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  4. Τμήμα Ιατρικής
  5. Άρθρα σε επιστημονικά περιοδικά ( Ανοικτά) - ΙΑΤ
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Please use this identifier to cite or link to this item: https://olympias.lib.uoi.gr/jspui/handle/123456789/18939
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dc.contributor.authorKaretsou, Z.en
dc.contributor.authorKretsovali, A.en
dc.contributor.authorMurphy, C.en
dc.contributor.authorTsolas, O.en
dc.contributor.authorPapamarcaki, T.en
dc.date.accessioned2015-11-24T18:55:50Z-
dc.date.available2015-11-24T18:55:50Z-
dc.identifier.issn1469-221X-
dc.identifier.urihttps://olympias.lib.uoi.gr/jspui/handle/123456789/18939-
dc.rightsDefault Licence-
dc.subjectAnimalsen
dc.subjectCREB-Binding Proteinen
dc.subjectCattleen
dc.subjectGlutathione Transferase/metabolismen
dc.subjectHeLa Cellsen
dc.subjectHumansen
dc.subjectNF-kappa B/metabolismen
dc.subjectNuclear Proteins/*metabolismen
dc.subjectPrecipitin Testsen
dc.subjectProtein Precursors/*metabolismen
dc.subjectRatsen
dc.subjectThymosin/*analogs & derivatives/*metabolismen
dc.subjectTrans-Activators/*metabolismen
dc.subjectTranscription Factor AP-1/metabolismen
dc.subjectTranscription, Genetic/*physiologyen
dc.titleProthymosin alpha interacts with the CREB-binding protein and potentiates transcriptionen
heal.typejournalArticle-
heal.type.enJournal articleen
heal.type.elΆρθρο Περιοδικούel
heal.identifier.primary10.1093/embo-reports/kvf071-
heal.identifier.secondaryhttp://www.ncbi.nlm.nih.gov/pubmed/11897665-
heal.identifier.secondaryhttp://www.nature.com/embor/journal/v3/n4/pdf/embor187.pdf-
heal.languageen-
heal.accesscampus-
heal.recordProviderΠανεπιστήμιο Ιωαννίνων. Σχολή Επιστημών Υγείας. Τμήμα Ιατρικήςel
heal.publicationDate2002-
heal.abstractProthymosin alpha (ProTalpha) is a histone H1-binding protein localized in sites of active transcription in the nucleus. We report here that ProTalpha physically interacts with the CREB-binding protein (CBP), which is a versatile transcription co-activator. Confocal laser scanning microscopy reveals that ProTalpha partially colocalizes with CBP in discrete subnuclear domains. Using transient transfections, we show that ProTalpha synergizes with CBP and stimulates AP1- and NF-kappaB-dependent transcription. Furthermore, overexpression of ProTalpha enhances the transactivation potential of CBP. These findings reveal a new function for ProTalpha in transcription activation, probably through CBP-mediated recruitment to different promoters.en
heal.journalNameEMBO Repen
heal.journalTypepeer-reviewed-
heal.fullTextAvailabilityTRUE-
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