A nucleated assembly mechanism of Alzheimer paired helical filaments. - Wikidata - awgldk - TriplyDB

A nucleated assembly mechanism of Alzheimer paired helical filaments.

A nucleated assembly mechanism of Alzheimer paired helical filaments.

http://www.wikidata.org/entity/Q33608410

about

Hyperphosphorylation induces self-assembly of tau into tangles of paired helical filaments/straight filaments Paired helical filaments from Alzheimer disease brain induce intracellular accumulation of Tau protein in aggresomes Structure-based design of non-natural amino-acid inhibitors of amyloid fibril formation Amyloid β-sheet mimics that antagonize protein aggregation and reduce amyloid toxicity Identification of Small Molecule Inhibitors of Tau Aggregation by Targeting Monomeric Tau As a Potential Therapeutic Approach for Tauopathies Alzheimer disease: a tale of two prions Nucleation-dependent tau filament formation: the importance of dimerization and an estimation of elementary rate constants Caspase-cleavage of tau is an early event in Alzheimer disease tangle pathology Pseudophosphorylation 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.Quantitative characterization of heparin binding to Tau protein: implication for inducer-mediated Tau filament formation.Characterization of tau fibrillization in vitro.Fibrillogenesis of tau: insights from tau missense mutations in FTDP-17.The role of the lipid bilayer in tau aggregation Fibrillization of human tau is accelerated by exposure to lead via interaction with His-330 and His-362.Human Tau isoforms assemble into ribbon-like fibrils that display polymorphic structure and stability.Structural Insight into Tau Protein's Paradox of Intrinsically Disordered Behavior, Self-Acetylation Activity, and Aggregation Frequent and symmetric deposition of misfolded tau oligomers within presynaptic and postsynaptic terminals in Alzheimer's disease.Pseudophosphorylation of tau protein directly modulates its aggregation kinetics.Seeding of normal Tau by pathological Tau conformers drives pathogenesis of Alzheimer-like tangles.Structure and mechanism of action of tau aggregation inhibitors.Protein disulfide isomerase interacts with tau protein and inhibits its fibrillization.Characterization of prefibrillar Tau oligomers in vitro and in Alzheimer disease.Understanding the kinetic roles of the inducer heparin and of rod-like protofibrils during amyloid fibril formation by Tau protein Secondary nucleating sequences affect kinetics and thermodynamics of tau aggregation.Stepwise proteolysis liberates tau fragments that nucleate the Alzheimer-like aggregation of full-length tau in a neuronal cell model.Conformational basis for asymmetric seeding barrier in filaments of three- and four-repeat tau.The role of caspase cleavage of tau in Alzheimer disease neuropathology.Fourier Transform Infrared (FTIR) Spectroscopy, Ultraviolet Resonance Raman (UVRR) Spectroscopy, and Atomic Force Microscopy (AFM) for Study of the Kinetics of Formation and Structural Characterization of Tau Fibrils.Selection and Characterization of Tau Binding ᴅ-Enantiomeric Peptides with Potential for Therapy of Alzheimer Disease.Cu(II) organizes beta-2-microglobulin oligomers but is released upon amyloid formation.Template-assisted filament growth by parallel stacking of tau.Remodeling of the conformational ensemble of the repeat domain of tau by an aggregation enhancer.EFhd2 is a novel amyloid protein associated with pathological tau in Alzheimer's disease.Assembly of tau protein into Alzheimer paired helical filaments depends on a local sequence motif ((306)VQIVYK(311)) forming beta structure.Histopathological and molecular heterogeneity among individuals with dementia associated with Presenilin mutations Aggregated, wild-type prion protein causes neurological dysfunction and synaptic abnormalities.Electrochemical investigations into kinase-catalyzed transformations of tau protein.Unique pathological tau conformers from Alzheimer's brains transmit tau pathology in nontransgenic mice.

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P2860

A nucleated assembly mechanism of Alzheimer paired helical filaments.

http://www.wikidata.org/entity/Q33608410

description

1998 nî lūn-bûn

@nan

1998 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած

@hyw

1998 թվականի դեկտեմբերին հրատարակված գիտական հոդված

@hy

1998年の論文

@ja

1998年論文

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1998年論文

@zh-hant

1998年論文

@zh-hk

1998年論文

@zh-mo

1998年論文

@zh-tw

1998年论文

@wuu

name

A nucleated assembly mechanism of Alzheimer paired helical filaments.

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A nucleated assembly mechanism of Alzheimer paired helical filaments.

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type

label

A nucleated assembly mechanism of Alzheimer paired helical filaments.

@ast

A nucleated assembly mechanism of Alzheimer paired helical filaments.

@en

prefLabel

A nucleated assembly mechanism of Alzheimer paired helical filaments.

@ast

A nucleated assembly mechanism of Alzheimer paired helical filaments.

@en

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P1433

Proceedings of the National Academy of Sciences of the United States of America

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A nucleated assembly mechanism of Alzheimer paired helical filaments.

@en

P2093

Davies P

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

Friedhoff P

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Mandelkow E

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von Bergen M

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P2860

Prion Protein Biology

Cloning and sequencing of the cDNA encoding an isoform of microtubule-associated protein tau containing four tandem repeats: differential expression of tau protein mRNAs in human brain

Neuropathological stageing of Alzheimer-related changes

The carboxy terminus of the beta amyloid protein is critical for the seeding of amyloid formation: implications for the pathogenesis of Alzheimer's disease

Structural studies of tau protein and Alzheimer paired helical filaments show no evidence for beta-structure

Neurofibrillary tangles but not senile plaques parallel duration and severity of Alzheimer's disease

Isolation of a fragment of tau derived from the core of the paired helical filament of Alzheimer disease.

The switch of tau protein to an Alzheimer-like state includes the phosphorylation of two serine-proline motifs upstream of the microtubule binding region

Oxidation of cysteine-322 in the repeat domain of microtubule-associated protein tau controls the in vitro assembly of paired helical filaments

Purification of tau, a microtubule-associated protein that induces assembly of microtubules from purified tubulin.

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15712-15717

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scholarly article

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10.1073/PNAS.95.26.15712

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26

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95

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Eva-Maria Mandelkow

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1998-12-01T00:00:00Z

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13426850

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9861035

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P921

Alzheimer's disease

P932

28109

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