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Tau deletion exacerbates the phenotype of Niemann-Pick type C mice and implicates autophagy in pathogenesis.Molecular Mechanisms in the Pathogenesis of Alzheimer's disease and Tauopathies-Prion-Like Seeded Aggregation and PhosphorylationTau mutant A152T, a risk factor for FTD/PSP, induces neuronal dysfunction and reduced lifespan independently of aggregation in a C. elegans Tauopathy modelStructure of tau exon 10 splicing regulatory element RNA and destabilization by mutations of frontotemporal dementia and parkinsonism linked to chromosome 17Structural basis for recognition of the RNA major groove in the tau exon 10 splicing regulatory element by aminoglycoside antibiotics.Tau Biology and Tau-Directed Therapies for Alzheimer's DiseaseRegulated association of microtubule-associated protein 2 (MAP2) with Src and Grb2: evidence for MAP2 as a scaffolding proteinPhosphorylation-mimicking glutamate clusters in the proline-rich region are sufficient to simulate the functional deficiencies of hyperphosphorylated tau proteinImmunophilin FKBP52 induces Tau-P301L filamentous assembly in vitro and modulates its activity in a model of tauopathy.Efficacy of small-molecule glycogen synthase kinase-3 inhibitors in the postnatal rat model of tau hyperphosphorylationFilamentous nerve cell inclusions in neurodegenerative diseases: tauopathies and alpha-synucleinopathies.Aberrant splicing of tau pre-mRNA caused by intronic mutations associated with the inherited dementia frontotemporal dementia with parkinsonism linked to chromosome 17.Proteases and proteolysis in Alzheimer disease: a multifactorial view on the disease process.Protein tau: prime cause of synaptic and neuronal degeneration in Alzheimer's disease.Presenile dementia syndromes: an update on taxonomy and diagnosis.Acceleration of oligomerization, not fibrillization, is a shared property of both alpha-synuclein mutations linked to early-onset Parkinson's disease: implications for pathogenesis and therapy.Hyperphosphorylated tau and neurofilament and cytoskeletal disruptions in mice overexpressing human p25, an activator of cdk5Drug therapy of frontotemporal dementia.Protein interacting with C kinase (PICK1) is a suppressor of spinocerebellar ataxia 3-associated neurodegeneration in Drosophila.Temporal accrual of complement proteins in amyloid plaques in Down's syndrome with Alzheimer's disease.RNA Structures as Mediators of Neurological Diseases and as Drug Targets.Selective neurodegeneration, without neurofibrillary tangles, in a mouse model of Niemann-Pick C disease.Biochemical classification of tauopathies by immunoblot, protein sequence and mass spectrometric analyses of sarkosyl-insoluble and trypsin-resistant tauThe intolerance to functional genetic variation of protein domains predicts the localization of pathogenic mutations within genes.Gene Therapy Models of Alzheimer's Disease and Other Dementias.Parkinsonism genes: culprits and clues.The Tau/A152T mutation, a risk factor for frontotemporal-spectrum disorders, leads to NR2B receptor-mediated excitotoxicity.Assembly of tau protein into Alzheimer paired helical filaments depends on a local sequence motif ((306)VQIVYK(311)) forming beta structure.Milestones in atypical and secondary Parkinsonisms.What is the pathological significance of tau oligomers?Correction of alternative splicing of tau in frontotemporal dementia and parkinsonism linked to chromosome 17.Motor neuron disease-frontotemporal dementia: a clinical continuum.Tau gene mutation K257T causes a tauopathy similar to Pick's disease.Abolishing Tau cleavage by caspases at Aspartate421 causes memory/synaptic plasticity deficits and pre-pathological Tau alterations.Cellular and molecular modifier pathways in tauopathies: the big picture from screening invertebrate models.Genetics of FTLD: overview and what else we can expect from genetic studies.The Role of the Carboxyl-Terminal Sequence of Tau and MAP2 in the Pathogenesis of DementiaMicrotubule dynamics and the neurodegenerative triad of Alzheimer's disease: The hidden connection.Missense point mutations of tau to segregate with FTDP-17 exhibit site-specific effects on microtubule structure in COS cells: a novel action of R406W mutation.Mutant (R406W) human tau is hyperphosphorylated and does not efficiently bind microtubules in a neuronal cortical cell model.
P2860
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P2860
description
1998 nî lūn-bûn
@nan
1998年の論文
@ja
1998年学术文章
@wuu
1998年学术文章
@zh-cn
1998年学术文章
@zh-hans
1998年学术文章
@zh-my
1998年学术文章
@zh-sg
1998年學術文章
@yue
1998年學術文章
@zh
1998年學術文章
@zh-hant
name
Tau mutations cause frontotemporal dementias.
@en
Tau mutations cause frontotemporal dementias.
@nl
type
label
Tau mutations cause frontotemporal dementias.
@en
Tau mutations cause frontotemporal dementias.
@nl
prefLabel
Tau mutations cause frontotemporal dementias.
@en
Tau mutations cause frontotemporal dementias.
@nl
P2093
P1433
P1476
Tau mutations cause frontotemporal dementias.
@en
P2093
Crowther RA
Spillantini MG
P304
P356
10.1016/S0896-6273(00)80615-7
P407
P577
1998-11-01T00:00:00Z