The formation of straight and twisted filaments from short tau peptides. - Wikidata - awgldk - TriplyDB

The formation of straight and twisted filaments from short tau peptides.

The formation of straight and twisted filaments from short tau peptides.

http://www.wikidata.org/entity/Q44853344

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Ubiquitous amyloids Mapping the conformational dynamics and pathways of spontaneous steric zipper Peptide oligomerization Structure-based design of non-natural amino-acid inhibitors of amyloid fibril formation Aggregation properties of a short peptide that mediates amyloid fibril formation in model proteins unrelated to disease.Synthesis and structural investigations of N-alkylated beta-peptidosulfonamide-peptide hybrids of the amyloidogenic amylin(20-29) sequence: Implications of supramolecular folding for the design of peptide-based bionanomaterials.Formation and growth of oligomers: a Monte Carlo study of an amyloid tau fragment Quantitative characterization of heparin binding to Tau protein: implication for inducer-mediated Tau filament formation.Impact on the replacement of Phe by Trp in a short fragment of Aβ amyloid peptide on the formation of fibrils.Identification of O-GlcNAc sites within peptides of the Tau protein and their impact on phosphorylation.X-ray diffraction from intact tau aggregates in human brain tissue 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 Development of a grape seed polyphenolic extract with anti-oligomeric activity as a novel treatment in progressive supranuclear palsy and other tauopathies Linker-determined drug release mechanism of free camptothecin from self-assembling drug amphiphiles.Interactions between amyloid-β and Tau fragments promote aberrant aggregates: implications for amyloid toxicity Structure of core domain of fibril-forming PHF/Tau fragments.Macrocyclic β-sheet peptides that inhibit the aggregation of a tau-protein-derived hexapeptide.Interactions between Aβ and mutated Tau lead to polymorphism and induce aggregation of Aβ-mutated tau oligomeric complexes Synergistic interactions between repeats in tau protein and Aβ amyloids may be responsible for accelerated aggregation via polymorphic states.Systematic examination of polymorphism in amyloid fibrils by molecular-dynamics simulation.Tau assembly: the dominant role of PHF6 (VQIVYK) in microtubule binding region repeat R3.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.Selection and Characterization of Tau Binding ᴅ-Enantiomeric Peptides with Potential for Therapy of Alzheimer Disease.Tau Aggregation Propensity Engrained in Its Solution State.Influence of temperature on formation of perfect tau fragment fibrils using PRIME20/DMD simulations Building Nanostructures with Drugs.Structural principles of tau and the paired helical filaments of Alzheimer's disease.Initiation of assembly of tau(273-284) and its ΔK280 mutant: an experimental and computational study.Role of grape seed polyphenols in Alzheimer's disease neuropathology.Self-assembly of giant peptide nanobelts Quick shear-flow alignment of biological filaments for X-ray fiber diffraction facilitated by methylcellulose Self-assembly of natural and synthetic drug amphiphiles into discrete supramolecular nanostructures.Polyphenolic compounds for treating neurodegenerative disorders involving protein misfolding.Therapeutic Strategies for Restoring Tau Homeostasis.Supramolecular nanostructures formed by anticancer drug assembly.Difficulties associated with the structural analysis of proteins susceptible to form aggregates: The case of Tau protein as a biomarker of Alzheimer's disease.Amyloidogenic sequences in native protein structures.Tau-derived-hexapeptide 306VQIVYK311 aggregation inhibitors: nitrocatechol moiety as a pharmacophore in drug design Tau protein assembles into isoform- and disulfide-dependent polymorphic fibrils with distinct structural properties.

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P2860

The formation of straight and twisted filaments from short tau peptides.

http://www.wikidata.org/entity/Q44853344

description

2004 nî lūn-bûn

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2004年の論文

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2004年学术文章

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2004年学术文章

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2004年学术文章

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2004年学术文章

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2004年学术文章

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2004年学术文章

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2004年學術文章

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2004年學術文章

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name

The formation of straight and twisted filaments from short tau peptides.

@en

The formation of straight and twisted filaments from short tau peptides.

@nl

type

label

The formation of straight and twisted filaments from short tau peptides.

@en

The formation of straight and twisted filaments from short tau peptides.

@nl

prefLabel

The formation of straight and twisted filaments from short tau peptides.

@en

The formation of straight and twisted filaments from short tau peptides.

@nl

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P1433

Journal of Biological Chemistry

P1476

The formation of straight and twisted filaments from short tau peptides.

@en

P2093

Anh D Nguyen

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

Daniel A Kirschner

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

Deepak Sharma

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

Hideyo Inouye

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

Kathryn Leak

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

Lauren Kopplin

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

Marni Rutkofsky

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

Vasanthi D Shanmuganandam

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

Warren J Goux

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

P2860

Cloning and sequencing of the cDNA encoding a core protein of the paired helical filament of Alzheimer disease: identification as the microtubule-associated protein tau

Familial multiple system tauopathy with presenile dementia: a disease with abundant neuronal and glial tau filaments

Calculation of protein extinction coefficients from amino acid sequence data

Phosphorylation that detaches tau protein from microtubules (Ser262, Ser214) also protects it against aggregation into Alzheimer paired helical filaments

Spectroscopic determination of tryptophan and tyrosine in proteins

Estimation of protein secondary structure from circular dichroism spectra: comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set

Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases

Abnormal phosphorylation of the microtubule-associated protein tau (tau) in Alzheimer cytoskeletal pathology

Dependence on solution conditions of aggregation and amyloid formation by an SH3 domain.

De novo amyloid proteins from designed combinatorial libraries

P304

26868-26875

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scholarly article

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10.1074/JBC.M402379200

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26

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279

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15100221

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