Conformational changes specific for pseudophosphorylation at serine 262 selectively impair binding of tau to microtubules.
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Constructing ensembles for intrinsically disordered proteinsThe Metamorphic Nature of the Tau Protein: Dynamic Flexibility Comes at a CostTangles, Toxicity, and Tau Secretion in AD - New Approaches to a Vexing ProblemShort and Long Term Behavioral and Pathological Changes in a Novel Rodent Model of Repetitive Mild Traumatic Brain InjuryTau physiology and pathomechanisms in frontotemporal lobar degenerationRapid changes in phospho-MAP/tau epitopes during neuronal stress: cofilin-actin rods primarily recruit microtubule binding domain epitopesProteasome inhibition drives HDAC6-dependent recruitment of tau to aggresomes.The role of hippocampal tau protein phosphorylation in isoflurane-induced cognitive dysfunction in transgenic APP695 mice.Tau mutants bind tubulin heterodimers with enhanced affinity.Microarray analysis of CA1 pyramidal neurons in a mouse model of tauopathy reveals progressive synaptic dysfunction.Causes versus effects: the increasing complexities of Alzheimer's disease pathogenesis.The role of tau kinases in Alzheimer's disease.Phosphorylation of tau at Thr212, Thr231, and Ser262 combined causes neurodegenerationExpanding the proteome: disordered and alternatively folded proteins.The diarylheptanoid (+)-aR,11S-myricanol and two flavones from bayberry (Myrica cerifera) destabilize the microtubule-associated protein tau.The toxicity of tau in Alzheimer disease: turnover, targets and potential therapeuticsTau phosphorylation at serine 396 residue is required for hippocampal LTDNon-aggregating tau phosphorylation by cyclin-dependent kinase 5 contributes to motor neuron degeneration in spinal muscular atrophy.Pseudohyperphosphorylation has differential effects on polymerization and function of tau isoforms.The many faces of tauStabilization 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.Glycogen synthase kinase 3: a point of integration in Alzheimer's disease and a therapeutic target?AMP-activated protein kinase modulates tau phosphorylation and tau pathology in vivo.The microtubule-associated tau protein has intrinsic acetyltransferase activity.Emerging roles of sumoylation in the regulation of actin, microtubules, intermediate filaments, and septinsTau protein modifications and interactions: their role in function and dysfunction.Protein phosphorylation in neurodegeneration: friend or foe?AMPK in Neurodegenerative Diseases.The Role of Microglia in the Etiology and Evolution of Chronic Traumatic Encephalopathy.Protein Phosphorylation is a Key Mechanism in Alzheimer's Disease.Microtubule affinity-regulating kinases are potential druggable targets for Alzheimer's disease.Accumulation of vesicle-associated human tau in distal dendrites drives degeneration and tau secretion in an in situ cellular tauopathy model.Truncated tau deregulates synaptic markers in rat model for human tauopathy.Pseudo-acetylation of multiple sites on human Tau proteins alters Tau phosphorylation and microtubule binding, and ameliorates amyloid beta toxicityStages and conformations of the Tau repeat domain during aggregation and its effect on neuronal toxicityAmyloid Beta and tau proteins as therapeutic targets for Alzheimer's disease treatment: rethinking the current strategy.Modeling intrinsically disordered proteins with bayesian statistics.Alternative conformations of the Tau repeat domain in complex with an engineered binding protein.Multiple mechanisms of extracellular tau spreading in a non-transgenic tauopathy model.Tau phosphorylation at Alzheimer's disease-related Ser356 contributes to tau stabilization when PAR-1/MARK activity is elevated.
P2860
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P2860
Conformational changes specific for pseudophosphorylation at serine 262 selectively impair binding of tau to microtubules.
description
2009 nî lūn-bûn
@nan
2009年の論文
@ja
2009年学术文章
@wuu
2009年学术文章
@zh
2009年学术文章
@zh-cn
2009年学术文章
@zh-hans
2009年学术文章
@zh-my
2009年学术文章
@zh-sg
2009年學術文章
@yue
2009年學術文章
@zh-hant
name
Conformational changes specifi ...... inding of tau to microtubules.
@en
Conformational changes specifi ...... inding of tau to microtubules.
@nl
type
label
Conformational changes specifi ...... inding of tau to microtubules.
@en
Conformational changes specifi ...... inding of tau to microtubules.
@nl
prefLabel
Conformational changes specifi ...... inding of tau to microtubules.
@en
Conformational changes specifi ...... inding of tau to microtubules.
@nl
P2093
P356
P1433
P1476
Conformational changes specifi ...... inding of tau to microtubules.
@en
P2093
Christian Griesinger
Daniela Fischer
Jacek Biernat
Marco D Mukrasch
Martin Blackledge
Stefan Bibow
P304
10047-10055
P356
10.1021/BI901090M
P407
P577
2009-10-01T00:00:00Z