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http://purl.uniprot.org/citations/22609403http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/22609403http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/22609403http://www.w3.org/2000/01/rdf-schema#comment"The predominant 18.5-kDa classic myelin basic protein (MBP) is mainly responsible for compaction of the myelin sheath in the central nervous system, but is multifunctional, having numerous interactions with Ca(2+)-calmodulin, actin, tubulin, and SH3-domains, and can tether these proteins to a lipid membrane in vitro. The full-length 21.5-kDa MBP isoform has an additional 26 residues encoded by exon-II of the classic gene, which causes it to be trafficked to the nucleus of oligodendrocytes (OLGs). We have performed site-directed mutagenesis of selected residues within this segment in red fluorescent protein (RFP)-tagged constructs, which were then transfected into the immortalized N19-OLG cell line to view protein localization using epifluorescence microscopy. We found that 21.5-kDa MBP contains two non-traditional PY-nuclear-localization signals, and that arginine and lysine residues within these motifs were involved in subcellular trafficking of this protein to the nucleus, where it may have functional roles during myelinogenesis."xsd:string
http://purl.uniprot.org/citations/22609403http://purl.org/dc/terms/identifier"doi:10.1016/j.bbrc.2012.05.051"xsd:string
http://purl.uniprot.org/citations/22609403http://purl.org/dc/terms/identifier"doi:10.1016/j.bbrc.2012.05.051"xsd:string
http://purl.uniprot.org/citations/22609403http://purl.uniprot.org/core/author"Harauz G."xsd:string
http://purl.uniprot.org/citations/22609403http://purl.uniprot.org/core/author"Harauz G."xsd:string
http://purl.uniprot.org/citations/22609403http://purl.uniprot.org/core/author"Smith G.S."xsd:string
http://purl.uniprot.org/citations/22609403http://purl.uniprot.org/core/author"Smith G.S."xsd:string
http://purl.uniprot.org/citations/22609403http://purl.uniprot.org/core/author"Boggs J.M."xsd:string
http://purl.uniprot.org/citations/22609403http://purl.uniprot.org/core/author"Boggs J.M."xsd:string
http://purl.uniprot.org/citations/22609403http://purl.uniprot.org/core/author"Seymour L.V."xsd:string
http://purl.uniprot.org/citations/22609403http://purl.uniprot.org/core/author"Seymour L.V."xsd:string
http://purl.uniprot.org/citations/22609403http://purl.uniprot.org/core/date"2012"xsd:gYear
http://purl.uniprot.org/citations/22609403http://purl.uniprot.org/core/date"2012"xsd:gYear
http://purl.uniprot.org/citations/22609403http://purl.uniprot.org/core/name"Biochem. Biophys. Res. Commun."xsd:string
http://purl.uniprot.org/citations/22609403http://purl.uniprot.org/core/name"Biochem. Biophys. Res. Commun."xsd:string
http://purl.uniprot.org/citations/22609403http://purl.uniprot.org/core/pages"670-675"xsd:string
http://purl.uniprot.org/citations/22609403http://purl.uniprot.org/core/pages"670-675"xsd:string
http://purl.uniprot.org/citations/22609403http://purl.uniprot.org/core/title"The 21.5-kDa isoform of myelin basic protein has a non-traditional PY-nuclear-localization signal."xsd:string
http://purl.uniprot.org/citations/22609403http://purl.uniprot.org/core/title"The 21.5-kDa isoform of myelin basic protein has a non-traditional PY-nuclear-localization signal."xsd:string
http://purl.uniprot.org/citations/22609403http://purl.uniprot.org/core/volume"422"xsd:string
http://purl.uniprot.org/citations/22609403http://purl.uniprot.org/core/volume"422"xsd:string
http://purl.uniprot.org/citations/22609403http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/22609403
http://purl.uniprot.org/citations/22609403http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/22609403