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http://purl.uniprot.org/citations/11377421http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11377421http://www.w3.org/2000/01/rdf-schema#comment"CASK, a member of the membrane-associated guanylate kinase (MAGUK) superfamily, binds to the carboxyl-terminus of beta-neurexins on the intracellular side of the presynaptic membrane. The guanylate kinase-like (GUK) domains of MAGUKs lack kinase activities, but might be important for mediating specific protein-protein interaction. By a yeast two-hybrid approach, we identified an interaction between the GUK domain of CASK and the C2B domain of rabphilin3a, a presynaptic protein involved in synaptic vesicle exocytosis. The interaction was confirmed by in vitro GST pull-down and co-immunoprecipitation assays. It was proposed that presynaptic vesicles might be guided to the vicinity of points of exocytosis defined by beta-neurexins via the interaction between rabphilin3a-CASK-beta-neurexins."xsd:string
http://purl.uniprot.org/citations/11377421http://purl.org/dc/terms/identifier"doi:10.1016/s0014-5793(01)02450-4"xsd:string
http://purl.uniprot.org/citations/11377421http://purl.uniprot.org/core/author"Hu G."xsd:string
http://purl.uniprot.org/citations/11377421http://purl.uniprot.org/core/author"Liu A."xsd:string
http://purl.uniprot.org/citations/11377421http://purl.uniprot.org/core/author"Zhang Y."xsd:string
http://purl.uniprot.org/citations/11377421http://purl.uniprot.org/core/author"Luan Z."xsd:string
http://purl.uniprot.org/citations/11377421http://purl.uniprot.org/core/date"2001"xsd:gYear
http://purl.uniprot.org/citations/11377421http://purl.uniprot.org/core/name"FEBS Lett"xsd:string
http://purl.uniprot.org/citations/11377421http://purl.uniprot.org/core/pages"99-102"xsd:string
http://purl.uniprot.org/citations/11377421http://purl.uniprot.org/core/title"The scaffolding protein CASK mediates the interaction between rabphilin3a and beta-neurexins."xsd:string
http://purl.uniprot.org/citations/11377421http://purl.uniprot.org/core/volume"497"xsd:string
http://purl.uniprot.org/citations/11377421http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/11377421
http://purl.uniprot.org/citations/11377421http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/11377421
http://purl.uniprot.org/uniprot/#_Q16650-mappedCitation-11377421http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/11377421
http://purl.uniprot.org/uniprot/#_O14936-mappedCitation-11377421http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/11377421
http://purl.uniprot.org/uniprot/#_Q9Y2J0-mappedCitation-11377421http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/11377421
http://purl.uniprot.org/uniprot/O14936http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/11377421
http://purl.uniprot.org/uniprot/Q9Y2J0http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/11377421
http://purl.uniprot.org/uniprot/Q16650http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/11377421