Probing structural features of Alzheimer's amyloid-β pores in bilayers using site-specific amino acid substitutions.
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.Biophysical insights into how surfaces, including lipid membranes, modulate protein aggregation related to neurodegeneration.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?Mechanisms of membrane binding of small GTPase K-Ras4B farnesylated hypervariable region.Structure-Based Peptide Design to Modulate Amyloid Beta Aggregation and Reduce CytotoxicityAnalyzing and Modeling the Kinetics of Amyloid Beta Pores Associated with Alzheimer's Disease Pathology.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.Molecular interactions of Alzheimer amyloid-β oligomers with neutral and negatively charged lipid bilayers.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.Activation of PARP by oxidative stress induced by β-amyloid: implications for Alzheimer's disease.Ion Channel Formation by Amyloid-β42 Oligomers but Not Amyloid-β40 in Cellular Membranes.Recent Progress in Alzheimer's Disease Research, Part 1: Pathology.Interaction of toxic and non-toxic HypF-N oligomers with lipid bilayers investigated at high resolution with atomic force microscopy.Stability of transmembrane amyloid β-peptide and membrane integrity tested by molecular modeling of site-specific Aβ42 mutations.Small molecule NPT-440-1 inhibits ionic flux through Aβ1-42 pores: Implications for Alzheimer's disease therapeutics.Ligand-receptor interaction catalyzes the aggregation of small molecules to induce cell necroptosis.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.Aromatic-interaction-mediated inhibition of β-amyloid assembly structures and cytotoxicity.
P2860
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P2860
Probing structural features of Alzheimer's amyloid-β pores in bilayers using site-specific amino acid substitutions.
description
2012 nî lūn-bûn
@nan
2012年の論文
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2012年論文
@yue
2012年論文
@zh-hant
2012年論文
@zh-hk
2012年論文
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2012年論文
@zh-tw
2012年论文
@wuu
2012年论文
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2012年论文
@zh-cn
name
Probing structural features of ...... ific amino acid substitutions.
@ast
Probing structural features of ...... ific amino acid substitutions.
@en
type
label
Probing structural features of ...... ific amino acid substitutions.
@ast
Probing structural features of ...... ific amino acid substitutions.
@en
prefLabel
Probing structural features of ...... ific amino acid substitutions.
@ast
Probing structural features of ...... ific amino acid substitutions.
@en
P2093
P2860
P356
P1433
P1476
Probing structural features of ...... ific amino acid substitutions.
@en
P2093
Bruce L Kagan
Hyunbum Jang
Ratnesh Lal
Samuel A Kotler
P2860
P304
P356
10.1021/BI2017427
P407
P577
2012-01-12T00:00:00Z