Experimental characterization of disordered and ordered aggregates populated during the process of amyloid fibril formation.
about
Mechanisms of amyloid formation revealed by solution NMRMapping the structure of amyloid nucleation precursors by protein engineering kinetic analysis.Intermolecular structure determination of amyloid fibrils with magic-angle spinning and dynamic nuclear polarization NMR.Effects of surface interactions on peptide aggregate morphology.High-resolution MAS NMR analysis of PI3-SH3 amyloid fibrils: backbone conformation and implications for protofilament assembly and structure .Stepwise organization of the β-structure identifies key regions essential for the propagation and cytotoxicity of insulin amyloid fibrils.The C-terminal threonine of Aβ43 nucleates toxic aggregation via structural and dynamical changes in monomers and protofibrils.Elongated oligomers in beta2-microglobulin amyloid assembly revealed by ion mobility spectrometry-mass spectrometry.Designed α-sheet peptides inhibit amyloid formation by targeting toxic oligomers.Nonamyloid aggregates arising from mature copper/zinc superoxide dismutases resemble those observed in amyotrophic lateral sclerosisCrucial role of nonspecific interactions in amyloid nucleation.Mass spectrometry: come of age for structural and dynamical biology.Protein solubility and protein homeostasis: a generic view of protein misfolding disorders.High-resolution NMR characterization of low abundance oligomers of amyloid-β without purificationCharacterizing methyl-bearing side chain contacts and dynamics mediating amyloid β protofibril interactions using ¹³C(methyl)-DEST and lifetime line broadening.Quantitative analysis of the time course of Aβ oligomerization and subsequent growth steps using tetramethylrhodamine-labeled AβAcute induction of anomalous and amyloidogenic blood clotting by molecular amplification of highly substoichiometric levels of bacterial lipopolysaccharideAdvances in ion mobility spectrometry-mass spectrometry reveal key insights into amyloid assembly.Structure and dynamics of oligomeric intermediates in β2-microglobulin self-assembly.Structural, morphological, and functional diversity of amyloid oligomers.Methodological approaches and insights on protein aggregation in biological systems.Uncovering the Early Assembly Mechanism for Amyloidogenic β2-Microglobulin Using Cross-linking and Native Mass Spectrometry.Mapping amyloid-β(16-22) nucleation pathways using fluorescence lifetime imaging microscopy.The non-core regions of human lysozyme amyloid fibrils influence cytotoxicity.Conformational-Sensitive Fast Photochemical Oxidation of Proteins and Mass Spectrometry Characterize Amyloid Beta 1-42 AggregationConformational dynamics of α-synuclein: insights from mass spectrometry.Direct observation of minimum-sized amyloid fibrils using solution NMR spectroscopy.Dynamic diversity of synthetic supramolecular polymers in water as revealed by hydrogen/deuterium exchange.Early aggregation preceding the nucleation of insulin amyloid fibrils as monitored by small angle X-ray scattering.Comparative fibril formation of analogs corresponding to the (12-24) segment of the β-amyloid peptide.The α-sheet: a missing-in-action secondary structure?Co-existence of two different α-synuclein oligomers with different core structures determined by hydrogen/deuterium exchange mass spectrometry.Direct observation of oligomerization by single molecule fluorescence reveals a multi-step aggregation mechanism for the yeast prion protein Ure2.Josef Rudinger Memorial Lecture: Use of peptides to modulate protein-protein interactions.Direct Conversion of an Enzyme from Native-like to Amyloid-like Aggregates within Inclusion Bodies.Quantitative Characterization of Metastability and Heterogeneity of Amyloid Aggregates.Mass spectrometry and the amyloid problem--how far can we go in the gas phase?Interplay between the hydrophobic effect and dipole interactions in peptide aggregation at interfaces.Mass and charge distributions of amyloid fibers involved in neurodegenerative diseases: mapping heterogeneity and polymorphism.
P2860
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P2860
Experimental characterization of disordered and ordered aggregates populated during the process of amyloid fibril formation.
description
2009 nî lūn-bûn
@nan
2009 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
2009 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
2009年の論文
@ja
2009年論文
@yue
2009年論文
@zh-hant
2009年論文
@zh-hk
2009年論文
@zh-mo
2009年論文
@zh-tw
2009年论文
@wuu
name
Experimental characterization ...... s of amyloid fibril formation.
@ast
Experimental characterization ...... s of amyloid fibril formation.
@en
type
label
Experimental characterization ...... s of amyloid fibril formation.
@ast
Experimental characterization ...... s of amyloid fibril formation.
@en
prefLabel
Experimental characterization ...... s of amyloid fibril formation.
@ast
Experimental characterization ...... s of amyloid fibril formation.
@en
P2860
P50
P356
P1476
Experimental characterization ...... s of amyloid fibril formation.
@en
P2093
Margarida Gairí
P2860
P304
P356
10.1073/PNAS.0812227106
P407
P577
2009-04-28T00:00:00Z