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http://purl.uniprot.org/citations/24012003http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/24012003http://www.w3.org/2000/01/rdf-schema#comment"Soluble amyloid-β oligomers (Aβo) trigger Alzheimer's disease (AD) pathophysiology and bind with high affinity to cellular prion protein (PrP(C)). At the postsynaptic density (PSD), extracellular Aβo bound to lipid-anchored PrP(C) activates intracellular Fyn kinase to disrupt synapses. Here, we screened transmembrane PSD proteins heterologously for the ability to couple Aβo-PrP(C) with Fyn. Only coexpression of the metabotropic glutamate receptor, mGluR5, allowed PrP(C)-bound Aβo to activate Fyn. PrP(C) and mGluR5 interact physically, and cytoplasmic Fyn forms a complex with mGluR5. Aβo-PrP(C) generates mGluR5-mediated increases of intracellular calcium in Xenopus oocytes and in neurons, and the latter is also driven by human AD brain extracts. In addition, signaling by Aβo-PrP(C)-mGluR5 complexes mediates eEF2 phosphorylation and dendritic spine loss. For mice expressing familial AD transgenes, mGluR5 antagonism reverses deficits in learning, memory, and synapse density. Thus, Aβo-PrP(C) complexes at the neuronal surface activate mGluR5 to disrupt neuronal function."xsd:string
http://purl.uniprot.org/citations/24012003http://purl.org/dc/terms/identifier"doi:10.1016/j.neuron.2013.06.036"xsd:string
http://purl.uniprot.org/citations/24012003http://purl.uniprot.org/core/author"Takahashi H."xsd:string
http://purl.uniprot.org/citations/24012003http://purl.uniprot.org/core/author"Wisniewski T."xsd:string
http://purl.uniprot.org/citations/24012003http://purl.uniprot.org/core/author"Koleske A.J."xsd:string
http://purl.uniprot.org/citations/24012003http://purl.uniprot.org/core/author"Stagi M."xsd:string
http://purl.uniprot.org/citations/24012003http://purl.uniprot.org/core/author"Strittmatter S.M."xsd:string
http://purl.uniprot.org/citations/24012003http://purl.uniprot.org/core/author"Um J.W."xsd:string
http://purl.uniprot.org/citations/24012003http://purl.uniprot.org/core/author"Vortmeyer A."xsd:string
http://purl.uniprot.org/citations/24012003http://purl.uniprot.org/core/author"Nygaard H.B."xsd:string
http://purl.uniprot.org/citations/24012003http://purl.uniprot.org/core/author"Kostylev M."xsd:string
http://purl.uniprot.org/citations/24012003http://purl.uniprot.org/core/author"Gunther E.C."xsd:string
http://purl.uniprot.org/citations/24012003http://purl.uniprot.org/core/author"Heiss J.K."xsd:string
http://purl.uniprot.org/citations/24012003http://purl.uniprot.org/core/author"Kaufman A.C."xsd:string
http://purl.uniprot.org/citations/24012003http://purl.uniprot.org/core/author"Kerrisk M.E."xsd:string
http://purl.uniprot.org/citations/24012003http://purl.uniprot.org/core/date"2013"xsd:gYear
http://purl.uniprot.org/citations/24012003http://purl.uniprot.org/core/name"Neuron"xsd:string
http://purl.uniprot.org/citations/24012003http://purl.uniprot.org/core/pages"887-902"xsd:string
http://purl.uniprot.org/citations/24012003http://purl.uniprot.org/core/title"Metabotropic glutamate receptor 5 is a coreceptor for Alzheimer abeta oligomer bound to cellular prion protein."xsd:string
http://purl.uniprot.org/citations/24012003http://purl.uniprot.org/core/volume"79"xsd:string
http://purl.uniprot.org/citations/24012003http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/24012003
http://purl.uniprot.org/citations/24012003http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/24012003
http://purl.uniprot.org/uniprot/P05067#attribution-980F2CAF8288F2906A3B8B42AE8DC31Ahttp://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/24012003
http://purl.uniprot.org/uniprot/P41594#attribution-3E0309D65F32142215D172E203EEF48Bhttp://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/24012003