{"@context":{"@vocab":"https://cir.nii.ac.jp/schema/1.0/","rdfs":"http://www.w3.org/2000/01/rdf-schema#","dc":"http://purl.org/dc/elements/1.1/","dcterms":"http://purl.org/dc/terms/","foaf":"http://xmlns.com/foaf/0.1/","prism":"http://prismstandard.org/namespaces/basic/2.0/","cinii":"http://ci.nii.ac.jp/ns/1.0/","datacite":"https://schema.datacite.org/meta/kernel-4/","ndl":"http://ndl.go.jp/dcndl/terms/","jpcoar":"https://github.com/JPCOAR/schema/blob/master/2.0/"},"@id":"https://cir.nii.ac.jp/crid/1363670318958140288.json","@type":"Article","productIdentifier":[{"identifier":{"@type":"DOI","@value":"10.1126/science.273.5280.1377"}},{"identifier":{"@type":"URI","@value":"https://www.science.org/doi/pdf/10.1126/science.273.5280.1377"}}],"dc:title":[{"@value":"Purification and Molecular Cloning of Plx1, a Cdc25-Regulatory Kinase from\n            <b>\n              <i>Xenopus</i>\n            </b>\n            Egg Extracts"}],"description":[{"type":"abstract","notation":[{"@value":"<jats:p>\n            Cdc2, the cyclin-dependent kinase that controls mitosis, is negatively regulated by phosphorylation on its threonine-14 and tyrosine-15 residues. Cdc25, the phosphatase that dephosphorylates both of these residues, undergoes activation and phosphorylation by multiple kinases at mitosis. Plx1, a kinase that associates with and phosphorylates the amino-terminal domain of Cdc25, was purified extensively from\n            <jats:italic>Xenopus</jats:italic>\n            egg extracts. Cloning of its complementary DNA revealed that Plx1 is related to the Polo family of protein kinases. Recombinant Plx1 phosphorylated Cdc25 and stimulated its activity in a purified system. Cdc25 phosphorylated by Plx1 reacted strongly with MPM-2, a monoclonal antibody to mitotic phosphoproteins. These studies indicate that Plx1 may participate in control of mitotic progression.\n          </jats:p>"}]}],"creator":[{"@id":"https://cir.nii.ac.jp/crid/1383670318958140288","@type":"Researcher","foaf:name":[{"@value":"Akiko Kumagai"}],"jpcoar:affiliationName":[{"@value":"Division of Biology, 216-76, Howard Hughes Medical Institute, California Institute of Technology, Pasadena, CA 91125, USA."}]},{"@id":"https://cir.nii.ac.jp/crid/1383670318958140289","@type":"Researcher","foaf:name":[{"@value":"William G. Dunphy"}],"jpcoar:affiliationName":[{"@value":"Division of Biology, 216-76, Howard Hughes Medical Institute, California Institute of Technology, Pasadena, CA 91125, USA."}]}],"publication":{"publicationIdentifier":[{"@type":"PISSN","@value":"00368075"},{"@type":"EISSN","@value":"10959203"}],"prism:publicationName":[{"@value":"Science"}],"dc:publisher":[{"@value":"American Association for the Advancement of Science (AAAS)"}],"prism:publicationDate":"1996-09-06","prism:volume":"273","prism:number":"5280","prism:startingPage":"1377","prism:endingPage":"1380"},"reviewed":"false","url":[{"@id":"https://www.science.org/doi/pdf/10.1126/science.273.5280.1377"}],"createdAt":"2006-10-27","modifiedAt":"2024-01-13","relatedProduct":[{"@id":"https://cir.nii.ac.jp/crid/1360283693122892160","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"Effect of <scp>AKT</scp>3 expression on <scp>MYC</scp>‐ and caspase‐8‐dependent apoptosis caused by polo‐like kinase inhibitors in <scp>HCT</scp> 116 cells"}]},{"@id":"https://cir.nii.ac.jp/crid/1360285712513122048","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"NFBD1/MDC1 Is Phosphorylated by PLK1 and Controls G2/M Transition through the Regulation of a TOPOIIα-Mediated Decatenation Checkpoint"}]},{"@id":"https://cir.nii.ac.jp/crid/1360565167340128896","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"LATS1/WARTS phosphorylates MYPT1 to counteract PLK1 and regulate mammalian mitotic progression"}]},{"@id":"https://cir.nii.ac.jp/crid/1360565170630762624","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"Calcium Signaling and Meiotic Exit at Fertilization in  Xenopus Egg"}]}],"dataSourceIdentifier":[{"@type":"CROSSREF","@value":"10.1126/science.273.5280.1377"},{"@type":"CROSSREF","@value":"10.1111/cas.13093_references_DOI_wFfMphJtaRl8POEeH0FLd7P95u"},{"@type":"CROSSREF","@value":"10.1371/journal.pone.0082744_references_DOI_wFfMphJtaRl8POEeH0FLd7P95u"},{"@type":"CROSSREF","@value":"10.1083/jcb.201110110_references_DOI_wFfMphJtaRl8POEeH0FLd7P95u"},{"@type":"CROSSREF","@value":"10.3390/ijms151018659_references_DOI_wFfMphJtaRl8POEeH0FLd7P95u"}]}