The proline-rich domain of tau plays a role in interactions with actin. - Wikidata - wikimedia - TriplyDB

The proline-rich domain of tau plays a role in interactions with actin.

The proline-rich domain of tau plays a role in interactions with actin.

http://www.wikidata.org/entity/Q33515434

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Connecting the dots between tau dysfunction and neurodegeneration Tangles, Toxicity, and Tau Secretion in AD - New Approaches to a Vexing Problem Tau physiology and pathomechanisms in frontotemporal lobar degeneration Curcumin suppresses soluble tau dimers and corrects molecular chaperone, synaptic, and behavioral deficits in aged human tau transgenic mice Rapid changes in phospho-MAP/tau epitopes during neuronal stress: cofilin-actin rods primarily recruit microtubule binding domain epitopes Non-microtubular localizations of microtubule-associated protein 6 (MAP6)Phosphatase 2A Inhibition Affects Endoplasmic Reticulum and Mitochondria Homeostasis Via Cytoskeletal Alterations in Brain Endothelial Cells Interactions between Tau and α-synuclein augment neurotoxicity in a Drosophila model of Parkinson's disease.Tau co-organizes dynamic microtubule and actin networks.Tunneling nanotube (TNT)-mediated neuron-to neuron transfer of pathological Tau protein assemblies Hirano bodies differentially modulate cell death induced by tau and the amyloid precursor protein intracellular domain.Roles of tau protein in health and disease.Tau association with synaptic vesicles causes presynaptic dysfunction.Frequent and symmetric deposition of misfolded tau oligomers within presynaptic and postsynaptic terminals in Alzheimer's disease.Tau mislocalization to dendritic spines mediates synaptic dysfunction independently of neurodegeneration.Tau reduction prevents Aβ-induced axonal transport deficits by blocking activation of GSK3β.CRMP4 and CRMP2 Interact to Coordinate Cytoskeleton Dynamics, Regulating Growth Cone Development and Axon Elongation Dual modification of Alzheimer's disease PHF-tau protein by lysine methylation and ubiquitylation: a mass spectrometry approach.Microtubule-associated proteins as direct crosslinkers of actin filaments and microtubules.The many faces of tau CRMP‑5 interacts with actin to regulate neurite outgrowth Tau protein modifications and interactions: their role in function and dysfunction.The Role of p38 MAPK and Its Substrates in Neuronal Plasticity and Neurodegenerative Disease.Identification of regions within the Legionella pneumophila VipA effector protein involved in actin binding and polymerization and in interference with eukaryotic organelle trafficking.Actin dynamics and cofilin-actin rods in alzheimer disease.Expression of Tau Produces Aberrant Plasma Membrane Blebbing in Glial Cells Through RhoA-ROCK-Dependent F-Actin Remodeling.Physiological and pathophysiological functions of Swiprosin-1/EFhd2 in the nervous system.Bin1 directly remodels actin dynamics through its BAR domain.Bar-coding neurodegeneration: identifying subcellular effects of human neurodegenerative disease proteins using Drosophila leg neurons.Yeast as a model system to study tau biology.Microtubule-associated protein 4 binds to actin filaments and modulates their properties.Multivalent cross-linking of actin filaments and microtubules through the microtubule-associated protein Tau.Tau-mediated Neurodegeneration and Potential Implications in Diagnosis and Treatment of Alzheimer's Disease.The Microtubule-Associated Protein Tau Mediates the Organization of Microtubules and Their Dynamic Exploration of Actin-Rich Lamellipodia and Filopodia of Cortical Growth Cones.A key function for microtubule-associated-protein 6 in activity-dependent stabilisation of actin filaments in dendritic spines

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P2860

The proline-rich domain of tau plays a role in interactions with actin.

http://www.wikidata.org/entity/Q33515434

description

2009 nî lūn-bûn

@nan

2009 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած

@hyw

2009 թվականի նոյեմբերին հրատարակված գիտական հոդված

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2009年の論文

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2009年論文

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2009年論文

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2009年論文

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2009年論文

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2009年論文

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2009年论文

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name

The proline-rich domain of tau plays a role in interactions with actin.

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The proline-rich domain of tau plays a role in interactions with actin.

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The proline-rich domain of tau plays a role in interactions with actin.

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type

label

The proline-rich domain of tau plays a role in interactions with actin.

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The proline-rich domain of tau plays a role in interactions with actin.

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The proline-rich domain of tau plays a role in interactions with actin.

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prefLabel

The proline-rich domain of tau plays a role in interactions with actin.

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The proline-rich domain of tau plays a role in interactions with actin.

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The proline-rich domain of tau plays a role in interactions with actin.

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1471-2121-10-81

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BMC Cell Biology

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The proline-rich domain of tau plays a role in interactions with actin.

@en

P2093

Dong Liang Wang

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

Hai Jin He

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

Ming Nan Liu

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

Rong Pan

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Rong Qiao He

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Xing Sheng Wang

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P2860

A protein factor essential for microtubule assembly

Modulation of the dynamic instability of tubulin assembly by the microtubule-associated protein tau

Microtubule bundling by tau proteins in vivo: analysis of functional domains

The regulation of rabbit skeletal muscle contraction. I. Biochemical studies of the interaction of the tropomyosin-troponin complex with actin and the proteolytic fragments of myosin

Tau and src family tyrosine kinases.

Binding to the minor groove of the double-strand, tau protein prevents DNA from damage by peroxidation.

Mechanical properties of actin filament networks depend on preparation, polymerization conditions, and storage of actin monomers

Viscometric analysis of the gelation of Acanthamoeba extracts and purification of two gelation factors.

Microtubule-associated proteins (MAPs) and the organization of actin filaments in vitro

Complementary dimerization of microtubule-associated tau protein: Implications for microtubule bundling and tau-mediated pathogenesis.

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1471-2121-10-81

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2784441

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