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dc.contributor.authorRaasakka, Arneen_US
dc.contributor.authorRuskamo, Sallaen_US
dc.contributor.authorKowal, Juliaen_US
dc.contributor.authorBarker, Roberten_US
dc.contributor.authorBaumann, Anneen_US
dc.contributor.authorMartel, Anneen_US
dc.contributor.authorTuusa, Jussien_US
dc.contributor.authorMyllykoski, Mattien_US
dc.contributor.authorBürck, Jochenen_US
dc.contributor.authorUlrich, Anne S.en_US
dc.contributor.authorStahlberg, Henningen_US
dc.contributor.authorKursula, Petrien_US
dc.date.accessioned2018-03-01T15:01:22Z
dc.date.available2018-03-01T15:01:22Z
dc.date.issued2017-07-10
dc.PublishedRaasakka A, Ruskamo S, Kowal, Barker, Baumann A, Martel, Tuusa, Myllykoski M, Bürck, Ulrich, Stahlberg, Kursula P. Membrane Association Landscape of Myelin Basic Protein Portrays Formation of the Myelin Major Dense Line. Scientific Reports. 2017;7:4974eng
dc.identifier.issn2045-2322
dc.identifier.urihttps://hdl.handle.net/1956/17446
dc.description.abstractCompact myelin comprises most of the dry weight of myelin, and its insulative nature is the basis for saltatory conduction of nerve impulses. The major dense line (MDL) is a 3-nm compartment between two cytoplasmic leaflets of stacked myelin membranes, mostly occupied by a myelin basic protein (MBP) phase. MBP is an abundant myelin protein involved in demyelinating diseases, such as multiple sclerosis. The association of MBP with lipid membranes has been studied for decades, but the MBP-driven formation of the MDL remains elusive at the biomolecular level. We employed complementary biophysical methods, including atomic force microscopy, cryo-electron microscopy, and neutron scattering, to investigate the formation of membrane stacks all the way from MBP binding onto a single membrane leaflet to the organisation of a stable MDL. Our results support the formation of an amorphous protein phase of MBP between two membrane bilayers and provide a molecular model for MDL formation during myelination, which is of importance when understanding myelin assembly and demyelinating conditions.en_US
dc.language.isoengeng
dc.publisherNature Publishing Groupeng
dc.relation.ispartof<a href="http://hdl.handle.net/1956/19951" target="blank"> The Characterization of Disordered Membrane-Binding Proteins of Myelin. A Biophysical Approach</a>
dc.rightsAttribution CC BYeng
dc.rights.urihttp://creativecommons.org/licenses/by/4.0eng
dc.titleMembrane Association Landscape of Myelin Basic Protein Portrays Formation of the Myelin Major Dense Lineen_US
dc.typePeer reviewed
dc.typeJournal article
dc.date.updated2018-01-05T11:26:39Z
dc.description.versionpublishedVersionen_US
dc.rights.holderCopyright 2017 The Author(s)
dc.identifier.doihttps://doi.org/10.1038/s41598-017-05364-3
dc.identifier.cristin1517282
dc.source.journalScientific Reports


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