In situ atomic force microscopy study of Alzheimer's beta-amyloid peptide on different substrates: new insights into mechanism of beta-sheet formation
about
Designed protein tetramer zipped together with a hydrophobic Alzheimer homology: A structural clue to amyloid assemblyLow levels of asparagine deamidation can have a dramatic effect on aggregation of amyloidogenic peptides: implications for the study of amyloid formationA mathematical model of the kinetics of beta-amyloid fibril growth from the denatured stateStepwise dynamics of epitaxially growing single amyloid fibrils.Ultrastructural organization of amyloid fibrils by atomic force microscopy.The role of Phe in the formation of well-ordered oligomers of amyloidogenic hexapeptide (NFGAIL) observed in molecular dynamics simulations with explicit solvent.Environmental impact of multi-wall carbon nanotubes in a novel model of exposure: systemic distribution, macrophage accumulation, and amyloid depositionNovel matrix proteins of Pteria penguin pearl oyster shell nacre homologous to the jacalin-related β-prism fold lectinsIdentification of a Novel Parallel β-Strand Conformation within Molecular Monolayer of Amyloid Peptideβ-sheet propensity controls the kinetic pathways and morphologies of seeded peptide aggregation.Induced beta-barrel formation of the Alzheimer's Abeta25-35 oligomers on carbon nanotube surfaces: implication for amyloid fibril inhibitionEffects of frustration, confinement, and surface interactions on the dimerization of an off-lattice beta-barrel protein.Biophysical insights into how surfaces, including lipid membranes, modulate protein aggregation related to neurodegeneration.Interprotofilament interactions between Alzheimer's Abeta1-42 peptides in amyloid fibrils revealed by cryoEMScanning probe acceleration microscopy (SPAM) in fluids: mapping mechanical properties of surfaces at the nanoscaleMutant huntingtin fragments form oligomers in a polyglutamine length-dependent manner in vitro and in vivo.Concentration effect on the aggregation of a self-assembling oligopeptide.Kinetic control of dimer structure formation in amyloid fibrillogenesisModification of hydrophilic and hydrophobic surfaces using an ionic-complementary peptideQuartz crystal microbalance studies of multilayer glucagon fibrillation at the solid-liquid interfacePreparation of fluorescently-labeled amyloid-beta peptide assemblies: the effect of fluorophore conjugation on structure and functionStructure-function relationships of pre-fibrillar protein assemblies in Alzheimer's disease and related disordersPoint mutations in Aβ result in the formation of distinct polymorphic aggregates in the presence of lipid bilayers.Amyloid-beta fibrillogenesis seeded by interface-induced peptide misfolding and self-assemblyProgress in transthyretin fibrillogenesis research strengthens the amyloid hypothesis.Astrocyte lipoproteins, effects of apoE on neuronal function, and role of apoE in amyloid-beta deposition in vivo.Effect of surfaces on amyloid fibril formation.A yeast toxic mutant of HET-s((218-289)) prion displays alternative intermediates of amyloidogenesisAmyloid-beta peptide assembly: a critical step in fibrillogenesis and membrane disruption.Assembly and kinetic folding pathways of a tetrameric beta-sheet complex: molecular dynamics simulations on simplified off-lattice protein modelsSubstrate-dependent morphology of supramolecular assemblies: fibrillin and type-VI collagen microfibrils.Memantine prevents memory consolidation failure induced by soluble beta amyloid in rats.Surface effects mediate self-assembly of amyloid-β peptides.Rubber elongation factor (REF), a major allergen component in Hevea brasiliensis latex has amyloid propertiesA hydrophobic gold surface triggers misfolding and aggregation of the amyloidogenic Josephin domain in monomeric form, while leaving the oligomers unaffectedExploring the influence of carbon nanoparticles on the formation of β-sheet-rich oligomers of IAPP₂₂₋₂₈ peptide by molecular dynamics simulation.Atomic force microscopy and MD simulations reveal pore-like structures of all-D-enantiomer of Alzheimer's β-amyloid peptide: relevance to the ion channel mechanism of AD pathology.Lipid-induced beta-amyloid peptide assemblage fragmentationPolymorphism of amyloid β peptide in different environments: implications for membrane insertion and pore formation.Two-dimensional sum-frequency generation (2D SFG) spectroscopy: summary of principles and its application to amyloid fiber monolayers.
P2860
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P2860
In situ atomic force microscopy study of Alzheimer's beta-amyloid peptide on different substrates: new insights into mechanism of beta-sheet formation
description
1999 nî lūn-bûn
@nan
1999年の論文
@ja
1999年学术文章
@wuu
1999年学术文章
@zh-cn
1999年学术文章
@zh-hans
1999年学术文章
@zh-my
1999年学术文章
@zh-sg
1999年學術文章
@yue
1999年學術文章
@zh
1999年學術文章
@zh-hant
name
In situ atomic force microscop ...... hanism of beta-sheet formation
@ast
In situ atomic force microscop ...... hanism of beta-sheet formation
@en
type
label
In situ atomic force microscop ...... hanism of beta-sheet formation
@ast
In situ atomic force microscop ...... hanism of beta-sheet formation
@en
prefLabel
In situ atomic force microscop ...... hanism of beta-sheet formation
@ast
In situ atomic force microscop ...... hanism of beta-sheet formation
@en
P2860
P356
P1476
In situ atomic force microscop ...... hanism of beta-sheet formation
@en
P2093
D M Holtzman
T Kowalewski
P2860
P304
P356
10.1073/PNAS.96.7.3688
P407
P577
1999-03-01T00:00:00Z