Interactions between Hsp70 and the hydrophobic core of alpha-synuclein inhibit fibril assembly
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The chaperone-like protein 14-3-3η interacts with human α-synuclein aggregation intermediates rerouting the amyloidogenic pathway and reducing α-synuclein cellular toxicityChaperone proteostasis in Parkinson's disease: stabilization of the Hsp70/alpha-synuclein complex by HipPhysicochemical properties of cells and their effects on intrinsically disordered proteins (IDPs)Molecular chaperones and co-chaperones in Parkinson diseaseThe HSP70 molecular chaperone is not beneficial in a mouse model of alpha-synucleinopathyIdentification of bilateral changes in TID1 expression in the 6-OHDA rat model of Parkinson's diseaseA computational procedure for functional characterization of potential marker genes from molecular data: Alzheimer's as a case studyHeat shock proteins: cellular and molecular mechanisms in the central nervous system.Heat shock proteins in neurodegenerative disorders and agingHeat shock protein 70 prevents both tau aggregation and the inhibitory effects of preexisting tau aggregates on fast axonal transport.The Hsp70/Hsp90 Chaperone Machinery in Neurodegenerative DiseasesMolecular chaperones and protein folding as therapeutic targets in Parkinson's disease and other synucleinopathiesHeat shock protein 90 in neurodegenerative diseasesThe analysis of differential induction of hsp70 in the related cerebral domains and nerve fibers of rats after proteasome inhibiton.Hsp70 and its molecular role in nervous system diseasesThe bacterial curli system possesses a potent and selective inhibitor of amyloid formation.Hsc70 protein interaction with soluble and fibrillar alpha-synucleinChaperoned amyloid proteins for immune manipulation: α-Synuclein/Hsp70 shifts immunity toward a modulatory phenotypeSIRT1 protects against α-synuclein aggregation by activating molecular chaperonesMolecular chaperones in Parkinson's disease--present and futureChemical induction of Hsp70 reduces α-synuclein aggregation in neuroglioma cells.Identification of protein interfaces between α-synuclein, the principal component of Lewy bodies in Parkinson disease, and the molecular chaperones human Hsc70 and the yeast Ssa1p.Rational design of potent domain antibody inhibitors of amyloid fibril assembly.The role of molecular chaperones in human misfolding diseases.The chaperonin CCT inhibits assembly of α-synuclein amyloid fibrils by a specific, conformation-dependent interaction.Protein Quality Control by Molecular Chaperones in Neurodegeneration.Molecular chaperones as rational drug targets for Parkinson's disease therapeutics.Molecular chaperones, α-synuclein, and neurodegeneration.Opportunities and challenges for molecular chaperone modulation to treat protein-conformational brain diseasesBiophysical approaches for the study of interactions between molecular chaperones and protein aggregates.Eukaryotic aggresomes: from a model of conformational diseases to an emerging type of immobilized biocatalyzers.Expanding role of molecular chaperones in regulating α-synuclein misfolding; implications in Parkinson's disease.Glutamine promotes Hsp70 and inhibits α-Synuclein accumulation in pheochromocytoma PC12 cells.Chaperone-dependent Neurodegeneration: A Molecular Perspective on Therapeutic Intervention.The Aggregation of Huntingtin and α-Synuclein.The molecular chaperone Hsp90 modulates intermediate steps of amyloid assembly of the Parkinson-related protein alpha-synuclein.Direct assessment in bacteria of prionoid propagation and phenotype selection by Hsp70 chaperone.Heat shock protein 70 reduces α-synuclein-induced predegenerative neuronal dystrophy in the α-synuclein viral gene transfer rat model of Parkinson's disease.Prolonged latency to CNS-O2 toxicity induced by heat acclimation in rats is associated with increased antioxidative defenses and metabolic energy preservation.FLZ Attenuates α-Synuclein-Induced Neurotoxicity by Activating Heat Shock Protein 70.
P2860
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P2860
Interactions between Hsp70 and the hydrophobic core of alpha-synuclein inhibit fibril assembly
description
2008 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
2008 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
artículu científicu espublizáu en 2008
@ast
im November 2008 veröffentlicher wissenschaftlicher Artikel
@de
scientific journal article
@en
wetenschappelijk artikel (gepubliceerd op 2008/11/25)
@nl
наукова стаття, опублікована в листопаді 2008
@uk
مقالة علمية (نشرت في 25-11-2008)
@ar
name
Interactions between Hsp70 and ...... uclein inhibit fibril assembly
@ast
Interactions between Hsp70 and ...... uclein inhibit fibril assembly
@en
type
label
Interactions between Hsp70 and ...... uclein inhibit fibril assembly
@ast
Interactions between Hsp70 and ...... uclein inhibit fibril assembly
@en
prefLabel
Interactions between Hsp70 and ...... uclein inhibit fibril assembly
@ast
Interactions between Hsp70 and ...... uclein inhibit fibril assembly
@en
P2093
P2860
P921
P356
P1433
P1476
Interactions between Hsp70 and ...... uclein inhibit fibril assembly
@en
P2093
Ian P Mills
John Q Trojanowski
Virginia M-Y Lee
P2860
P304
12614-12625
P356
10.1021/BI801475R
P407
P50
P577
2008-11-01T00:00:00Z