| http://purl.uniprot.org/citations/8135828 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/8135828 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/8135828 | http://www.w3.org/2000/01/rdf-schema#comment | "Trifunctional protein deficiency, a typical mitochondrial long-chain fatty acid beta-oxidation defect, is caused by the abnormality of mitochondrial long-chain enoyl-CoA hydratase/3-hydroxyacyl-CoA dehydrogenase/3-ketoacyl-CoA thiolase trifunctional protein consisting of four moles of alpha-subunit and four moles of beta-subunit. We cloned, sequenced, and expressed the following cDNAs for the alpha- and beta-subunits of human trifunctional protein. The 2,690-bp cDNA clone had a 2,289-bp open reading frame encoding a 82,958-Da precursor and a 78,969-Da mature subunit (alpha-subunit). Expression of this cDNA in mammalian cells yielded a polypeptide with the long-chain enoyl-CoA hydratase and long-chain 3-hydroxyacyl-CoA dehydrogenase activities. The 1,991-bp cDNA clone had a 1,422-bp open reading frame encoding a 51,293-Da precursor and a 47,484-Da mature subunit (beta-subunit). Expression of this cDNA in mammalian cells yielded a polypeptide with the long-chain 3-ketoacyl-CoA thiolase activity."xsd:string |
| http://purl.uniprot.org/citations/8135828 | http://purl.org/dc/terms/identifier | "doi:10.1006/bbrc.1994.1302"xsd:string |
| http://purl.uniprot.org/citations/8135828 | http://purl.org/dc/terms/identifier | "doi:10.1006/bbrc.1994.1302"xsd:string |
| http://purl.uniprot.org/citations/8135828 | http://purl.uniprot.org/core/author | "Hashimoto T."xsd:string |
| http://purl.uniprot.org/citations/8135828 | http://purl.uniprot.org/core/author | "Hashimoto T."xsd:string |
| http://purl.uniprot.org/citations/8135828 | http://purl.uniprot.org/core/author | "Kamijo T."xsd:string |
| http://purl.uniprot.org/citations/8135828 | http://purl.uniprot.org/core/author | "Kamijo T."xsd:string |
| http://purl.uniprot.org/citations/8135828 | http://purl.uniprot.org/core/author | "Aoyama T."xsd:string |
| http://purl.uniprot.org/citations/8135828 | http://purl.uniprot.org/core/author | "Aoyama T."xsd:string |
| http://purl.uniprot.org/citations/8135828 | http://purl.uniprot.org/core/author | "Komiyama A."xsd:string |
| http://purl.uniprot.org/citations/8135828 | http://purl.uniprot.org/core/author | "Komiyama A."xsd:string |
| http://purl.uniprot.org/citations/8135828 | http://purl.uniprot.org/core/date | "1994"xsd:gYear |
| http://purl.uniprot.org/citations/8135828 | http://purl.uniprot.org/core/date | "1994"xsd:gYear |
| http://purl.uniprot.org/citations/8135828 | http://purl.uniprot.org/core/name | "Biochem. Biophys. Res. Commun."xsd:string |
| http://purl.uniprot.org/citations/8135828 | http://purl.uniprot.org/core/name | "Biochem. Biophys. Res. Commun."xsd:string |
| http://purl.uniprot.org/citations/8135828 | http://purl.uniprot.org/core/pages | "818-825"xsd:string |
| http://purl.uniprot.org/citations/8135828 | http://purl.uniprot.org/core/pages | "818-825"xsd:string |
| http://purl.uniprot.org/citations/8135828 | http://purl.uniprot.org/core/title | "Structural analysis of cDNAs for subunits of human mitochondrial fatty acid beta-oxidation trifunctional protein."xsd:string |
| http://purl.uniprot.org/citations/8135828 | http://purl.uniprot.org/core/title | "Structural analysis of cDNAs for subunits of human mitochondrial fatty acid beta-oxidation trifunctional protein."xsd:string |
| http://purl.uniprot.org/citations/8135828 | http://purl.uniprot.org/core/volume | "199"xsd:string |
| http://purl.uniprot.org/citations/8135828 | http://purl.uniprot.org/core/volume | "199"xsd:string |
| http://purl.uniprot.org/citations/8135828 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/8135828 |
| http://purl.uniprot.org/citations/8135828 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/8135828 |