Mechanism of islet amyloid polypeptide fibrillation at lipid interfaces studied by infrared reflection absorption spectroscopy.
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A hIAPP-derived all-D-amino-acid inhibits hIAPP fibrillation efficiently at membrane surface by targeting α-helical oligomeric intermediatesStructures of rat and human islet amyloid polypeptide IAPP(1-19) in micelles by NMR spectroscopyNew Insights from Sum Frequency Generation Vibrational Spectroscopy into the Interactions of Islet Amyloid Polypeptides with Lipid MembranesThe Effects of Lipid Membranes, Crowding and Osmolytes on the Aggregation, and Fibrillation Propensity of Human IAPPDynamics of the formation of a hydrogel by a pathogenic amyloid peptide: islet amyloid polypeptide.Atomic structures of IAPP (amylin) fusions suggest a mechanism for fibrillation and the role of insulin in the processRanaspumin-2: Structure and Function of a Surfactant Protein from the Foam Nests of a Tropical FrogBisphenol A accelerates toxic amyloid formation of human islet amyloid polypeptide: a possible link between bisphenol A exposure and type 2 diabetesAmyloidogenesis abolished by proline substitutions but enhanced by lipid binding.The effect of Aβ on IAPP aggregation in the presence of an isolated β-cell membrane.Effects of several quinones on insulin aggregation.Lipid interaction and membrane perturbation of human islet amyloid polypeptide monomer and dimer by molecular dynamics simulations.Prediction and analysis of antibody amyloidogenesis from sequences.Amyloid fiber formation and membrane disruption are separate processes localized in two distinct regions of IAPP, the type-2-diabetes-related peptide.Amyloid aggregation and deposition of human islet amyloid polypeptide at membrane interfaces.Chiral vibrational structures of proteins at interfaces probed by sum frequency generation spectroscopy.Amphiphilic adsorption of human islet amyloid polypeptide aggregates to lipid/aqueous interfaces.Broad-Bandwidth Chiral Sum Frequency Generation Spectroscopy for Probing the Kinetics of Proteins at Interfaces.Human islet amyloid polypeptide at the air-aqueous interface: a Langmuir monolayer approach.Membrane damage by human islet amyloid polypeptide through fibril growth at the membraneAdsorption and Orientation of Human Islet Amyloid Polypeptide (hIAPP) Monomer at Anionic Lipid Bilayers: Implications for Membrane-Mediated AggregationAmyloid formation in heterogeneous environments: islet amyloid polypeptide glycosaminoglycan interactionsRecent insights in islet amyloid polypeptide-induced membrane disruption and its role in beta-cell death in type 2 diabetes mellitusInteraction of IAPP and insulin with model interfaces studied using neutron reflectometry.Membrane permeation induced by aggregates of human islet amyloid polypeptidesMethods for structural characterization of prefibrillar intermediates and amyloid fibrils.Facet-Dependent Interactions of Islet Amyloid Polypeptide with Gold Nanoparticles: Implications for Fibril Formation and Peptide-Induced Lipid Membrane Disruption.C4b-binding Protein Protects β-Cells from Islet Amyloid Polypeptide-induced Cytotoxicity.Mapping amyloid-β(16-22) nucleation pathways using fluorescence lifetime imaging microscopy.Amylin uncovered: a review on the polypeptide responsible for type II diabetes.Fluorescence microscopy studies on islet amyloid polypeptide fibrillation at heterogeneous and cellular membrane interfaces and its inhibition by resveratrol.Structural Properties of Human IAPP Dimer in Membrane Environment Studied by All-Atom Molecular Dynamics Simulations.Combined effects of agitation, macromolecular crowding, and interfaces on amyloidogenesisProbing amylin fibrillation at an early stage via a tetracysteine-recognising fluorophore.Enrichment of amyloidogenesis at an air-water interface.Interaction of membrane-bound islet amyloid polypeptide with soluble and crystalline insulinGanglioside-induced amyloid formation by human islet amyloid polypeptide in lipid rafts.The air-water interface determines the outcome of seeding during amyloidogenesis.A direct fluorescence-based technique for cellular localization of amylin.Cross-amyloid interaction of Aβ and IAPP at lipid membranes.
P2860
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P2860
Mechanism of islet amyloid polypeptide fibrillation at lipid interfaces studied by infrared reflection absorption spectroscopy.
description
2007 nî lūn-bûn
@nan
2007年の論文
@ja
2007年論文
@yue
2007年論文
@zh-hant
2007年論文
@zh-hk
2007年論文
@zh-mo
2007年論文
@zh-tw
2007年论文
@wuu
2007年论文
@zh
2007年论文
@zh-cn
name
Mechanism of islet amyloid pol ...... ction absorption spectroscopy.
@en
type
label
Mechanism of islet amyloid pol ...... ction absorption spectroscopy.
@en
prefLabel
Mechanism of islet amyloid pol ...... ction absorption spectroscopy.
@en
P2093
P2860
P1433
P1476
Mechanism of islet amyloid pol ...... ction absorption spectroscopy.
@en
P2093
P2860
P304
P356
10.1529/BIOPHYSJ.107.110635
P407
P577
2007-07-27T00:00:00Z