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http://purl.uniprot.org/citations/17015443http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17015443http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17015443http://www.w3.org/2000/01/rdf-schema#comment"Nuclear export of the large ribosomal subunit requires the adapter protein Nmd3p to provide a leucine-rich nuclear export signal that is recognized by the export receptor Crm1. Nmd3p binds to the pre-60 S subunit in the nucleus. After export to the cytoplasm, the release of Nmd3p depends on the ribosomal protein Rpl10p and the GTPase Lsg1p. Here, we have carried out a mutational analysis of Nmd3 to better define the domains responsible for nucleocytoplasmic shuttling and ribosome binding. We show that mutations in two regions of Nmd3p affect 60 S binding, suggesting that its binding to the subunit is multivalent."xsd:string
http://purl.uniprot.org/citations/17015443http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m606798200"xsd:string
http://purl.uniprot.org/citations/17015443http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m606798200"xsd:string
http://purl.uniprot.org/citations/17015443http://purl.uniprot.org/core/author"Johnson A.W."xsd:string
http://purl.uniprot.org/citations/17015443http://purl.uniprot.org/core/author"Johnson A.W."xsd:string
http://purl.uniprot.org/citations/17015443http://purl.uniprot.org/core/author"Chen Y.I."xsd:string
http://purl.uniprot.org/citations/17015443http://purl.uniprot.org/core/author"Chen Y.I."xsd:string
http://purl.uniprot.org/citations/17015443http://purl.uniprot.org/core/author"West M."xsd:string
http://purl.uniprot.org/citations/17015443http://purl.uniprot.org/core/author"West M."xsd:string
http://purl.uniprot.org/citations/17015443http://purl.uniprot.org/core/author"Bussiere C."xsd:string
http://purl.uniprot.org/citations/17015443http://purl.uniprot.org/core/author"Bussiere C."xsd:string
http://purl.uniprot.org/citations/17015443http://purl.uniprot.org/core/author"Hedges J."xsd:string
http://purl.uniprot.org/citations/17015443http://purl.uniprot.org/core/author"Hedges J."xsd:string
http://purl.uniprot.org/citations/17015443http://purl.uniprot.org/core/date"2006"xsd:gYear
http://purl.uniprot.org/citations/17015443http://purl.uniprot.org/core/date"2006"xsd:gYear
http://purl.uniprot.org/citations/17015443http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/17015443http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/17015443http://purl.uniprot.org/core/pages"36579-36587"xsd:string
http://purl.uniprot.org/citations/17015443http://purl.uniprot.org/core/pages"36579-36587"xsd:string
http://purl.uniprot.org/citations/17015443http://purl.uniprot.org/core/title"Mapping the functional domains of yeast NMD3, the nuclear export adapter for the 60 S ribosomal subunit."xsd:string
http://purl.uniprot.org/citations/17015443http://purl.uniprot.org/core/title"Mapping the functional domains of yeast NMD3, the nuclear export adapter for the 60 S ribosomal subunit."xsd:string
http://purl.uniprot.org/citations/17015443http://purl.uniprot.org/core/volume"281"xsd:string
http://purl.uniprot.org/citations/17015443http://purl.uniprot.org/core/volume"281"xsd:string