GammaD-crystallin associated protein aggregation and lens fiber cell denucleation
about
Cataract-linked γD-crystallin mutants have weak affinity to lens chaperones α-crystallinsThe retinal proteome in experimental diabetic retinopathy: up-regulation of crystallins and reversal by systemic and periocular insulinCataract-causing defect of a mutant γ-crystallin proceeds through an aggregation pathway which bypasses recognition by the α-crystallin chaperone.Altered chaperone-like activity of alpha-crystallins promotes cataractogenesis.The cellular and molecular mechanisms of vertebrate lens development.Overexpression of human γC-crystallin 5 bp duplication disrupts lens morphology in transgenic mice.Roles of the 15-kDa selenoprotein (Sep15) in redox homeostasis and cataract development revealed by the analysis of Sep 15 knockout miceFunctional analysis of the Hsf4(lop11) allele responsible for cataracts in lop11 mice.A γA-Crystallin Mouse Mutant Secc with Small Eye, Cataract and Closed Eyelid.Focus on lens connexins.A conserved role of αA-crystallin in the development of the zebrafish embryonic lens.Enhancement of ubiquitin conjugation activity reduces intracellular aggregation of V76D mutant γD-crystallin.Protein misfolding and aggregation in cataract disease and prospects for prevention.A mutation in the start codon of γ-crystallin D leads to nuclear cataracts in the Dahl SS/Jr-Ctr strain.On the mechanism of organelle degradation in the vertebrate lens.Hydrophobic core mutations associated with cataract development in mice destabilize human gammaD-crystallin.Structural and aggregation behavior of the human γD-crystallin mutant E107A, associated with congenital nuclear cataractTrimethylamine N-oxide alleviates the severe aggregation and ER stress caused by G98R alphaA-crystallin.Patterns of gene expression in microarrays and expressed sequence tags from normal and cataractous lensesA novel mutation impairing the tertiary structure and stability of γC-crystallin (CRYGC) leads to cataract formation in humans and zebrafish lens.Expression of Cataract-linked γ-Crystallin Variants in Zebrafish Reveals a Proteostasis Network That Senses Protein Stability.
P2860
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P2860
GammaD-crystallin associated protein aggregation and lens fiber cell denucleation
description
2007 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
2007 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
artículu científicu espublizáu en 2007
@ast
im August 2007 veröffentlichter wissenschaftlicher Artikel
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scientific journal article
@en
vedecký článok (publikovaný 2007/08/01)
@sk
vědecký článek publikovaný v roce 2007
@cs
wetenschappelijk artikel (gepubliceerd op 2007/08/01)
@nl
наукова стаття, опублікована в серпні 2007
@uk
مقالة علمية (نشرت في أغسطس 2007)
@ar
name
GammaD-crystallin associated protein aggregation and lens fiber cell denucleation
@ast
GammaD-crystallin associated protein aggregation and lens fiber cell denucleation
@en
GammaD-crystallin associated protein aggregation and lens fiber cell denucleation
@nl
type
label
GammaD-crystallin associated protein aggregation and lens fiber cell denucleation
@ast
GammaD-crystallin associated protein aggregation and lens fiber cell denucleation
@en
GammaD-crystallin associated protein aggregation and lens fiber cell denucleation
@nl
prefLabel
GammaD-crystallin associated protein aggregation and lens fiber cell denucleation
@ast
GammaD-crystallin associated protein aggregation and lens fiber cell denucleation
@en
GammaD-crystallin associated protein aggregation and lens fiber cell denucleation
@nl
P2093
P3181
P356
P1476
GammaD-crystallin associated protein aggregation and lens fiber cell denucleation
@en
P2093
Catherine Cheng
Chun-Hong Xia
Haiquan Liu
Joseph Horwitz
Kaijun Wang
Peiqing Sun
Qingling Huang
Xiaohua Gong
P304
P3181
P356
10.1167/IOVS.06-1487
P407
P577
2007-08-01T00:00:00Z