Role of aggregation conditions in structure, stability, and toxicity of intermediates in the Abeta fibril formation pathway
about
Targeting the proper amyloid-beta neuronal toxins: a path forward for Alzheimer's disease immunotherapeuticsThe strain-encoded relationship between PrP replication, stability and processing in neurons is predictive of the incubation period of diseaseXanthene food dye, as a modulator of Alzheimer's disease amyloid-beta peptide aggregation and the associated impaired neuronal cell function.Suppressing mutation-induced protein aggregation in mammalian cells by mutating residues significantly displaced upon the original mutationCis-suppression to arrest protein aggregation in mammalian cells.A revisited folding reporter for quantitative assay of protein misfolding and aggregation in mammalian cells.Membrane interactions of a self-assembling model peptide that mimics the self-association, structure and toxicity of Abeta(1-40).Techniques for Monitoring Protein Misfolding and Aggregation in Vitro and in Living CellsA safe, blood-brain barrier permeable triphenylmethane dye inhibits amyloid-β neurotoxicity by generating nontoxic aggregatesTwo disaccharides and trimethylamine N-oxide affect Abeta aggregation differently, but all attenuate oligomer-induced membrane permeability.Kinetic study of beta-amyloid residue accessibility using reductive alkylation and mass spectrometry.Structural differences between Abeta(1-40) intermediate oligomers and fibrils elucidated by proteolytic fragmentation and hydrogen/deuterium exchange.Simultaneous monitoring of peptide aggregate distributions, structure, and kinetics using amide hydrogen exchange: application to Abeta(1-40) fibrillogenesisExploring the mechanism of beta-amyloid toxicity attenuation by multivalent sialic acid polymers through the use of mathematical models.Structure-function relationships of pre-fibrillar protein assemblies in Alzheimer's disease and related disordersSmall molecule microarrays enable the discovery of compounds that bind the Alzheimer's Aβ peptide and reduce its cytotoxicity.Elucidating the role of disulfide bond on amyloid formation and fibril reversibility of somatostatin-14: relevance to its storage and secretionA brief overview of amyloids and Alzheimer's disease.Isolating toxic insulin amyloid reactive species that lack β-sheets and have wide pH stabilityThe elusive nature and diagnostics of misfolded Aβ oligomers.Mammalian prions: tracking the infectious entitiesSoluble Aβ seeds are potent inducers of cerebral β-amyloid depositionInsights into Kinetics of Agitation-Induced Aggregation of Hen Lysozyme under Heat and Acidic Conditions from Various Spectroscopic Methods.High-affinity Anticalins with aggregation-blocking activity directed against the Alzheimer β-amyloid peptide.Effects of peptides derived from terminal modifications of the aβ central hydrophobic core on aβ fibrillization.Rationally Designed CeNP@MnMoS4 Core-Shell Nanoparticles for Modulating Multiple Facets of Alzheimer's Disease.Conformational differences between two amyloid β oligomers of similar size and dissimilar toxicity.A novel inhibitor of amyloid β (Aβ) peptide aggregation: from high throughput screening to efficacy in an animal model of Alzheimer disease.Systematic analysis of nucleation-dependent polymerization reveals new insights into the mechanism of amyloid self-assemblyNanofluidic biosensing for beta-amyloid detection using surface enhanced Raman spectroscopyBiochemical and biophysical features of both oligomer/fibril and cell membrane in amyloid cytotoxicity.Metal attenuating therapies in neurodegenerative disease.On the subject of rigor in the study of amyloid β-protein assembly.Structurally distinct toxicity inhibitors bind at common loci on β-amyloid fibril.The effect of concentration, temperature and stirring on hen egg white lysozyme amyloid formation.Structure-activity relationships in peptide modulators of β-amyloid protein aggregation: variation in α,α-disubstitution results in altered aggregate size and morphologyCan size alone explain some of the differences in toxicity between beta-amyloid oligomers and fibrils?Fibril fragmentation enhances amyloid cytotoxicity.Aromatic small molecules remodel toxic soluble oligomers of amyloid beta through three independent pathwaysMonitoring Alzheimer Amyloid Peptide Aggregation by EPR
P2860
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P2860
Role of aggregation conditions in structure, stability, and toxicity of intermediates in the Abeta fibril formation pathway
description
2007 nî lūn-bûn
@nan
2007 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2007 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
2007年の論文
@ja
2007年論文
@yue
2007年論文
@zh-hant
2007年論文
@zh-hk
2007年論文
@zh-mo
2007年論文
@zh-tw
2007年论文
@wuu
name
Role of aggregation conditions ...... Abeta fibril formation pathway
@ast
Role of aggregation conditions ...... Abeta fibril formation pathway
@en
type
label
Role of aggregation conditions ...... Abeta fibril formation pathway
@ast
Role of aggregation conditions ...... Abeta fibril formation pathway
@en
prefLabel
Role of aggregation conditions ...... Abeta fibril formation pathway
@ast
Role of aggregation conditions ...... Abeta fibril formation pathway
@en
P2860
P356
P1433
P1476
Role of aggregation conditions ...... Abeta fibril formation pathway
@en
P2093
Erik J Fernandez
Theresa A Good
P2860
P304
P356
10.1110/PS.062514807
P50
P577
2007-02-27T00:00:00Z