Crucial role of nonspecific interactions in amyloid nucleation.
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Two-Step Amyloid Aggregation: Sequential Lag Phase IntermediatesAn Atomistic View of Amyloidogenic Self-assembly: Structure and Dynamics of Heterogeneous Conformational States in the Pre-nucleation Phase.Oligomers of Heat-Shock Proteins: Structures That Don't Imply Function.Determination of critical nucleation number for a single nucleation amyloid-β aggregation model.A minimal conformational switching-dependent model for amyloid self-assembly.Quantitative computational models of molecular self-assembly in systems biology.An Account of Amyloid Oligomers: Facts and Figures Obtained from Experiments and Simulations.Glycation induces conformational changes in the amyloid-β peptide and enhances its aggregation propensity: molecular insights.Self-assembling peptide and protein amyloids: from structure to tailored function in nanotechnology.Fatty Acid Concentration and Phase Transitions Modulate Aβ Aggregation Pathways.Kinetics of spontaneous filament nucleation via oligomers: Insights from theory and simulation.Scaling behaviour and rate-determining steps in filamentous self-assembly.Hydrodynamic effects on β-amyloid (16-22) peptide aggregation.Thermodynamics of amyloid formation and the role of intersheet interactions.A specific form of prefibrillar aggregates that functions as a precursor of amyloid nucleation.Recent progress on understanding the mechanisms of amyloid nucleation.The Levinthal Problem in Amyloid Aggregation: Sampling of a Flat Reaction Space.An adaptive bias - hybrid MD/kMC algorithm for protein folding and aggregation.Direct observation of oligomerization by single molecule fluorescence reveals a multi-step aggregation mechanism for the yeast prion protein Ure2.The attachment of α-synuclein to a fiber: A coarse-grain approach.Mechanisms and rates of nucleation of amyloid fibrils.Dynamics of the conformational transitions during the dimerization of an intrinsically disordered peptide: a case study on the human islet amyloid polypeptide fragment.Amyloid and the origin of life: self-replicating catalytic amyloids as prebiotic informational and protometabolic entities.Physical determinants of the self-replication of protein fibrilsScaling and dimensionality in the chemical kinetics of protein filament formation
P2860
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P2860
Crucial role of nonspecific interactions in amyloid nucleation.
description
2014 nî lūn-bûn
@nan
2014 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2014 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
2014年の論文
@ja
2014年論文
@yue
2014年論文
@zh-hant
2014年論文
@zh-hk
2014年論文
@zh-mo
2014年論文
@zh-tw
2014年论文
@wuu
name
Crucial role of nonspecific interactions in amyloid nucleation.
@ast
Crucial role of nonspecific interactions in amyloid nucleation.
@en
Crucial role of nonspecific interactions in amyloid nucleation.
@nl
type
label
Crucial role of nonspecific interactions in amyloid nucleation.
@ast
Crucial role of nonspecific interactions in amyloid nucleation.
@en
Crucial role of nonspecific interactions in amyloid nucleation.
@nl
prefLabel
Crucial role of nonspecific interactions in amyloid nucleation.
@ast
Crucial role of nonspecific interactions in amyloid nucleation.
@en
Crucial role of nonspecific interactions in amyloid nucleation.
@nl
P2860
P50
P356
P1476
Crucial role of nonspecific interactions in amyloid nucleation
@en
P2093
Tuomas P J Knowles
P2860
P304
17869-17874
P356
10.1073/PNAS.1410159111
P407
P577
2014-12-01T00:00:00Z