http://purl.uniprot.org/citations/1518827 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/1518827 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/1518827 | http://www.w3.org/2000/01/rdf-schema#comment | "We have isolated a homolog for the flavoprotein subunit of succinate dehydrogenase [succinate:(acceptor) oxidoreductase, EC 1.3.99.1] from Saccharomyces cerevisiae and used the obtained peptide sequences to clone and characterize the corresponding gene. It contained an open reading frame of 1923 base pairs and encoded a protein of 640 amino acids (M(r), 70,238) that showed approximately 49% and approximately 28% identity with the Escherichia coli and Bacillus subtilis enzymes, respectively. All features of the FAD cofactor binding site were completely conserved. Comparison of the deduced protein sequence with the N-terminal sequence determined from the isolated protein revealed an N-terminal extension of 28 amino acids that presumably represents a mitochondrial signal sequence. After in vitro transcription and translation, the preprotein was efficiently imported into isolated yeast mitochondria, cleaved to its mature form, and assembled into the membrane-bound succinate dehydrogenase complex."xsd:string |
http://purl.uniprot.org/citations/1518827 | http://purl.org/dc/terms/identifier | "doi:10.1073/pnas.89.17.8011"xsd:string |
http://purl.uniprot.org/citations/1518827 | http://purl.org/dc/terms/identifier | "doi:10.1073/pnas.89.17.8011"xsd:string |
http://purl.uniprot.org/citations/1518827 | http://purl.uniprot.org/core/author | "Blobel G."xsd:string |
http://purl.uniprot.org/citations/1518827 | http://purl.uniprot.org/core/author | "Blobel G."xsd:string |
http://purl.uniprot.org/citations/1518827 | http://purl.uniprot.org/core/author | "Pain D."xsd:string |
http://purl.uniprot.org/citations/1518827 | http://purl.uniprot.org/core/author | "Pain D."xsd:string |
http://purl.uniprot.org/citations/1518827 | http://purl.uniprot.org/core/author | "Schuelke N."xsd:string |
http://purl.uniprot.org/citations/1518827 | http://purl.uniprot.org/core/author | "Schuelke N."xsd:string |
http://purl.uniprot.org/citations/1518827 | http://purl.uniprot.org/core/date | "1992"xsd:gYear |
http://purl.uniprot.org/citations/1518827 | http://purl.uniprot.org/core/date | "1992"xsd:gYear |
http://purl.uniprot.org/citations/1518827 | http://purl.uniprot.org/core/name | "Proc. Natl. Acad. Sci. U.S.A."xsd:string |
http://purl.uniprot.org/citations/1518827 | http://purl.uniprot.org/core/name | "Proc. Natl. Acad. Sci. U.S.A."xsd:string |
http://purl.uniprot.org/citations/1518827 | http://purl.uniprot.org/core/pages | "8011-8015"xsd:string |
http://purl.uniprot.org/citations/1518827 | http://purl.uniprot.org/core/pages | "8011-8015"xsd:string |
http://purl.uniprot.org/citations/1518827 | http://purl.uniprot.org/core/title | "Primary structure, import, and assembly of the yeast homolog of succinate dehydrogenase flavoprotein."xsd:string |
http://purl.uniprot.org/citations/1518827 | http://purl.uniprot.org/core/title | "Primary structure, import, and assembly of the yeast homolog of succinate dehydrogenase flavoprotein."xsd:string |
http://purl.uniprot.org/citations/1518827 | http://purl.uniprot.org/core/volume | "89"xsd:string |
http://purl.uniprot.org/citations/1518827 | http://purl.uniprot.org/core/volume | "89"xsd:string |
http://purl.uniprot.org/citations/1518827 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/1518827 |
http://purl.uniprot.org/citations/1518827 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/1518827 |
http://purl.uniprot.org/citations/1518827 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/1518827 |
http://purl.uniprot.org/citations/1518827 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/1518827 |