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Phosphoproteomic Analysis of the Mouse Brain Cytosol Reveals a Predominance of Protein Phosphorylation in Regions of Intrinsic Sequence DisorderTau Proteins and Neurofibrillary DegenerationRNA helicase p68 (DDX5) regulates tau exon 10 splicing by modulating a stem-loop structure at the 5' splice siteMicrotubule-associated protein/microtubule affinity-regulating kinase (p110mark). A novel protein kinase that regulates tau-microtubule interactions and dynamic instability by phosphorylation at the Alzheimer-specific site serine 262Tau protein binds to microtubules through a flexible array of distributed weak sitesTau deletion exacerbates the phenotype of Niemann-Pick type C mice and implicates autophagy in pathogenesis.Cloning and expression of a human kinesin heavy chain gene: interaction of the COOH-terminal domain with cytoplasmic microtubules in transfected CV-1 cellsHyperphosphorylation of microtubule-associated protein tau: a promising therapeutic target for Alzheimer diseaseMAP2 and tau bind longitudinally along the outer ridges of microtubule protofilamentsCharacterization of the tubulin-tyrosine ligaseThe role of tau in neurodegenerative diseases and its potential as a therapeutic targetDirect force measurements reveal that protein Tau confers short-range attractions and isoform-dependent steric stabilization to microtubules.Solution structure of the microtubule-targeting COS domain of MID1BIK1, a protein required for microtubule function during mating and mitosis in Saccharomyces cerevisiae, colocalizes with tubulin.Comparative biochemistry of tau in progressive supranuclear palsy, corticobasal degeneration, FTDP-17 and Pick's diseaseDifferential binding regulation of microtubule-associated proteins MAP1A, MAP1B, and MAP2 by tubulin polyglutamylationThe ubiquitin-proteasome system in Alzheimer's diseaseTau exons 2 and 10, which are misregulated in neurodegenerative diseases, are partly regulated by silencers which bind a SRp30c.SRp55 complex that either recruits or antagonizes htra2beta1Microtubule bundling by tau proteins in vivo: analysis of functional domainsMicrotubule-dependent oligomerization of tau. Implications for physiological tau function and tauopathiesMicrotubule-associated protein tau is essential for long-term depression in the hippocampusA novel mRNA binding protein complex promotes localized plasminogen activator inhibitor-1 accumulation at the myoendothelial junction.FTDP-17 mutations in Tau alter the regulation of microtubule dynamics: an "alternative core" model for normal and pathological Tau action.The amino terminus of tau inhibits kinesin-dependent axonal transport: implications for filament toxicity.Tau isoform regulation is region- and cell-specific in mouse brain.GPHN, a novel partner gene fused to MLL in a leukemia with t(11;14)(q23;q24).Propagation of tau pathology: hypotheses, discoveries, and yet unresolved questions from experimental and human brain studies.Binding to the minor groove of the double-strand, tau protein prevents DNA from damage by peroxidation.Tau interactome mapping based identification of Otub1 as Tau deubiquitinase involved in accumulation of pathological Tau forms in vitro and in vivo.Tau mutants bind tubulin heterodimers with enhanced affinity.Toxic neuronal apoptosis and modifications of tau and APP gene and protein expressions.Death-associated protein kinase 1 has a critical role in aberrant tau protein regulation and function.The role of the lipid bilayer in tau aggregationAberrant splicing of tau pre-mRNA caused by intronic mutations associated with the inherited dementia frontotemporal dementia with parkinsonism linked to chromosome 17.Monte carlo simulations of tau proteins: effect of phosphorylation.The cytoskeleton in neurodegenerative diseases.Hereditary frontotemporal dementia caused by Tau gene mutations.Competition for microtubule-binding with dual expression of tau missense and splice isoforms.Combinatorial Tau pseudophosphorylation: markedly different regulatory effects on microtubule assembly and dynamic instability than the sum of the individual partsCyclic AMP-dependent protein kinase regulates the alternative splicing of tau exon 10: a mechanism involved in tau pathology of Alzheimer disease.
P2860
Q22061729-043E79CF-7DAA-4158-92C2-62B8E5A1385EQ22242304-94E123B1-4BE5-4CEA-B88E-FD2F8D026644Q24293776-3F127F9E-CA9F-499F-8148-BBAC7A75188AQ24313123-CEEE07C3-F1CE-4E68-8217-61A402612A08Q24323891-FC469EEB-987E-49EF-B025-A9993E40D200Q24328779-4F16CEA6-85F7-4164-9763-6BF2A9BED75EQ24643162-2C80090B-83A9-4276-A63E-79B2BB0B8607Q24657243-15C6A0C2-24FA-49F7-B368-F4181E52C6CEQ24672581-B2817F55-9D24-4D5C-AC5A-F6ECDF5D1BBDQ24675050-1A1B0BD5-C69E-4DB5-9CEC-EB87B7EF6016Q27005032-FC4C15EA-44F1-4832-B95F-27447B13C271Q27319980-769B0C88-3770-4235-947B-793BA9478DA4Q27715733-2FF63E58-8DB6-4A0A-B17A-477EE4610BC7Q27938125-5D7C9C3B-65A2-4541-9CE9-447928151960Q28145739-CB36329D-BAFA-463E-8B01-90D781A69811Q28208458-05B3101B-5D39-44BD-86D1-D6FC8A7DDE48Q28268311-F2BB18AD-18BC-4722-91A8-037244AEDB65Q28306183-EB7700F3-4F92-4A7E-BE93-569062515707Q28565528-CA95B5E1-12F6-43A5-887C-D39383AC6C0CQ28576082-6B2C3FEF-6390-444C-B7A6-0DE395D3FF7CQ28584008-85C282D3-B3B5-4E33-B6A1-020B04421DC1Q30419477-AD0535B1-EEA9-4D8C-9F8B-02D4BC3B383BQ30485126-C22E57E0-BC0F-45BA-843A-681905793BC7Q30490027-953754AF-861F-4D80-953F-C45F5827B0B2Q30493882-BF4729AE-1A66-4CC9-BCB2-8159A7110439Q30727023-9399BE89-01CE-413E-AA56-38AD0DD2AB81Q31024674-4A17EFD7-63B8-4F4F-8C36-B5A8900A05E8Q33348647-A476BFDB-3BF2-4C7E-9F50-5F2014ECC5F1Q33559307-515EB22B-9913-40C0-BABB-3D8E7C558B97Q33674452-F86A6BF8-A9A9-47EA-8E58-6B6964BA4D4FQ33719823-DB68E5DF-0B41-4AF5-903E-3BBA6FC710B4Q33720139-FB182AAA-5D61-4DC4-8B80-1109E78CDD94Q33880243-FC63C80E-688A-45A3-9BA1-A27337F19C5AQ33963856-C1B9AB4B-D491-4AAB-AD20-51F4B67894E0Q34201391-19AC67A3-99FB-426E-AAAC-F73D510D8C4EQ34446779-11ECE30E-94EC-40C8-B288-63FC5B8078CCQ34627056-333EB863-4046-4CC1-B6DB-E7D5FB6E5649Q34674767-570C784A-9258-4EE1-A313-801507491DE6Q34800214-36D91A11-C73A-4E02-BFBF-4D99C7D343D0Q34800508-A8C4D461-7BBB-4B86-A7E3-EA967EECA45D
P2860
description
1989 nî lūn-bûn
@nan
1989 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
1989 թվականի հունիսին հրատարակված գիտական հոդված
@hy
1989年の論文
@ja
1989年論文
@yue
1989年論文
@zh-hant
1989年論文
@zh-hk
1989年論文
@zh-mo
1989年論文
@zh-tw
1989年论文
@wuu
name
The microtubule binding domain of tau protein.
@ast
The microtubule binding domain of tau protein.
@en
type
label
The microtubule binding domain of tau protein.
@ast
The microtubule binding domain of tau protein.
@en
prefLabel
The microtubule binding domain of tau protein.
@ast
The microtubule binding domain of tau protein.
@en
P1433
P1476
The microtubule binding domain of tau protein
@en
P2093
P304
P356
10.1016/0896-6273(89)90050-0
P407
P50
P577
1989-06-01T00:00:00Z