide, and N- and C-terminal extensions. Gamma-crystallins are a homogeneous group of highly symmetrical, monomeric proteins typically lacking connecting peptides and terminal extensions. They are differentially regulated after early development. Four gamma-crystallin genes (gamma-A through gamma-D) and three pseudogenes (gamma-E, gamma-F, gamma-G) are tandemly organized in a genomic segment as a gene cluster. Whether due to aging or mutations in specific genes, gamma-crystallins have been involved in cataract formation.
crystallin, gamma polypeptide 3
, gamma-crystallin 2-1
, gamma-crystallin C
, crystallin, gamma-3
, gamma-crystallin 3
, gamma-crystallin IIIA
, crystallin, gamma C