Phosphorylation regulates tau interactions with Src homology 3 domains of phosphatidylinositol 3-kinase, phospholipase Cgamma1, Grb2, and Src family kinases. - Wikidata - wikimedia - TriplyDB

Phosphorylation regulates tau interactions with Src homology 3 domains of phosphatidylinositol 3-kinase, phospholipase Cgamma1, Grb2, and Src family kinases.

Phosphorylation regulates tau interactions with Src homology 3 domains of phosphatidylinositol 3-kinase, phospholipase Cgamma1, Grb2, and Src family kinases.

http://www.wikidata.org/entity/Q30157679

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Tau Protein Hyperphosphorylation and Aggregation in Alzheimer's Disease and Other Tauopathies, and Possible Neuroprotective Strategies Tau Oligomers: The Toxic Player at Synapses in Alzheimer's Disease Tau and tauopathies Maintenance of synaptic stability requires calcium-independent phospholipase A₂ activity Tau mutant A152T, a risk factor for FTD/PSP, induces neuronal dysfunction and reduced lifespan independently of aggregation in a C. elegans Tauopathy model Zebrafish models of Tauopathy Critical residues involved in tau binding to fyn: implications for tau phosphorylation in Alzheimer's disease.Tau phosphorylation regulates the interaction between BIN1's SH3 domain and Tau's proline-rich domain Microtubule-associated protein 6 mediates neuronal connectivity through Semaphorin 3E-dependent signalling for axonal growth.The N2-Src neuronal splice variant of C-Src has altered SH3 domain ligand specificity and a higher constitutive activity than N1-Src.AlphaScreen HTS and live-cell bioluminescence resonance energy transfer (BRET) assays for identification of Tau-Fyn SH3 interaction inhibitors for Alzheimer disease.A dynamic view of domain-motif interactions.Tyrosine phosphorylation of tau regulates its interactions with Fyn SH2 domains, but not SH3 domains, altering the cellular localization of tau.Semaphorin 4D signaling requires the recruitment of phospholipase C gamma into the plexin-B1 receptor complex.Roles of tau protein in health and disease.Phosphorylation of tau at Y18, but not tau-fyn binding, is required for tau to modulate NMDA receptor-dependent excitotoxicity in primary neuronal culture.GAB2 as an Alzheimer disease susceptibility gene: follow-up of genomewide association results Cellular levels of Grb2 and cytoskeleton stability are correlated in a neurodegenerative scenario.A knowledge-based weighting framework to boost the power of genome-wide association studies.PTL-1 regulates neuronal integrity and lifespan in C. elegans.Tau potentiates nerve growth factor-induced mitogen-activated protein kinase signaling and neurite initiation without a requirement for microtubule binding.Structure and pathology of tau protein in Alzheimer disease.Proteomic analysis of novel targets associated with TrkA-mediated tyrosine phosphorylation signaling pathways in SK-N-MC neuroblastoma cells.Oligomer formation of tau protein hyperphosphorylated in cells.Is tau a suitable therapeutical target in tauopathies?Tyrosine Kinase Inhibition Regulates Early Systemic Immune Changes and Modulates the Neuroimmune Response in α-Synucleinopathy Granular expression of prolyl-peptidyl isomerase PIN1 is a constant and specific feature of Alzheimer's disease pathology and is independent of tau, Aβ and TDP-43 pathology Tau phosphorylation at serine 396 residue is required for hippocampal LTD Advances in tau-based drug discovery.Non-aggregating tau phosphorylation by cyclin-dependent kinase 5 contributes to motor neuron degeneration in spinal muscular atrophy.Tau reduction prevents Aβ-induced axonal transport deficits by blocking activation of GSK3β.Dual modification of Alzheimer's disease PHF-tau protein by lysine methylation and ubiquitylation: a mass spectrometry approach.The many faces of tau The protein phosphatase PP2A/Bα binds to the microtubule-associated proteins Tau and MAP2 at a motif also recognized by the kinase Fyn: implications for tauopathies.Tau Hyperphosphorylation and Oxidative Stress, a Critical Vicious Circle in Neurodegenerative Tauopathies?The Human Tau Interactome: Binding to the Ribonucleoproteome, and Impaired Binding of the Proline-to-Leucine Mutant at Position 301 (P301L) to Chaperones and the Proteasome.Signal transduction in mammalian oocytes during fertilization.Advances in the pathogenesis of Alzheimer's disease: focusing on tau-mediated neurodegeneration.The importance of tau phosphorylation for neurodegenerative diseases The role of tau in neurodegeneration

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P2860

Phosphorylation regulates tau interactions with Src homology 3 domains of phosphatidylinositol 3-kinase, phospholipase Cgamma1, Grb2, and Src family kinases.

http://www.wikidata.org/entity/Q30157679

description

2008 nî lūn-bûn

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2008 թուականի Մայիսին հրատարակուած գիտական յօդուած

@hyw

2008 թվականի մայիսին հրատարակված գիտական հոդված

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2008年の論文

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2008年論文

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2008年論文

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2008年論文

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2008年論文

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2008年論文

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2008年论文

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name

Phosphorylation regulates tau ...... Grb2, and Src family kinases.

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Phosphorylation regulates tau ...... Grb2, and Src family kinases.

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type

label

Phosphorylation regulates tau ...... Grb2, and Src family kinases.

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Phosphorylation regulates tau ...... Grb2, and Src family kinases.

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prefLabel

Phosphorylation regulates tau ...... Grb2, and Src family kinases.

@ast

Phosphorylation regulates tau ...... Grb2, and Src family kinases.

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Journal of Biological Chemistry

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Phosphorylation regulates tau ...... Grb2, and Src family kinases.

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Alice Yang

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Brian H Anderton

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C Hugh Reynolds

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Caroline Price

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Claire J Garwood

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Ian M Varndell

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Paul W Sheppard

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Timothy Perera

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18177-18186

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scholarly article

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10.1074/JBC.M709715200

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26

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283

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Diane P. Hanger

Marketa J Zvelebil

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2008-05-08T00:00:00Z

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18467332

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phosphorylation