Rapid assembly of Alzheimer-like paired helical filaments from microtubule-associated protein tau monitored by fluorescence in solution.
about
Selective interaction of lansoprazole and astemizole with tau polymers: potential new clinical use in diagnosis of Alzheimer's diseaseNMR Meets Tau: Insights into Its Function and PathologyRescue from tau-induced neuronal dysfunction produces insoluble tau oligomersThe physiological link between metabolic rate depression and tau phosphorylation in mammalian hibernationStructural basis for recognition of the RNA major groove in the tau exon 10 splicing regulatory element by aminoglycoside antibiotics.Crystal Structure of Thioflavin T Bound to the Peripheral Site of Torpedo californica Acetylcholinesterase Reveals How Thioflavin T Acts as a Sensitive Fluorescent Reporter of Ligand Binding to the Acylation SiteStructure-based design of non-natural amino-acid inhibitors of amyloid fibril formationThe fluorescent Congo red derivative, (trans, trans)-1-bromo-2,5-bis-(3-hydroxycarbonyl-4-hydroxy)styrylbenzene (BSB), labels diverse beta-pleated sheet structures in postmortem human neurodegenerative disease brainsBinding mode of Thioflavin T and other molecular probes in the context of amyloid fibrils-current statusA computational approach for identifying the chemical factors involved in the glycosaminoglycans-mediated acceleration of amyloid fibril formationIdentification of Small Molecule Inhibitors of Tau Aggregation by Targeting Monomeric Tau As a Potential Therapeutic Approach for TauopathiesFunctional anthology of intrinsic disorder. 3. Ligands, post-translational modifications, and diseases associated with intrinsically disordered proteins.Nucleation-dependent tau filament formation: the importance of dimerization and an estimation of elementary rate constantsPseudophosphorylation and glycation of tau protein enhance but do not trigger fibrillization in vitro.Anthraquinones inhibit tau aggregation and dissolve Alzheimer's paired helical filaments in vitro and in cells.Different associational and conformational behaviors between the second and third repeat fragments in the tau microtubule-binding domain.Differentiating Alzheimer disease-associated aggregates with small molecules.Evolution of amyloid: what normal protein folding may tell us about fibrillogenesis and disease.A nucleated assembly mechanism of Alzheimer paired helical filaments.Quantitative characterization of heparin binding to Tau protein: implication for inducer-mediated Tau filament formation.Tau pathology generated by overexpression of tau.The role of the lipid bilayer in tau aggregationEntropically driven self-assembly of multichannel rosette nanotubes.Inhibition of heparin-induced tau filament formation by phenothiazines, polyphenols, and porphyrins.Pseudophosphorylation of tau protein directly modulates its aggregation kinetics.Macrocyclic β-sheet peptides that inhibit the aggregation of a tau-protein-derived hexapeptide.Oligomer formation of tau protein hyperphosphorylated in cells.PE859, a novel tau aggregation inhibitor, reduces aggregated tau and prevents onset and progression of neural dysfunction in vivo.Induced pluripotent stem cell-derived neuronal cells from a sporadic Alzheimer's disease donor as a model for investigating AD-associated gene regulatory networks.Functional genomic screen and network analysis reveal novel modifiers of tauopathy dissociated from tau phosphorylation.Pseudohyperphosphorylation has differential effects on polymerization and function of tau isoforms.Understanding the kinetic roles of the inducer heparin and of rod-like protofibrils during amyloid fibril formation by Tau proteinSecondary nucleating sequences affect kinetics and thermodynamics of tau aggregation.Amyloid properties of the mouse egg zona pellucida14-3-3ζ Mediates Tau Aggregation in Human Neuroblastoma M17 Cells.The role of secondary structure in the entropically driven amelogenin self-assembly.Selection and Characterization of Tau Binding ᴅ-Enantiomeric Peptides with Potential for Therapy of Alzheimer Disease.Identification of an aggregation-prone structure of tau.Ligand electronic properties modulate tau filament binding site densityTaxol-stabilized microtubules promote the formation of filaments from unmodified full-length Tau in vitro.
P2860
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P2860
Rapid assembly of Alzheimer-like paired helical filaments from microtubule-associated protein tau monitored by fluorescence in solution.
description
1998 nî lūn-bûn
@nan
1998年の論文
@ja
1998年学术文章
@wuu
1998年学术文章
@zh-cn
1998年学术文章
@zh-hans
1998年学术文章
@zh-my
1998年学术文章
@zh-sg
1998年學術文章
@yue
1998年學術文章
@zh
1998年學術文章
@zh-hant
name
Rapid assembly of Alzheimer-li ...... d by fluorescence in solution.
@en
Rapid assembly of Alzheimer-li ...... d by fluorescence in solution.
@nl
type
label
Rapid assembly of Alzheimer-li ...... d by fluorescence in solution.
@en
Rapid assembly of Alzheimer-li ...... d by fluorescence in solution.
@nl
prefLabel
Rapid assembly of Alzheimer-li ...... d by fluorescence in solution.
@en
Rapid assembly of Alzheimer-li ...... d by fluorescence in solution.
@nl
P2093
P356
P1433
P1476
Rapid assembly of Alzheimer-li ...... d by fluorescence in solution.
@en
P2093
Friedhoff P
Mandelkow E
Schneider A
P304
10223-10230
P356
10.1021/BI980537D
P407
P577
1998-07-01T00:00:00Z