Atomic force microscopy reveals defects within mica supported lipid bilayers induced by the amyloidogenic human amylin peptide.
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Membrane fragmentation by an amyloidogenic fragment of human Islet Amyloid Polypeptide detected by solid-state NMR spectroscopy of membrane nanotubesMolecular 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 DerivativesThree-Dimensional Structure and Orientation of Rat Islet Amyloid Polypeptide Protein in a Membrane Environment by Solution NMR SpectroscopyMembrane Curvature-sensing and Curvature-inducing Activity of Islet Amyloid Polypeptide and Its Implications for Membrane Disruption.Expression of wild-type and mutant S20G hIAPP in physiologic knock-in mouse models fails to induce islet amyloid formation, but induces mild glucose intoleranceAmyloid ion channels: a common structural link for protein-misfolding diseaseDirect observation of defects and increased ion permeability of a membrane induced by structurally disordered Cu/Zn-superoxide dismutase aggregates.Effects of Various Flavonoids on the α-Synuclein Fibrillation Process.Amyloid beta-protein assembly and Alzheimer disease.Distinct internalization pathways of human amylin monomers and its cytotoxic oligomers in pancreatic cellsIslet amyloid polypeptide demonstrates a persistent capacity to disrupt membrane integrityAmyloid aggregation and deposition of human islet amyloid polypeptide at membrane interfaces.Membrane disruption and early events in the aggregation of the diabetes related peptide IAPP from a molecular perspectiveHow type II diabetes-related islet amyloid polypeptide damages lipid bilayers.Membrane-mediated amyloid formation of PrP 106-126: A kinetic study.Phosphatidylethanolamine enhances amyloid fiber-dependent membrane fragmentation.Cations as switches of amyloid-mediated membrane disruption mechanisms: calcium and IAPP.Membrane damage by human islet amyloid polypeptide through fibril growth at the membraneMechanism of Inhibition of Human Islet Amyloid Polypeptide-Induced Membrane Damage by a Small Organic Fluorogen.Nanotools for megaproblems: probing protein misfolding diseases using nanomedicine modus operandiAmyloid beta ion channel: 3D structure and relevance to amyloid channel paradigm.Soluble amyloid beta-oligomers affect dielectric membrane properties by bilayer insertion and domain formation: implications for cell toxicityA Novel Form of Compensation in the Tg2576 Amyloid Mouse Model of Alzheimer's Disease.Poloxamer 188 (p188) as a membrane resealing reagent in biomedical applications.Induction of negative curvature as a mechanism of cell toxicity by amyloidogenic peptides: the case of islet amyloid polypeptide.Recent insights in islet amyloid polypeptide-induced membrane disruption and its role in beta-cell death in type 2 diabetes mellitusIslet amyloid polypeptide toxicity and membrane interactionsBayesian total internal reflection fluorescence correlation spectroscopy reveals hIAPP-induced plasma membrane domain organization in live cells.AFM of biological complexes: what can we learn?Oxidative stress and cell membranes in the pathogenesis of Alzheimer's disease.2DIR spectroscopy of human amylin fibrils reflects stable β-sheet structure.Polyglutamine aggregates impair lipid membrane integrity and enhance lipid membrane rigidity.Implications of peptide assemblies in amyloid diseases.Fluorescence microscopy studies on islet amyloid polypeptide fibrillation at heterogeneous and cellular membrane interfaces and its inhibition by resveratrol.Induction of endoplasmic reticulum stress-induced beta-cell apoptosis and accumulation of polyubiquitinated proteins by human islet amyloid polypeptide.Membrane disordering is not sufficient for membrane permeabilization by islet amyloid polypeptide: studies of IAPP(20-29) fragmentsMechanism of islet amyloid polypeptide fibrillation at lipid interfaces studied by infrared reflection absorption spectroscopy.A positive feedback cell signaling nucleation model of astrocyte dynamics.
P2860
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P2860
Atomic force microscopy reveals defects within mica supported lipid bilayers induced by the amyloidogenic human amylin peptide.
description
2004 nî lūn-bûn
@nan
2004 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2004 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
2004年の論文
@ja
2004年論文
@yue
2004年論文
@zh-hant
2004年論文
@zh-hk
2004年論文
@zh-mo
2004年論文
@zh-tw
2004年论文
@wuu
name
Atomic force microscopy reveal ...... idogenic human amylin peptide.
@ast
Atomic force microscopy reveal ...... idogenic human amylin peptide.
@en
Atomic force microscopy reveal ...... idogenic human amylin peptide.
@nl
type
label
Atomic force microscopy reveal ...... idogenic human amylin peptide.
@ast
Atomic force microscopy reveal ...... idogenic human amylin peptide.
@en
Atomic force microscopy reveal ...... idogenic human amylin peptide.
@nl
prefLabel
Atomic force microscopy reveal ...... idogenic human amylin peptide.
@ast
Atomic force microscopy reveal ...... idogenic human amylin peptide.
@en
Atomic force microscopy reveal ...... idogenic human amylin peptide.
@nl
P2093
P1476
Atomic force microscopy reveal ...... oidogenic human amylin peptide
@en
P2093
Goldsbury C
Li Blatter X
P304
P356
10.1016/J.JMB.2004.07.052
P407
P577
2004-09-01T00:00:00Z