Please use this identifier to cite or link to this item: https://olympias.lib.uoi.gr/jspui/handle/123456789/24336
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dc.contributor.authorWorman, H. J.en
dc.contributor.authorYuan, J.en
dc.contributor.authorBlobel, G.en
dc.contributor.authorGeorgatos, S. D.en
dc.date.accessioned2015-11-24T19:40:20Z-
dc.date.available2015-11-24T19:40:20Z-
dc.identifier.issn0027-8424-
dc.identifier.urihttps://olympias.lib.uoi.gr/jspui/handle/123456789/24336-
dc.rightsDefault Licence-
dc.subjectAnimalsen
dc.subjectCell Membrane/metabolismen
dc.subjectErythrocytes/metabolismen
dc.subjectFluorescent Antibody Techniqueen
dc.subjectKineticsen
dc.subjectLamin Type Aen
dc.subjectLamin Type Ben
dc.subjectLaminsen
dc.subjectMembrane Proteins/*metabolismen
dc.subjectNuclear Envelope/*metabolismen
dc.subjectNuclear Proteins/*blooden
dc.subjectReceptors, Cell Surface/*metabolismen
dc.subject*Receptors, Cytoplasmic and Nuclearen
dc.subjectTurkeysen
dc.titleA lamin B receptor in the nuclear envelopeen
heal.typejournalArticle-
heal.type.enJournal articleen
heal.type.elΆρθρο Περιοδικούel
heal.identifier.secondaryhttp://www.ncbi.nlm.nih.gov/pubmed/2847165-
heal.identifier.secondaryhttp://www.pnas.org/content/85/22/8531.full.pdf-
heal.languageen-
heal.accesscampus-
heal.recordProviderΠανεπιστήμιο Ιωαννίνων. Σχολή Επιστημών Υγείας. Τμήμα Ιατρικήςel
heal.publicationDate1988-
heal.abstractUsing a solution binding assay, we show that purified 125I-labeled lamin B binds in a saturable and specific fashion to lamin-depleted avian erythrocyte nuclear membranes with a Kd of approximately 0.2 microM. This binding is significantly greater than the binding of 125I-labeled lamin A and is competitively inhibited by unlabeled ligand. We demonstrate that a 58-kDa integral membrane protein (p58) is a lamin B receptor by virtue of its abundance in the nuclear envelope and association with 125I-labeled lamin B in ligand blotting assays. Specific antibodies raised against p58 recognize one protein in isolated nuclei and partially block 125I-labeled lamin B binding to lamin-depleted nuclear membranes. Cell fractionation and indirect immunofluorescence microscopy show that p58 is located in the periphery of the nucleus. This protein may serve as a membrane attachment site for the nuclear lamina by acting as a specific receptor for lamin B.en
heal.journalNameProc Natl Acad Sci U S Aen
heal.journalTypepeer-reviewed-
heal.fullTextAvailabilityTRUE-
Appears in Collections:Άρθρα σε επιστημονικά περιοδικά ( Ανοικτά) - ΙΑΤ

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