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Two-Step Amyloid Aggregation: Sequential Lag Phase IntermediatesN-Terminal Extensions Retard Aβ42 Fibril Formation but Allow Cross-Seeding and Coaggregation with Aβ42Nanoscale Control of Amyloid Self-Assembly Using Protein Phase Transfer by Host-Guest ChemistryControlling amyloid fibril formation by partial stirring.Co-fibrillogenesis of Wild-type and D76N β2-Microglobulin: THE CRUCIAL ROLE OF FIBRILLAR SEEDS.The LC Domain of hnRNPA2 Adopts Similar Conformations in Hydrogel Polymers, Liquid-like Droplets, and Nuclei.Recruitment of Light Chains by Homologous and Heterologous Fibrils Shows Distinctive Kinetic and Conformational Specificity.Strain-specific Fibril Propagation by an Aβ Dodecamer.Direct High Affinity Interaction between Aβ42 and GSK3α Stimulates Hyperphosphorylation of Tau. A New Molecular Link in Alzheimer's Disease?Growth-incompetent monomers of human calcitonin lead to a non-canonical direct relationship between peptide concentration and lag time.Nucleation and growth of a bacterial functional amyloid at single-fiber resolution.Sodium louroyl sarcosinate (sarkosyl) modulate amyloid fibril formation in hen egg white lysozyme (HEWL) at alkaline pH: a molecular insight study.The activities of amyloids from a structural perspective.Differences in Protein Concentration Dependence for Nucleation and Elongation in Light Chain Amyloid Formation.Prion-Like Characteristics of Polyglutamine-Containing Proteins.Protein aggregation, misfolding and consequential human neurodegenerative diseases.Self-assembling peptide and protein amyloids: from structure to tailored function in nanotechnology.Molecular interactions of amyloid nanofibrils with biological aggregation modifiers: implications for cytotoxicity mechanisms and biomaterial design.Implications of peptide assemblies in amyloid diseases.The interplay of aggregation, fibrillization and gelation of an unexpected low molecular weight gelator: glycylalanylglycine in ethanol/water.Glycerol inhibits the primary pathways and transforms the secondary pathway of insulin aggregation.Kinetic analysis reveals the diversity of microscopic mechanisms through which molecular chaperones suppress amyloid formationMonomer-dependent secondary nucleation in amyloid formation.Fatty Acid Concentration and Phase Transitions Modulate Aβ Aggregation Pathways.Probing amylin fibrillation at an early stage via a tetracysteine-recognising fluorophore.Pyroglutamate-modified Aβ(3-42) affects aggregation kinetics of Aβ(1-42) by accelerating primary and secondary pathways.Secondary nucleation of monomers on fibril surface dominates α-synuclein aggregation and provides autocatalytic amyloid amplification.Factors affecting the physical stability (aggregation) of peptide therapeutics.A Free Energy Barrier Caused by the Refolding of an Oligomeric Intermediate Controls the Lag Time of Amyloid Formation by hIAPP.Cellular prion protein targets amyloid-β fibril ends via its C-terminal domain to prevent elongation.Estimation of the lag time in a subsequent monomer addition model for fibril elongation.Doliroside A from Dolichos falcata Klein suppressing amyloid β-protein 42 fibrillogenesis: An insight at molecular level.Real-Time Observation of the Interaction between Thioflavin T and an Amyloid Protein by Using High-Sensitivity Rheo-NMR.Aggregate Size-Dependence of Amyloid Adsorption onto Charged Interfaces.Recent progress on understanding the mechanisms of amyloid nucleation.The Unexpected Role of Aβ1-42 Monomers in the Pathogenesis of Alzheimer's Disease.Electrostatic lipid-protein interactions sequester the curli amyloid fold on the lipopolysaccharide membrane surface.Modification of C Terminus Provides New Insights into the Mechanism of α-Synuclein Aggregation.Biophysical Aspects of Alzheimer's Disease: Implications for Pharmaceutical Sciences : Theme: Drug Discovery, Development and Delivery in Alzheimer's Disease Guest Editor: Davide Brambilla.Fluorescent Probe DCVJ Shows High Sensitivity for Characterization of Amyloid β-Peptide Early in the Lag Phase.
P2860
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P2860
description
2015 nî lūn-bûn
@nan
2015年の論文
@ja
2015年論文
@yue
2015年論文
@zh-hant
2015年論文
@zh-hk
2015年論文
@zh-mo
2015年論文
@zh-tw
2015年论文
@wuu
2015年论文
@zh
2015年论文
@zh-cn
name
On the lag phase in amyloid fibril formation.
@en
type
label
On the lag phase in amyloid fibril formation.
@en
prefLabel
On the lag phase in amyloid fibril formation.
@en
P2860
P356
P1476
On the lag phase in amyloid fibril formation.
@en
P2093
Paolo Arosio
Tuomas P J Knowles
P2860
P304
P356
10.1039/C4CP05563B
P407
P577
2015-03-01T00:00:00Z
2015-03-28T00:00:00Z