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http://purl.uniprot.org/citations/16025111http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16025111http://www.w3.org/2000/01/rdf-schema#comment"Amyloid-beta peptide is elevated in the brains of patients with Alzheimer disease and is believed to be causative in the disease process. Amyloid-beta reduces glutamatergic transmission and inhibits synaptic plasticity, although the underlying mechanisms are unknown. We found that application of amyloid-beta promoted endocytosis of NMDA receptors in cortical neurons. In addition, neurons from a genetic mouse model of Alzheimer disease expressed reduced amounts of surface NMDA receptors. Reducing amyloid-beta by treating neurons with a gamma-secretase inhibitor restored surface expression of NMDA receptors. Consistent with these data, amyloid-beta application produced a rapid and persistent depression of NMDA-evoked currents in cortical neurons. Amyloid-beta-dependent endocytosis of NMDA receptors required the alpha-7 nicotinic receptor, protein phosphatase 2B (PP2B) and the tyrosine phosphatase STEP. Dephosphorylation of the NMDA receptor subunit NR2B at Tyr1472 correlated with receptor endocytosis. These data indicate a new mechanism by which amyloid-beta can cause synaptic dysfunction and contribute to Alzheimer disease pathology."xsd:string
http://purl.uniprot.org/citations/16025111http://purl.org/dc/terms/identifier"doi:10.1038/nn1503"xsd:string
http://purl.uniprot.org/citations/16025111http://purl.uniprot.org/core/author"Greengard P."xsd:string
http://purl.uniprot.org/citations/16025111http://purl.uniprot.org/core/author"Nairn A.C."xsd:string
http://purl.uniprot.org/citations/16025111http://purl.uniprot.org/core/author"Paul S."xsd:string
http://purl.uniprot.org/citations/16025111http://purl.uniprot.org/core/author"Choi E.Y."xsd:string
http://purl.uniprot.org/citations/16025111http://purl.uniprot.org/core/author"Salter M.W."xsd:string
http://purl.uniprot.org/citations/16025111http://purl.uniprot.org/core/author"Snyder E.M."xsd:string
http://purl.uniprot.org/citations/16025111http://purl.uniprot.org/core/author"Lombroso P.J."xsd:string
http://purl.uniprot.org/citations/16025111http://purl.uniprot.org/core/author"Moran T."xsd:string
http://purl.uniprot.org/citations/16025111http://purl.uniprot.org/core/author"Nong Y."xsd:string
http://purl.uniprot.org/citations/16025111http://purl.uniprot.org/core/author"Gouras G.K."xsd:string
http://purl.uniprot.org/citations/16025111http://purl.uniprot.org/core/author"Almeida C.G."xsd:string
http://purl.uniprot.org/citations/16025111http://purl.uniprot.org/core/date"2005"xsd:gYear
http://purl.uniprot.org/citations/16025111http://purl.uniprot.org/core/name"Nat Neurosci"xsd:string
http://purl.uniprot.org/citations/16025111http://purl.uniprot.org/core/pages"1051-1058"xsd:string
http://purl.uniprot.org/citations/16025111http://purl.uniprot.org/core/title"Regulation of NMDA receptor trafficking by amyloid-beta."xsd:string
http://purl.uniprot.org/citations/16025111http://purl.uniprot.org/core/volume"8"xsd:string
http://purl.uniprot.org/citations/16025111http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/16025111
http://purl.uniprot.org/citations/16025111http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/16025111
http://purl.uniprot.org/uniprot/P12023#attribution-D16CFB5E844D13ADCACB9B0694762477http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/16025111
http://purl.uniprot.org/uniprot/P49582#attribution-D16CFB5E844D13ADCACB9B0694762477http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/16025111
http://purl.uniprot.org/uniprot/P35438#attribution-2C982BC85B5851C36DACAF2F65A8763Chttp://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/16025111
http://purl.uniprot.org/uniprot/P54830#attribution-D16CFB5E844D13ADCACB9B0694762477http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/16025111