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

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

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

http://www.wikidata.org/entity/Q24633016

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A single mutation in the nonamyloidogenic region of islet amyloid polypeptide greatly reduces toxicity Molecular Structure, Membrane Interactions, and Toxicity of the Islet Amyloid Polypeptide in Type 2 Diabetes Mellitus The magic of bicelles lights up membrane protein structure 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 NMR Structure in a Membrane Environment Reveals Putative Amyloidogenic Regions of the SEVI Precursor Peptide PAP 248−286 Structure and membrane orientation of IAPP in its natively amidated form at physiological pH in a membrane environment Bisphenol A accelerates toxic amyloid formation of human islet amyloid polypeptide: a possible link between bisphenol A exposure and type 2 diabetes Mapping the structure of amyloid nucleation precursors by protein engineering kinetic analysis.Considering protonation as a posttranslational modification regulating protein structure and function.Ionization Properties of Histidine Residues in the Lipid Bilayer Membrane Environment.α-helical structures drive early stages of self-assembly of amyloidogenic amyloid polypeptide aggregate formation in membranes.Amyloidogenesis abolished by proline substitutions but enhanced by lipid binding.Solution state structures of human pancreatic amylin and pramlintide.Selection for nonamyloidogenic mutants of islet amyloid polypeptide (IAPP) identifies an extended region for amyloidogenicity.The amyloidogenic SEVI precursor, PAP248-286, is highly unfolded in solution despite an underlying helical tendency.Aromaticity and amyloid formation: effect of π-electron distribution and aryl substituent geometry on the self-assembly of peptides derived from hIAPP(22-29).Biphasic effects of insulin on islet amyloid polypeptide membrane disruption.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.Islet amyloid polypeptide demonstrates a persistent capacity to disrupt membrane integrity Short Peptides as Inhibitors of Amyloid Aggregation Misfolded proteins in Alzheimer's disease and type II diabetes.Membrane disruption and early events in the aggregation of the diabetes related peptide IAPP from a molecular perspective Concentration-dependent transitions govern the subcellular localization of islet amyloid polypeptide 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.Inhibition of Toxic IAPP Amyloid by Extracts of Common Fruits Identification of Plant Extracts that Inhibit the Formation of Diabetes-Linked IAPP Amyloid Amylin structure-function relationships and receptor pharmacology: implications for amylin mimetic drug development.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.A critical assessment of the role of helical intermediates in amyloid formation by natively unfolded proteins and polypeptides.Islet amyloid polypeptide toxicity and membrane interactions Evidence for a partially structured state of the amylin monomer Apoptosis induced by islet amyloid polypeptide soluble oligomers is neutralized by diabetes-associated specific antibodies.IAPP aggregation and cellular toxicity are inhibited by 1,2,3,4,6-penta-O-galloyl-β-D-glucose.

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

http://www.wikidata.org/entity/Q24633016

description

2008 nî lūn-bûn

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2008 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած

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Ravi Prakash Reddy Nanga

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P2860

A single mutation in the nonamyloidogenic region of islet amyloid polypeptide greatly reduces toxicity

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

Solution structure of the Alzheimer amyloid beta-peptide (1-42) in an apolar microenvironment. Similarity with a virus fusion domain

Conformational preferences of the amylin nucleation site in SDS micelles: an NMR study

NMR solution structure and topological orientation of monomeric phospholamban in dodecylphosphocholine micelles

VMD: visual molecular dynamics

AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR

The Xplor-NIH NMR molecular structure determination package

NMRPipe: a multidimensional spectral processing system based on UNIX pipes

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