Two-step mechanism of membrane disruption by Aβ through membrane fragmentation and pore formation
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Transient dynamics of Aβ contribute to toxicity in Alzheimer's diseaseInhibition of IAPP Aggregation and Toxicity by Natural Products and DerivativesChanges in membrane sphingolipid composition modulate dynamics and adhesion of integrin nanoclusters.β2-Microglobulin amyloid fibril-induced membrane disruption is enhanced by endosomal lipids and acidic pHMapping the structure of amyloid nucleation precursors by protein engineering kinetic analysis.Biophysical insights into how surfaces, including lipid membranes, modulate protein aggregation related to neurodegeneration.Effects of membrane interaction and aggregation of amyloid β-peptide on lipid mobility and membrane domain structure.α-helical structures drive early stages of self-assembly of amyloidogenic amyloid polypeptide aggregate formation in membranes.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.rAAV/ABAD-DP-6His attenuates oxidative stress-induced injury of PC12 cells.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.Ultrasensitive Measurement of Ca2+ Influx into Lipid Vesicles Induced by Protein Aggregates.The role of calcium, lipid membranes and islet amyloid polypeptide in the onset of type 2 diabetes: innocent bystanders or partners in a crime?Binding, conformational transition and dimerization of amyloid-β peptide on GM1-containing ternary membrane: insights from molecular dynamics simulation.Small molecule screening in context: lipid-catalyzed amyloid formation.General amyloid inhibitors? A critical examination of the inhibition of IAPP amyloid formation by inositol stereoisomers.Monitoring of single vesicle cytochrome-c release illuminates BAK as a novel target of Aβ oligomers.Chirality-assisted ring-like aggregation of aβ(1-40) at liquid-solid interfaces: a stereoselective two-step assembly process.ALS-Causing Mutations Significantly Perturb the Self-Assembly and Interaction with Nucleic Acid of the Intrinsically Disordered Prion-Like Domain of TDP-43.Phosphatidylethanolamine enhances amyloid fiber-dependent membrane fragmentation.Amyloid-β adopts a conserved, partially folded structure upon binding to zwitterionic lipid bilayers prior to amyloid formationCations as switches of amyloid-mediated membrane disruption mechanisms: calcium and IAPP.A High Affinity Red Fluorescence and Colorimetric Probe for Amyloid β Aggregates.Distinct Membrane Disruption Pathways Are Induced by 40-Residue β-Amyloid Peptides.Lipid composition-dependent membrane fragmentation and pore-forming mechanisms of membrane disruption by pexiganan (MSI-78)Apoptosis induced by islet amyloid polypeptide soluble oligomers is neutralized by diabetes-associated specific antibodies.Role of plasma membrane lipid composition on cellular homeostasis: learning from cell line models expressing fatty acid desaturases.Glucose directs amyloid-beta into membrane-active oligomers.Antimicrobial Peptides: Insights into Membrane Permeabilization, Lipopolysaccharide Fragmentation and Application in Plant Disease Control.Physico-chemical stress induced amyloid formation in insulin: Amyloid characterization, cytotoxicity analysis against human neuroblastoma cell lines and its prevention using black seeds (Nigella sativa).Structure based aggregation studies reveal the presence of helix-rich intermediate during α-Synuclein aggregation.β-Amyloid peptides display protective activity against the human Alzheimer's disease-associated herpes simplex virus-1.Endogenous Brain Lipids Inhibit Prion Amyloid Formation In Vitro.Modeling the Aggregation Propensity and Toxicity of Amyloid-β Variants.Membrane disordering is not sufficient for membrane permeabilization by islet amyloid polypeptide: studies of IAPP(20-29) fragmentsAggregation modulators interfere with membrane interactions of β2-microglobulin fibrils.
P2860
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P2860
Two-step mechanism of membrane disruption by Aβ through membrane fragmentation and pore formation
description
2012 nî lūn-bûn
@nan
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
2012年论文
@zh
2012年论文
@zh-cn
name
Two-step mechanism of membrane ...... agmentation and pore formation
@ast
Two-step mechanism of membrane ...... agmentation and pore formation
@en
type
label
Two-step mechanism of membrane ...... agmentation and pore formation
@ast
Two-step mechanism of membrane ...... agmentation and pore formation
@en
prefLabel
Two-step mechanism of membrane ...... agmentation and pore formation
@ast
Two-step mechanism of membrane ...... agmentation and pore formation
@en
P2093
P2860
P50
P1433
P1476
Two-step mechanism of membrane ...... agmentation and pore formation
@en
P2093
Dong-kuk Lee
Jennifer Chen
Samuel A Kotler
P2860
P304
P356
10.1016/J.BPJ.2012.06.045
P407
P577
2012-08-01T00:00:00Z