Amyloid beta-protein dimers rapidly form stable synaptotoxic protofibrils.
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The coexistence of an equal amount of Alzheimer's amyloid-β 40 and 42 forms structurally stable and toxic oligomers through a distinct pathwayThe Role of Amyloid-β Oligomers in Toxicity, Propagation, and ImmunotherapyMolecular basis of -amyloid oligomer recognition with a conformational antibody fragmentDirect observation of single amyloid-β(1-40) oligomers on live cells: binding and growth at physiological concentrationsProtective effects of positive lysosomal modulation in Alzheimer's disease transgenic mouse modelsNa, K-ATPase α3 is a death target of Alzheimer patient amyloid-β assembly.Large aggregates are the major soluble Aβ species in AD brain fractionated with density gradient ultracentrifugationStructural basis of β-amyloid-dependent synaptic dysfunctions.Alzheimer brain-derived amyloid β-protein impairs synaptic remodeling and memory consolidation.Tissue transglutaminase-mediated glutamine deamidation of beta-amyloid peptide increases peptide solubility, whereas enzymatic cross-linking and peptide fragmentation may serve as molecular triggers for rapid peptide aggregationα-synuclein reactive antibodies as diagnostic biomarkers in blood sera of Parkinson's disease patients.Design of β-amyloid aggregation inhibitors from a predicted structural motif.Amyloid-β(1-42) protofibrils stimulate a quantum of secreted IL-1β despite significant intracellular IL-1β accumulation in microglia.Multivariate analyses of amyloid-beta oligomer populations indicate a connection between pore formation and cytotoxicityA human monoclonal IgG that binds aβ assemblies and diverse amyloids exhibits anti-amyloid activities in vitro and in vivo.Human anti-Aβ IgGs target conformational epitopes on synthetic dimer assemblies and the AD brain-derived peptide.Bioluminescence imaging of Abeta deposition in bigenic mouse models of Alzheimer's disease.Two distinct amyloid beta-protein (Abeta) assembly pathways leading to oligomers and fibrils identified by combined fluorescence correlation spectroscopy, morphology, and toxicity analyses.Soluble amyloid beta-protein dimers isolated from Alzheimer cortex directly induce Tau hyperphosphorylation and neuritic degeneration.Membrane Incorporation, Channel Formation, and Disruption of Calcium Homeostasis by Alzheimer's β-Amyloid Protein.Insight into amyloid structure using chemical probes.Microglia constitute a barrier that prevents neurotoxic protofibrillar Aβ42 hotspots around plaquesProbing amyloid fibril growth by two-dimensional near-ultraviolet spectroscopySynergistic interactions between Alzheimer's Aβ40 and Aβ42 on the surface of primary neurons revealed by single molecule microscopy.Improvement of memory deficits and amyloid-β clearance in aged APP23 mice treated with a combination of anti-amyloid-β antibody and LXR agonistInteraction between prion protein and toxic amyloid β assemblies can be therapeutically targeted at multiple sitesDi-tyrosine cross-link decreases the collisional cross-section of aβ peptide dimers and trimers in the gas phase: an ion mobility study.Intracellular selection of peptide inhibitors that target disulphide-bridged Aβ42 oligomersA highly sensitive novel immunoassay specifically detects low levels of soluble Aβ oligomers in human cerebrospinal fluid.A monoclonal antibody against synthetic Aβ dimer assemblies neutralizes brain-derived synaptic plasticity-disrupting Aβ.Intrinsic determinants of Aβ(12-24) pH-dependent self-assembly revealed by combined computational and experimental studies.The Aβ oligomer hypothesis for synapse failure and memory loss in Alzheimer's disease.Submicromolar Aβ42 reduces hippocampal glutamate receptors and presynaptic markers in an aggregation-dependent manner.Soluble amyloid-β oligomers as synaptotoxins leading to cognitive impairment in Alzheimer's diseaseSoluble Aβ oligomer production and toxicity.IgG Conformer's Binding to Amyloidogenic Aggregates.Critical role of soluble amyloid-β for early hippocampal hyperactivity in a mouse model of Alzheimer's disease.Expression in drosophila of tandem amyloid β peptides provides insights into links between aggregation and neurotoxicityPurified and synthetic Alzheimer's amyloid beta (Aβ) prions.Isolated amyloid-β(1-42) protofibrils, but not isolated fibrils, are robust stimulators of microglia.
P2860
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P2860
Amyloid beta-protein dimers rapidly form stable synaptotoxic protofibrils.
description
2010 nî lūn-bûn
@nan
2010 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
name
Amyloid beta-protein dimers rapidly form stable synaptotoxic protofibrils.
@ast
Amyloid beta-protein dimers rapidly form stable synaptotoxic protofibrils.
@en
Amyloid beta-protein dimers rapidly form stable synaptotoxic protofibrils.
@nl
type
label
Amyloid beta-protein dimers rapidly form stable synaptotoxic protofibrils.
@ast
Amyloid beta-protein dimers rapidly form stable synaptotoxic protofibrils.
@en
Amyloid beta-protein dimers rapidly form stable synaptotoxic protofibrils.
@nl
prefLabel
Amyloid beta-protein dimers rapidly form stable synaptotoxic protofibrils.
@ast
Amyloid beta-protein dimers rapidly form stable synaptotoxic protofibrils.
@en
Amyloid beta-protein dimers rapidly form stable synaptotoxic protofibrils.
@nl
P2093
P2860
P1476
Amyloid beta-protein dimers rapidly form stable synaptotoxic protofibrils.
@en
P2093
Andrew J Nicoll
Brian O'Nuallain
Caroline E Herron
Darragh B Freir
Dominic M Walsh
Emmanuel Risse
John Collinge
Neil Ferguson
P2860
P304
14411-14419
P356
10.1523/JNEUROSCI.3537-10.2010
P407
P577
2010-10-01T00:00:00Z