In vitro polymerization of tau protein monitored by laser light scattering: method and application to the study of FTDP-17 mutants.
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Caspase cleavage of tau: linking amyloid and neurofibrillary tangles in Alzheimer's diseaseThe role of tau in neurodegenerative diseases and its potential as a therapeutic targetTau and tauopathiesMicrotubule-dependent oligomerization of tau. Implications for physiological tau function and tauopathiesFTDP-17 mutations in Tau alter the regulation of microtubule dynamics: an "alternative core" model for normal and pathological Tau action.Phosphorylation in the amino terminus of tau prevents inhibition of anterograde axonal transport.Heat shock protein 70 prevents both tau aggregation and the inhibitory effects of preexisting tau aggregates on fast axonal transport.Modulation of microtubule dynamics by tau in living cells: implications for development and neurodegenerationPseudophosphorylation and glycation of tau protein enhance but do not trigger fibrillization in vitro.Protein aggregation and protein instability govern familial amyotrophic lateral sclerosis patient survival.Tau mutants bind tubulin heterodimers with enhanced affinity.TOC1: a valuable tool in assessing disease progression in the rTg4510 mouse model of tauopathy.Tau-directed drug discovery for Alzheimer's disease and related tauopathies: a focus on tau assembly inhibitors.Targeting Abeta and tau in Alzheimer's disease, an early interim reportThe cytoskeleton in neurodegenerative diseases.Peroxynitrite-induced nitrative and oxidative modifications alter tau filament formation.Distinct FTDP-17 missense mutations in tau produce tau aggregates and other pathological phenotypes in transfected CHO cells.Interactions between Aβ and mutated Tau lead to polymorphism and induce aggregation of Aβ-mutated tau oligomeric complexesA novel MAPT mutation, G55R, in a frontotemporal dementia patient leads to altered Tau function.Aminothienopyridazine inhibitors of tau aggregation: evaluation of structure-activity relationship leads to selection of candidates with desirable in vivo properties.Synergistic interactions between repeats in tau protein and Aβ amyloids may be responsible for accelerated aggregation via polymorphic states.Characterization of prefibrillar Tau oligomers in vitro and in Alzheimer disease.Differential regulation of microtubule dynamics by three- and four-repeat tau: implications for the onset of neurodegenerative diseasePseudohyperphosphorylation has differential effects on polymerization and function of tau isoforms.Tau assembly in inducible transfectants expressing wild-type or FTDP-17 tau.Detection and quantification of tau aggregation using a membrane filter assay.Tau phosphorylation, aggregation, and cell toxicityDisease modifying therapy for AD?TOC1: characterization of a selective oligomeric tau antibody.Tau as a therapeutic target in neurodegenerative disease.Pathogenic missense MAPT mutations differentially modulate tau aggregation propensity at nucleation and extension steps.Microtubule-associated protein tau in bovine retinal photoreceptor rod outer segments: comparison with brain tauTau-based treatment strategies in neurodegenerative diseasesEvidence that non-fibrillar tau causes pathology linked to neurodegeneration and behavioral impairments.Tau aggregation and toxicity in tauopathic neurodegenerative diseases.Tau mutations in neurodegenerative diseases.Advances in tau-focused drug discovery for Alzheimer's disease and related tauopathies.Cell-based Models To Investigate Tau Aggregation.Cellular factors modulating the mechanism of tau protein aggregation.Unlocking truths of γ-secretase in Alzheimer's disease: what is the translational potential?
P2860
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P2860
In vitro polymerization of tau protein monitored by laser light scattering: method and application to the study of FTDP-17 mutants.
description
2000 nî lūn-bûn
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2000 թուականի Մայիսին հրատարակուած գիտական յօդուած
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2000 թվականի մայիսին հրատարակված գիտական հոդված
@hy
2000年の論文
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2000年学术文章
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2000年学术文章
@zh-cn
2000年学术文章
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2000年学术文章
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2000年学术文章
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2000年學術文章
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name
In vitro polymerization of tau ...... the study of FTDP-17 mutants.
@ast
In vitro polymerization of tau ...... the study of FTDP-17 mutants.
@en
type
label
In vitro polymerization of tau ...... the study of FTDP-17 mutants.
@ast
In vitro polymerization of tau ...... the study of FTDP-17 mutants.
@en
prefLabel
In vitro polymerization of tau ...... the study of FTDP-17 mutants.
@ast
In vitro polymerization of tau ...... the study of FTDP-17 mutants.
@en
P2093
P356
P1433
P1476
In vitro polymerization of tau ...... the study of FTDP-17 mutants.
@en
P2093
Gamblin TC
P304
P356
10.1021/BI000201F
P407
P577
2000-05-01T00:00:00Z