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  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/123456789/21194
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dc.contributor.authorPolioudaki, H.en
dc.contributor.authorKourmouli, N.en
dc.contributor.authorDrosou, V.en
dc.contributor.authorBakou, A.en
dc.contributor.authorTheodoropoulos, P. A.en
dc.contributor.authorSingh, P. B.en
dc.contributor.authorGiannakouros, T.en
dc.contributor.authorGeorgatos, S. D.en
dc.date.accessioned2015-11-24T19:13:29Z-
dc.date.available2015-11-24T19:13:29Z-
dc.identifier.issn1469-221X-
dc.identifier.urihttps://olympias.lib.uoi.gr/jspui/handle/123456789/21194-
dc.rightsDefault Licence-
dc.subjectAcetylationen
dc.subjectAnimalsen
dc.subjectBinding Sitesen
dc.subjectBlotting, Westernen
dc.subjectCell Nucleus/metabolismen
dc.subjectDose-Response Relationship, Drugen
dc.subjectElectrophoresis, Polyacrylamide Gelen
dc.subjectFishesen
dc.subjectGlutathione Transferase/metabolismen
dc.subjectHeterochromatin/metabolismen
dc.subjectHistones/*metabolismen
dc.subjectIntracellular Membranes/metabolismen
dc.subjectMiceen
dc.subjectModels, Biologicalen
dc.subjectPlasmids/metabolismen
dc.subjectPrecipitin Testsen
dc.subjectProtein Bindingen
dc.subjectProtein Structure, Tertiaryen
dc.subjectRecombinant Fusion Proteins/metabolismen
dc.subjectRecombinant Proteins/metabolismen
dc.subjectTurkeysen
dc.titleHistones H3/H4 form a tight complex with the inner nuclear membrane protein LBR and heterochromatin protein 1en
heal.typejournalArticle-
heal.type.enJournal articleen
heal.type.elΆρθρο Περιοδικούel
heal.identifier.primary10.1093/embo-reports/kve199-
heal.identifier.secondaryhttp://www.ncbi.nlm.nih.gov/pubmed/11571267-
heal.identifier.secondaryhttp://www.nature.com/embor/journal/v2/n10/pdf/embor322.pdf-
heal.languageen-
heal.accesscampus-
heal.recordProviderΠανεπιστήμιο Ιωαννίνων. Σχολή Επιστημών Υγείας. Τμήμα Ιατρικήςel
heal.publicationDate2001-
heal.abstractWe have recently shown that heterochromatin protein 1 (HP1) interacts with the nuclear envelope in an acetylation-dependent manner. Using purified components and in vitro assays, we now demonstrate that HP1 forms a quaternary complex with the inner nuclear membrane protein LBR and a sub-set of core histones. This complex involves histone H3/H4 oligomers, which mediate binding of LBR to HP1 and cross-link these two proteins that do not interact directly with each other. Consistent with previous observations, HP1 and LBR binding to core histones is strongly inhibited when H3/H4 are modified by recombinant CREB-binding protein, revealing a new mechanism for anchoring domains of under-acetylated chromatin to the inner nuclear membrane.en
heal.journalNameEMBO Repen
heal.journalTypepeer-reviewed-
heal.fullTextAvailabilityTRUE-
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