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  5. Άρθρα σε επιστημονικά περιοδικά ( Ανοικτά). ΧΗΜ
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Please use this identifier to cite or link to this item: https://olympias.lib.uoi.gr/jspui/handle/123456789/9659
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dc.contributor.authorTzartos, S. J.en
dc.contributor.authorCung, M. T.en
dc.contributor.authorDemange, P.en
dc.contributor.authorLoutrari, H.en
dc.contributor.authorMamalaki, A.en
dc.contributor.authorMarraud, M.en
dc.contributor.authorPapadouli, I.en
dc.contributor.authorSakarellos, C.en
dc.contributor.authorTsikaris, V.en
dc.date.accessioned2015-11-24T16:50:55Z-
dc.date.available2015-11-24T16:50:55Z-
dc.identifier.issn0893-7648-
dc.identifier.urihttps://olympias.lib.uoi.gr/jspui/handle/123456789/9659-
dc.rightsDefault Licence-
dc.subjectnicotinic acetylcholine receptoren
dc.subjectmyasthenia gravisen
dc.subjectmonoclonal antibodiesen
dc.subjectmain immunogenic regionen
dc.subjectepitopeen
dc.subjectsynthetic peptideen
dc.subjectantigenic modulationen
dc.subjectantibody competitionen
dc.subjectautoimmune myasthenia-gravisen
dc.subjectbungarotoxin binding-siteen
dc.subjectmedulloblastoma cell-lineen
dc.subjecthigh-affinity bindingen
dc.subjectmonoclonal-antibodiesen
dc.subjectalpha-subuniten
dc.subjectsynthetic peptidesen
dc.subjectantigenic modulationen
dc.subjecttorpedo-californicaen
dc.subjectligand-bindingen
dc.titleThe Main Immunogenic Region (Mir) of the Nicotinic Acetylcholine-Receptor and the Anti-Mir Antibodiesen
heal.typejournalArticle-
heal.type.enJournal articleen
heal.type.elΆρθρο Περιοδικούel
heal.identifier.secondary<Go to ISI>://A1991HH12800001-
heal.identifier.secondaryhttp://www.springerlink.com/content/j8l2137514t28n64/-
heal.languageen-
heal.accesscampus-
heal.recordProviderΠανεπιστήμιο Ιωαννίνων. Σχολή Θετικών Επιστημών. Τμήμα Χημείαςel
heal.publicationDate1991-
heal.abstractMyasthenia gravis (MG) is caused by autoantibodies against the nicotinic acetylcholine receptor (AChR) of the neuromuscular junction. The anti-AChR antibodies are heterogeneous. However, a small region on the extracellular part of the AChR-alpha-subunit, called the main immunogenic region (MIR), seems to be the major target of the anti-AChR antibodies, but not of the specific T-cells, in experimental animals and possibly in MG patients. The major loop of the overlapping epitopes for all testable anti-MIR monoclonal antibodies (MAbs) was localized within residues 67-76 (WNPADYGGIK for Torpedo and WNPDDYGGVK for human AChR) of the alpha-subunit. The N-terminal half of alpha-67-76 is the most critical, Asn68 and Asp71 being indispensable for binding. Yet anti-MIR antibodies are functionally and structurally quite heterogeneous. Anti-MIR MAbs do not affect channel gating, but they are very potent in mediating acceleration of AChR degradation (antigenic modulation) in cell cultures and in transferring experimental MG in animals. Fab fragments of anti-MIR MAbs bound to the AChR prevent the majority of the MG patients' antibodies from binding to and causing loss of the AChR. Whether this inhibition means that most MG antibodies bind on the same small region or is a result of broad steric/allosteric effects is under current investigation.en
heal.journalNameMolecular Neurobiologyen
heal.journalTypepeer reviewed-
heal.fullTextAvailabilityTRUE-
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