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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/123456789/20010
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dc.contributor.authorPolioudaki, H.en
dc.contributor.authorMarkaki, Y.en
dc.contributor.authorKourmouli, N.en
dc.contributor.authorDialynas, G.en
dc.contributor.authorTheodoropoulos, P. A.en
dc.contributor.authorSingh, P. B.en
dc.contributor.authorGeorgatos, S. D.en
dc.date.accessioned2015-11-24T19:04:17Z-
dc.date.available2015-11-24T19:04:17Z-
dc.identifier.issn0014-5793-
dc.identifier.urihttps://olympias.lib.uoi.gr/jspui/handle/123456789/20010-
dc.rightsDefault Licence-
dc.subjectAmino Acid Sequenceen
dc.subjectAnimalsen
dc.subjectBlotting, Westernen
dc.subjectCell Fractionationen
dc.subjectCell Nucleus/chemistryen
dc.subjectErythrocyte Membrane/chemistryen
dc.subjectErythrocytes/cytologyen
dc.subjectGlutathione Transferase/metabolismen
dc.subjectHeterochromatin/chemistryen
dc.subjectHistones/chemistry/*metabolismen
dc.subjectMitosisen
dc.subjectNuclear Envelope/chemistryen
dc.subjectPhosphorylationen
dc.subjectProtein Processing, Post-Translational/immunologyen
dc.subjectRecombinant Fusion Proteins/chemistry/metabolismen
dc.subjectThreonine/*metabolismen
dc.subjectTurkeys/blooden
dc.titleMitotic phosphorylation of histone H3 at threonine 3en
heal.typejournalArticle-
heal.type.enJournal articleen
heal.type.elΆρθρο Περιοδικούel
heal.identifier.primary10.1016/S0014-5793(04)00060-2-
heal.identifier.secondaryhttp://www.ncbi.nlm.nih.gov/pubmed/14987995-
heal.identifier.secondaryhttp://www.sciencedirect.com/science/article/pii/S0014579304000602-
heal.languageen-
heal.accesscampus-
heal.recordProviderΠανεπιστήμιο Ιωαννίνων. Σχολή Επιστημών Υγείας. Τμήμα Ιατρικήςel
heal.publicationDate2004-
heal.abstractNuclear envelope-peripheral heterochromatin fractions contain multiple histone kinase activities. In vitro assays and amino-terminal sequencing show that one of these activities co-isolates with heterochromatin protein 1 (HP1) and phosphorylates histone H3 at threonine 3. Antibodies recognizing this post-translational modification reveal that in vivo phosphorylation at threonine 3 commences at early prophase in the vicinity of the nuclear envelope, spreads to pericentromeric chromatin during prometaphase and is fully reversed by late anaphase. This spatio-temporal pattern is distinct from H3 phosphorylation at serine 10, which also occurs during cell division, suggesting segregation of differentially phosphorylated chromatin to different regions of mitotic chromosomes.en
heal.journalNameFEBS Letten
heal.journalTypepeer-reviewed-
heal.fullTextAvailabilityTRUE-
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