The frontotemporal dementia mutation R406W blocks tau's interaction with the membrane in an annexin A2-dependent manner.
about
Frontotemporal lobar degeneration: old knowledge and new insight into the pathogenetic mechanisms of tau mutationsPhysiological and pathological phosphorylation of tau by Cdk5Tau mutant A152T, a risk factor for FTD/PSP, induces neuronal dysfunction and reduced lifespan independently of aggregation in a C. elegans Tauopathy modelTau physiology and pathomechanisms in frontotemporal lobar degenerationTau Biology and Tau-Directed Therapies for Alzheimer's DiseaseRapid changes in phospho-MAP/tau epitopes during neuronal stress: cofilin-actin rods primarily recruit microtubule binding domain epitopesmTOR and neuronal cell cycle reentry: How impaired brain insulin signaling promotes Alzheimer's disease.Single-molecule tracking of tau reveals fast kiss-and-hop interaction with microtubules in living neuronsHirano bodies differentially modulate cell death induced by tau and the amyloid precursor protein intracellular domain.Roles of tau protein in health and disease.RNA protein granules modulate tau isoform expression and induce neuronal sproutingTau binds to lipid membrane surfaces via short amphipathic helices located in its microtubule-binding repeatsInterplay between phosphorylation and palmitoylation mediates plasma membrane targeting and sorting of GAP43.Extracellular α-synuclein leads to microtubule destabilization via GSK-3β-dependent Tau phosphorylation in PC12 cellsPseudohyperphosphorylation has differential effects on polymerization and function of tau isoforms.Optical highlighter molecules in neurobiology.An evolutionary roadmap to the microtubule-associated protein MAP TauRegion-specific dendritic simplification induced by Aβ, mediated by tau via dysregulation of microtubule dynamics: a mechanistic distinct event from other neurodegenerative processes.NMDA receptor subunit composition determines beta-amyloid-induced neurodegeneration and synaptic loss.Identification of Novel Tau Interactions with Endoplasmic Reticulum Proteins in Alzheimer's Disease Brain.Mobility and subcellular localization of endogenous, gene-edited Tau differs from that of over-expressed human wild-type and P301L mutant TauAnnexin A2 system in human biology: cell surface and beyond.Presence of a carboxy-terminal pseudorepeat and disease-like pseudohyperphosphorylation critically influence tau's interaction with microtubules in axon-like processes.Astrocyte pathology in a human neural stem cell model of frontotemporal dementia caused by mutant TAU protein.Biochemistry and cell biology of tau protein in neurofibrillary degenerationMicroglia: an active player in the regulation of synaptic activity.Protein phosphorylation in neurodegeneration: friend or foe?Is membrane homeostasis the missing link between inflammation and neurodegenerative diseases?Chronic consumption of Annona muricata juice triggers and aggravates cerebral tau phosphorylation in wild-type and MAPT transgenic mice.Microtubule dynamics and the neurodegenerative triad of Alzheimer's disease: The hidden connection.Signaling pathways and posttranslational modifications of tau in Alzheimer's disease: the humanization of yeast cells.Quantitative and combinatory determination of in situ phosphorylation of tau and its FTDP-17 mutants.A refined reaction-diffusion model of tau-microtubule dynamics and its application in FDAP analysis.Structural transitions in tau k18 on micelle binding suggest a hierarchy in the efficacy of individual microtubule-binding repeats in filament nucleation.Tau phosphorylation affects its axonal transport and degradation.FTDP-17 tau mutations induce distinct effects on aggregation and microtubule interactions.Derailed intraneuronal signalling drives pathogenesis in sporadic and familial Alzheimer's disease.Discovery and characterization of stable and toxic Tau/phospholipid oligomeric complexes.Can numerical modeling help understand the fate of tau protein in the axon terminal?Extracellular Tau and Its Potential Role in the Propagation of Tau Pathology.
P2860
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P2860
The frontotemporal dementia mutation R406W blocks tau's interaction with the membrane in an annexin A2-dependent manner.
description
2011 nî lūn-bûn
@nan
2011 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2011 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
2011年の論文
@ja
2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
@wuu
name
The frontotemporal dementia mu ...... n annexin A2-dependent manner.
@ast
The frontotemporal dementia mu ...... n annexin A2-dependent manner.
@en
The frontotemporal dementia mu ...... n annexin A2-dependent manner.
@nl
type
label
The frontotemporal dementia mu ...... n annexin A2-dependent manner.
@ast
The frontotemporal dementia mu ...... n annexin A2-dependent manner.
@en
The frontotemporal dementia mu ...... n annexin A2-dependent manner.
@nl
prefLabel
The frontotemporal dementia mu ...... n annexin A2-dependent manner.
@ast
The frontotemporal dementia mu ...... n annexin A2-dependent manner.
@en
The frontotemporal dementia mu ...... n annexin A2-dependent manner.
@nl
P2093
P2860
P356
P1476
The frontotemporal dementia mu ...... an annexin A2-dependent manner
@en
P2093
Anne Gauthier-Kemper
Carina Weissmann
Jürgen J Heinisch
Nataliya Golovyashkina
Roland Brandt
Volker Gerke
Zsofia Sebö-Lemke
P2860
P304
P356
10.1083/JCB.201007161
P407
P577
2011-02-01T00:00:00Z