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.
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Competitive Mirror Image Phage Display Derived Peptide Modulates Amyloid Beta Aggregation and ToxicityFamilial Alzheimer's disease Osaka mutant (ΔE22) β-barrels suggest an explanation for the different Aβ1-40/42 preferred conformational states observed by experiment.All-d-Enantiomer of β-Amyloid Peptide Forms Ion Channels in Lipid Bilayers.Effect of metals on kinetic pathways of amyloid-β aggregationAmyloid β Protein and Alzheimer's Disease: When Computer Simulations Complement Experimental Studies.Activity and architecture of pyroglutamate-modified amyloid-β (AβpE3-42) poresDisordered amyloidogenic peptides may insert into the membrane and assemble into common cyclic structural motifs.Insight into the stability of cross-β amyloid fibril from VEALYL short peptide with molecular dynamics simulation.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?Role of the fast kinetics of pyroglutamate-modified amyloid-β oligomers in membrane binding and membrane permeability.Multivariate analyses of amyloid-beta oligomer populations indicate a connection between pore formation and cytotoxicityGraphene nanopore support system for simultaneous high-resolution AFM imaging and conductance measurements.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.Microbiome-generated amyloid and potential impact on amyloidogenesis in Alzheimer's disease (AD).QIAD assay for quantitating a compound's efficacy in elimination of toxic Aβ oligomersIon Channel Formation by Tau Protein: Implications for Alzheimer's Disease and Tauopathies.Computational modeling of the relationship between amyloid and disease.The higher level of complexity of K-Ras4B activation at the membrane.Amyloid beta oligomers induce neuronal elasticity changes in age-dependent manner: a force spectroscopy study on living hippocampal neurons.Molecular interactions of Alzheimer amyloid-β oligomers with neutral and negatively charged lipid bilayers.Molecular dynamics simulations of mechanical failure in polymorphic arrangements of amyloid fibrils containing structural defects.Mechanism of membrane permeation induced by synthetic β-hairpin peptides.Membrane permeation induced by aggregates of human islet amyloid polypeptidesNon-selective ion channel activity of polymorphic human islet amyloid polypeptide (amylin) double channels.Treadmill exercise prevents learning and memory impairment in Alzheimer's disease-like pathology.Amyloid pore-channel hypothesis: effect of ethanol on aggregation state using frog oocytes for an Alzheimer's disease study.Molecular understanding of a potential functional link between antimicrobial and amyloid peptides.Changes in lipid membranes may trigger amyloid toxicity in Alzheimer's disease.Recent Progress in Alzheimer's Disease Research, Part 1: Pathology.Noninvasive label-free nanoplasmonic optical imaging for real-time monitoring of in vitro amyloid fibrogenesis.Alzheimer Aβ peptide interactions with lipid membranes: fibrils, oligomers and polymorphic amyloid channels.Ring-like N-fold Models of Aβ42 fibrils.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.The diphenylpyrazole compound anle138b blocks Aβ channels and rescues disease phenotypes in a mouse model for amyloid pathology.Modulation of Alzheimer's amyloid β peptide oligomerization and toxicity by extracellular Hsp70.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.β-barrel Oligomers as Common Intermediates of Peptides Self-Assembling into Cross-β Aggregates.
P2860
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P2860
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.
description
2012 nî lūn-bûn
@nan
2012 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2012 թվականի հունվարին 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
Atomic force microscopy and MD ...... nel mechanism of AD pathology.
@ast
Atomic force microscopy and MD ...... nel mechanism of AD pathology.
@en
type
label
Atomic force microscopy and MD ...... nel mechanism of AD pathology.
@ast
Atomic force microscopy and MD ...... nel mechanism of AD pathology.
@en
prefLabel
Atomic force microscopy and MD ...... nel mechanism of AD pathology.
@ast
Atomic force microscopy and MD ...... nel mechanism of AD pathology.
@en
P2093
P2860
P50
P356
P1476
Atomic force microscopy and MD ...... nel mechanism of AD pathology.
@en
P2093
Bruce L Kagan
Hyunbum Jang
Laura Connelly
Ratnesh Lal
Samuel A Kotler
P2860
P304
P356
10.1021/JP2108126
P407
P577
2012-01-25T00:00:00Z