Elucidating amyloid beta-protein folding and assembly: A multidisciplinary approach.
about
Amyloid beta-protein monomer folding: free-energy surfaces reveal alloform-specific differencesChemical cross-linking and native mass spectrometry: A fruitful combination for structural biologyDimer formation enhances structural differences between amyloid β-protein (1-40) and (1-42): an explicit-solvent molecular dynamics studyModulating self-assembly of amyloidogenic proteins as a therapeutic approach for neurodegenerative diseases: strategies and mechanismsContrasting effects of nanoparticle-protein attraction on amyloid aggregationAmyloid β-Protein Assembly: The Effect of Molecular Tweezers CLR01 and CLR03Environmental conditions affect the kinetics of nucleation of amyloid fibrils and determine their morphology.Human islet amyloid polypeptide monomers form ordered beta-hairpins: a possible direct amyloidogenic precursor.Structural reorganisation and potential toxicity of oligomeric species formed during the assembly of amyloid fibrils.A resorcinarene for inhibition of Aβ fibrillation.The importance of hydrogen bonding between the glutamine side chains to the formation of amyloid VQIVYK parallel beta-sheets: an ONIOM DFT/AM1 study.Atomistic simulations of the effects of polyglutamine chain length and solvent quality on conformational equilibria and spontaneous homodimerizationHigh-resolution conformation and backbone dynamics of a soluble aggregate of apomyoglobin119.Globular state in the oligomers formed by Abeta peptides.Effects of the English (H6R) and Tottori (D7N) familial Alzheimer disease mutations on amyloid beta-protein assembly and toxicity.Mechanistic investigation of the inhibition of Abeta42 assembly and neurotoxicity by Abeta42 C-terminal fragmentsKinetics of amyloid beta monomer-to-oligomer exchange by NMR relaxation.Atomic-resolution dynamics on the surface of amyloid-β protofibrils probed by solution NMRSynthetic Flavonoids, Aminoisoflavones: Interaction and Reactivity with Metal-Free and Metal-Associated Amyloid-β SpeciesExploring the role of hydration and confinement in the aggregation of amyloidogenic peptides Aβ(16-22) and Sup35(7-13) in AOT reverse micellesBinding of nonsteroidal anti-inflammatory drugs to Abeta fibrilAmyloid beta-protein assembly and Alzheimer disease.Gas-phase structure of amyloid-β (12-28) peptide investigated by infrared spectroscopy, electron capture dissociation and ion mobility mass spectrometry.Structural basis for Aβ1–42 toxicity inhibition by Aβ C-terminal fragments: discrete molecular dynamics study.Deconvoluting Protein (Un)folding Structural Ensembles Using X-Ray Scattering, Nuclear Magnetic Resonance Spectroscopy and Molecular Dynamics Simulation.Structural and mechanistic commonalities of amyloid-β and the prion proteinRole of electrostatic interactions in amyloid beta-protein (A beta) oligomer formation: a discrete molecular dynamics studyZ-Phe-Ala-diazomethylketone (PADK) disrupts and remodels early oligomer states of the Alzheimer disease Aβ42 protein.Dynamics of metastable β-hairpin structures in the folding nucleus of amyloid β-protein.The inverted free energy landscape of an intrinsically disordered peptide by simulations and experiments.Protein anisotropy turns solubility on its head.Mechanisms of protein fibril formation: nucleated polymerization with competing off-pathway aggregationFolding of pig gastric mucin non-glycosylated domains: a discrete molecular dynamics study.Experimental and computational studies reveal an alternative supramolecular structure for fmoc-dipeptide self-assembly.Stabilizing Off-pathway Oligomers by Polyphenol Nanoassemblies for IAPP Aggregation InhibitionMonomeric Aβ(1-40) and Aβ(1-42) Peptides in Solution Adopt Very Similar Ramachandran Map Distributions That Closely Resemble Random Coil.Opposing Effects of Cucurbit[7]uril and 1,2,3,4,6-Penta-O-galloyl-β-d-glucopyranose on Amyloid β25-35 Assembly.Reactivity of diphenylpropynone derivatives toward metal-associated amyloid-β species.Folding and assembly of large macromolecular complexes monitored by hydrogen-deuterium exchange and mass spectrometry.Mechanism of C-Terminal Fragments of Amyloid β-Protein as Aβ Inhibitors: Do C-Terminal Interactions Play a Key Role in Their Inhibitory Activity?
P2860
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P2860
Elucidating amyloid beta-protein folding and assembly: A multidisciplinary approach.
description
2006 nî lūn-bûn
@nan
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
2006年论文
@zh
2006年论文
@zh-cn
name
Elucidating amyloid beta-protein folding and assembly: A multidisciplinary approach.
@ast
Elucidating amyloid beta-protein folding and assembly: A multidisciplinary approach.
@en
type
label
Elucidating amyloid beta-protein folding and assembly: A multidisciplinary approach.
@ast
Elucidating amyloid beta-protein folding and assembly: A multidisciplinary approach.
@en
prefLabel
Elucidating amyloid beta-protein folding and assembly: A multidisciplinary approach.
@ast
Elucidating amyloid beta-protein folding and assembly: A multidisciplinary approach.
@en
P2093
P50
P356
P1476
Elucidating amyloid beta-protein folding and assembly: A multidisciplinary approach.
@en
P2093
Andrij Baumketner
David B Teplow
Joan-Emma Shea
Michael T Bowers
Summer Bernstein
Thomas Wyttenbach
P304
P356
10.1021/AR050063S
P407
P577
2006-09-01T00:00:00Z