A single mutation in the nonamyloidogenic region of islet amyloid polypeptide greatly reduces toxicity
about
Structures of rat and human islet amyloid polypeptide IAPP(1-19) in micelles by NMR spectroscopyThe Effects of Lipid Membranes, Crowding and Osmolytes on the Aggregation, and Fibrillation Propensity of Human IAPPThree-Dimensional Structure and Orientation of Rat Islet Amyloid Polypeptide Protein in a Membrane Environment by Solution NMR SpectroscopyNMR Structure in a Membrane Environment Reveals Putative Amyloidogenic Regions of the SEVI Precursor Peptide PAP 248−286Structure and membrane orientation of IAPP in its natively amidated form at physiological pH in a membrane environmentRole of Cholesterol and Phospholipids in Amylin Misfolding, Aggregation and Etiology of Islet AmyloidosisExploring new biological functions of amyloids: bacteria cell agglutination mediated by host protein aggregationInfluence of Aluminium and EGCG on Fibrillation and Aggregation of Human Islet Amyloid PolypeptideLow molecular weight oligomers of amyloid peptides display beta-barrel conformations: a replica exchange molecular dynamics study in explicit solvent.Membrane Curvature-sensing and Curvature-inducing Activity of Islet Amyloid Polypeptide and Its Implications for Membrane Disruption.Considering protonation as a posttranslational modification regulating protein structure and function.Amyloidogenesis abolished by proline substitutions but enhanced by lipid binding.Solution state structures of human pancreatic amylin and pramlintide.Copper(II)-human amylin complex protects pancreatic cells from amylin toxicity.The amyloidogenic SEVI precursor, PAP248-286, is highly unfolded in solution despite an underlying helical tendency.Synthetic alpha-helix mimetics as agonists and antagonists of islet amyloid polypeptide aggregation.Disordered amyloidogenic peptides may insert into the membrane and assemble into common cyclic structural motifs.Biphasic effects of insulin on islet amyloid polypeptide membrane disruption.Amide proton solvent protection in amylin fibrils probed by quenched hydrogen exchange NMR.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.Distinct internalization pathways of human amylin monomers and its cytotoxic oligomers in pancreatic cellsAmyloid aggregation and deposition of human islet amyloid polypeptide at membrane interfaces.Misfolded proteins in Alzheimer's disease and type II diabetes.Beta structure motifs of islet amyloid polypeptides identified through surface-mediated assembliesStructure-Based Small Molecule Modulation of a Pre-Amyloid State: Pharmacological Enhancement of IAPP Membrane-Binding and Toxicity.Membrane disruption and early events in the aggregation of the diabetes related peptide IAPP from a molecular perspectiveConcentration-dependent transitions govern the subcellular localization of islet amyloid polypeptideAmphiphilic adsorption of human islet amyloid polypeptide aggregates to lipid/aqueous interfaces.Phosphatidylethanolamine enhances amyloid fiber-dependent membrane fragmentation.Islet Amyloid Polypeptide: Structure, Function, and Pathophysiology.Human islet amyloid polypeptide at the air-aqueous interface: a Langmuir monolayer approach.Cations as switches of amyloid-mediated membrane disruption mechanisms: calcium and IAPP.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.Induction of negative curvature as a mechanism of cell toxicity by amyloidogenic peptides: the case of islet amyloid polypeptide.Lipid composition-dependent membrane fragmentation and pore-forming mechanisms of membrane disruption by pexiganan (MSI-78)Membrane permeation induced by aggregates of human islet amyloid polypeptidesK3 fragment of amyloidogenic beta(2)-microglobulin forms ion channels: implication for dialysis related amyloidosis.Evidence for a partially structured state of the amylin monomer
P2860
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P2860
A single mutation in the nonamyloidogenic region of islet amyloid polypeptide greatly reduces toxicity
description
2008 nî lūn-bûn
@nan
2008 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2008 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
name
A single mutation in the nonam ...... ptide greatly reduces toxicity
@ast
A single mutation in the nonam ...... ptide greatly reduces toxicity
@en
A single mutation in the nonam ...... ptide greatly reduces toxicity
@nl
type
label
A single mutation in the nonam ...... ptide greatly reduces toxicity
@ast
A single mutation in the nonam ...... ptide greatly reduces toxicity
@en
A single mutation in the nonam ...... ptide greatly reduces toxicity
@nl
prefLabel
A single mutation in the nonam ...... ptide greatly reduces toxicity
@ast
A single mutation in the nonam ...... ptide greatly reduces toxicity
@en
A single mutation in the nonam ...... ptide greatly reduces toxicity
@nl
P2860
P50
P356
P1433
P1476
A single mutation in the nonam ...... ptide greatly reduces toxicity
@en
P2093
Kendra R Reid
Kevin Hartman
P2860
P304
P356
10.1021/BI801427C
P407
P577
2008-12-02T00:00:00Z