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dc.contributor.authorUENO, Sayoja
dc.contributor.authorYANAGITA, Ryo C.ja
dc.contributor.authorMURAKAMI, Kazumaja
dc.contributor.authorMURAKAMI, Akiraja
dc.contributor.authorTOKUDA, Harukunija
dc.contributor.authorSUZUKI, Nobutakaja
dc.contributor.authorFUJIWARA, Takeshija
dc.contributor.authorIRIE, Kazuhiroja
dc.contributor.alternative入江, 一浩ja
dc.date.accessioned2013-08-02T05:04:25Z-
dc.date.available2013-08-02T05:04:25Z-
dc.date.issued2012-05-
dc.identifier.issn0916-8451ja
dc.identifier.urihttp://hdl.handle.net/2433/176984-
dc.description.abstractSix bryostatins were isolated from Japanese bryozoan by evaluating their binding to the C1B domain of protein kinase Cδ (PKCδ). Structure-activity studies of bryostatins 4, 10, and 14 suggested that the ester group at C20 was not necessary for binding to and activating PKCδ. These bryostatins showed significant anti-tumor-promoting activity in induction tests with the Epstein-Barr virus early antigen.ja
dc.format.mimetypeapplication/pdfja
dc.language.isoengja
dc.publisherJapan Society for Bioscience, Biotechnology, and Agrochemistryja
dc.rights© 2012 by Japan Society for Bioscience, Biotechnology, and Agrochemistryja
dc.subjectprotein kinase Cja
dc.subjectbryostatinja
dc.subjectBugula neritinaja
dc.subjecttumor promotionja
dc.subjectEpstein-Barr virusja
dc.titleIdentification and Biological Activities of Bryostatins from Japanese Bryozoanja
dc.type.niitypeJournal Articleja
dc.identifier.ncidAA10824164ja
dc.identifier.jtitleBioscience, Biotechnology, and Biochemistryja
dc.identifier.volume76ja
dc.identifier.issue5ja
dc.identifier.spage1041ja
dc.identifier.epage1043ja
dc.relation.doi10.1271/bbb.120026ja
dc.textversionpublisherja
dc.relation.urlhttps://www.jstage.jst.go.jp/article/bbb/76/5/76_120026/_articleja
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