{"@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/1363670320504425344.json","@type":"Article","productIdentifier":[{"identifier":{"@type":"DOI","@value":"10.1093/oxfordjournals.jbchem.a123611"}},{"identifier":{"@type":"URI","@value":"http://academic.oup.com/jb/article-pdf/110/4/508/2363571/110-4-508.pdf"}},{"identifier":{"@type":"PMID","@value":"1838110"}}],"dc:title":[{"@value":"Role of Actin in the Myosin-Linked Ca2+-Regulation of ATP-Dependent Interaction between Actin and Myosin of a Lower Eukaryote, Physarum polycephalum1"}],"description":[{"notation":[{"@value":"Actin-activated ATPase activity of myosin from Physarum polycephalum decreases when it binds Ca2+ and increases when it loses Ca2+. This Ca-inhibition is observed with phosphorylated myosin [Kohama, K. (1990) Trend, Pharmacol. Sci. 11, 433-435]. The activity of dephosphorylated myosin remained at a low level both in the presence and absence of Ca2+, although Ca(2+)-binding ability was much the same as that of the phosphorylated myosin. The effect of phosphorylation has been studied at a conventional actin concentration, which is comparable with that of myosin by weight. When the concentration of actin was increased by 10 times, the dephosphorylated myosin became actin-activatable in the absence of Ca2+, and Ca-inhibition was recovered. As actin exists quite abundantly in non-muscle cells of Physarum, myosin phosphorylation plays virtually no role in regulating actin-myosin-ATP interaction in vivo. Physiologically the interaction may be regulated by Ca2+ by binding to and subsequent release from myosin. Latex beads coated by either phosphorylated or dephosphorylated myosin moved ATP-dependently on the actin cables of Characeae cells to the same extent in the absence of Ca2+, but the movement was abolished by increasing Ca2+. When the interaction was examined by monitoring the movement of actin filaments on myosin fixed on a coverslip, the movement and Ca-inhibition of the movement were detected with phosphorylated, not dephosphorylated, myosin [Okagaki, T., Higashi-Fujime, S.,Kohama, K. (1989) J. Biochem. 106, 955-957].(ABSTRACT TRUNCATED AT 250 WORDS)"}]}],"creator":[{"@id":"https://cir.nii.ac.jp/crid/1383670320504425345","@type":"Researcher","foaf:name":[{"@value":"Kazuhiro Kohama"}]},{"@id":"https://cir.nii.ac.jp/crid/1383670320504425344","@type":"Researcher","foaf:name":[{"@value":"Tadashi Kohno"}]},{"@id":"https://cir.nii.ac.jp/crid/1383670320504425346","@type":"Researcher","foaf:name":[{"@value":"Tsuyoshi Okagaki"}]},{"@id":"https://cir.nii.ac.jp/crid/1383670320504425347","@type":"Researcher","foaf:name":[{"@value":"Teruo Shimmen"}]}],"publication":{"publicationIdentifier":[{"@type":"EISSN","@value":"17562651"},{"@type":"PISSN","@value":"0021924X"},{"@type":"PISSN","@value":"https://id.crossref.org/issn/0021924X"}],"prism:publicationName":[{"@value":"The Journal of Biochemistry"}],"dc:publisher":[{"@value":"Oxford University Press (OUP)"}],"prism:publicationDate":"1991-10","prism:volume":"110","prism:number":"4","prism:startingPage":"508","prism:endingPage":"513"},"reviewed":"false","url":[{"@id":"http://academic.oup.com/jb/article-pdf/110/4/508/2363571/110-4-508.pdf"}],"createdAt":"2017-02-03","modifiedAt":"2017-08-23","foaf:topic":[{"@id":"https://cir.nii.ac.jp/all?q=Myosins","dc:title":"Myosins"},{"@id":"https://cir.nii.ac.jp/all?q=Actins","dc:title":"Actins"},{"@id":"https://cir.nii.ac.jp/all?q=Enzyme%20Activation","dc:title":"Enzyme Activation"},{"@id":"https://cir.nii.ac.jp/all?q=Kinetics","dc:title":"Kinetics"},{"@id":"https://cir.nii.ac.jp/all?q=Adenosine%20Triphosphate","dc:title":"Adenosine Triphosphate"},{"@id":"https://cir.nii.ac.jp/all?q=Physarum%20polycephalum","dc:title":"Physarum polycephalum"},{"@id":"https://cir.nii.ac.jp/all?q=Animals","dc:title":"Animals"},{"@id":"https://cir.nii.ac.jp/all?q=Calcium","dc:title":"Calcium"},{"@id":"https://cir.nii.ac.jp/all?q=Phosphorylation","dc:title":"Phosphorylation"}],"relatedProduct":[{"@id":"https://cir.nii.ac.jp/crid/1360567184372320256","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"Transport of single cells using an actin bundle–myosin bionanomotor transport system"}]},{"@id":"https://cir.nii.ac.jp/crid/1390282679123033856","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@language":"en","@value":"Calcium inhibition as an intracellular signal for actin–myosin interaction"}]}],"dataSourceIdentifier":[{"@type":"CROSSREF","@value":"10.1093/oxfordjournals.jbchem.a123611"},{"@type":"OPENAIRE","@value":"doi_dedup___::c9e6da07c44168b81188bddeb322323e"},{"@type":"CROSSREF","@value":"10.1088/0957-4484/22/24/245101_references_DOI_U7UuCJ0WZOceQIj6cVIFf92TeUi"},{"@type":"CROSSREF","@value":"10.2183/pjab.92.478_references_DOI_U7UuCJ0WZOceQIj6cVIFf92TeUi"}]}