Triggers of full-length tau aggregation: a role for partially folded intermediates.
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Tau Oligomers: The Toxic Player at Synapses in Alzheimer's DiseaseTangles, Toxicity, and Tau Secretion in AD - New Approaches to a Vexing ProblemNucleation-dependent tau filament formation: the importance of dimerization and an estimation of elementary rate constantsAmyloid-like aggregates of neuronal tau induced by formaldehyde promote apoptosis of neuronal cellsPotency of a tau fibrillization inhibitor is influenced by its aggregation stateDifferentiating Alzheimer disease-associated aggregates with small molecules.Model discrimination and mechanistic interpretation of kinetic data in protein aggregation studies.Quantitative characterization of heparin binding to Tau protein: implication for inducer-mediated Tau filament formation.Characterization of tau fibrillization in vitro.In silico theoretical molecular modeling for Alzheimer's disease: the nicotine-curcumin paradigm in neuroprotection and neurotherapy.The role of the lipid bilayer in tau aggregationFibrillization of human tau is accelerated by exposure to lead via interaction with His-330 and His-362.Pseudophosphorylation of tau protein directly modulates its aggregation kinetics.Lysine methylation is an endogenous post-translational modification of tau protein in human brain and a modulator of aggregation propensity.Characterization of prefibrillar Tau oligomers in vitro and in Alzheimer disease.Calpain-mediated tau cleavage: a mechanism leading to neurodegeneration shared by multiple tauopathiesUnderstanding the kinetic roles of the inducer heparin and of rod-like protofibrils during amyloid fibril formation by Tau proteinInteraction of tau protein with model lipid membranes induces tau structural compaction and membrane disruption.Fiber-dependent amyloid formation as catalysis of an existing reaction pathway.Tau isoform composition influences rate and extent of filament formationTargeting intrinsically disordered proteins in neurodegenerative and protein dysfunction diseases: another illustration of the D(2) concept.Evidence for a role of the rare p.A152T variant in MAPT in increasing the risk for FTD-spectrum and Alzheimer's diseases.Potent inhibition of tau fibrillization with a multivalent ligand.Identification of an aggregation-prone structure of tau.Detection and quantification of tau aggregation using a membrane filter assay.Pathogenic missense MAPT mutations differentially modulate tau aggregation propensity at nucleation and extension steps.Modulation and detection of tau aggregation with small-molecule ligandsAmyloidogenesis of natively unfolded proteins.Accelerated neurodegeneration through chaperone-mediated oligomerization of tau.Tau aggregation and toxicity in tauopathic neurodegenerative diseases.Inhibition of tau polymerization with a cyanine dye in two distinct model systemsRole of metal ions in aggregation of intrinsically disordered proteins in neurodegenerative diseases.Biochemistry and cell biology of tau protein in neurofibrillary degenerationInteractions between Microtubule-Associated Protein Tau (MAPT) and Small Molecules.Tau aggregation and toxicity in a cell culture model of tauopathy.Difficulties associated with the structural analysis of proteins susceptible to form aggregates: The case of Tau protein as a biomarker of Alzheimer's disease.Hsp70 alters tau function and aggregation in an isoform specific mannerFormation and propagation of tau oligomeric seeds.Signature of an aggregation-prone conformation of tau.Are tau aggregates toxic or protective in tauopathies?
P2860
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P2860
Triggers of full-length tau aggregation: a role for partially folded intermediates.
description
2005 nî lūn-bûn
@nan
2005年の論文
@ja
2005年学术文章
@wuu
2005年学术文章
@zh
2005年学术文章
@zh-cn
2005年学术文章
@zh-hans
2005年学术文章
@zh-my
2005年学术文章
@zh-sg
2005年學術文章
@yue
2005年學術文章
@zh-hant
name
Triggers of full-length tau aggregation: a role for partially folded intermediates.
@en
Triggers of full-length tau aggregation: a role for partially folded intermediates.
@nl
type
label
Triggers of full-length tau aggregation: a role for partially folded intermediates.
@en
Triggers of full-length tau aggregation: a role for partially folded intermediates.
@nl
prefLabel
Triggers of full-length tau aggregation: a role for partially folded intermediates.
@en
Triggers of full-length tau aggregation: a role for partially folded intermediates.
@nl
P2093
P356
P1433
P1476
Triggers of full-length tau aggregation: a role for partially folded intermediates
@en
P2093
Carmen N Chirita
Haishan Yin
Jeff Kuret
P304
P356
10.1021/BI0500123
P407
P577
2005-04-01T00:00:00Z