Phosphatidylethanolamine enhances amyloid fiber-dependent membrane fragmentation.
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Molecular Structure, Membrane Interactions, and Toxicity of the Islet Amyloid Polypeptide in Type 2 Diabetes MellitusThe Effects of Lipid Membranes, Crowding and Osmolytes on the Aggregation, and Fibrillation Propensity of Human IAPPInhibition of IAPP Aggregation and Toxicity by Natural Products and DerivativesOn the Environmental Factors Affecting the Structural and Cytotoxic Properties of IAPP Peptidesβ2-Microglobulin amyloid fibril-induced membrane disruption is enhanced by endosomal lipids and acidic pHDifferences 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.Alzheimer's disease: which type of amyloid-preventing drug agents to employ?The role of calcium, lipid membranes and islet amyloid polypeptide in the onset of type 2 diabetes: innocent bystanders or partners in a crime?Structural similarities and differences between amyloidogenic and non-amyloidogenic islet amyloid polypeptide (IAPP) sequences and implications for the dual physiological and pathological activities of these peptides.Plasma lipid profiling shows similar associations with prediabetes and type 2 diabetes.Amyloid aggregation and deposition of human islet amyloid polypeptide at membrane interfaces.Small molecule screening in context: lipid-catalyzed amyloid formation.Membrane interaction of antimicrobial peptides using E. coli lipid extract as model bacterial cell membranes and SFG spectroscopyChirality-assisted ring-like aggregation of aβ(1-40) at liquid-solid interfaces: a stereoselective two-step assembly process.N-terminal lipid conjugation of amyloid β(1-40) leads to the formation of highly ordered N-terminally extended fibrils.Binding Orientations and Lipid Interactions of Human Amylin at Zwitterionic and Anionic Lipid BilayersCations as switches of amyloid-mediated membrane disruption mechanisms: calcium and IAPP.Lipid composition-dependent membrane fragmentation and pore-forming mechanisms of membrane disruption by pexiganan (MSI-78)Molecular understanding of a potential functional link between antimicrobial and amyloid peptides.Mechanistic Contributions of Biological Cofactors in Islet Amyloid Polypeptide Amyloidogenesis.Structural studies and cytotoxicity assays of "aggregation-prone" IAPP(8-16) and its non-amyloidogenic variants suggest its important role in fibrillogenesis and cytotoxicity of human amylin.Molecular interactions of amyloid nanofibrils with biological aggregation modifiers: implications for cytotoxicity mechanisms and biomaterial design.Membrane disordering is not sufficient for membrane permeabilization by islet amyloid polypeptide: studies of IAPP(20-29) fragmentsMembrane effects of N-terminal fragment of apolipoprotein A-I: a fluorescent probe study.Cholesterol modulates the interaction of the islet amyloid polypeptide with membranes.The Role of Cholesterol in Driving IAPP-Membrane Interactions.Role of aromatic residues in amyloid fibril formation of human calcitonin by solid-state 13C NMR and molecular dynamics simulation.Membrane-mediated amyloid deposition of human islet amyloid polypeptide.Spontaneous Lipid Nanodisc Fomation by Amphiphilic Polymethacrylate Copolymers.Islet Amyloid Polypeptide Membrane Interactions: Effects of Membrane Composition.Impact of membrane curvature on amyloid aggregation.Effect of Phosphatidylserine and Cholesterol on Membrane-mediated Fibril Formation by the N-terminal Amyloidogenic Fragment of Apolipoprotein A-I.Role and Cytotoxicity of Amylin and Protection of Pancreatic Islet β-Cells from Amylin Cytotoxicity
P2860
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P2860
Phosphatidylethanolamine enhances amyloid fiber-dependent membrane fragmentation.
description
2012 nî lūn-bûn
@nan
2012年の論文
@ja
2012年学术文章
@wuu
2012年学术文章
@zh-cn
2012年学术文章
@zh-hans
2012年学术文章
@zh-my
2012年学术文章
@zh-sg
2012年學術文章
@yue
2012年學術文章
@zh
2012年學術文章
@zh-hant
name
Phosphatidylethanolamine enhances amyloid fiber-dependent membrane fragmentation.
@ast
Phosphatidylethanolamine enhances amyloid fiber-dependent membrane fragmentation.
@en
type
label
Phosphatidylethanolamine enhances amyloid fiber-dependent membrane fragmentation.
@ast
Phosphatidylethanolamine enhances amyloid fiber-dependent membrane fragmentation.
@en
prefLabel
Phosphatidylethanolamine enhances amyloid fiber-dependent membrane fragmentation.
@ast
Phosphatidylethanolamine enhances amyloid fiber-dependent membrane fragmentation.
@en
P2860
P50
P356
P1433
P1476
Phosphatidylethanolamine enhances amyloid fiber-dependent membrane fragmentation
@en
P2093
Dong-Kuk Lee
P2860
P304
P356
10.1021/BI3009888
P407
P577
2012-09-21T00:00:00Z