Small heat-shock proteins and their potential role in human disease.
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The thermal structural transition of α-crystallin inhibits the heat induced self-aggregationExpression of hsp 27, hsp 60, hsc 70, and hsp 70 stress response genes in cultured human urothelial cells (UROtsa) exposed to lethal and sublethal concentrations of sodium arsenite.Unfolding crystallins: the destabilizing role of a beta-hairpin cysteine in betaB2-crystallin by simulation and experimentCrystal Structure of R120G Disease Mutant of Human αB-Crystallin Domain Dimer Shows Closure of a GrooveStructural features and chaperone activity of the NudC protein family.Some properties of human small heat shock protein Hsp20 (HspB6)Influence of trehalose on the molecular chaperone activity of p26, a small heat shock/alpha-crystallin proteinThe thermal structural transition of alpha-crystallin modulates subunit interactions and increases protein solubilityFunctional similarities between the small heat shock proteins Mycobacterium tuberculosis HSP 16.3 and human alphaB-crystallincDNA, genomic sequence and overexpression of crystallin alpha-B Gene (CRYAB) of the Giant PandaRole of the C-terminal extensions of alpha-crystallins. Swapping the C-terminal extension of alpha-crystallin to alphaB-crystallin results in enhanced chaperone activityCharacterization of acid-induced unfolding intermediates of glucose/xylose isomerase.Behavioral defects in chaperone-deficient Alzheimer's disease model mice.The R116C mutation in alpha A-crystallin diminishes its protective ability against stress-induced lens epithelial cell apoptosis.Alterations of chaperone protein expression in presenilin mutant neurons in response to glutamate excitotoxicity.Site-directed mutations in the C-terminal extension of human alphaB-crystallin affect chaperone function and block amyloid fibril formationDetection and architecture of small heat shock protein monomers.Quaternary dynamics and plasticity underlie small heat shock protein chaperone functionLight-induced phosphorylation of crystallins in the retinal pigment epithelium.Approaches for probing the sequence space of substrates recognized by molecular chaperonesA novel quaternary structure of the dimeric alpha-crystallin domain with chaperone-like activity.Alpha-crystallin-type heat shock proteins: socializing minichaperones in the context of a multichaperone network.AlphaB-crystallin is a novel oncoprotein that predicts poor clinical outcome in breast cancer.Adaptive evolution of small heat shock protein/alpha B-crystallin promoter activity of the blind subterranean mole rat, Spalax ehrenbergi.Getting a grip on non-native proteinsIs the small heat shock protein alphaB-crystallin an oncogene?Modulation of lipopolysaccharide-induced NF-κB signaling pathway by 635 nm irradiation via heat shock protein 27 in human gingival fibroblast cells.The function of the beta3 interactive domain in the small heat shock protein and molecular chaperone, human alphaB crystallinOn the mechanism of chaperone activity of the small heat-shock protein of Methanococcus jannaschii.Hsp27-actin interaction.Protein alterations in women with chronic widespread pain--An explorative proteomic study of the trapezius muscle.A conserved role of αA-crystallin in the development of the zebrafish embryonic lens.Dissecting heterogeneous molecular chaperone complexes using a mass spectrum deconvolution approach.Small heat shock proteins and α-crystallins: dynamic proteins with flexible functions.Expression of αB-crystallin overrides the anti-apoptotic activity of XIAP.Formation of amyloid fibrils in vitro by human gammaD-crystallin and its isolated domains.alphaB-crystallin protects retinal tissue during Staphylococcus aureus-induced endophthalmitisAlpha-crystallin binds to the aggregation-prone molten-globule state of alkaline protease: implications for preventing irreversible thermal denaturation.Small heat shock protein IbpB acts as a robust chaperone in living cells by hierarchically activating its multi-type substrate-binding residues.An unusual dimeric small heat shock protein provides insight into the mechanism of this class of chaperones.
P2860
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P2860
Small heat-shock proteins and their potential role in human disease.
description
2000 nî lūn-bûn
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2000 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի փետրվարին հրատարակված գիտական հոդված
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2000年の論文
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2000年論文
@yue
2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
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2000年论文
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name
Small heat-shock proteins and their potential role in human disease.
@ast
Small heat-shock proteins and their potential role in human disease.
@en
type
label
Small heat-shock proteins and their potential role in human disease.
@ast
Small heat-shock proteins and their potential role in human disease.
@en
prefLabel
Small heat-shock proteins and their potential role in human disease.
@ast
Small heat-shock proteins and their potential role in human disease.
@en
P1476
Small heat-shock proteins and their potential role in human disease.
@en
P2093
P J Muchowski
P356
10.1016/S0959-440X(99)00048-2
P577
2000-02-01T00:00:00Z