Structure and membrane orientation of IAPP in its natively amidated form at physiological pH in a membrane environment
about
A hIAPP-derived all-D-amino-acid inhibits hIAPP fibrillation efficiently at membrane surface by targeting α-helical oligomeric intermediatesMolecular Structure, Membrane Interactions, and Toxicity of the Islet Amyloid Polypeptide in Type 2 Diabetes MellitusA flash in the pan: dissecting dynamic amyloid intermediates using fluorescenceOn the Environmental Factors Affecting the Structural and Cytotoxic Properties of IAPP PeptidesBisphenol A accelerates toxic amyloid formation of human islet amyloid polypeptide: a possible link between bisphenol A exposure and type 2 diabetesInter-species cross-seeding: stability and assembly of rat-human amylin aggregatesSecondary Structure of Rat and Human Amylin across Force FieldsMembrane 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.Considering protonation as a posttranslational modification regulating protein structure and function.Sodium dodecyl sulfate monomers induce XAO peptide polyproline II to α-helix transition.α-helical structures drive early stages of self-assembly of amyloidogenic amyloid polypeptide aggregate formation in membranes.Resolving the paradox for protein aggregation diseases: NMR structure and dynamics of the membrane-embedded P56S-MSP causing ALS imply a common mechanism for aggregation-prone proteins to attack membranesLipid interaction and membrane perturbation of human islet amyloid polypeptide monomer and dimer by molecular dynamics simulations.Conformations of islet amyloid polypeptide monomers in a membrane environment: implications for fibril formation.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.Amyloid aggregation and deposition of human islet amyloid polypeptide at membrane interfaces.Structure-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 perspectiveRapid assessment of human amylin aggregation and its inhibition by copper(II) ions by laser ablation electrospray ionization mass spectrometry with ion mobility separationProbing 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 BilayersHuman islet amyloid polypeptide at the air-aqueous interface: a Langmuir monolayer approach.Amylin-Aβ oligomers at atomic resolution using molecular dynamics simulations: a link between Type 2 diabetes and Alzheimer's diseaseStabilizing Off-pathway Oligomers by Polyphenol Nanoassemblies for IAPP Aggregation InhibitionCations as switches of amyloid-mediated membrane disruption mechanisms: calcium and IAPP.Adsorption and Orientation of Human Islet Amyloid Polypeptide (hIAPP) Monomer at Anionic Lipid Bilayers: Implications for Membrane-Mediated AggregationIslet amyloid: from fundamental biophysics to mechanisms of cytotoxicity.Conformational Ensemble of hIAPP Dimer: Insight into the Molecular Mechanism by which a Green Tea Extract inhibits hIAPP Aggregation.In silico cross seeding of Aβ and amylin fibril-like oligomers.Effect of Post-Translational Amidation on Islet Amyloid Polypeptide Conformational Ensemble: Implications for Its Aggregation Early Steps.Mutations and seeding of amylin fibril-like oligomers.Apoptosis induced by islet amyloid polypeptide soluble oligomers is neutralized by diabetes-associated specific antibodies.The redox environment triggers conformational changes and aggregation of hIAPP in Type II Diabetes.Structure-activity relationships for α-calcitonin gene-related peptide.Mechanistic Contributions of Biological Cofactors in Islet Amyloid Polypeptide Amyloidogenesis.Structural studies and cytotoxicity assays of "aggregation-prone" IAPP(8-16) and its non-amyloidogenic variants suggest its important role in fibrillogenesis and cytotoxicity of human amylin.Implications of peptide assemblies in amyloid diseases.
P2860
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P2860
Structure and membrane orientation of IAPP in its natively amidated form at physiological pH in a membrane environment
description
2011 nî lūn-bûn
@nan
2011 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2011 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
2011年の論文
@ja
2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
@wuu
name
Structure and membrane orienta ...... l pH in a membrane environment
@ast
Structure and membrane orienta ...... l pH in a membrane environment
@en
Structure and membrane orienta ...... l pH in a membrane environment
@nl
type
label
Structure and membrane orienta ...... l pH in a membrane environment
@ast
Structure and membrane orienta ...... l pH in a membrane environment
@en
Structure and membrane orienta ...... l pH in a membrane environment
@nl
prefLabel
Structure and membrane orienta ...... l pH in a membrane environment
@ast
Structure and membrane orienta ...... l pH in a membrane environment
@en
Structure and membrane orienta ...... l pH in a membrane environment
@nl
P2860
P3181
P1476
Structure and membrane orienta ...... l pH in a membrane environment
@en
P2093
Ravi Prakash Reddy Nanga
Subramanian Vivekanandan
P2860
P304
P3181
P356
10.1016/J.BBAMEM.2011.06.012
P407
P577
2011-06-23T00:00:00Z