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Crystallins are separated into two classes taxon-specific, or enzyme, and ubiquitous. Zusätzlich bieten wir Ihnen CRYGC Antikörper (38) und viele weitere Produktgruppen zu diesem Protein an.
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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 (zeige GJA8 Proteine), CRYGC, PAX6 (zeige PAX6 Proteine) and CYP1B1 (zeige CYP1B1 Proteine).
We confirm that congenital cataract is associated with a CRYGC gene mutation.
identified a CRYAA (zeige CRYAA Proteine) 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 (zeige CRYAB Proteine), CRYGC, CRYGD (zeige CRYGD Proteine), and GJA8 (zeige GJA8 Proteine), were observed.
In gammaD-crystallin, methylation is exclusively at Cys (zeige DNAJC5 Proteine) 110, whereas in gammaC- and gammaB-crystallins, the principal methylation site is Cys (zeige DNAJC5 Proteine) 22 with minor methylation at Cys (zeige DNAJC5 Proteine) 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.
This is the first case of phenotypic heterogeneity in the primary congenital cataract specifically associated with the R168W mutation in the CRYGC gene.
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 (zeige CRYAB Proteine) 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