The amyloid formation mechanism in human IAPP: dimers have β-strand monomer-monomer interfaces
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New Insights from Sum Frequency Generation Vibrational Spectroscopy into the Interactions of Islet Amyloid Polypeptides with Lipid MembranesSecondary Structure of Rat and Human Amylin across Force FieldsIntegrating mass spectrometry of intact protein complexes into structural proteomicsNovel insights into protein misfolding diseases revealed by ion mobility-mass spectrometry.Protein structural and surface water rearrangement constitute major events in the earliest aggregation stages of tau.α-helical structures drive early stages of self-assembly of amyloidogenic amyloid polypeptide aggregate formation in membranes.Amyloidogenic peptide oligomer accumulation in autophagy-deficient β cells induces diabetes.Defining the molecular basis of amyloid inhibitors: human islet amyloid polypeptide-insulin interactions.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.Ion mobility spectrometry-mass spectrometry defines the oligomeric intermediates in amylin amyloid formation and the mode of action of inhibitorsMutational analysis of preamyloid intermediates: the role of his-tyr interactions in islet amyloid formationStructure-Based Small Molecule Modulation of a Pre-Amyloid State: Pharmacological Enhancement of IAPP Membrane-Binding and Toxicity.Rapid assessment of human amylin aggregation and its inhibition by copper(II) ions by laser ablation electrospray ionization mass spectrometry with ion mobility separationZ-Phe-Ala-diazomethylketone (PADK) disrupts and remodels early oligomer states of the Alzheimer disease Aβ42 protein.Role of β-hairpin formation in aggregation: the self-assembly of the amyloid-β(25-35) peptide.Insights into the consequences of co-polymerisation in the early stages of IAPP and Aβ peptide assembly from mass spectrometry.Solvent-induced tuning of internal structure in a protein amyloid protofibril.Analysis of the ability of pramlintide to inhibit amyloid formation by human islet amyloid polypeptide reveals a balance between optimal recognition and reduced amyloidogenicity.Mechanism of Inhibition of Human Islet Amyloid Polypeptide-Induced Membrane Damage by a Small Organic Fluorogen.Early Events in the Amyloid Formation of the A546T Mutant of Transforming Growth Factor β-Induced Protein in Corneal Dystrophies Compared to the Nonfibrillating R555W and R555Q MutantsAdsorption and Orientation of Human Islet Amyloid Polypeptide (hIAPP) Monomer at Anionic Lipid Bilayers: Implications for Membrane-Mediated Aggregationα-helix to β-hairpin transition of human amylin monomer.Initiation of assembly of tau(273-284) and its ΔK280 mutant: an experimental and computational study.Islet amyloid: from fundamental biophysics to mechanisms of cytotoxicity.Effect of proline mutations on the monomer conformations of amylin.Cyclic N-terminal loop of amylin forms non amyloid fibers.Conformational Ensemble of hIAPP Dimer: Insight into the Molecular Mechanism by which a Green Tea Extract inhibits hIAPP Aggregation.Effect of Post-Translational Amidation on Islet Amyloid Polypeptide Conformational Ensemble: Implications for Its Aggregation Early Steps.Aggregation of islet amyloid polypeptide: from physical chemistry to cell biology.Advances in ion mobility spectrometry-mass spectrometry reveal key insights into amyloid assembly.Mechanistic Contributions of Biological Cofactors in Islet Amyloid Polypeptide Amyloidogenesis.An Account of Amyloid Oligomers: Facts and Figures Obtained from Experiments and Simulations.2DIR spectroscopy of human amylin fibrils reflects stable β-sheet structure.Rational design of an orthosteric regulator of hIAPP aggregation.The role of copper(II) in the aggregation of human amylin.An infrared spectroscopy approach to follow β-sheet formation in peptide amyloid assemblies.Implications of peptide assemblies in amyloid diseases.β-Hairpin of Islet Amyloid Polypeptide Bound to an Aggregation InhibitorConformational dynamics of α-synuclein: insights from mass spectrometry.Structural Properties of Human IAPP Dimer in Membrane Environment Studied by All-Atom Molecular Dynamics Simulations.
P2860
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P2860
The amyloid formation mechanism in human IAPP: dimers have β-strand monomer-monomer interfaces
description
2011 nî lūn-bûn
@nan
2011 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
2011 թվականի ապրիլին 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
The amyloid formation mechanis ...... and monomer-monomer interfaces
@ast
The amyloid formation mechanis ...... and monomer-monomer interfaces
@en
The amyloid formation mechanis ...... and monomer-monomer interfaces
@nl
type
label
The amyloid formation mechanis ...... and monomer-monomer interfaces
@ast
The amyloid formation mechanis ...... and monomer-monomer interfaces
@en
The amyloid formation mechanis ...... and monomer-monomer interfaces
@nl
prefLabel
The amyloid formation mechanis ...... and monomer-monomer interfaces
@ast
The amyloid formation mechanis ...... and monomer-monomer interfaces
@en
The amyloid formation mechanis ...... and monomer-monomer interfaces
@nl
P2093
P2860
P356
P1476
The amyloid formation mechanis ...... and monomer-monomer interfaces
@en
P2093
Joan-Emma Shea
Michael T Bowers
Nicholas F Dupuis
P2860
P304
P356
10.1021/JA1081537
P407
P50
P577
2011-04-25T00:00:00Z