Islet amyloid polypeptide demonstrates a persistent capacity to disrupt membrane integrity - Wikidata - wikimedia - TriplyDB

Islet amyloid polypeptide demonstrates a persistent capacity to disrupt membrane integrity

Islet amyloid polypeptide demonstrates a persistent capacity to disrupt membrane integrity

http://www.wikidata.org/entity/Q35034994

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Dynamic pathology of islet endocrine cells in type 2 diabetes: β-Cell growth, death, regeneration and their clinical implications A flash in the pan: dissecting dynamic amyloid intermediates using fluorescence Atomic View of a Toxic Amyloid Small Oligomer The Hsp70/90 cochaperone, Sti1, suppresses proteotoxicity by regulating spatial quality control of amyloid-like proteins.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.α-helical structures drive early stages of self-assembly of amyloidogenic amyloid polypeptide aggregate formation in membranes.The human serum protein C4b-binding protein inhibits pancreatic IAPP-induced inflammasome activation.Lipid interaction and membrane perturbation of human islet amyloid polypeptide monomer and dimer by molecular dynamics simulations.Distinct annular oligomers captured along the assembly and disassembly pathways of transthyretin amyloid protofibrils Conformations of islet amyloid polypeptide monomers in a membrane environment: implications for fibril formation.Short Peptides as Inhibitors of Amyloid Aggregation Structure-Based Small Molecule Modulation of a Pre-Amyloid State: Pharmacological Enhancement of IAPP Membrane-Binding and Toxicity.Concentration-dependent transitions govern the subcellular localization of islet amyloid polypeptide Foldamer scaffolds suggest distinct structures are associated with alternative gains-of-function in a preamyloid toxin.Two-step mechanism of membrane disruption by Aβ through membrane fragmentation and pore formation Probing ion channel activity of human islet amyloid polypeptide (amylin).Phosphatidylethanolamine enhances amyloid fiber-dependent membrane fragmentation.Islet Amyloid Polypeptide: Structure, Function, and Pathophysiology.Binding Orientations and Lipid Interactions of Human Amylin at Zwitterionic and Anionic Lipid Bilayers Cations as switches of amyloid-mediated membrane disruption mechanisms: calcium and IAPP.Aliphatic peptides show similar self-assembly to amyloid core sequences, challenging the importance of aromatic interactions in amyloidosis Mechanism of Inhibition of Human Islet Amyloid Polypeptide-Induced Membrane Damage by a Small Organic Fluorogen.Common mechanism unites membrane poration by amyloid and antimicrobial peptides.A common landscape for membrane-active peptides.Islet amyloid: from fundamental biophysics to mechanisms of cytotoxicity.Islet amyloid polypeptide toxicity and membrane interactions Bayesian total internal reflection fluorescence correlation spectroscopy reveals hIAPP-induced plasma membrane domain organization in live cells.Shedding light on protein folding landscapes by single-molecule fluorescence.Aggregation of islet amyloid polypeptide: from physical chemistry to cell biology.Facet-Dependent Interactions of Islet Amyloid Polypeptide with Gold Nanoparticles: Implications for Fibril Formation and Peptide-Induced Lipid Membrane Disruption.Pore formation by human stefin B in its native and oligomeric states and the consequent amyloid induced toxicity.Misfolding of amyloidogenic proteins and their interactions with membranes.An Account of Amyloid Oligomers: Facts and Figures Obtained from Experiments and Simulations.Islet amyloid-induced cell death and bilayer integrity loss share a molecular origin targetable with oligopyridylamide-based α-helical mimetics Fiber-dependent and -independent toxicity of islet amyloid polypeptide.Dewetting transition assisted clearance of (NFGAILS) amyloid fibrils from cell membranes by graphene.Membrane destabilization by monomeric hIAPP observed by imaging fluorescence correlation spectroscopy.Implications of peptide assemblies in amyloid diseases.Membrane disordering is not sufficient for membrane permeabilization by islet amyloid polypeptide: studies of IAPP(20-29) fragments

P2860

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P2860

Islet amyloid polypeptide demonstrates a persistent capacity to disrupt membrane integrity

http://www.wikidata.org/entity/Q35034994

description

2011 nî lūn-bûn

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2011 թուականի Մայիսին հրատարակուած գիտական յօդուած

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2011 թվականի մայիսին հրատարակված գիտական հոդված

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2011年の論文

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2011年論文

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2011年論文

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2011年論文

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2011年論文

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2011年論文

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2011年论文

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name

Islet amyloid polypeptide demo ...... to disrupt membrane integrity

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Islet amyloid polypeptide demo ...... to disrupt membrane integrity

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type

label

Islet amyloid polypeptide demo ...... to disrupt membrane integrity

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Islet amyloid polypeptide demo ...... to disrupt membrane integrity

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prefLabel

Islet amyloid polypeptide demo ...... to disrupt membrane integrity

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Islet amyloid polypeptide demo ...... to disrupt membrane integrity

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PNAS.1102356108

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Proceedings of the National Academy of Sciences of the United States of America

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Islet amyloid polypeptide demo ...... to disrupt membrane integrity

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P2093

Andrew D Miranker

http://www.w3.org/2001/XMLSchema#string

Elizabeth Rhoades

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Nicholas B Last

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P2860

Protein-induced photophysical changes to the amyloid indicator dye thioflavin T

Structures of rat and human islet amyloid polypeptide IAPP(1-19) in micelles by NMR spectroscopy

A chaotic pore model of polypeptide antibiotic action

Islet amyloid in type 2 diabetes, and the toxic oligomer hypothesis

Protein misfolding, functional amyloid, and human disease

Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid beta-peptide

Common mechanisms of amyloid oligomer pathogenesis in degenerative disease

Antimicrobial peptides: pore formers or metabolic inhibitors in bacteria?

Folding of beta-sheet membrane proteins: a hydrophobic hexapeptide model.

The lipid dependence of melittin action investigated by dual-color fluorescence burst analysis.

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9460-9465

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scholarly article

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10.1073/PNAS.1102356108

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