Design of a mimic of nonamyloidogenic and bioactive human islet amyloid polypeptide (IAPP) as nanomolar affinity inhibitor of IAPP cytotoxic fibrillogenesis
about
Molecular Structure, Membrane Interactions, and Toxicity of the Islet Amyloid Polypeptide in Type 2 Diabetes MellitusMechanisms of islet amyloidosis toxicity in type 2 diabetesOn the Environmental Factors Affecting the Structural and Cytotoxic Properties of IAPP PeptidesAtomic structure of the cross-β spine of islet amyloid polypeptide (amylin)Atomic structures of IAPP (amylin) fusions suggest a mechanism for fibrillation and the role of insulin in the processConverting the Highly Amyloidogenic Human Calcitonin into a Powerful Fibril Inhibitor by Three-dimensional Structure Homology with a Non-amyloidogenic AnalogueInteraction between amyloid beta peptide and an aggregation blocker peptide mimicking islet amyloid polypeptideMetal ion-dependent, reversible, protein filament formation by designed beta-roll polypeptides.Solution state structures of human pancreatic amylin and pramlintide.Neprilysin impedes islet amyloid formation by inhibition of fibril formation rather than peptide degradation.Analysis of the inhibition and remodeling of islet amyloid polypeptide amyloid fibers by flavanolsRationally designed, nontoxic, nonamyloidogenic analogues of human islet amyloid polypeptide with improved solubilityMorin hydrate inhibits amyloid formation by islet amyloid polypeptide and disaggregates amyloid fibers.The flavanol (-)-epigallocatechin 3-gallate inhibits amyloid formation by islet amyloid polypeptide, disaggregates amyloid fibrils, and protects cultured cells against IAPP-induced toxicity.The amyloid formation mechanism in human IAPP: dimers have β-strand monomer-monomer interfacesStructural 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.Ion mobility spectrometry-mass spectrometry defines the oligomeric intermediates in amylin amyloid formation and the mode of action of inhibitorsExploring the influence of EGCG on the β-sheet-rich oligomers of human islet amyloid polypeptide (hIAPP1-37) and identifying its possible binding sites from molecular dynamics simulation.N-Methylated sst2 Selective Somatostatin Cyclic Peptide Analogue as a Potent Candidate for Treating Neurogenic Inflammation.General amyloid inhibitors? A critical examination of the inhibition of IAPP amyloid formation by inositol stereoisomers.New insights into the mechanism of Alzheimer amyloid-beta fibrillogenesis inhibition by N-methylated peptides.Nucleobindin 1 caps human islet amyloid polypeptide protofibrils to prevent amyloid fibril formationAnalysis of the ability of pramlintide to inhibit amyloid formation by human islet amyloid polypeptide reveals a balance between optimal recognition and reduced amyloidogenicity.Islet Amyloid Polypeptide: Structure, Function, and Pathophysiology.Amylin-Aβ oligomers at atomic resolution using molecular dynamics simulations: a link between Type 2 diabetes and Alzheimer's diseaseMechanism of Inhibition of Human Islet Amyloid Polypeptide-Induced Membrane Damage by a Small Organic Fluorogen.Coexistence of ribbon and helical fibrils originating from hIAPP(20-29) revealed by quantitative nanomechanical atomic force microscopy.Novel therapeutic strategies for the treatment of protein-misfolding diseases.Conformationally restricted short peptides inhibit human islet amyloid polypeptide (hIAPP) fibrillization.Electrochemical Assay of Human Islet Amyloid Polypeptide and Its AggregationAmyloid formation in heterogeneous environments: islet amyloid polypeptide glycosaminoglycan interactionsIslet amyloid: from fundamental biophysics to mechanisms of cytotoxicity.Recent insights in islet amyloid polypeptide-induced membrane disruption and its role in beta-cell death in type 2 diabetes mellitusTwo-dimensional IR spectroscopy and isotope labeling defines the pathway of amyloid formation with residue-specific resolution.Islet amyloid polypeptide toxicity and membrane interactionsMechanism of IAPP amyloid fibril formation involves an intermediate with a transient β-sheet.Intrinsically disordered proteins: from sequence and conformational properties toward drug discovery.N-methylation of peptides and proteins: an important element for modulating biological functions.The effect of glycosaminoglycans (GAGs) on amyloid aggregation and toxicity.Toward the discovery of effective polycyclic inhibitors of alpha-synuclein amyloid assembly.
P2860
Q26774381-AD911076-7344-417D-8A70-CD37E62B0902Q26823708-584EDD22-187D-4B7B-89A2-107AA8B70A48Q27022467-FC590D8D-2692-46A2-8BCE-7CBC0E97288BQ27650849-1526D45D-0811-4ED5-90FC-C52A1106D47BQ27655644-C01F6237-9957-42C0-9F11-5A0EB1C0219AQ27665898-777C65AF-A738-46E3-AA96-B50F927C12AAQ28478284-DA0E9B20-5E67-455C-B1F3-D38E15116AA0Q33301065-2782F1AE-B61B-4B6D-AFC4-1D0748EFB905Q33481542-6973A154-5F4D-4C7A-81F6-CA5899ED68D0Q33897696-C5FD2B5F-6D91-45BB-AE30-AB4E5BF18F4AQ34191817-A9F37633-4FF2-4811-87E9-5EB42913F17EQ34230460-3599AF7C-9BA3-4A84-84C8-CA3C09356EABQ34246438-125B54D0-D5EB-4E07-A032-7A35DECCE3FCQ34660220-3ACA9243-1917-4C6D-9C91-281EDD086610Q34978500-C3B566D9-CF07-43CC-8BBA-8B782840E803Q34979345-4AA497F2-8E39-4435-9D37-07F6B4B21543Q35076599-571A18EC-E78D-4C35-BD09-8F52275BC136Q35150371-EDE075E7-2DD4-4449-B7E1-889CA1583044Q35181901-B305D33C-0360-4D1C-96C2-E534CB04F78CQ35280161-A6E1FF28-BE17-4206-B694-DD59759BD6CDQ36069678-00DBE695-FAEB-4F63-9D06-32B39BA445A0Q36098963-6CBFBFB0-4492-484A-A47E-3E11FA9367FEQ36307453-00F2CB31-9653-4632-A4BE-F97A195F05FDQ36327915-09FFCE72-51D0-43FE-9039-766AE6E2F924Q36483911-60727D65-CB4A-41FB-AC3D-B801BAE99A3FQ36591538-37FFFFE1-DD70-44FB-ABD4-D6A6F6C9849CQ36637254-F36E2F84-EE0C-490E-8B9C-C9D013A47C28Q36863389-46706B76-7134-40BA-AA7C-B9D71C6CAD91Q36935342-D0BAD68D-001D-4E6F-AF5F-BC152C40D8B2Q36994614-013CB1F6-B0CE-4F65-9BB4-ECD0B916DDDFQ37120788-ABE42909-03BB-4A6B-9F64-7D0C3596EF25Q37120813-BDE04798-FDE4-4A0E-B3D8-42FFCC47F1B9Q37165186-3D41D0A9-E85C-4A48-BA5B-89F353FBB17FQ37167746-B70308B9-DAA4-4155-9656-CFD665B17BDFQ37353189-B1FB33DF-D16B-4C70-A87A-BE44D100D036Q37353196-9DB78085-2EDE-4D57-AE09-C9E6B7BE12D3Q38002804-A46FFF40-F725-498C-A605-D3B380A656B2Q38060675-DA465B29-A11D-4EA4-80A8-B80964EA7821Q38343014-6682D095-3D60-4069-8371-410757DA9F57Q38422514-1B3E9C4B-A533-4E6B-ABCC-5CC94217DE2E
P2860
Design of a mimic of nonamyloidogenic and bioactive human islet amyloid polypeptide (IAPP) as nanomolar affinity inhibitor of IAPP cytotoxic fibrillogenesis
description
2006 nî lūn-bûn
@nan
2006 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2006 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
2006年の論文
@ja
2006年論文
@yue
2006年論文
@zh-hant
2006年論文
@zh-hk
2006年論文
@zh-mo
2006年論文
@zh-tw
2006年论文
@wuu
name
Design of a mimic of nonamyloi ...... IAPP cytotoxic fibrillogenesis
@ast
Design of a mimic of nonamyloi ...... IAPP cytotoxic fibrillogenesis
@en
Design of a mimic of nonamyloidogenic and bioactive human islet amyloid polypeptide
@nl
type
label
Design of a mimic of nonamyloi ...... IAPP cytotoxic fibrillogenesis
@ast
Design of a mimic of nonamyloi ...... IAPP cytotoxic fibrillogenesis
@en
Design of a mimic of nonamyloidogenic and bioactive human islet amyloid polypeptide
@nl
prefLabel
Design of a mimic of nonamyloi ...... IAPP cytotoxic fibrillogenesis
@ast
Design of a mimic of nonamyloi ...... IAPP cytotoxic fibrillogenesis
@en
Design of a mimic of nonamyloidogenic and bioactive human islet amyloid polypeptide
@nl
P2093
P2860
P356
P1476
Design of a mimic of nonamyloi ...... IAPP cytotoxic fibrillogenesis
@en
P2093
Aleksandra Velkova
Aphrodite Kapurniotu
Athanasios Kazantzis
Li-Mei Yan
Marianna Tatarek-Nossol
P2860
P304
P356
10.1073/PNAS.0507471103
P407
P577
2006-02-07T00:00:00Z