| http://purl.uniprot.org/citations/8384482 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/8384482 | http://www.w3.org/2000/01/rdf-schema#comment | "Protein kinase C (PKC) phosphorylated a synthetic peptide (CBP) that included the Thr-286 phosphorylation sequence and calmodulin binding domain of Ca2+/calmodulin-dependent protein kinase type II (CaM-kinase). Studies with a variety of truncated peptides suggested that the amino acid phosphorylated by PKC was Thr-286, the same amino acid that when autophosphorylated by Ca2+/calmodulin activation of CaM-kinase results in Ca2+/calmodulin-independent activity. These peptide studies also suggested that the C-terminal region of CBP is required to obtain maximal phosphorylation of Thr-286 by PKC. PKC also phosphorylated purified CaM-kinase from rat forebrain. Phosphopeptide analysis by one- and two-dimensional proteolytic maps of autophosphorylated CaM-kinase and CaM-kinase phosphorylated with PKC identified that there are both similar and unique sites phosphorylated. Phosphoamino acid analysis of CaM-kinase phosphorylated by PKC indicated that both Ser and Thr residues were phosphorylated. Even though Thr-286 of CaM-kinase appeared to be phosphorylated by PKC, no Ca2+/calmodulin-independent activity was detected, and, additionally, no significant change in Ca2+/CaM-dependent activation was detected. These results provide the first indication that these two important protein kinases may communicate directly through interenzyme phosphorylation."xsd:string |
| http://purl.uniprot.org/citations/8384482 | http://purl.org/dc/terms/identifier | "doi:10.1021/bi00062a024"xsd:string |
| http://purl.uniprot.org/citations/8384482 | http://purl.uniprot.org/core/author | "Waxham M.N."xsd:string |
| http://purl.uniprot.org/citations/8384482 | http://purl.uniprot.org/core/author | "Aronowski J."xsd:string |
| http://purl.uniprot.org/citations/8384482 | http://purl.uniprot.org/core/date | "1993"xsd:gYear |
| http://purl.uniprot.org/citations/8384482 | http://purl.uniprot.org/core/name | "Biochemistry"xsd:string |
| http://purl.uniprot.org/citations/8384482 | http://purl.uniprot.org/core/pages | "2923-2930"xsd:string |
| http://purl.uniprot.org/citations/8384482 | http://purl.uniprot.org/core/title | "Ca2+/calmodulin-dependent protein kinase II is phosphorylated by protein kinase C in vitro."xsd:string |
| http://purl.uniprot.org/citations/8384482 | http://purl.uniprot.org/core/volume | "32"xsd:string |
| http://purl.uniprot.org/citations/8384482 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/8384482 |
| http://purl.uniprot.org/citations/8384482 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/8384482 |
| http://purl.uniprot.org/uniprot/#_P11275-mappedCitation-8384482 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/8384482 |
| http://purl.uniprot.org/uniprot/P11275 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/8384482 |