{"@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/1361699994580723072.json","@type":"Article","productIdentifier":[{"identifier":{"@type":"DOI","@value":"10.1016/s0021-9258(18)43938-5"}},{"identifier":{"@type":"URI","@value":"https://api.elsevier.com/content/article/PII:S0021925818439385?httpAccept=text/xml"}},{"identifier":{"@type":"URI","@value":"https://api.elsevier.com/content/article/PII:S0021925818439385?httpAccept=text/plain"}},{"identifier":{"@type":"PMID","@value":"7961961"}}],"dc:title":[{"@value":"Mycalolide B, a novel actin depolymerizing agent."}],"description":[{"notation":[{"@value":"We investigated the effects of a novel marine toxin, mycalolide B, on actin polymerization and actin-activated myosin Mg(2+)-ATPase activity using purified actin and myosin from rabbit skeletal muscle. The results were compared with cytochalasin D which inhibits actin polymerization by binding to the barbed end of F-actin. By monitoring fluorescent intensity of pyrenyl-actin, mycalolide B did not accelerate actin polymerization but quickly depolymerized F-actin, whereas cytochalasin D accelerated actin nucleation and depolymerized F-actin at slower rate. The kinetics of depolymerization suggest that mycalolide B severs F-actin. The relationship between the concentration of total actin and F-actin at different concentration of mycalolide B suggests that mycalolide B forms 1:1 complex with G-actin. Viscometry and electron microscopic observation further suggest that actin filament was depolymerized by mycalolide B. Unlike cytochalasin D, furthermore, mycalolide B suppressed actin-activated myosin Mg(2+)-ATPase activity. We concluded that mycalolide B severs F-actin and sequesters G-actin and may serve as a novel pharmacological tool for analyzing actin-mediated cell functions."}]}],"creator":[{"@id":"https://cir.nii.ac.jp/crid/1380007593047004800","@type":"Researcher","foaf:name":[{"@value":"S Saito"}]},{"@id":"https://cir.nii.ac.jp/crid/1381699994580723076","@type":"Researcher","foaf:name":[{"@value":"S Watabe"}]},{"@id":"https://cir.nii.ac.jp/crid/1381699994580723073","@type":"Researcher","foaf:name":[{"@value":"H Ozaki"}]},{"@id":"https://cir.nii.ac.jp/crid/1381699994580723072","@type":"Researcher","foaf:name":[{"@value":"N Fusetani"}]},{"@id":"https://cir.nii.ac.jp/crid/1381699994580723074","@type":"Researcher","foaf:name":[{"@value":"H Karaki"}]}],"publication":{"publicationIdentifier":[{"@type":"PISSN","@value":"00219258"},{"@type":"PISSN","@value":"http://id.crossref.org/issn/00219258"},{"@type":"PISSN","@value":"https://id.crossref.org/issn/00219258"}],"prism:publicationName":[{"@value":"Journal of Biological Chemistry"}],"dc:publisher":[{"@value":"Elsevier BV"}],"prism:publicationDate":"1994-11","prism:volume":"269","prism:number":"47","prism:startingPage":"29710","prism:endingPage":"29714"},"reviewed":"false","dcterms:accessRights":"http://purl.org/coar/access_right/c_abf2","dc:rights":["https://www.elsevier.com/tdm/userlicense/1.0/","https://www.elsevier.com/legal/tdmrep-license","http://creativecommons.org/licenses/by/4.0/"],"url":[{"@id":"https://api.elsevier.com/content/article/PII:S0021925818439385?httpAccept=text/xml"},{"@id":"https://api.elsevier.com/content/article/PII:S0021925818439385?httpAccept=text/plain"}],"createdAt":"2021-01-05","modifiedAt":"2025-09-18","foaf:topic":[{"@id":"https://cir.nii.ac.jp/all?q=Actins","dc:title":"Actins"},{"@id":"https://cir.nii.ac.jp/all?q=Porifera","dc:title":"Porifera"},{"@id":"https://cir.nii.ac.jp/all?q=Kinetics","dc:title":"Kinetics"},{"@id":"https://cir.nii.ac.jp/all?q=Microscopy,%20Electron","dc:title":"Microscopy, Electron"},{"@id":"https://cir.nii.ac.jp/all?q=Biopolymers","dc:title":"Biopolymers"},{"@id":"https://cir.nii.ac.jp/all?q=Animals","dc:title":"Animals"},{"@id":"https://cir.nii.ac.jp/all?q=Marine%20Toxins","dc:title":"Marine Toxins"},{"@id":"https://cir.nii.ac.jp/all?q=Rabbits","dc:title":"Rabbits"},{"@id":"https://cir.nii.ac.jp/all?q=Muscle,%20Skeletal","dc:title":"Muscle, Skeletal"},{"@id":"https://cir.nii.ac.jp/all?q=Oxazoles","dc:title":"Oxazoles"}],"relatedProduct":[{"@id":"https://cir.nii.ac.jp/crid/1050001202640336896","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@language":"en","@value":"Analysis of the aplyronine A-induced protein-protein interaction between actin and tubulin by surface plasmon resonance"}]},{"@id":"https://cir.nii.ac.jp/crid/1050001202661292032","@type":"Article","resourceType":"学術雑誌論文(journal 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