Annular structures as intermediates in fibril formation of Alzheimer Abeta17-42
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Structural Conversion of Aβ17-42 Peptides from Disordered Oligomers to U-Shape Protofilaments via Multiple Kinetic PathwaysA multiscale approach to characterize the early aggregation steps of the amyloid-forming peptide GNNQQNY from the yeast prion sup-35Low 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.Structural differences between Abeta(1-40) intermediate oligomers and fibrils elucidated by proteolytic fragmentation and hydrogen/deuterium exchange.Aggregation and fibril morphology of the Arctic mutation of Alzheimer's Aβ peptide by CD, TEM, STEM and in situ AFMHydration profiles of amyloidogenic molecular structures.Atomic-scale simulations confirm that soluble beta-sheet-rich peptide self-assemblies provide amyloid mimics presenting similar conformational properties.Polymorphic structures of Alzheimer's β-amyloid globulomers.Structural determination of Abeta25-35 micelles by molecular dynamics simulations.Structural convergence among diverse, toxic beta-sheet ion channels.Polymorphism in Alzheimer Abeta amyloid organization reflects conformational selection in a rugged energy landscape.Distinct annular oligomers captured along the assembly and disassembly pathways of transthyretin amyloid protofibrilsBinding of nonsteroidal anti-inflammatory drugs to Abeta fibrilA Protocol for the Design of Protein and Peptide Nanostructure Self-Assemblies Exploiting Synthetic Amino Acids.Molecular interactions of Alzheimer amyloid-β oligomers with neutral and negatively charged lipid bilayers.Mutational analysis and allosteric effects in the HIV-1 capsid protein carboxyl-terminal dimerization domain.Microscopic factors that control beta-sheet registry in amyloid fibrils formed by fragment 11-25 of amyloid beta peptide: insights from computer simulations.Polymorphism of Alzheimer's Abeta17-42 (p3) oligomers: the importance of the turn location and its conformationMolecular dynamics simulations of Ibuprofen binding to Abeta peptidesA model of amyloid's role in disease based on fibril fracture.Misfolded amyloid ion channels present mobile beta-sheet subunits in contrast to conventional ion channelsPolymorphism of fibrillar structures depending on the size of assembled Aβ17-42 peptides.Structures of beta-amyloid peptide 1-40, 1-42, and 1-55-the 672-726 fragment of APP-in a membrane environment with implications for interactions with gamma-secretaseMolecular understanding of a potential functional link between antimicrobial and amyloid peptides.Structural Rearrangement from Oligomer to Fibril Detected with FRET in a Designed Amphiphilic Peptide.Structural diversity of Alzheimer's disease amyloid-β dimers and their role in oligomerization and fibril formation.Effect of dehydration on the aggregation kinetics of two amyloid peptides.Existence of different structural intermediates on the fibrillation pathway of human serum albumin.Role of the N-terminus for the stability of an amyloid-β fibril with three-fold symmetry.An oligomeric equilibrium intermediate as the precursory nucleus of globular and fibrillar supramacromolecular assemblies in a PDZ domain.In silico investigation and targeting of amyloid β oligomers of different size.Diversity of kinetic pathways in amyloid fibril formation.Probing oligomerization of amyloid beta peptide in silico.Investigation of the interaction of amyloid β peptide (11-42) oligomers with a 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine (POPC) membrane using molecular dynamics simulation.Ultrastructural analysis of amyloidoma.
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Annular structures as intermediates in fibril formation of Alzheimer Abeta17-42
description
article científic
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article scientifique
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articolo scientifico
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artigo científico
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bilimsel makale
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scientific article published on 06 May 2008
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vedecký článok
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vetenskaplig artikel
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videnskabelig artikel
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vědecký článek
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name
Annular structures as intermediates in fibril formation of Alzheimer Abeta17-42
@en
Annular structures as intermediates in fibril formation of Alzheimer Abeta17-42.
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type
label
Annular structures as intermediates in fibril formation of Alzheimer Abeta17-42
@en
Annular structures as intermediates in fibril formation of Alzheimer Abeta17-42.
@nl
prefLabel
Annular structures as intermediates in fibril formation of Alzheimer Abeta17-42
@en
Annular structures as intermediates in fibril formation of Alzheimer Abeta17-42.
@nl
P2860
P50
P356
P1476
Annular structures as intermediates in fibril formation of Alzheimer Abeta17-42
@en
P2093
Hyunbum Jang
P2860
P304
P356
10.1021/JP711335B
P407
P577
2008-05-06T00:00:00Z