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http://purl.uniprot.org/citations/7877986http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/7877986http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/7877986http://www.w3.org/2000/01/rdf-schema#comment"Glutamate receptor ion channels are colocalized in postsynaptic densities with Ca2+/calmodulin-dependent protein kinase II (CaM-kinase II), which can phosphorylate and strongly enhance non-N-methyl-D-aspartate (NMDA) glutamate receptor current. In this study, CaM-kinase II enhanced kainate currents of expressed glutamate receptor 6 in 293 cells and of wild-type glutamate receptor 1, but not the Ser-627 to Ala mutant, in Xenopus oocytes. A synthetic peptide corresponding to residues 620-638 in GluR1 was phosphorylated in vitro by CaM-kinase II but not by cAMP-dependent protein kinase or protein kinase C. The 32P-labeled peptide map of this synthetic peptide appears to be the same as the two-dimensional peptide map of alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionate (AMPA) glutamate receptors phosphorylated in cultured hippocampal neurons by CaM-kinase II described elsewhere. This CaM-kinase II regulatory phosphorylation site is conserved in all AMPA/kainate-type glutamate receptors, and its phosphorylation may be important in enhancing postsynaptic responsiveness as occurs during synaptic plasticity."xsd:string
http://purl.uniprot.org/citations/7877986http://purl.org/dc/terms/identifier"doi:10.1073/pnas.92.5.1376"xsd:string
http://purl.uniprot.org/citations/7877986http://purl.org/dc/terms/identifier"doi:10.1073/pnas.92.5.1376"xsd:string
http://purl.uniprot.org/citations/7877986http://purl.uniprot.org/core/author"Brickey D.A."xsd:string
http://purl.uniprot.org/citations/7877986http://purl.uniprot.org/core/author"Brickey D.A."xsd:string
http://purl.uniprot.org/citations/7877986http://purl.uniprot.org/core/author"Soderling T.R."xsd:string
http://purl.uniprot.org/citations/7877986http://purl.uniprot.org/core/author"Soderling T.R."xsd:string
http://purl.uniprot.org/citations/7877986http://purl.uniprot.org/core/author"Derkach V.A."xsd:string
http://purl.uniprot.org/citations/7877986http://purl.uniprot.org/core/author"Derkach V.A."xsd:string
http://purl.uniprot.org/citations/7877986http://purl.uniprot.org/core/author"Vissavajjhala P."xsd:string
http://purl.uniprot.org/citations/7877986http://purl.uniprot.org/core/author"Vissavajjhala P."xsd:string
http://purl.uniprot.org/citations/7877986http://purl.uniprot.org/core/author"Yakel J.L."xsd:string
http://purl.uniprot.org/citations/7877986http://purl.uniprot.org/core/author"Yakel J.L."xsd:string
http://purl.uniprot.org/citations/7877986http://purl.uniprot.org/core/date"1995"xsd:gYear
http://purl.uniprot.org/citations/7877986http://purl.uniprot.org/core/date"1995"xsd:gYear
http://purl.uniprot.org/citations/7877986http://purl.uniprot.org/core/name"Proc. Natl. Acad. Sci. U.S.A."xsd:string
http://purl.uniprot.org/citations/7877986http://purl.uniprot.org/core/name"Proc. Natl. Acad. Sci. U.S.A."xsd:string
http://purl.uniprot.org/citations/7877986http://purl.uniprot.org/core/pages"1376-1380"xsd:string
http://purl.uniprot.org/citations/7877986http://purl.uniprot.org/core/pages"1376-1380"xsd:string
http://purl.uniprot.org/citations/7877986http://purl.uniprot.org/core/title"Identification of a Ca2+/calmodulin-dependent protein kinase II regulatory phosphorylation site in non-N-methyl-D-aspartate glutamate receptors."xsd:string
http://purl.uniprot.org/citations/7877986http://purl.uniprot.org/core/title"Identification of a Ca2+/calmodulin-dependent protein kinase II regulatory phosphorylation site in non-N-methyl-D-aspartate glutamate receptors."xsd:string
http://purl.uniprot.org/citations/7877986http://purl.uniprot.org/core/volume"92"xsd:string
http://purl.uniprot.org/citations/7877986http://purl.uniprot.org/core/volume"92"xsd:string