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An analytical solution to the kinetics of breakable filament assembly.

An analytical solution to the kinetics of breakable filament assembly.

http://www.wikidata.org/entity/Q34087905

about

Mechanisms of amyloid formation revealed by solution NMR Prion-like polymerization as a signaling mechanism Fragmentation and Coagulation in Supramolecular (Co)polymerization Kinetics Atomic structure and hierarchical assembly of a cross- amyloid fibril Protective hinge in insulin opens to enable its receptor engagement Interaction of the molecular chaperone DNAJB6 with growing amyloid-beta 42 (Aβ42) aggregates leads to sub-stoichiometric inhibition of amyloid formation A multiscale approach to characterize the early aggregation steps of the amyloid-forming peptide GNNQQNY from the yeast prion sup-35 Biochemical properties of highly neuroinvasive prion strains Mechanistic insight into the relationship between N-terminal acetylation of α-synuclein and fibril formation rates by NMR and fluorescence β2-Microglobulin amyloid fibril-induced membrane disruption is enhanced by endosomal lipids and acidic pH Porcine prion protein amyloid The extracellular chaperone clusterin sequesters oligomeric forms of the amyloid-β(1-40) peptide Two-Step Amyloid Aggregation: Sequential Lag Phase Intermediates Mapping the structure of amyloid nucleation precursors by protein engineering kinetic analysis.Modulation of the stability of amyloidogenic precursors by anion binding strongly influences the rate of amyloid nucleation.Early amyloidogenic oligomerization studied through fluorescence lifetime correlation spectroscopy.The binding of apolipoprotein E to oligomers and fibrils of amyloid-β alters the kinetics of amyloid aggregation.Truncation of a β-barrel scaffold dissociates intrinsic stability from its propensity to aggregation.Enhanced Fibril Fragmentation of N-Terminally Truncated and Pyroglutamyl-Modified Aβ Peptides.Enzymatically Active Microgels from Self-Assembling Protein Nanofibrils for Microflow Chemistry Lattice model for amyloid peptides: OPEP force field parametrization and applications to the nucleus size of Alzheimer's peptides.Observation of spatial propagation of amyloid assembly from single nuclei Mechanistic and environmental control of the prevalence and lifetime of amyloid oligomers Increased in vivo amyloid-β42 production, exchange, and loss in presenilin mutation carriers The Dynamics and Turnover of Tau Aggregates in Cultured Cells: INSIGHTS INTO THERAPIES FOR TAUOPATHIES.Dynamics of protein aggregation and oligomer formation governed by secondary nucleation.Structural basis for the dissociation of α-synuclein fibrils triggered by pressure perturbation of the hydrophobic core.Biophysical underpinnings of the repeat length dependence of polyglutamine amyloid formation Solution conditions determine the relative importance of nucleation and growth processes in α-synuclein aggregation Controlling the growth and shape of chiral supramolecular polymers in water.Differences in nucleation behavior underlie the contrasting aggregation kinetics of the Aβ40 and Aβ42 peptides Amyloid β Protein and Alzheimer's Disease: When Computer Simulations Complement Experimental Studies.Nanoscale Control of Amyloid Self-Assembly Using Protein Phase Transfer by Host-Guest Chemistry Evaluating nuclei concentration in amyloid fibrillation reactions using back-calculation approach.Sulfate anion delays the self-assembly of human insulin by modifying the aggregation pathway.Kinetics of amyloid beta monomer-to-oligomer exchange by NMR relaxation.Probing small molecule binding to amyloid fibrils.A yeast toxic mutant of HET-s((218-289)) prion displays alternative intermediates of amyloidogenesis Stabilization of neurotoxic Alzheimer amyloid-beta oligomers by protein engineering Sensitivity of amyloid formation by human islet amyloid polypeptide to mutations at residue 20

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P2860

An analytical solution to the kinetics of breakable filament assembly.

http://www.wikidata.org/entity/Q34087905

description

2009 nî lūn-bûn

@nan

2009 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2009 թվականի դեկտեմբերին հրատարակված գիտական հոդված

@hy

2009年の論文

@ja

2009年論文

@yue

2009年論文

@zh-hant

2009年論文

@zh-hk

2009年論文

@zh-mo

2009年論文

@zh-tw

2009年论文

@wuu

name

An analytical solution to the kinetics of breakable filament assembly.

@ast

An analytical solution to the kinetics of breakable filament assembly.

@en

An analytical solution to the kinetics of breakable filament assembly.

@nl

type

label

An analytical solution to the kinetics of breakable filament assembly.

@ast

An analytical solution to the kinetics of breakable filament assembly.

@en

An analytical solution to the kinetics of breakable filament assembly.

@nl

prefLabel

An analytical solution to the kinetics of breakable filament assembly.

@ast

An analytical solution to the kinetics of breakable filament assembly.

@en

An analytical solution to the kinetics of breakable filament assembly.

@nl

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An analytical solution to the kinetics of breakable filament assembly.

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Glyn L Devlin

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Mark E Welland

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Samuel I A Cohen

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Tuomas P J Knowles

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P2860

Mechanism of prion propagation: amyloid growth occurs by monomer addition

Emergence of Scaling in Random Networks

Protein misfolding, functional amyloid, and human disease

Molecular self-assembly and nanochemistry: a chemical strategy for the synthesis of nanostructures

Molecular recycling within amyloid fibrils.

Measurement of the scrapie agent using an incubation time interval assay.

The importance of sequence diversity in the aggregation and evolution of proteins.

Rapid amyloid fiber formation from the fast-folding WW domain FBP28.

Fiber-dependent amyloid formation as catalysis of an existing reaction pathway.

Systematic analysis of nucleation-dependent polymerization reveals new insights into the mechanism of amyloid self-assembly

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1533-1537

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scholarly article

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10.1126/SCIENCE.1178250

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5959

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326

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Michele Vendruscolo

Christopher A Waudby

Eugene M. Terentjev

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2009-12-01T00:00:00Z

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40685651

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20007899

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