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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/123456789/19837
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dc.contributor.authorBozidis, P.en
dc.contributor.authorLazaridis, I.en
dc.contributor.authorPagoulatos, G. N.en
dc.contributor.authorAngelidis, C. E.en
dc.date.accessioned2015-11-24T19:02:48Z-
dc.date.available2015-11-24T19:02:48Z-
dc.identifier.issn0014-2956-
dc.identifier.urihttps://olympias.lib.uoi.gr/jspui/handle/123456789/19837-
dc.rightsDefault Licence-
dc.subjectAnimalsen
dc.subjectCarrier Proteins/genetics/*metabolismen
dc.subjectCell Nucleus/metabolismen
dc.subjectCells, Cultureden
dc.subjectDNA, Complementary/isolation & purificationen
dc.subjectHSC70 Heat-Shock Proteinsen
dc.subjectHSP40 Heat-Shock Proteinsen
dc.subjectHSP70 Heat-Shock Proteins/*metabolismen
dc.subjectHaplorhinien
dc.subjectHeat-Shock Proteins/genetics/*metabolismen
dc.subjectMaleen
dc.subjectMiceen
dc.subjectRNA, Messenger/analysisen
dc.titleMydj2 as a potent partner of hsc70 in mammalian cellsen
heal.typejournalArticle-
heal.type.enJournal articleen
heal.type.elΆρθρο Περιοδικούel
heal.identifier.secondaryhttp://www.ncbi.nlm.nih.gov/pubmed/11874471-
heal.identifier.secondaryhttp://onlinelibrary.wiley.com/store/10.1046/j.1432-1033.2002.02807.x/asset/j.1432-1033.2002.02807.x.pdf?v=1&t=h2bp4a5z&s=661696463a74c5cef4f50820f5470cebe5d45432-
heal.languageen-
heal.accesscampus-
heal.recordProviderΠανεπιστήμιο Ιωαννίνων. Σχολή Επιστημών Υγείας. Τμήμα Ιατρικήςel
heal.publicationDate2002-
heal.abstractDj2 is a member of the DnaJ family of proteins, which regulate the chaperoning function of the hsp70s. We isolated a monkey cDNA dj2 clone corresponding to the large mRNA species encoded by the gene. This mRNA differs from the small mRNA produced by the same gene in that it contains a long 3' untranslated region. Both messages were found to be equally stable and to produce the same protein, which is susceptible to farnesylation. Studies in mouse tissues and various cell lines revealed that these messages and their products are differentially expressed. Surprisingly, we found that only the nonfarnesylated form of dj2 is capable of translocating to the cell nucleus, especially after heat shock. Finally, based on protein interaction studies, our results indicate that dj2 is a specific partner for hsc70 and not for hsp70.en
heal.journalNameEur J Biochemen
heal.journalTypepeer-reviewed-
heal.fullTextAvailabilityTRUE-
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