Axonal transport rates in vivo are unaffected by tau deletion or overexpression in mice. - Wikidata - wikimedia - TriplyDB

Axonal transport rates in vivo are unaffected by tau deletion or overexpression in mice.

Axonal transport rates in vivo are unaffected by tau deletion or overexpression in mice.

http://www.wikidata.org/entity/Q33623043

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Hyperphosphorylation of microtubule-associated protein tau: a promising therapeutic target for Alzheimer disease The role of tau in neurodegenerative diseases and its potential as a therapeutic target Prion-like properties of Tau protein: the importance of extracellular Tau as a therapeutic target Tau and tauopathies Tau physiology and pathomechanisms in frontotemporal lobar degeneration Tau Biology and Tau-Directed Therapies for Alzheimer's Disease Effects of optineurin siRNA on apoptotic genes and apoptosis in RGC-5 cells Tau reduction prevents Abeta-induced defects in axonal transport.Increased dendritic spine density and tau expression are associated with individual differences in steroidal regulation of male sexual behavior.Neurofilaments form a highly stable stationary cytoskeleton after reaching a critical level in axons.Anchored FRET sensors detect local caspase activation prior to neuronal degeneration Amyloid-β/Fyn-induced synaptic, network, and cognitive impairments depend on tau levels in multiple mouse models of Alzheimer's disease.Amyloid-β oligomers induce tau-independent disruption of BDNF axonal transport via calcineurin activation in cultured hippocampal neurons Single-molecule tracking of tau reveals fast kiss-and-hop interaction with microtubules in living neurons In vivo axonal transport deficits in a mouse model of fronto-temporal dementia.The myosin Va head domain binds to the neurofilament-L rod and modulates endoplasmic reticulum (ER) content and distribution within axons Tau potentiates nerve growth factor-induced mitogen-activated protein kinase signaling and neurite initiation without a requirement for microtubule binding.Microarray analysis of CA1 pyramidal neurons in a mouse model of tauopathy reveals progressive synaptic dysfunction.Motor and cognitive deficits in aged tau knockout mice in two background strains.GSK3β is involved in the relief of mitochondria pausing in a Tau-dependent manner Increased Human Wildtype Tau Attenuates Axonal Transport Deficits Caused by Loss of APP in Mouse Models Reduced axonal transport and increased excitotoxic retinal ganglion cell degeneration in mice transgenic for human mutant P301S tau.Loss of the m-AAA protease subunit AFG₃L₂ causes mitochondrial transport defects and tau hyperphosphorylation.The C-terminal domains of NF-H and NF-M subunits maintain axonal neurofilament content by blocking turnover of the stationary neurofilament network The Ca2+ sensor protein swiprosin-1/EFhd2 is present in neurites and involved in kinesin-mediated transport in neurons.Pre-synaptic C-terminal truncated tau is released from cortical synapses in Alzheimer's disease Tau reduction prevents Aβ-induced axonal transport deficits by blocking activation of GSK3β.Dissociation of Axonal Neurofilament Content from Its Transport Rate The many faces of tau Lessons from tau-deficient mice Pathogenic forms of tau inhibit kinesin-dependent axonal transport through a mechanism involving activation of axonal phosphotransferases Tau Hyperphosphorylation and Oxidative Stress, a Critical Vicious Circle in Neurodegenerative Tauopathies?Soluble forms of tau are toxic in Alzheimer's disease.Absence of Tau triggers age-dependent sciatic nerve morphofunctional deficits and motor impairment PATHOLOGIES OF AXONAL TRANSPORT IN NEURODEGENERATIVE DISEASES Non-invasive, in vivo monitoring of neuronal transport impairment in a mouse model of tauopathy using MEMRI Tau pathology-mediated presynaptic dysfunction Dissociation of tau toxicity and phosphorylation: role of GSK-3beta, MARK and Cdk5 in a Drosophila model Phosphorylated tau: toxic, protective, or none of the above Tau aggregation and toxicity in tauopathic neurodegenerative diseases.

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P2860

Axonal transport rates in vivo are unaffected by tau deletion or overexpression in mice.

http://www.wikidata.org/entity/Q33623043

description

2008 nî lūn-bûn

@nan

2008 թուականի Փետրուարին հրատարակուած գիտական յօդուած

@hyw

2008 թվականի փետրվարին հրատարակված գիտական հոդված

@hy

2008年の論文

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2008年論文

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2008年論文

@zh-hant

2008年論文

@zh-hk

2008年論文

@zh-mo

2008年論文

@zh-tw

2008年论文

@wuu

name

Axonal transport rates in vivo are unaffected by tau deletion or overexpression in mice.

@ast

Axonal transport rates in vivo are unaffected by tau deletion or overexpression in mice.

@en

type

label

Axonal transport rates in vivo are unaffected by tau deletion or overexpression in mice.

@ast

Axonal transport rates in vivo are unaffected by tau deletion or overexpression in mice.

@en

prefLabel

Axonal transport rates in vivo are unaffected by tau deletion or overexpression in mice.

@ast

Axonal transport rates in vivo are unaffected by tau deletion or overexpression in mice.

@en

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P356

JNEUROSCI.5242-07.2008

P1433

Journal of Neuroscience

P1476

Axonal transport rates in vivo are unaffected by tau deletion or overexpression in mice.

@en

P2093

Aidong Yuan

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Asok Kumar

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

Corrinne Peterhoff

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Karen Duff

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Ralph A Nixon

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

P2860

Neurofilament transport in vivo minimally requires hetero-oligomer formation

Altered microtubule organization in small-calibre axons of mice lacking tau protein

Tau-mediated neurodegeneration in Alzheimer's disease and related disorders

Loss of brain tau defines novel sporadic and familial tauopathies with frontotemporal dementia.

Microtubule-binding drugs offset tau sequestration by stabilizing microtubules and reversing fast axonal transport deficits in a tauopathy model

Developmentally regulated expression of specific tau sequences.

Molecular motors and mechanisms of directional transport in neurons.

Phosphorylation on carboxyl terminus domains of neurofilament proteins in retinal ganglion cell neurons in vivo: influences on regional neurofilament accumulation, interneurofilament spacing, and axon caliber.

Tau blocks traffic of organelles, neurofilaments, and APP vesicles in neurons and enhances oxidative stress.

The slow axonal transport of the microtubule-associated protein tau and the transport rates of different isoforms and mutants in cultured neurons.

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1682-1687

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10.1523/JNEUROSCI.5242-07.2008

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18272688

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2814454

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