Perturbation of membranes by the amyloid beta-peptide--a molecular dynamics study.
about
Ubiquitous amyloidsComputational analysis of local membrane properties.Roles for dysfunctional sphingolipid metabolism in Alzheimer's disease neuropathogenesis.A molecular dynamics study of the early stages of amyloid-beta(1-42) oligomerization: the role of lipid membranes.Binding, conformational transition and dimerization of amyloid-β peptide on GM1-containing ternary membrane: insights from molecular dynamics simulation.Binding of β-amyloid (1-42) peptide to negatively charged phospholipid membranes in the liquid-ordered state: modeling and experimental studiesMolecular interactions of Alzheimer amyloid-β oligomers with neutral and negatively charged lipid bilayers.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-secretaseBiochemistry of amyloid β-protein and amyloid deposits in Alzheimer disease.The role of molecular simulations in the development of inhibitors of amyloid β-peptide aggregation for the treatment of Alzheimer's diseaseMolecular understanding of a potential functional link between antimicrobial and amyloid peptides.Molecular dynamics simulations reveal the protective role of cholesterol in β-amyloid protein-induced membrane disruptions in neuronal membrane mimics.Lipid composition influences the release of Alzheimer's amyloid β-peptide from membranes.Scaling and alpha-helix regulation of protein relaxation in a lipid bilayer.Identification of Distinct Conformations of the Angiotensin-II Type 1 Receptor Associated with the Gq/11 Protein Pathway and the β-Arrestin Pathway Using Molecular Dynamics Simulations.Stability of transmembrane amyloid β-peptide and membrane integrity tested by molecular modeling of site-specific Aβ42 mutations.Critical hydrogen bond formation for activation of the angiotensin II type 1 receptor.Kinetic pathways to peptide aggregation on surfaces: the effects of β-sheet propensity and surface attraction.Insight into the interactions, residue snorkeling, and membrane disordering potency of a single antimicrobial peptide into different lipid bilayers.Molecular dynamics simulations of β2-microglobulin interaction with hydrophobic surfaces.The molecular behavior of a single β-amyloid inside a dipalmitoylphosphatidylcholine bilayer at three different temperatures: An atomistic simulation study: Aβ interaction with DPPC: Atomistic simulation.
P2860
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P2860
Perturbation of membranes by the amyloid beta-peptide--a molecular dynamics study.
description
2009 nî lūn-bûn
@nan
2009年の論文
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2009年学术文章
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2009年学术文章
@zh-cn
2009年学术文章
@zh-hans
2009年学术文章
@zh-my
2009年学术文章
@zh-sg
2009年學術文章
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2009年學術文章
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2009年學術文章
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name
Perturbation of membranes by the amyloid beta-peptide--a molecular dynamics study.
@en
Perturbation of membranes by the amyloid beta-peptide--a molecular dynamics study.
@nl
type
label
Perturbation of membranes by the amyloid beta-peptide--a molecular dynamics study.
@en
Perturbation of membranes by the amyloid beta-peptide--a molecular dynamics study.
@nl
prefLabel
Perturbation of membranes by the amyloid beta-peptide--a molecular dynamics study.
@en
Perturbation of membranes by the amyloid beta-peptide--a molecular dynamics study.
@nl
P2860
P1433
P1476
Perturbation of membranes by the amyloid beta-peptide--a molecular dynamics study.
@en
P2860
P304
P356
10.1111/J.1742-4658.2009.07024.X
P407
P577
2009-04-22T00:00:00Z