Monitoring protein assembly using quasielastic light scattering spectroscopy.
about
Structural Characterization of the E2 Domain of APL-1, a Caenorhabditis elegans Homolog of Human Amyloid Precursor Protein, and Its Heparin Binding SiteCrystal structure of Cu / Zn superoxide dismutase from Taenia solium reveals metal-mediated self-assemblyStructure-function relationships of pre-fibrillar protein assemblies in Alzheimer's disease and related disordersInhibitors of catalase-amyloid interactions protect cells from beta-amyloid-induced oxidative stress and toxicity.Nonamyloid aggregates arising from mature copper/zinc superoxide dismutases resemble those observed in amyotrophic lateral sclerosisAmyloid beta -protein (Abeta) assembly: Abeta 40 and Abeta 42 oligomerize through distinct pathways.Decreased stability and increased formation of soluble aggregates by immature superoxide dismutase do not account for disease severity in ALS.Characterization of the nanoscale properties of individual amyloid fibrilsA multi-pathway perspective on protein aggregation: implications for control of the rate and extent of amyloid formation.Increased T cell reactivity to amyloid beta protein in older humans and patients with Alzheimer diseaseQuantitative analysis of the time course of Aβ oligomerization and subsequent growth steps using tetramethylrhodamine-labeled AβBiophysical characterization of Abeta42 C-terminal fragments: inhibitors of Abeta42 neurotoxicity.Fibril fragmentation in amyloid assembly and cytotoxicity: when size matters.Sedimentation velocity analysis of flexible macromolecules: self-association and tangling of amyloid fibrils.Gly25-Ser26 amyloid β-protein structural isomorphs produce distinct Aβ42 conformational dynamics and assembly characteristics.The Aggregation Paths and Products of Aβ42 Dimers Are Distinct from Those of the Aβ42 Monomer.Amyloid fibril formation in microwell plates for screening of inhibitors.Possible role of each repeat structure of the microtubule-binding domain of the tau protein in in vitro aggregation.Formation of heat-induced cottonseed congossypin(7S) fibrils at pH 2.0.A cyclic KLVFF-derived peptide aggregation inhibitor induces the formation of less-toxic off-pathway amyloid-β oligomers.Ac-LPFFD-Th: A Trehalose-Conjugated Peptidomimetic as a Strong Suppressor of Amyloid-β Oligomer Formation and Cytotoxicity.
P2860
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P2860
Monitoring protein assembly using quasielastic light scattering spectroscopy.
description
1999 nî lūn-bûn
@nan
1999 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի հունվարին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
name
Monitoring protein assembly using quasielastic light scattering spectroscopy.
@ast
Monitoring protein assembly using quasielastic light scattering spectroscopy.
@en
type
label
Monitoring protein assembly using quasielastic light scattering spectroscopy.
@ast
Monitoring protein assembly using quasielastic light scattering spectroscopy.
@en
prefLabel
Monitoring protein assembly using quasielastic light scattering spectroscopy.
@ast
Monitoring protein assembly using quasielastic light scattering spectroscopy.
@en
P2093
P1476
Monitoring protein assembly using quasielastic light scattering spectroscopy.
@en
P2093
P304
P356
10.1016/S0076-6879(99)09029-1
P407
P577
1999-01-01T00:00:00Z