A knock-in mouse model for the R120G mutation of αB-crystallin recapitulates human hereditary myopathy and cataracts.
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αB-crystallin/sHSP protects cytochrome c and mitochondrial function against oxidative stress in lens and retinal cellsIn vivo substrates of the lens molecular chaperones αA-crystallin and αB-crystallinTryptophan and Non-Tryptophan Fluorescence of the Eye Lens Proteins Provides Diagnostics of Cataract at the Molecular LevelThe specificity of the interaction between αB-crystallin and desmin filaments and its impact on filament aggregation and cell viability.Pharmacological chaperone for α-crystallin partially restores transparency in cataract modelsMyofibrillar myopathies: new developments.Small heat shock proteins in redox metabolism: implications for cardiovascular diseases.Comparative proteomic analysis identifies age-dependent increases in the abundance of specific proteins after deletion of the small heat shock proteins αA- and αB-crystallin.Differential role of arginine mutations on the structure and functions of α-crystallin.p62 expression and autophagy in αB-crystallin R120G mutant knock-in mouse model of hereditary cataract.Contribution of small heat shock proteins to muscle development and function.The detection and characterization of pleiotropy: discovery, progress, and promise.A novel p.T139M mutation in HSPB1 highlighting the phenotypic spectrum in a family.Myofibrillar Myopathies: New Perspectives from Animal Models to Potential Therapeutic Approaches.Small heat shock proteins in ageing and age-related diseases.Aggregate-prone R120GCRYAB triggers multifaceted modifications of the thioredoxin system.Acetylation of αA-crystallin in the human lens: effects on structure and chaperone function.Acetylation of lysine 92 improves the chaperone and anti-apoptotic activities of human αB-crystallin.Autophagy and UPR in alpha-crystallin mutant knock-in mouse models of hereditary cataractsOligomerization with wt αA- and αB-crystallins reduces proteasome-mediated degradation of C-terminally truncated αA-crystallin.Probing the changes in gene expression due to α-crystallin mutations in mouse models of hereditary human cataract.αB-Crystallin interacts and attenuates the tyrosine phosphatase activity of Shp2 in cardiomyocytes under mechanical stress.
P2860
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P2860
A knock-in mouse model for the R120G mutation of αB-crystallin recapitulates human hereditary myopathy and cataracts.
description
2011 nî lūn-bûn
@nan
2011 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
2011 թվականի մարտին հրատարակված գիտական հոդված
@hy
2011年の論文
@ja
2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
@wuu
name
A knock-in mouse model for the ...... ditary myopathy and cataracts.
@ast
A knock-in mouse model for the ...... ditary myopathy and cataracts.
@en
A knock-in mouse model for the ...... ditary myopathy and cataracts.
@nl
type
label
A knock-in mouse model for the ...... ditary myopathy and cataracts.
@ast
A knock-in mouse model for the ...... ditary myopathy and cataracts.
@en
A knock-in mouse model for the ...... ditary myopathy and cataracts.
@nl
prefLabel
A knock-in mouse model for the ...... ditary myopathy and cataracts.
@ast
A knock-in mouse model for the ...... ditary myopathy and cataracts.
@en
A knock-in mouse model for the ...... ditary myopathy and cataracts.
@nl
P2093
P2860
P1433
P1476
A knock-in mouse model for the ...... editary myopathy and cataracts
@en
P2093
Conrad C Weihl
Nathan Ravi
Paul D Hamilton
P2860
P304
P356
10.1371/JOURNAL.PONE.0017671
P407
P577
2011-03-18T00:00:00Z