Structure determination of micelle-like intermediates in amyloid beta -protein fibril assembly by using small angle neutron scattering - Wikidata - wikimedia - TriplyDB

Structure determination of micelle-like intermediates in amyloid beta -protein fibril assembly by using small angle neutron scattering

Structure determination of micelle-like intermediates in amyloid beta -protein fibril assembly by using small angle neutron scattering

http://www.wikidata.org/entity/Q33896874

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Rationally designed turn promoting mutation in the amyloid-β peptide sequence stabilizes oligomers in solution Overview of Alzheimer's Disease and Some Therapeutic Approaches Targeting Aβ by Using Several Synthetic and Herbal Compounds Molecular basis of -amyloid oligomer recognition with a conformational antibody fragment Folding events in the 21-30 region of amyloid beta-protein (Abeta) studied in silico Role of aggregation conditions in structure, stability, and toxicity of intermediates in the Abeta fibril formation pathway Kinetic control of dimer structure formation in amyloid fibrillogenesis Formation and growth of oligomers: a Monte Carlo study of an amyloid tau fragment Structural determination of Abeta25-35 micelles by molecular dynamics simulations.Solvent and mutation effects on the nucleation of amyloid beta-protein folding Early events in insulin fibrillization studied by time-lapse atomic force microscopy.In silico study of amyloid beta-protein folding and oligomerization.Stabilities and conformations of Alzheimer's beta -amyloid peptide oligomers (Abeta 16-22, Abeta 16-35, and Abeta 10-35): Sequence effects.What drives amyloid molecules to assemble into oligomers and fibrils?The molecular basis of distinct aggregation pathways of islet amyloid polypeptide.Crucial role of nonspecific interactions in amyloid nucleation.P3 peptide, a truncated form of A beta devoid of synaptotoxic effect, does not assemble into soluble oligomers.Monomeric Amyloid Beta Peptide in Hexafluoroisopropanol Detected by Small Angle Neutron Scattering NMR characterization of monomeric and oligomeric conformations of human calcitonin and its interaction with EGCG.Mechanisms of protein fibril formation: nucleated polymerization with competing off-pathway aggregation Side-chain dynamics reveals transient association of Aβ(1-40) monomers with amyloid fibers.Hsp20, a novel alpha-crystallin, prevents Abeta fibril formation and toxicity.Urea modulation of beta-amyloid fibril growth: experimental studies and kinetic models.Immunogenicity, efficacy, safety, and mechanism of action of epitope vaccine (Lu AF20513) for Alzheimer's disease: prelude to a clinical trial Structures and free-energy landscapes of the wild type and mutants of the Abeta(21-30) peptide are determined by an interplay between intrapeptide electrostatic and hydrophobic interactions.Self-assembling peptides: from bio-inspired materials to bone regeneration.Amyloid protofibrils of lysozyme nucleate and grow via oligomer fusion.Statistical mechanical treatments of protein amyloid formation.A kinetic model for beta-amyloid adsorption at the air/solution interface and its implication to the beta-amyloid aggregation process.Molecular dynamics simulation of amyloid beta dimer formation.Human beta-synuclein rendered fibrillogenic by designed mutations.Fatty Acid Concentration and Phase Transitions Modulate Aβ Aggregation Pathways.Protein folding, misfolding and aggregation: The importance of two-electron stabilizing interactions.Aβ42 pentamers/hexamers are the smallest detectable oligomers in solution.Kinetics of spontaneous filament nucleation via oligomers: Insights from theory and simulation.Amyloid oligomers and protofibrils, but not filaments, self-replicate from native lysozyme.A statistical-mechanical theory of fibril formation in dilute protein solutions.Oxidation of methionine 35 attenuates formation of amyloid beta -peptide 1-40 oligomers.Expansion of polyglutamine induces the formation of quasi-aggregate in the early stage of protein fibrillization.Human amylin oligomer growth and fibril elongation define two distinct phases in amyloid formation.Elucidation of amyloid beta-protein oligomerization mechanisms: discrete molecular dynamics study.

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P2860

Structure determination of micelle-like intermediates in amyloid beta -protein fibril assembly by using small angle neutron scattering

http://www.wikidata.org/entity/Q33896874

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2001 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած

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2001 թվականի դեկտեմբերին հրատարակված գիտական հոդված

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2001年の論文

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

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Structure determination of mic ...... small angle neutron scattering

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Aleksey Lomakin

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

David B Teplow

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George B Benedek

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

Marina D Kirkitadze

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Sow-Hsin Chen

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Winnie Yong

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P2860

Abeta amyloid fibrils possess a core structure highly resistant to hydrogen exchange

Translating cell biology into therapeutic advances in Alzheimer's disease.

Targeting small Abeta oligomers: the solution to an Alzheimer's disease conundrum?

The Alzheimer family of diseases: many etiologies, one pathogenesis?

Kinetic theory of fibrillogenesis of amyloid beta-protein.

The molecular pathology of Alzheimer's disease.

Temperature dependence of amyloid beta-protein fibrillization.

On the nucleation and growth of amyloid beta-protein fibrils: detection of nuclei and quantitation of rate constants.

Kinetics of the exchange of individual amide protons in the basic pancreatic trypsin inhibitor.

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