Monomer adds to preformed structured oligomers of Abeta-peptides by a two-stage dock-lock mechanism.
about
Alzheimer's disease--a panorama glimpseOligomerization of Peptides LVEALYL and RGFFYT and Their Binding Affinity to InsulinStructural Conversion of Aβ17-42 Peptides from Disordered Oligomers to U-Shape Protofilaments via Multiple Kinetic PathwaysA condensation-ordering mechanism in nanoparticle-catalyzed peptide aggregation.Mapping the conformational dynamics and pathways of spontaneous steric zipper Peptide oligomerizationInfluence of preformed Asp23-Lys28 salt bridge on the conformational fluctuations of monomers and dimers of Abeta peptides with implications for rates of fibril formationDiscovery of dihydrochalcone as potential lead for Alzheimer's disease: in silico and in vitro studyβ-sheet propensity controls the kinetic pathways and morphologies of seeded peptide aggregation.Effects of surface interactions on peptide aggregate morphology.Low molecular weight oligomers of amyloid peptides display beta-barrel conformations: a replica exchange molecular dynamics study in explicit solvent.Induced beta-barrel formation of the Alzheimer's Abeta25-35 oligomers on carbon nanotube surfaces: implication for amyloid fibril inhibitionEffect of beta-sheet propensity on peptide aggregation.Lattice model for amyloid peptides: OPEP force field parametrization and applications to the nucleus size of Alzheimer's peptides.Structural differences between Abeta(1-40) intermediate oligomers and fibrils elucidated by proteolytic fragmentation and hydrogen/deuterium exchange.Structural and fluctuational difference between two ends of Aβ amyloid fibril: MD simulations predict only one end has open conformations.Free cholesterol induces higher β-sheet content in Aβ peptide oligomers by aromatic interaction with Phe19.Structural reorganisation and potential toxicity of oligomeric species formed during the assembly of amyloid fibrils.Prion protein insertional mutations increase aggregation propensity but not fiber stability.Finite size effects in simulations of protein aggregation.A generic mechanism of emergence of amyloid protofilaments from disordered oligomeric aggregates.Formation and growth of oligomers: a Monte Carlo study of an amyloid tau fragmentGranular assembly of alpha-synuclein leading to the accelerated amyloid fibril formation with shear stress.Amyloidogenesis abolished by proline substitutions but enhanced by lipid binding.Association thermodynamics and conformational stability of beta-sheet amyloid beta(17-42) oligomers: effects of E22Q (Dutch) mutation and charge neutralizationPrinciples governing oligomer formation in amyloidogenic peptides.Crowding alone cannot account for cosolute effect on amyloid aggregationComputational backbone mutagenesis of Abeta peptides: probing the role of backbone hydrogen bonds in aggregation.Unfolding of the amyloid β-peptide central helix: mechanistic insights from molecular dynamics simulations.Amyloid β Protein and Alzheimer's Disease: When Computer Simulations Complement Experimental Studies.Polymorphism in Alzheimer Abeta amyloid organization reflects conformational selection in a rugged energy landscape.Fibril elongation by Aβ(17-42): kinetic network analysis of hybrid-resolution molecular dynamics simulationsExtending the PRIME model for protein aggregation to all 20 amino acids.Mechanism of fiber assembly: treatment of Aβ peptide aggregation with a coarse-grained united-residue force field.Amyloid peptide Aβ40 inhibits aggregation of Aβ42: evidence from molecular dynamics simulations.Thermodynamic perspective on the dock-lock growth mechanism of amyloid fibrils.Effects of hydroxylated carbon nanotubes on the aggregation of Aβ16-22 peptides: a combined simulation and experimental study.Impact of sequence on the molecular assembly of short amyloid peptides.Connecting macroscopic observables and microscopic assembly events in amyloid formation using coarse grained simulationsNonsteroidal anti-inflammatory drug naproxen destabilizes Aβ amyloid fibrils: a molecular dynamics investigation.Effects of macromolecular crowding on amyloid beta (16-22) aggregation using coarse-grained simulations.
P2860
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P2860
Monomer adds to preformed structured oligomers of Abeta-peptides by a two-stage dock-lock mechanism.
description
2006 nî lūn-bûn
@nan
2006年の論文
@ja
2006年論文
@yue
2006年論文
@zh-hant
2006年論文
@zh-hk
2006年論文
@zh-mo
2006年論文
@zh-tw
2006年论文
@wuu
2006年论文
@zh
2006年论文
@zh-cn
name
Monomer adds to preformed stru ...... two-stage dock-lock mechanism.
@ast
Monomer adds to preformed stru ...... two-stage dock-lock mechanism.
@en
type
label
Monomer adds to preformed stru ...... two-stage dock-lock mechanism.
@ast
Monomer adds to preformed stru ...... two-stage dock-lock mechanism.
@en
prefLabel
Monomer adds to preformed stru ...... two-stage dock-lock mechanism.
@ast
Monomer adds to preformed stru ...... two-stage dock-lock mechanism.
@en
P2093
P2860
P356
P1476
Monomer adds to preformed stru ...... two-stage dock-lock mechanism
@en
P2093
D Thirumalai
Gerhard Stock
John E Straub
Phuong H Nguyen
P2860
P304
P356
10.1073/PNAS.0607440104
P407
P50
P577
2006-12-26T00:00:00Z