Amyloid-beta oligomers increase the localization of prion protein at the cell surface.
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Hijacking PrP(c)-dependent signal transduction: when prions impair Aβ clearanceZebrafish prion protein PrP2 controls collective migration process during lateral line sensory system developmentNeurotoxicity of prion peptides mimicking the central domain of the cellular prion proteinPrion protein-mediated toxicity of amyloid-β oligomers requires lipid rafts and the transmembrane LRP1Effects of FlAsH/tetracysteine (TC) Tag on PrP proteolysis and PrPres formation by TC-scanning.The Hsp70/Hsp90 Chaperone Machinery in Neurodegenerative DiseasesAβ-dependent reduction of NCAM2-mediated synaptic adhesion contributes to synapse loss in Alzheimer's disease.The Aβ oligomer hypothesis for synapse failure and memory loss in Alzheimer's disease.Soluble amyloid-β oligomers as synaptotoxins leading to cognitive impairment in Alzheimer's diseasePrion protein at the crossroads of physiology and disease.Cellular prion protein is essential for oligomeric amyloid-β-induced neuronal cell death.α-Secretase-derived fragment of cellular prion, N1, protects against monomeric and oligomeric amyloid β (Aβ)-associated cell death.Disease-associated mutations in the prion protein impair laminin-induced process outgrowth and survivalPathogenic prions deviate PrP(C) signaling in neuronal cells and impair A-beta clearanceThe complex PrP(c)-Fyn couples human oligomeric Aβ with pathological tau changes in Alzheimer's disease.The cellular prion protein traps Alzheimer's Aβ in an oligomeric form and disassembles amyloid fibers.Alzheimer's amyloid-β oligomers rescue cellular prion protein induced tau reduction via the Fyn pathway.The Biological Function of the Prion Protein: A Cell Surface Scaffold of Signaling ModulesAllosteric function and dysfunction of the prion protein.Proteolytic processing of the prion protein in health and disease.Roles of endoproteolytic α-cleavage and shedding of the prion protein in neurodegeneration.Prion disease: a tale of folds and strains.Biophysical studies of the amyloid β-peptide: interactions with metal ions and small molecules.LRP/LR Antibody Mediated Rescuing of Amyloid-β-Induced Cytotoxicity is Dependent on PrPc in Alzheimer's Disease.Amyloid-β Oligomers Interact with Neurexin and Diminish Neurexin-mediated Excitatory Presynaptic Organization.Unraveling the neuroprotective mechanisms of PrP (C) in excitotoxicity.Regulation of Amyloid β Oligomer Binding to Neurons and Neurotoxicity by the Prion Protein-mGluR5 Complex.The heat shock response is modulated by and interferes with toxic effects of scrapie prion protein and amyloid β.Cellular prion protein mediates toxic signaling of amyloid beta.Prion protein gene in Alzheimer's disease.α-synuclein interacts with PrPC to induce cognitive impairment through mGluR5 and NMDAR2B.How many amyloid-β peptides can a neuron bind before it dies?Soluble Aβ aggregates can inhibit prion propagation.Increased prion protein processing and expression of metabotropic glutamate receptor 1 in a mouse model of Alzheimer's disease.Protein Misfolding in Prion and Prion-Like Diseases: Reconsidering a Required Role for Protein Loss-of-Function.The Amyloid-β Oligomer Hypothesis: Beginning of the Third Decade.LRP/LR specific antibody IgG1-iS18 impedes neurodegeneration in Alzheimer's disease mice.
P2860
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P2860
Amyloid-beta oligomers increase the localization of prion protein at the cell surface.
description
2011 nî lūn-bûn
@nan
2011年の論文
@ja
2011年学术文章
@wuu
2011年学术文章
@zh
2011年学术文章
@zh-cn
2011年学术文章
@zh-hans
2011年学术文章
@zh-my
2011年学术文章
@zh-sg
2011年學術文章
@yue
2011年學術文章
@zh-hant
name
Amyloid-beta oligomers increase the localization of prion protein at the cell surface.
@en
Amyloid-beta oligomers increase the localization of prion protein at the cell surface.
@nl
type
label
Amyloid-beta oligomers increase the localization of prion protein at the cell surface.
@en
Amyloid-beta oligomers increase the localization of prion protein at the cell surface.
@nl
prefLabel
Amyloid-beta oligomers increase the localization of prion protein at the cell surface.
@en
Amyloid-beta oligomers increase the localization of prion protein at the cell surface.
@nl
P2093
P50
P1476
Amyloid-beta oligomers increase the localization of prion protein at the cell surface.
@en
P2093
Ana Paula Wasilewska-Sampaio
Daisy Y-L Wong
Fabiana A Caetano
Fernanda G De Felice
Flavio H Beraldo
Ivana Souza
Pedro H F Hirata
R Jane Rylett
Sergio T Ferreira
Sofia Jürgensen
P304
P356
10.1111/J.1471-4159.2011.07225.X
P407
P50
P577
2011-03-23T00:00:00Z