Evidence for two distinct binding sites for tau on microtubules - Wikidata - wikimedia - TriplyDB

Evidence for two distinct binding sites for tau on microtubules

Evidence for two distinct binding sites for tau on microtubules

http://www.wikidata.org/entity/Q33697205

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Interaction of tau protein with the dynactin complex The MAP2/Tau family of microtubule-associated proteins NMR Meets Tau: Insights into Its Function and Pathology Folding of the Tau Protein on Microtubules Nucleation-dependent tau filament formation: the importance of dimerization and an estimation of elementary rate constants Tau induces cooperative Taxol binding to microtubules.Viscoelasticity of tau proteins leads to strain rate-dependent breaking of microtubules during axonal stretch injury: predictions from a mathematical model.Tau mutants bind tubulin heterodimers with enhanced affinity.Vulnerabilities in the tau network and the role of ultrasensitive points in tau pathophysiology.Distinct pose of discodermolide in taxol binding pocket drives a complementary mode of microtubule stabilization.Microtubule-associated protein tau: a marker of paclitaxel sensitivity in breast cancer Quantitative analysis of tau-microtubule interaction using FRET.Hallmarks of molecular action of microtubule stabilizing agents: effects of epothilone B, ixabepilone, peloruside A, and laulimalide on microtubule conformation.The nucleotide-binding state of microtubules modulates kinesin processivity and the ability of Tau to inhibit kinesin-mediated transport.Tau stabilizes microtubules by binding at the interface between tubulin heterodimers.Polyanions and the proteome.Tau alternative splicing and frontotemporal dementia.Mechanical Effects of Dynamic Binding between Tau Proteins on Microtubules during Axonal Injury Tau protein diffuses along the microtubule lattice Taxol-stabilized microtubules promote the formation of filaments from unmodified full-length Tau in vitro.Mechanical properties of doubly stabilized microtubule filaments.Structural principles of tau and the paired helical filaments of Alzheimer's disease.Pathogenic missense MAPT mutations differentially modulate tau aggregation propensity at nucleation and extension steps.Tau aggregation in Alzheimer's disease: what role for phosphorylation?Structural evidence for cooperative microtubule stabilization by Taxol and the endogenous dynamics regulator MAP4.The cochaperone BAG2 sweeps paired helical filament- insoluble tau from the microtubule.Transformation of taxol-stabilized microtubules into inverted tubulin tubules triggered by a tubulin conformation switch.Biochemistry and cell biology of tau protein in neurofibrillary degeneration FRET and FRAP imaging: approaches to characterise tau and stathmin interactions with microtubules in cells.MAPping out distribution routes for kinesin couriers.Transport and diffusion of Tau protein in neurons.Intracellular and extracellular microtubule associated protein tau as a therapeutic target in Alzheimer disease and other tauopathies.The Distance between N and C Termini of Tau and of FTDP-17 Mutants Is Modulated by Microtubule Interactions in Living Cells.Dynein light chain 1 (LC8) association enhances microtubule stability and promotes microtubule bundling.The +TIP coordinating protein EB1 is highly dynamic and diffusive on microtubules, sensitive to GTP analog, ionic strength, and EB1 concentration.The DeltaK280 mutation in MAP tau favors exon 10 skipping in vivo.Disruption of tubulin polymerization and cell proliferation by 1-naphthylarsonic acid.Measurement of Tau Filament Fragmentation Provides Insights into Prion-like Spreading.Two Tau binding sites on tubulin revealed by thiol-disulfide exchanges

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Evidence for two distinct binding sites for tau on microtubules

http://www.wikidata.org/entity/Q33697205

description

2004 nî lūn-bûn

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2004 թուականի Ապրիլին հրատարակուած գիտական յօդուած

@hyw

2004 թվականի ապրիլին հրատարակված գիտական հոդված

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2004年の論文

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2004年論文

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2004年論文

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2004年論文

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2004年論文

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2004年論文

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2004年论文

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name

Evidence for two distinct binding sites for tau on microtubules

@ast

Evidence for two distinct binding sites for tau on microtubules

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type

label

Evidence for two distinct binding sites for tau on microtubules

@ast

Evidence for two distinct binding sites for tau on microtubules

@en

prefLabel

Evidence for two distinct binding sites for tau on microtubules

@ast

Evidence for two distinct binding sites for tau on microtubules

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PNAS.0400992101

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Proceedings of the National Academy of Sciences of the United States of America

P1476

Evidence for two distinct binding sites for tau on microtubules

@en

P2093

John Lew

http://www.w3.org/2001/XMLSchema#string

Michelle R Massie

http://www.w3.org/2001/XMLSchema#string

Stuart C Feinstein

http://www.w3.org/2001/XMLSchema#string

Victoria Makrides

http://www.w3.org/2001/XMLSchema#string

P2860

A protein factor essential for microtubule assembly

Tau protein binds to microtubules through a flexible array of distributed weak sites

Repeat motifs of tau bind to the insides of microtubules in the absence of taxol

MAP2 and tau bind longitudinally along the outer ridges of microtubule protofilaments

The microtubule-associated protein tau cross-links to two distinct sites on each alpha and beta tubulin monomer via separate domains

Microtubule-dependent oligomerization of tau. Implications for physiological tau function and tauopathies

Structural studies of tau protein and Alzheimer paired helical filaments show no evidence for beta-structure

The Microtubule-Associated Protein Tau Cross-Links to Two Distinct Sites on Each α and β Tubulin Monomer via Separate Domains †

Neurodegenerative tauopathies

Mechanism of action of antitumor drugs that interact with microtubules and tubulin.

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17

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