Phosphorylation of tau at Thr212, Thr231, and Ser262 combined causes neurodegeneration - Wikidata - thesis-toulmin - TriplyDB

Phosphorylation of tau at Thr212, Thr231, and Ser262 combined causes neurodegeneration

Phosphorylation of tau at Thr212, Thr231, and Ser262 combined causes neurodegeneration

http://www.wikidata.org/entity/Q34155383

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Therapeutic benefits of a component of coffee in a rat model of Alzheimer's disease.Phosphoprotein phosphatase 2A: a novel druggable target for Alzheimer's disease JNK Signaling: Regulation and Functions Based on Complex Protein-Protein Partnerships New Features about Tau Function and Dysfunction Tau: The Center of a Signaling Nexus in Alzheimer's Disease Olive Oil and the Hallmarks of Aging Frontotemporal lobar degeneration: old knowledge and new insight into the pathogenetic mechanisms of tau mutations Induced tauopathy in a novel 3D-culture model mediates neurodegenerative processes: a real-time study on biochips Neuroprotective Sirtuin ratio reversed by ApoE4 β-carboline compounds, including harmine, inhibit DYRK1A and tau phosphorylation at multiple Alzheimer's disease-related sites mTOR and neuronal cell cycle reentry: How impaired brain insulin signaling promotes Alzheimer's disease.Mammalian target of rapamycin (mTor) mediates tau protein dyshomeostasis: implication for Alzheimer disease The role of hippocampal tau protein phosphorylation in isoflurane-induced cognitive dysfunction in transgenic APP695 mice.MARK4 and MARK3 associate with early tau phosphorylation in Alzheimer's disease granulovacuolar degeneration bodies.Paraquat, but not maneb, induces synucleinopathy and tauopathy in striata of mice through inhibition of proteasomal and autophagic pathways Cytoplasmic retention of protein phosphatase 2A inhibitor 2 (I2PP2A) induces Alzheimer-like abnormal hyperphosphorylation of Tau.Identification of the sites of tau hyperphosphorylation and activation of tau kinases in synucleinopathies and Alzheimer's diseases.The toxicity of tau in Alzheimer disease: turnover, targets and potential therapeutics Stabilization of Microtubule-Unbound Tau via Tau Phosphorylation at Ser262/356 by Par-1/MARK Contributes to Augmentation of AD-Related Phosphorylation and Aβ42-Induced Tau Toxicity.Oleocanthal enhances amyloid-β clearance from the brains of TgSwDI mice and in vitro across a human blood-brain barrier model Taxol-stabilized microtubules promote the formation of filaments from unmodified full-length Tau in vitro.Abnormal tau induces cognitive impairment through two different mechanisms: synaptic dysfunction and neuronal loss Microtubule-associated protein tau in bovine retinal photoreceptor rod outer segments: comparison with brain tau Global analysis of phosphorylation of tau by the checkpoint kinases Chk1 and Chk2 in vitro Stressing Out Hsp90 in Neurotoxic Proteinopathies.Tau antagonizes end-binding protein tracking at microtubule ends through a phosphorylation-dependent mechanism.Tau pathology involves protein phosphatase 2A in parkinsonism-dementia of Guam.Threonine175, a novel pathological phosphorylation site on tau protein linked to multiple tauopathies.The power and richness of modelling tauopathies in Drosophila.Spreading of tau pathology in Alzheimer's disease by cell-to-cell transmission.Tau-induced neurodegeneration: mechanisms and targets.Invited review: Drug development for tauopathies.Physical Exercise and Brain Mitochondrial Fitness: The Possible Role Against Alzheimer's Disease.High glucose induces formation of tau hyperphosphorylation via Cav-1-mTOR pathway: A potential molecular mechanism for diabetes-induced cognitive dysfunction.Amyloid β1-42 (Aβ1-42) Induces the CDK2-Mediated Phosphorylation of Tau through the Activation of the mTORC1 Signaling Pathway While Promoting Neuronal Cell Death.The influence of phospho-τ on dendritic spines of cortical pyramidal neurons in patients with Alzheimer's disease."Clicked" sugar-curcumin conjugate: modulator of amyloid-β and tau peptide aggregation at ultralow concentrations.Tau Phosphorylation by GSK3 in Different Conditions.Activation of Glycogen Synthase Kinase-3 Mediates the Olfactory Deficit-Induced Hippocampal Impairments.Potentiating tangle formation reduces acute toxicity of soluble tau species in the rat.

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Phosphorylation of tau at Thr212, Thr231, and Ser262 combined causes neurodegeneration

http://www.wikidata.org/entity/Q34155383

description

2010 nî lūn-bûn

@nan

2010 թուականի Յուլիսին հրատարակուած գիտական յօդուած

@hyw

2010 թվականի հուլիսին հրատարակված գիտական հոդված

@hy

2010年の論文

@ja

2010年論文

@yue

2010年論文

@zh-hant

2010年論文

@zh-hk

2010年論文

@zh-mo

2010年論文

@zh-tw

2010年论文

@wuu

name

Phosphorylation of tau at Thr212, Thr231, and Ser262 combined causes neurodegeneration

@ast

Phosphorylation of tau at Thr212, Thr231, and Ser262 combined causes neurodegeneration

@en

Phosphorylation of tau at Thr212, Thr231, and Ser262 combined causes neurodegeneration

@nl

type

label

Phosphorylation of tau at Thr212, Thr231, and Ser262 combined causes neurodegeneration

@ast

Phosphorylation of tau at Thr212, Thr231, and Ser262 combined causes neurodegeneration

@en

Phosphorylation of tau at Thr212, Thr231, and Ser262 combined causes neurodegeneration

@nl

prefLabel

Phosphorylation of tau at Thr212, Thr231, and Ser262 combined causes neurodegeneration

@ast

Phosphorylation of tau at Thr212, Thr231, and Ser262 combined causes neurodegeneration

@en

Phosphorylation of tau at Thr212, Thr231, and Ser262 combined causes neurodegeneration

@nl

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JBC.M110.110957

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Journal of Biological Chemistry

P1476

Phosphorylation of tau at Thr212, Thr231, and Ser262 combined causes neurodegeneration

@en

P2093

Alejandra D Alonso

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

Bin Li

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

Christopher P Corbo

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

John Di Clerico

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

Khalid Iqbal

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

Maria E Alaniz

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

P2860

A protein factor essential for microtubule assembly

Caspase cleavage of tau: linking amyloid and neurofibrillary tangles in Alzheimer's disease

Microtubule-associated protein/microtubule affinity-regulating kinase (p110mark). A novel protein kinase that regulates tau-microtubule interactions and dynamic instability by phosphorylation at the Alzheimer-specific site serine 262

Hyperphosphorylation induces self-assembly of tau into tangles of paired helical filaments/straight filaments

Accumulation of abnormally phosphorylated tau precedes the formation of neurofibrillary tangles in Alzheimer's disease

Association of missense and 5'-splice-site mutations in tau with the inherited dementia FTDP-17

Phosphorylation of tau at both Thr 231 and Ser 262 is required for maximal inhibition of its binding to microtubules

Multiple isoforms of human microtubule-associated protein tau: sequences and localization in neurofibrillary tangles of Alzheimer's disease

Abnormal phosphorylation of the microtubule-associated protein tau (tau) in Alzheimer cytoskeletal pathology

Neurodegenerative tauopathies

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30851-30860

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scholarly article

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10.1074/JBC.M110.110957

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P433

40

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285

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Inge Grundke-Iqbal

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2010-07-27T00:00:00Z

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20663882

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

P921

phosphorylation

P932

2945578

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