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  2. ΑΠΟΘΕΤΗΡΙΟ "ΟΛΥΜΠΙΑΣ"
  3. Σχολή Επιστημών Υγείας
  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/123456789/24253
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dc.contributor.authorMakatsori, D.en
dc.contributor.authorKourmouli, N.en
dc.contributor.authorPolioudaki, H.en
dc.contributor.authorShultz, L. D.en
dc.contributor.authorMcLean, K.en
dc.contributor.authorTheodoropoulos, P. A.en
dc.contributor.authorSingh, P. B.en
dc.contributor.authorGeorgatos, S. D.en
dc.date.accessioned2015-11-24T19:39:31Z-
dc.date.available2015-11-24T19:39:31Z-
dc.identifier.issn0021-9258-
dc.identifier.urihttps://olympias.lib.uoi.gr/jspui/handle/123456789/24253-
dc.rightsDefault Licence-
dc.subjectAnimalsen
dc.subjectHeLa Cellsen
dc.subjectHeterochromatin/*chemistryen
dc.subjectHumansen
dc.subjectMass Spectrometryen
dc.subjectNuclear Envelope/*chemistryen
dc.subjectReceptors, Cytoplasmic and Nuclear/*chemistryen
dc.titleThe inner nuclear membrane protein lamin B receptor forms distinct microdomains and links epigenetically marked chromatin to the nuclear envelopeen
heal.typejournalArticle-
heal.type.enJournal articleen
heal.type.elΆρθρο Περιοδικούel
heal.identifier.primary10.1074/jbc.M313606200-
heal.identifier.secondaryhttp://www.ncbi.nlm.nih.gov/pubmed/15056654-
heal.identifier.secondaryhttp://www.jbc.org/content/279/24/25567.full.pdf-
heal.languageen-
heal.accesscampus-
heal.recordProviderΠανεπιστήμιο Ιωαννίνων. Σχολή Επιστημών Υγείας. Τμήμα Ιατρικήςel
heal.publicationDate2004-
heal.abstractUsing heterochromatin-enriched fractions, we have detected specific binding of mononucleosomes to the N-terminal domain of the inner nuclear membrane protein lamin B receptor. Mass spectrometric analysis reveals that LBR-associated particles contain complex patterns of methylated/acetylated histones and are devoid of "euchromatic" epigenetic marks. LBR binds heterochromatin as a higher oligomer and forms distinct nuclear envelope microdomains in vivo. The organization of these membrane assemblies is affected significantly in heterozygous ic (ichthyosis) mutants, resulting in a variety of structural abnormalities and nuclear defects.en
heal.journalNameJ Biol Chemen
heal.journalTypepeer-reviewed-
heal.fullTextAvailabilityTRUE-
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