All-d-Enantiomer of β-Amyloid Peptide Forms Ion Channels in Lipid Bilayers. - Test2 - elhamkhani - TriplyDB

All-d-Enantiomer of β-Amyloid Peptide Forms Ion Channels in Lipid Bilayers.

All-d-Enantiomer of β-Amyloid Peptide Forms Ion Channels in Lipid Bilayers.

http://www.wikidata.org/entity/Q30155354

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) pores Differences 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 formation The 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 polypeptides Amyloid 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.

http://www.wikidata.org/entity/Q30155354

description

2012 nî lūn-bûn

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2012 թուականի Փետրուարին հրատարակուած գիտական յօդուած

@hyw

2012 թվականի փետրվարին հրատարակված գիտական հոդված

@hy

2012年の論文

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2012年論文

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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

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name

All-d-Enantiomer of β-Amyloid Peptide Forms Ion Channels in Lipid Bilayers.

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All-d-Enantiomer of β-Amyloid Peptide Forms Ion Channels in Lipid Bilayers.

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type

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All-d-Enantiomer of β-Amyloid Peptide Forms Ion Channels in Lipid Bilayers.

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All-d-Enantiomer of β-Amyloid Peptide Forms Ion Channels in Lipid Bilayers.

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All-d-Enantiomer of β-Amyloid Peptide Forms Ion Channels in Lipid Bilayers.

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All-d-Enantiomer of β-Amyloid Peptide Forms Ion Channels in Lipid Bilayers.

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P1433

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P1433

Journal of Chemical Theory and Computation

P1476

All-d-Enantiomer of β-Amyloid Peptide Forms Ion Channels in Lipid Bilayers.

@en

P2093

Bruce L Kagan

http://www.w3.org/2001/XMLSchema#string

Hyunbum Jang

http://www.w3.org/2001/XMLSchema#string

Laura Connelly

http://www.w3.org/2001/XMLSchema#string

Ratnesh Lal

http://www.w3.org/2001/XMLSchema#string

Samuel A Kotler

http://www.w3.org/2001/XMLSchema#string

P2860

The Alzheimer's disease-associated amyloid beta-protein is an antimicrobial peptide

Neurotrophic and neurotoxic effects of amyloid beta protein: reversal by tachykinin neuropeptides

Lipid matrix plays a role in Abeta fibril kinetics and morphology

Hexokinase II detachment from the mitochondria potentiates cisplatin induced cytotoxicity through a caspase-2 dependent mechanism

Crystal structure of the amyloid-β p3 fragment provides a model for oligomer formation in Alzheimer's disease

Scalable molecular dynamics with NAMD

Alzheimer disease amyloid beta protein forms calcium channels in bilayer membranes: blockade by tromethamine and aluminum

Experimental constraints on quaternary structure in Alzheimer's beta-amyloid fibrils

Extending the treatment of backbone energetics in protein force fields: limitations of gas-phase quantum mechanics in reproducing protein conformational distributions in molecular dynamics simulations

3D structure of Alzheimer's amyloid-beta(1-42) fibrils

P304

1143-1152

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scholarly article

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10.1021/CT200885R

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3

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8

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Srinivasan Ramachandran

Fernando Teran Arce

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2012-02-03T00:00:00Z

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221897513

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22423218

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P932

3302213

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