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http://purl.uniprot.org/citations/8755482http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/8755482http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/8755482http://www.w3.org/2000/01/rdf-schema#comment"Chapsyn-110, a novel membrane-associated putative guanylate kinase (MAGUK) that binds directly to N-methyl-D-aspartate (NMDA) receptor and Shaker K+ channel subunits, is 70%-80% identical to, and shares an identical domain organization with, PSD-95/SAP90 and SAP97. In rat brain, chapsyn-110 protein shows a somatodendritic expression pattern that overlaps partly with PSD-95 but that contrasts with the axonal distribution of SAP97. Chapsyn-110 associates tightly with the postsynaptic density in brain, and mediates the clustering of both NMDA receptors and K+ channels in heterologous cells. Indeed, chapsyn-110 and PSD-95 can heteromultimerize with each other and are recruited into the same NMDA receptor and K+ channel clusters. Thus, chapsyn-110 and PSD-95 may interact at postsynaptic sites to form a multimeric scaffold for the clustering of receptors, ion channels, and associated signalling proteins."xsd:string
http://purl.uniprot.org/citations/8755482http://purl.org/dc/terms/identifier"doi:10.1016/s0896-6273(00)80284-6"xsd:string
http://purl.uniprot.org/citations/8755482http://purl.org/dc/terms/identifier"doi:10.1016/s0896-6273(00)80284-6"xsd:string
http://purl.uniprot.org/citations/8755482http://purl.uniprot.org/core/author"Kim E."xsd:string
http://purl.uniprot.org/citations/8755482http://purl.uniprot.org/core/author"Kim E."xsd:string
http://purl.uniprot.org/citations/8755482http://purl.uniprot.org/core/author"Sheng M."xsd:string
http://purl.uniprot.org/citations/8755482http://purl.uniprot.org/core/author"Sheng M."xsd:string
http://purl.uniprot.org/citations/8755482http://purl.uniprot.org/core/author"Cho K.-O."xsd:string
http://purl.uniprot.org/citations/8755482http://purl.uniprot.org/core/author"Cho K.-O."xsd:string
http://purl.uniprot.org/citations/8755482http://purl.uniprot.org/core/author"Rothschild A."xsd:string
http://purl.uniprot.org/citations/8755482http://purl.uniprot.org/core/author"Rothschild A."xsd:string
http://purl.uniprot.org/citations/8755482http://purl.uniprot.org/core/date"1996"xsd:gYear
http://purl.uniprot.org/citations/8755482http://purl.uniprot.org/core/date"1996"xsd:gYear
http://purl.uniprot.org/citations/8755482http://purl.uniprot.org/core/name"Neuron"xsd:string
http://purl.uniprot.org/citations/8755482http://purl.uniprot.org/core/name"Neuron"xsd:string
http://purl.uniprot.org/citations/8755482http://purl.uniprot.org/core/pages"103-113"xsd:string
http://purl.uniprot.org/citations/8755482http://purl.uniprot.org/core/pages"103-113"xsd:string
http://purl.uniprot.org/citations/8755482http://purl.uniprot.org/core/title"Heteromultimerization and NMDA receptor-clustering activity of Chapsyn-110, a member of the PSD-95 family of proteins."xsd:string
http://purl.uniprot.org/citations/8755482http://purl.uniprot.org/core/title"Heteromultimerization and NMDA receptor-clustering activity of Chapsyn-110, a member of the PSD-95 family of proteins."xsd:string
http://purl.uniprot.org/citations/8755482http://purl.uniprot.org/core/volume"17"xsd:string
http://purl.uniprot.org/citations/8755482http://purl.uniprot.org/core/volume"17"xsd:string
http://purl.uniprot.org/citations/8755482http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/8755482
http://purl.uniprot.org/citations/8755482http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/8755482