Structure of alpha-helical membrane-bound human islet amyloid polypeptide and its implications for membrane-mediated misfolding. - Wikidata - awgldk - TriplyDB

Structure of alpha-helical membrane-bound human islet amyloid polypeptide and its implications for membrane-mediated misfolding.

Structure of alpha-helical membrane-bound human islet amyloid polypeptide and its implications for membrane-mediated misfolding.

http://www.wikidata.org/entity/Q39143073

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A hIAPP-derived all-D-amino-acid inhibits hIAPP fibrillation efficiently at membrane surface by targeting α-helical oligomeric intermediates Structures of rat and human islet amyloid polypeptide IAPP(1-19) in micelles by NMR spectroscopy The Effects of Lipid Membranes, Crowding and Osmolytes on the Aggregation, and Fibrillation Propensity of Human IAPP On the Environmental Factors Affecting the Structural and Cytotoxic Properties of IAPP Peptides Dynamic -Helix Structure of Micelle-bound Human Amylin Three-Dimensional Structure and Orientation of Rat Islet Amyloid Polypeptide Protein in a Membrane Environment by Solution NMR Spectroscopy Atomic structures of IAPP (amylin) fusions suggest a mechanism for fibrillation and the role of insulin in the process Structure and membrane orientation of IAPP in its natively amidated form at physiological pH in a membrane environment Secondary Structure of Rat and Human Amylin across Force Fields Membrane Curvature-sensing and Curvature-inducing Activity of Islet Amyloid Polypeptide and Its Implications for Membrane Disruption.Membrane remodeling by amyloidogenic and non-amyloidogenic proteins studied by EPR.Amyloidogenesis abolished by proline substitutions but enhanced by lipid binding.Selection for nonamyloidogenic mutants of islet amyloid polypeptide (IAPP) identifies an extended region for amyloidogenicity.Synthetic alpha-helix mimetics as agonists and antagonists of islet amyloid polypeptide aggregation.Amyloidogenic peptide oligomer accumulation in autophagy-deficient β cells induces diabetes.Tau binds to lipid membrane surfaces via short amphipathic helices located in its microtubule-binding repeats Lipid interaction and membrane perturbation of human islet amyloid polypeptide monomer and dimer by molecular dynamics simulations.Beta-cell selective K(ATP)-channel activation protects beta-cells and human islets from human islet amyloid polypeptide induced toxicity.Conformations of islet amyloid polypeptide monomers in a membrane environment: implications for fibril formation.Stable and metastable states of human amylin in solution.The N-terminal helix controls the transition between the soluble and amyloid states of an FF domain Islet amyloid polypeptide demonstrates a persistent capacity to disrupt membrane integrity Short Peptides as Inhibitors of Amyloid Aggregation Amyloid aggregation and deposition of human islet amyloid polypeptide at membrane interfaces.Concentration-dependent transitions govern the subcellular localization of islet amyloid polypeptide How type II diabetes-related islet amyloid polypeptide damages lipid bilayers.Amphiphilic adsorption of human islet amyloid polypeptide aggregates to lipid/aqueous interfaces.Amyloidogenic Mutation Promotes Fibril Formation of the N-terminal Apolipoprotein A-I on Lipid Membranes.Phosphatidylethanolamine enhances amyloid fiber-dependent membrane fragmentation.Binding Orientations and Lipid Interactions of Human Amylin at Zwitterionic and Anionic Lipid Bilayers Human islet amyloid polypeptide at the air-aqueous interface: a Langmuir monolayer approach.β-Cell failure in type 2 diabetes: a case of asking too much of too few?Inhibition of Toxic IAPP Amyloid by Extracts of Common Fruits Identification of Plant Extracts that Inhibit the Formation of Diabetes-Linked IAPP Amyloid Common mechanism unites membrane poration by amyloid and antimicrobial peptides.Adsorption and Orientation of Human Islet Amyloid Polypeptide (hIAPP) Monomer at Anionic Lipid Bilayers: Implications for Membrane-Mediated Aggregation A common landscape for membrane-active peptides.Aggregation of Chameleon Peptides: Implications of α-Helicity in Fibril Formation Induction of negative curvature as a mechanism of cell toxicity by amyloidogenic peptides: the case of islet amyloid polypeptide.Diabetic Risk Factors Promote Islet Amyloid Polypeptide Misfolding by a Common, Membrane-mediated Mechanism.

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P2860

Structure of alpha-helical membrane-bound human islet amyloid polypeptide and its implications for membrane-mediated misfolding.

http://www.wikidata.org/entity/Q39143073

description

2008 nî lūn-bûn

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2008年の論文

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2008年論文

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2008年論文

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2008年論文

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2008年論文

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2008年論文

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2008年论文

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2008年论文

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2008年论文

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name

Structure of alpha-helical mem ...... membrane-mediated misfolding.

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Structure of alpha-helical mem ...... membrane-mediated misfolding.

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type

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Structure of alpha-helical mem ...... membrane-mediated misfolding.

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Structure of alpha-helical mem ...... membrane-mediated misfolding.

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prefLabel

Structure of alpha-helical mem ...... membrane-mediated misfolding.

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Structure of alpha-helical mem ...... membrane-mediated misfolding.

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Journal of Biological Chemistry

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Structure of alpha-helical mem ...... membrane-mediated misfolding.

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Melania Apostolidou

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Ralf Langen

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Sajith A Jayasinghe

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P2860

Pancreatic islet cell toxicity of amylin associated with type-2 diabetes mellitus

Membrane-bound alpha-synuclein has a high aggregation propensity and the ability to seed the aggregation of the cytosolic form

Direct detection of transient alpha-helical states in islet amyloid polypeptide

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17205-17210

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scholarly article

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10.1074/JBC.M801383200

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25

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283

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2008-04-28T00:00:00Z

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18442979

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2427348

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