A transgenic mouse model for human autosomal dominant cataract
about
Temperature-dependent structural and functional properties of a mutant (F71L) αA-crystallin: molecular basis for early onset of age-related cataractCrystal Structure of an Activated Variant of Small Heat Shock Protein Hsp16.5Interactions between small heat shock protein alpha-crystallin and galectin-related interfiber protein (GRIFIN) in the ocular lensIn vivo substrates of the lens molecular chaperones αA-crystallin and αB-crystallinMechanism of small heat shock protein function in vivo: a knock-in mouse model demonstrates that the R49C mutation in alpha A-crystallin enhances protein insolubility and cell deathAlphaA-crystallin R49Cneo mutation influences the architecture of lens fiber cell membranes and causes posterior and nuclear cataracts in mice.Aldo-keto reductases in the eye.Cat-Map: putting cataract on the mapMolecular mechanism of formation of cortical opacity in CRYAAN101D transgenic mice.Mechanism of cataract formation in alphaA-crystallin Y118D mutation.The common modification in alphaA-crystallin in the lens, N101D, is associated with increased opacity in a mouse model.Activation of unfolded protein response in transgenic mouse lenses.Mutation analysis of two families with inherited congenital cataracts.Chemical modulation of the chaperone function of human alphaA-crystallin.Phenotype of cardiomyopathy in cardiac-specific heat shock protein B8 K141N transgenic mouse.Differential role of arginine mutations on the structure and functions of α-crystallin.Structure and mechanism of protein stability sensors: chaperone activity of small heat shock proteins.Lens crystallin modifications and cataract in transgenic mice overexpressing acylpeptide hydrolase.Small heat-shock proteins: important players in regulating cellular proteostasis.Effect of Geranylgeranylacetone on Ultraviolet Radiation Type B-Induced Cataract in Heat-Shock Transcription Factor 1 Heterozygous Mouse.Acetylation of lysine 92 improves the chaperone and anti-apoptotic activities of human αB-crystallin.Hydroimidazolone modification of human alphaA-crystallin: Effect on the chaperone function and protein refolding ability.Role of cysteine residues in the enhancement of chaperone function in methylglyoxal-modified human alpha A-crystallin.AP-2α is required after lens vesicle formation to maintain lens integrity.Real-time heterogeneous protein-protein interaction between αA-crystallin N-terminal mutants and αB-crystallin using quartz crystal microbalance (QCM).
P2860
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P2860
A transgenic mouse model for human autosomal dominant cataract
description
2006 nî lūn-bûn
@nan
2006年の論文
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2006年論文
@yue
2006年論文
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2006年論文
@zh-hk
2006年論文
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2006年論文
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name
A transgenic mouse model for human autosomal dominant cataract
@ast
A transgenic mouse model for human autosomal dominant cataract
@en
type
label
A transgenic mouse model for human autosomal dominant cataract
@ast
A transgenic mouse model for human autosomal dominant cataract
@en
prefLabel
A transgenic mouse model for human autosomal dominant cataract
@ast
A transgenic mouse model for human autosomal dominant cataract
@en
P2093
P2860
P356
P1476
A transgenic mouse model for human autosomal dominant cataract
@en
P2093
Cheng-Da Hsu
J Mark Petrash
Steven Kymes
P2860
P304
P356
10.1167/IOVS.05-0524
P407
P577
2006-05-01T00:00:00Z