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dc.contributor.authorKamisuki, Shinjien
dc.contributor.authorMao, Qianen
dc.contributor.authorAbu-Elheiga, Lutfien
dc.contributor.authorGu, Ziweien
dc.contributor.authorKugimiya, Akiraen
dc.contributor.authorKwon, Youngjooen
dc.contributor.authorShinohara, Tokuyukien
dc.contributor.authorKawazoe, Yoshinorien
dc.contributor.authorSato, Shin-ichien
dc.contributor.authorAsakura, Kokoen
dc.contributor.authorChoo, Hea-Young Parken
dc.contributor.authorSakai, Juroen
dc.contributor.authorWakil, Salih Jen
dc.contributor.authorUesugi, Motonarien
dc.contributor.alternative上杉, 志成ja
dc.date.accessioned2010-05-20T01:26:33Z-
dc.date.available2010-05-20T01:26:33Z-
dc.date.issued2009-08-28-
dc.identifier.issn1879-1301-
dc.identifier.urihttp://hdl.handle.net/2433/112665-
dc.description.abstractSterol regulatory element binding proteins (SREBPs) are transcription factors that activate transcription of the genes involved in cholesterol and fatty acid biosynthesis. In the present study, we show that a small synthetic molecule we previously discovered to block adipogenesis is an inhibitor of the SREBP activation. The diarylthiazole derivative, now called fatostatin, impairs the activation process of SREBPs, thereby decreasing the transcription of lipogenic genes in cells. Our analysis suggests that fatostatin inhibits the ER-Golgi translocation of SREBPs through binding to their escort protein, the SREBP cleavage-activating protein (SCAP), at a distinct site from the sterol-binding domain. Fatostatin blocked increases in body weight, blood glucose, and hepatic fat accumulation in obese ob/ob mice, even under uncontrolled food intake. Fatostatin may serve as a tool for gaining further insights into the regulation of SREBP.en
dc.format.mimetypeapplication/pdf-
dc.language.isoeng-
dc.publisherElsevieren
dc.rights© 2009 Elsevieren
dc.rightsThis is not the published version. Please cite only the published version.en
dc.rightsこの論文は出版社版でありません。引用の際には出版社版をご確認ご利用ください。ja
dc.subjectCHEMBIOen
dc.subjectCELLBIOen
dc.subject.meshAnimalsen
dc.subject.meshBlood Glucose/metabolismen
dc.subject.meshBody Weighten
dc.subject.meshCHO Cellsen
dc.subject.meshCricetinaeen
dc.subject.meshCricetulusen
dc.subject.meshFatty Acids/biosynthesisen
dc.subject.meshFatty Acids/metabolismen
dc.subject.meshHumansen
dc.subject.meshIntracellular Signaling Peptides and Proteins/metabolismen
dc.subject.meshMembrane Proteins/metabolismen
dc.subject.meshMiceen
dc.subject.meshMice, Obeseen
dc.subject.meshProtein Bindingen
dc.subject.meshProtein Structure, Tertiaryen
dc.subject.meshPyridines/chemistryen
dc.subject.meshPyridines/pharmacologyen
dc.subject.meshSterol Regulatory Element Binding Proteins/antagonists & inhibitorsen
dc.subject.meshSterol Regulatory Element Binding Proteins/chemistryen
dc.subject.meshSterol Regulatory Element Binding Proteins/metabolismen
dc.subject.meshThiazoles/chemistryen
dc.subject.meshThiazoles/pharmacologyen
dc.subject.meshTranscription, Geneticen
dc.titleA small molecule that blocks fat synthesis by inhibiting the activation of SREBPen
dc.typejournal article-
dc.type.niitypeJournal Article-
dc.identifier.ncidAA11072585-
dc.identifier.jtitleChemistry & biologyen
dc.identifier.volume16-
dc.identifier.issue8-
dc.identifier.spage882-
dc.identifier.epage892-
dc.relation.doi10.1016/j.chembiol.2009.07.007-
dc.textversionauthor-
dc.identifier.pmid19716478-
dcterms.accessRightsopen access-
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