The cardiomyopathy and lens cataract mutation in alphaB-crystallin alters its protein structure, chaperone activity, and interaction with intermediate filaments in vitro.
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Changes in the quaternary structure and function of MjHSP16.5 attributable to deletion of the IXI motif and introduction of the substitution, R107G, in the -crystallin domainHSP22, a new member of the small heat shock protein superfamily, interacts with mimic of phosphorylated HSP27 ((3D)HSP27)Interactive domains in the molecular chaperone human alphaB crystallin modulate microtubule assembly and disassemblyFunctional similarities between the small heat shock proteins Mycobacterium tuberculosis HSP 16.3 and human alphaB-crystallinAlpha B-crystallin suppresses pressure overload cardiac hypertrophyAltered aggregation properties of mutant gamma-crystallins cause inherited cataractThe specificity of the interaction between αB-crystallin and desmin filaments and its impact on filament aggregation and cell viability.Phosphorylation-induced change of the oligomerization state of alpha B-crystallin.Chaperone function of mutant versions of alpha A- and alpha B-crystallin prepared to pinpoint chaperone binding sites.Desmin aggregate formation by R120G alphaB-crystallin is caused by altered filament interactions and is dependent upon network status in cellsαB-crystallin is a sensor for assembly intermediates and for the subunit topology of desmin intermediate filaments.Oligomers of mutant glial fibrillary acidic protein (GFAP) Inhibit the proteasome system in alexander disease astrocytes, and the small heat shock protein alphaB-crystallin reverses the inhibition.BAG3 directly interacts with mutated alphaB-crystallin to suppress its aggregation and toxicity.Intermediate filaments interact with dormant ezrin in intestinal epithelial cells.Alpha-crystallin-type heat shock proteins: socializing minichaperones in the context of a multichaperone network.Structural and functional changes in the alpha A-crystallin R116C mutant in hereditary cataracts.Small heat shock proteins, the cytoskeleton, and inclusion body formation.Stress and molecular chaperones in disease.Multiple sites in αB-crystallin modulate its interactions with desmin filaments assembled in vitro.Alpha-B crystallin gene (CRYAB) mutation causes dominant congenital posterior polar cataract in humansHuman alpha B-crystallin mutation causes oxido-reductive stress and protein aggregation cardiomyopathy in miceSelective degradation of aggregate-prone CryAB mutants by HSPB1 is mediated by ubiquitin-proteasome pathwaysCataract-causing defect of a mutant γ-crystallin proceeds through an aggregation pathway which bypasses recognition by the α-crystallin chaperone.Hemoglobin interactions with αB crystallin: a direct test of sensitivity to protein instability.Altered chaperone-like activity of alpha-crystallins promotes cataractogenesis.Conformational changes resulting from pseudophosphorylation of mammalian small heat shock proteins--a two-hybrid study.A knock-in mouse model for the R120G mutation of αB-crystallin recapitulates human hereditary myopathy and cataracts.The NADPH metabolic network regulates human αB-crystallin cardiomyopathy and reductive stress in Drosophila melanogasterMuscle giants: molecular scaffolds in sarcomerogenesis.Shadows of complexity: what biological networks reveal about epistasis and pleiotropy.Desmin-related cardiomyopathy: an unfolding storyA transgenic mouse model for human autosomal dominant cataractAnalysis of the alphaB-crystallin domain responsible for inhibiting tubulin aggregationProtein-protein interactions between lens vimentin and alphaB-crystallin using FRET acceptor photobleaching.Glial fibrillary acidic protein filaments can tolerate the incorporation of assembly-compromised GFAP-delta, but with consequences for filament organization and alphaB-crystallin association.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.αB-crystallin is essential for the TGF-β2-mediated epithelial to mesenchymal transition of lens epithelial cellsProtein-protein interactions and lens transparency.Lens intermediate filaments
P2860
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P2860
The cardiomyopathy and lens cataract mutation in alphaB-crystallin alters its protein structure, chaperone activity, and interaction with intermediate filaments in vitro.
description
1999 nî lūn-bûn
@nan
1999 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
name
The cardiomyopathy and lens ca ...... termediate filaments in vitro.
@ast
The cardiomyopathy and lens ca ...... termediate filaments in vitro.
@en
type
label
The cardiomyopathy and lens ca ...... termediate filaments in vitro.
@ast
The cardiomyopathy and lens ca ...... termediate filaments in vitro.
@en
prefLabel
The cardiomyopathy and lens ca ...... termediate filaments in vitro.
@ast
The cardiomyopathy and lens ca ...... termediate filaments in vitro.
@en
P2093
P2860
P356
P1476
The cardiomyopathy and lens ca ...... termediate filaments in vitro.
@en
P2093
A M Hutcheson
P J Muchowski
P van Den IJssel
R A Quinlan
P2860
P304
33235-33243
P356
10.1074/JBC.274.47.33235
P407
P577
1999-11-01T00:00:00Z