Alzheimer's disease hyperphosphorylated tau sequesters normal tau into tangles of filaments and disassembles microtubules.
about
The Opitz syndrome gene product, MID1, associates with microtubulesTau deletion exacerbates the phenotype of Niemann-Pick type C mice and implicates autophagy in pathogenesis.Hyperphosphorylation induces self-assembly of tau into tangles of paired helical filaments/straight filamentsCurcumin and its derivatives: their application in neuropharmacology and neuroscience in the 21st centuryHyperphosphorylation of microtubule-associated protein tau: a promising therapeutic target for Alzheimer diseaseRapid neurofibrillary tangle formation after localized gene transfer of mutated tauUp-regulation of phosphorylated/activated p70 S6 kinase and its relationship to neurofibrillary pathology in Alzheimer's diseaseNMR Meets Tau: Insights into Its Function and PathologyNew Features about Tau Function and DysfunctionBrain-penetrant microtubule-stabilizing compounds as potential therapeutic agents for tauopathiesMicrotubule-stabilizing agents as potential therapeutics for neurodegenerative diseaseDeveloping therapeutic approaches to tau, selected kinases, and related neuronal protein targetsTherapeutic and diagnostic challenges for frontotemporal dementiaEarly etiology of Alzheimer's disease: tipping the balance toward autophagy or endosomal dysfunction?The physiological link between metabolic rate depression and tau phosphorylation in mammalian hibernationFunctional Impact of Corticotropin-Releasing Factor Exposure on Tau Phosphorylation and Axon TransportTau physiology and pathomechanisms in frontotemporal lobar degenerationCharacterization of the in vitro phosphorylation of human tau by tau protein kinase II (cdk5/p20) using mass spectrometryInvolvement of aberrant glycosylation in phosphorylation of tau by cdk5 and GSK-3betaI1PP2A affects tau phosphorylation via association with the catalytic subunit of protein phosphatase 2APaternal spatial training enhances offspring's cognitive performance and synaptic plasticity in wild-type but not improve memory deficit in Alzheimer's mice.Hyperphosphorylated tau in parahippocampal cortex impairs place learning in aged mice expressing wild-type human tauAnalysis of N-glycans of pathological tau: possible occurrence of aberrant processing of tau in Alzheimer's disease.Pseudophosphorylation and glycation of tau protein enhance but do not trigger fibrillization in vitro.Cholesterol-dependent modulation of tau phosphorylation in cultured neurons.The excitotoxin quinolinic acid induces tau phosphorylation in human neuronsLoss of MAP function leads to hippocampal synapse loss and deficits in the Morris Water Maze with agingVulnerabilities in the tau network and the role of ultrasensitive points in tau pathophysiology.Biomarkers in Alzheimer's disease: past, present and future.Tau pathology generated by overexpression of tau.A DNA damage-activated checkpoint kinase phosphorylates tau and enhances tau-induced neurodegeneration.Evidence for the involvement of apoptosis-inducing factor-mediated caspase-independent neuronal death in Alzheimer diseaseTau-directed drug discovery for Alzheimer's disease and related tauopathies: a focus on tau assembly inhibitors.Mechanisms of tau-induced neurodegeneration.Tau Ser262 phosphorylation is critical for Abeta42-induced tau toxicity in a transgenic Drosophila model of Alzheimer's disease.Okadaic acid induces tau phosphorylation in SH-SY5Y cells in an estrogen-preventable mannerCauses versus effects: the increasing complexities of Alzheimer's disease pathogenesis.Phosphorylation of tau at Thr212, Thr231, and Ser262 combined causes neurodegenerationInfantile postnatal exposure to lead (Pb) enhances tau expression in the cerebral cortex of aged mice: relevance to AD.Cytoplasmic retention of protein phosphatase 2A inhibitor 2 (I2PP2A) induces Alzheimer-like abnormal hyperphosphorylation of Tau.
P2860
Q22009027-056FC71C-CD9A-4F96-BDC6-5F6E0DAB4088Q24328779-F620AFC9-01FD-42DA-9B60-5834C7589BCEQ24599152-A65D6AB6-70F4-4C8B-B3B2-C3BAE85BD3B5Q24630927-5C99D3DB-1740-4B8E-A8B2-B56AEC15C316Q24657243-3C57E109-0E1C-4BB1-AFD3-8595F3BCFF41Q24675907-C4FA34A7-A5D6-455F-8CC3-872E1A8E5415Q24685592-A82BF09F-1E5E-4275-A2AC-D2040E227DC3Q26747418-220F1424-358C-4558-8AF8-E83AA8F8F77CQ26750922-FCB4BF03-EE1B-4EE1-9F2E-3F845ABC5272Q26861683-87C3A916-3534-42E5-91A8-25F495552C68Q26865234-F4251748-2455-40F6-90F8-29027D746C5EQ26865654-89CB8207-AE7F-4F85-B4A8-482B51453200Q26998919-70DCA970-C8A9-45F3-853B-D10E383AC75AQ27026907-EFBB1731-B963-4126-97E0-81A672B6EE9AQ27314753-78EA007A-84D1-4AF8-ACC7-691D99398BF3Q27329404-38624F9C-3E83-464E-907C-984F179013BBQ28070250-318BB684-3B80-4F4A-B0B8-17094BA4472EQ28200189-4ADDE5EA-1781-47DD-831D-95FE8025AA19Q28208444-5A0AA35A-502C-4F07-885C-B9E7CA905787Q28566668-C67E0BA3-ED09-4470-9DFA-A00545F41D9DQ29994749-ADB05592-724A-474D-923E-2D4F3A73B487Q30480843-1D41A495-9FB8-4EF0-9BE4-0B16FDBADC95Q30989522-4EF299AC-9B81-4C7B-859C-C9E7AE6A448FQ31111749-83F40B74-F4A5-4C92-B7B8-851DE0746FC4Q32034732-0E82F020-3DAC-4D87-BDB8-F7F6442CBF46Q33485236-55C88C46-F9E1-41C7-B518-5BD970FA4543Q33639450-2A4130E0-0584-4055-B6C2-E4A0F5A1DF23Q33750129-F4E7C0A7-6184-4C0D-8DC8-A72E8BC88DB1Q33791646-2F88CDE9-D933-4478-A9FD-8887E4399BD6Q33793293-56EA35C8-6831-4C61-A3F0-9FE43B7A96A6Q33815578-085F5292-C953-425F-8759-4D4F26EDA7DDQ33816311-BCE51102-9D04-4CA2-B9ED-FE70F718042BQ33828966-0E74B5B4-D67D-4DD3-8BC8-9FFD92807B8AQ33859830-4E100E0D-9345-4DD5-A049-DE6D44DE8A1FQ33980306-12A35AD6-65E6-48E4-83A1-D29B97938B09Q34035745-A123953A-34B6-4FF1-8B9D-3B09BBCCC89DQ34112184-FFCD57CC-4EC5-41FF-BEA6-5D2976E9B7E1Q34155383-5A26C2A3-7799-43F4-9ABF-92446F42269CQ34243873-7246C4CF-5C74-427C-A687-A52A47A1A66BQ34283467-EB9AF130-24C4-48BB-B548-1782F7430526
P2860
Alzheimer's disease hyperphosphorylated tau sequesters normal tau into tangles of filaments and disassembles microtubules.
description
1996 nî lūn-bûn
@nan
1996年の論文
@ja
1996年学术文章
@wuu
1996年学术文章
@zh
1996年学术文章
@zh-cn
1996年学术文章
@zh-hans
1996年学术文章
@zh-my
1996年学术文章
@zh-sg
1996年學術文章
@yue
1996年學術文章
@zh-hant
name
Alzheimer's disease hyperphosp ...... and disassembles microtubules.
@en
Alzheimer's disease hyperphosp ...... and disassembles microtubules.
@nl
type
label
Alzheimer's disease hyperphosp ...... and disassembles microtubules.
@en
Alzheimer's disease hyperphosp ...... and disassembles microtubules.
@nl
prefLabel
Alzheimer's disease hyperphosp ...... and disassembles microtubules.
@en
Alzheimer's disease hyperphosp ...... and disassembles microtubules.
@nl
P2093
P356
P1433
P1476
Alzheimer's disease hyperphosp ...... and disassembles microtubules.
@en
P2093
Grundke-Iqbal I
P2888
P304
P356
10.1038/NM0796-783
P407
P577
1996-07-01T00:00:00Z