Please use this identifier to cite or link to this item: https://olympias.lib.uoi.gr/jspui/handle/123456789/23976
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dc.contributor.authorGounari, F.en
dc.contributor.authorKaragianni, N.en
dc.contributor.authorMincheva, A.en
dc.contributor.authorLichter, P.en
dc.contributor.authorGeorgatos, S. D.en
dc.contributor.authorSchirrmacher, V.en
dc.date.accessioned2015-11-24T19:37:00Z-
dc.date.available2015-11-24T19:37:00Z-
dc.identifier.issn0014-5793-
dc.identifier.urihttps://olympias.lib.uoi.gr/jspui/handle/123456789/23976-
dc.rightsDefault Licence-
dc.subjectAmino Acid Sequenceen
dc.subjectAnimalsen
dc.subjectBase Sequenceen
dc.subjectChromosome Mappingen
dc.subjectCloning, Molecularen
dc.subjectConserved Sequenceen
dc.subjectDNA, Complementary/geneticsen
dc.subject*Evolution, Molecularen
dc.subjectExons/geneticsen
dc.subjectEye Proteins/*geneticsen
dc.subjectFemaleen
dc.subjectGene Dosageen
dc.subjectGenes/*geneticsen
dc.subjectIntermediate Filament Proteins/*geneticsen
dc.subjectIntrons/geneticsen
dc.subjectMiceen
dc.subjectMice, Inbred BALB Cen
dc.subjectMolecular Sequence Dataen
dc.subjectSequence Analysis, DNAen
dc.subjectSequence Homology, Amino Aciden
dc.titleThe mouse filensin gene: structure and evolutionary relation to other intermediate filament genesen
heal.typejournalArticle-
heal.type.enJournal articleen
heal.type.elΆρθρο Περιοδικούel
heal.identifier.secondaryhttp://www.ncbi.nlm.nih.gov/pubmed/9280315-
heal.identifier.secondaryhttp://www.sciencedirect.com/science/article/pii/S001457939700937X-
heal.languageen-
heal.accesscampus-
heal.recordProviderΠανεπιστήμιο Ιωαννίνων. Σχολή Επιστημών Υγείας. Τμήμα Ιατρικήςel
heal.publicationDate1997-
heal.abstractFilensin and phakinin are two lens-specific members of the intermediate filament (IF) superfamily of proteins. They coassemble to form a beaded submembraneous filamentous network, the beaded filaments (BFs). The low sequence homology and differences in assembly compared to other IF proteins do not allow their classification in any of the five IF subgroups. The organization of the phakinin gene exon/intron boundaries provides evidence that this partner may be sharing a common origin with type I cytokeratin genes. Here we report the molecular cloning, sequence and characterization of the mouse filensin gene. The filensin gene consists of 8 exons and 7 introns, with 6 introns interrupting its rod domain in a highly conserved manner characteristic of type III IF genes, like vimentin, desmin, or peripherin. Of the two tail domain exons the one adjacent to the rod domain, compares to exon 7 of the non-neuronal cytoplasmic IF gene of helix aspersa and to the lamin region bridging the end of the rod domain to the nuclear localization signal. Altogether, these observations indicate that the lens beaded filaments form an independent class of IF.en
heal.journalNameFEBS Letten
heal.journalTypepeer-reviewed-
heal.fullTextAvailabilityTRUE-
Appears in Collections:Άρθρα σε επιστημονικά περιοδικά ( Ανοικτά) - ΙΑΤ

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