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http://purl.uniprot.org/citations/20206597http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/20206597http://www.w3.org/2000/01/rdf-schema#comment"The switch from gluconeogenesis to glycolysis in yeast has been shown to require ubiquitin-proteasome dependent elimination of the key enzyme fructose-1,6-bisphosphatase (FBPase). Prior to proteasomal degradation, polyubiquitination of the enzyme occurs via the ubiquitin-conjugating enzymes Ubc1, Ubc4, Ubc5 and Ubc8 in conjunction with a novel multi-subunit ubiquitin ligase, the Gid complex. As an additional machinery required for the catabolite degradation process, we identified the trimeric Cdc48(Ufd1-Npl4) complex and the ubiquitin receptors Dsk2 and Rad23. We show that this machinery acts between polyubiquitination of FBPase and its degradation by the proteasome."xsd:string
http://purl.uniprot.org/citations/20206597http://purl.org/dc/terms/identifier"doi:10.1016/j.bbrc.2010.03.005"xsd:string
http://purl.uniprot.org/citations/20206597http://purl.uniprot.org/core/author"Wolf D.H."xsd:string
http://purl.uniprot.org/citations/20206597http://purl.uniprot.org/core/author"Santt O."xsd:string
http://purl.uniprot.org/citations/20206597http://purl.uniprot.org/core/author"Barbin L."xsd:string
http://purl.uniprot.org/citations/20206597http://purl.uniprot.org/core/author"Eisele F."xsd:string
http://purl.uniprot.org/citations/20206597http://purl.uniprot.org/core/date"2010"xsd:gYear
http://purl.uniprot.org/citations/20206597http://purl.uniprot.org/core/name"Biochem Biophys Res Commun"xsd:string
http://purl.uniprot.org/citations/20206597http://purl.uniprot.org/core/pages"335-341"xsd:string
http://purl.uniprot.org/citations/20206597http://purl.uniprot.org/core/title"The Cdc48-Ufd1-Npl4 complex is central in ubiquitin-proteasome triggered catabolite degradation of fructose-1,6-bisphosphatase."xsd:string
http://purl.uniprot.org/citations/20206597http://purl.uniprot.org/core/volume"394"xsd:string
http://purl.uniprot.org/citations/20206597http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/20206597
http://purl.uniprot.org/citations/20206597http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/20206597
http://purl.uniprot.org/uniprot/P25694#attribution-F36A5BAD6A358C9CE56C88C41138AD4Bhttp://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/20206597
http://purl.uniprot.org/uniprot/P33755#attribution-F36A5BAD6A358C9CE56C88C41138AD4Bhttp://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/20206597
http://purl.uniprot.org/uniprot/P53044#attribution-F36A5BAD6A358C9CE56C88C41138AD4Bhttp://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/20206597
http://purl.uniprot.org/uniprot/#_A0A6A5PV82-mappedCitation-20206597http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/20206597
http://purl.uniprot.org/uniprot/#_P25694-mappedCitation-20206597http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/20206597
http://purl.uniprot.org/uniprot/#_P33755-mappedCitation-20206597http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/20206597
http://purl.uniprot.org/uniprot/#_P09201-mappedCitation-20206597http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/20206597
http://purl.uniprot.org/uniprot/#_P48510-mappedCitation-20206597http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/20206597
http://purl.uniprot.org/uniprot/#_P32628-mappedCitation-20206597http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/20206597
http://purl.uniprot.org/uniprot/#_P53044-mappedCitation-20206597http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/20206597
http://purl.uniprot.org/uniprot/#_P54730-mappedCitation-20206597http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/20206597