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http://purl.uniprot.org/citations/15802566http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15802566http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15802566http://www.w3.org/2000/01/rdf-schema#comment"The existence of specialized molecular chaperones that interact directly with ribosomes is well established in microorganisms. Such proteins bind polypeptides exiting the ribosomal tunnel and provide a physical link between translation and protein folding. We report that ribosome-associated molecular chaperones have been maintained throughout eukaryotic evolution, as illustrated by Mpp11, the human ortholog of the yeast ribosome-associated J protein Zuo. When expressed in yeast, Mpp11 partially substituted for Zuo by partnering with the multipurpose Hsp70 Ssa, the homolog of mammalian Hsc70. We propose that in metazoans, ribosome-associated Mpp11 recruits the multifunctional soluble Hsc70 to nascent polypeptide chains as they exit the ribosome."xsd:string
http://purl.uniprot.org/citations/15802566http://purl.org/dc/terms/identifier"doi:10.1126/science.1109247"xsd:string
http://purl.uniprot.org/citations/15802566http://purl.org/dc/terms/identifier"doi:10.1126/science.1109247"xsd:string
http://purl.uniprot.org/citations/15802566http://purl.uniprot.org/core/author"Craig E.A."xsd:string
http://purl.uniprot.org/citations/15802566http://purl.uniprot.org/core/author"Craig E.A."xsd:string
http://purl.uniprot.org/citations/15802566http://purl.uniprot.org/core/author"Hundley H.A."xsd:string
http://purl.uniprot.org/citations/15802566http://purl.uniprot.org/core/author"Hundley H.A."xsd:string
http://purl.uniprot.org/citations/15802566http://purl.uniprot.org/core/author"Walter W."xsd:string
http://purl.uniprot.org/citations/15802566http://purl.uniprot.org/core/author"Walter W."xsd:string
http://purl.uniprot.org/citations/15802566http://purl.uniprot.org/core/author"Bairstow S."xsd:string
http://purl.uniprot.org/citations/15802566http://purl.uniprot.org/core/author"Bairstow S."xsd:string
http://purl.uniprot.org/citations/15802566http://purl.uniprot.org/core/date"2005"xsd:gYear
http://purl.uniprot.org/citations/15802566http://purl.uniprot.org/core/date"2005"xsd:gYear
http://purl.uniprot.org/citations/15802566http://purl.uniprot.org/core/name"Science"xsd:string
http://purl.uniprot.org/citations/15802566http://purl.uniprot.org/core/name"Science"xsd:string
http://purl.uniprot.org/citations/15802566http://purl.uniprot.org/core/pages"1032-1034"xsd:string
http://purl.uniprot.org/citations/15802566http://purl.uniprot.org/core/pages"1032-1034"xsd:string
http://purl.uniprot.org/citations/15802566http://purl.uniprot.org/core/title"Human Mpp11 J protein: ribosome-tethered molecular chaperones are ubiquitous."xsd:string
http://purl.uniprot.org/citations/15802566http://purl.uniprot.org/core/title"Human Mpp11 J protein: ribosome-tethered molecular chaperones are ubiquitous."xsd:string
http://purl.uniprot.org/citations/15802566http://purl.uniprot.org/core/volume"308"xsd:string
http://purl.uniprot.org/citations/15802566http://purl.uniprot.org/core/volume"308"xsd:string
http://purl.uniprot.org/citations/15802566http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/15802566
http://purl.uniprot.org/citations/15802566http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/15802566