All-d-Enantiomer of β-Amyloid Peptide Forms Ion Channels in Lipid Bilayers.
about
Familial Alzheimer's disease Osaka mutant (ΔE22) β-barrels suggest an explanation for the different Aβ1-40/42 preferred conformational states observed by experiment.Activity and architecture of pyroglutamate-modified amyloid-β (AβpE3-42) poresDifferences between amyloid-β aggregation in solution and on the membrane: insights into elucidation of the mechanistic details of Alzheimer's disease.Disordered amyloidogenic peptides may insert into the membrane and assemble into common cyclic structural motifs.Mechanisms for the Insertion of Toxic, Fibril-like β-Amyloid Oligomers into the Membrane.Alzheimer's disease: which type of amyloid-preventing drug agents to employ?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.Mechanisms of membrane binding of small GTPase K-Ras4B farnesylated hypervariable region.Probing structural features of Alzheimer's amyloid-β pores in bilayers using site-specific amino acid substitutions.Two-step mechanism of membrane disruption by Aβ through membrane fragmentation and pore formationThe higher level of complexity of K-Ras4B activation at the membrane.Distinct Membrane Disruption Pathways Are Induced by 40-Residue β-Amyloid Peptides.Mechanism of membrane permeation induced by synthetic β-hairpin peptides.Membrane permeation induced by aggregates of human islet amyloid polypeptidesAmyloid β-protein oligomers and Alzheimer's disease.Treadmill exercise prevents learning and memory impairment in Alzheimer's disease-like pathology.Small molecule NPT-440-1 inhibits ionic flux through Aβ1-42 pores: Implications for Alzheimer's disease therapeutics.Amyloid β Ion Channels in a Membrane Comprising Brain Total Lipid Extracts.Enantiomeric and diastereoisomeric (mixed) L/ D-octaarginine derivatives - a simple way of modulating the properties of cell-penetrating peptides.All-atom molecular dynamics simulations of an artificial sodium channel in a lipid bilayer: the effect of water solvation/desolvation of the sodium ion.
P2860
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P2860
All-d-Enantiomer of β-Amyloid Peptide Forms Ion Channels in Lipid Bilayers.
description
2012 nî lūn-bûn
@nan
2012 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2012 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
2012年の論文
@ja
2012年論文
@yue
2012年論文
@zh-hant
2012年論文
@zh-hk
2012年論文
@zh-mo
2012年論文
@zh-tw
2012年论文
@wuu
name
All-d-Enantiomer of β-Amyloid Peptide Forms Ion Channels in Lipid Bilayers.
@ast
All-d-Enantiomer of β-Amyloid Peptide Forms Ion Channels in Lipid Bilayers.
@en
type
label
All-d-Enantiomer of β-Amyloid Peptide Forms Ion Channels in Lipid Bilayers.
@ast
All-d-Enantiomer of β-Amyloid Peptide Forms Ion Channels in Lipid Bilayers.
@en
prefLabel
All-d-Enantiomer of β-Amyloid Peptide Forms Ion Channels in Lipid Bilayers.
@ast
All-d-Enantiomer of β-Amyloid Peptide Forms Ion Channels in Lipid Bilayers.
@en
P2093
P2860
P50
P356
P1476
All-d-Enantiomer of β-Amyloid Peptide Forms Ion Channels in Lipid Bilayers.
@en
P2093
Bruce L Kagan
Hyunbum Jang
Laura Connelly
Ratnesh Lal
Samuel A Kotler
P2860
P304
P356
10.1021/CT200885R
P577
2012-02-03T00:00:00Z