Molecular chaperones as modulators of polyglutamine protein aggregation and toxicity
about
Huntingtin and the molecular pathogenesis of Huntington's disease. Fourth in molecular medicine review seriesCystamine and cysteamine increase brain levels of BDNF in Huntington disease via HSJ1b and transglutaminase.Hsp70 chaperones: cellular functions and molecular mechanismUnscrambling an egg: protein disaggregation by AAA+ proteinsA genetic screening strategy identifies novel regulators of the proteostasis networkThe yeast HtrA orthologue Ynm3 is a protease with chaperone activity that aids survival under heat stress.A brain-specific isoform of small glutamine-rich tetratricopeptide repeat-containing protein binds to Hsc70 and the cysteine string proteinHAP1 can sequester a subset of TBP in cytoplasmic inclusions via specific interaction with the conserved TBP(CORE).Nuclear aggregation of polyglutamine-expanded ataxin-3: fragments escape the cytoplasmic quality control.Interdependence of amyloid formation in yeast: implications for polyglutamine disorders and biological functions.cAMP-response element-binding protein and heat-shock protein 70 additively suppress polyglutamine-mediated toxicity in DrosophilaProtein homeostasis and aging: The importance of exquisite quality control.Getting folded: chaperone proteins in muscle development, maintenance and disease.Pharmacological induction of heat-shock proteins alleviates polyglutamine-mediated motor neuron disease.Defective protein folding and aggregation as the basis of neurodegenerative diseases: the darker aspect of proteins.Cellular strategies of protein quality control.Cysteine string protein (CSP) inhibition of N-type calcium channels is blocked by mutant huntingtin.Protein aggregation can inhibit clathrin-mediated endocytosis by chaperone competition.Chaperoning brain degeneration.Differences in the chaperone-like activities of the four main small heat shock proteins of Drosophila melanogaster.Sequestration of cellular interacting partners by protein aggregates: implication in a loss-of-function pathology.Hsp70 chaperones accelerate protein translocation and the unfolding of stable protein aggregates by entropic pulling.Compositional biases and polyalanine runs in humans.DNAJB3/HSP-40 cochaperone is downregulated in obese humans and is restored by physical exercise.Molecular parameters of hyperthermia for radiosensitization.Design of a flexible cell-based assay for the evaluation of heat shock protein 70 expression modulatorsER stress-induced eIF2-alpha phosphorylation underlies sensitivity of striatal neurons to pathogenic huntingtinSignature changes in ubiquilin expression in the R6/2 mouse model of Huntington's disease.Focused cerebellar laser light induced hyperthermia improves symptoms and pathology of polyglutamine disease SCA1 in a mouse model.Proteins with Intrinsically Disordered Domains Are Preferentially Recruited to Polyglutamine Aggregates.The histone deacetylase Hos2 forms an Hsp42-dependent cytoplasmic granule in quiescent yeast cellsA molecular chaperone breaks the catalytic cycle that generates toxic Aβ oligomersSwedish Alzheimer mutation induces mitochondrial dysfunction mediated by HSP60 mislocalization of amyloid precursor protein (APP) and beta-amyloid.A new Caenorhabditis elegans model of human huntingtin 513 aggregation and toxicity in body wall musclesA polymer physics perspective on driving forces and mechanisms for protein aggregationTargeting expression of expanded polyglutamine proteins to the endoplasmic reticulum or mitochondria prevents their aggregation.Celastrol inhibits polyglutamine aggregation and toxicity though induction of the heat shock response.Sex-dependent effect of BAG1 in ameliorating motor deficits of Huntington disease transgenic mice.Therapeutic perspectives for the treatment of Huntington's disease: treating the whole bodyAltered Function of the DnaJ Family Cochaperone DNJ-17 Modulates Locomotor Circuit Activity in a Caenorhabditis elegans Seizure Model.
P2860
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P2860
Molecular chaperones as modulators of polyglutamine protein aggregation and toxicity
description
2002 nî lūn-bûn
@nan
2002 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
2002 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
2002年の論文
@ja
2002年学术文章
@wuu
2002年学术文章
@zh-cn
2002年学术文章
@zh-hans
2002年学术文章
@zh-my
2002年学术文章
@zh-sg
2002年學術文章
@yue
name
Molecular chaperones as modulators of polyglutamine protein aggregation and toxicity
@ast
Molecular chaperones as modulators of polyglutamine protein aggregation and toxicity
@en
Molecular chaperones as modulators of polyglutamine protein aggregation and toxicity
@nl
type
label
Molecular chaperones as modulators of polyglutamine protein aggregation and toxicity
@ast
Molecular chaperones as modulators of polyglutamine protein aggregation and toxicity
@en
Molecular chaperones as modulators of polyglutamine protein aggregation and toxicity
@nl
prefLabel
Molecular chaperones as modulators of polyglutamine protein aggregation and toxicity
@ast
Molecular chaperones as modulators of polyglutamine protein aggregation and toxicity
@en
Molecular chaperones as modulators of polyglutamine protein aggregation and toxicity
@nl
P2860
P356
P1476
Molecular chaperones as modulators of polyglutamine protein aggregation and toxicity
@en
P2093
Hideki Sakahira
Peter Breuer
P2860
P304
16412-16418
P356
10.1073/PNAS.182426899
P407
P478
99 Suppl 4
P577
2002-08-20T00:00:00Z