| http://purl.uniprot.org/citations/11095947 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/11095947 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/11095947 | http://www.w3.org/2000/01/rdf-schema#comment | "The human ADH5 gene was reported to lack the last exon compared to other mammalian ADHs and consequently should be expressed as a truncated protein. Here we show with PCR amplification of 3'-cDNA ends that the ADH5 gene harbors the "missing" exon. Besides a cDNA identical to the published sequence, we found full-length transcripts that contained additional codons for eight amino acid residues. Northern blot analysis established the full-length variant as the major transcript with the strongest signal from adult liver. Sequence analysis of genomic DNA confirmed that the ADH5 gene displays composite internal/terminal exons, which can be differentially processed; i.e., 3'-end generation is a result of competition between polyadenylation and splicing."xsd:string |
| http://purl.uniprot.org/citations/11095947 | http://purl.org/dc/terms/identifier | "doi:10.1006/bbrc.2000.3837"xsd:string |
| http://purl.uniprot.org/citations/11095947 | http://purl.org/dc/terms/identifier | "doi:10.1006/bbrc.2000.3837"xsd:string |
| http://purl.uniprot.org/citations/11095947 | http://purl.uniprot.org/core/author | "Hoog J.O."xsd:string |
| http://purl.uniprot.org/citations/11095947 | http://purl.uniprot.org/core/author | "Hoog J.O."xsd:string |
| http://purl.uniprot.org/citations/11095947 | http://purl.uniprot.org/core/author | "Stromberg P."xsd:string |
| http://purl.uniprot.org/citations/11095947 | http://purl.uniprot.org/core/author | "Stromberg P."xsd:string |
| http://purl.uniprot.org/citations/11095947 | http://purl.uniprot.org/core/date | "2000"xsd:gYear |
| http://purl.uniprot.org/citations/11095947 | http://purl.uniprot.org/core/date | "2000"xsd:gYear |
| http://purl.uniprot.org/citations/11095947 | http://purl.uniprot.org/core/name | "Biochem. Biophys. Res. Commun."xsd:string |
| http://purl.uniprot.org/citations/11095947 | http://purl.uniprot.org/core/name | "Biochem Biophys Res Commun"xsd:string |
| http://purl.uniprot.org/citations/11095947 | http://purl.uniprot.org/core/pages | "544-549"xsd:string |
| http://purl.uniprot.org/citations/11095947 | http://purl.uniprot.org/core/pages | "544-549"xsd:string |
| http://purl.uniprot.org/citations/11095947 | http://purl.uniprot.org/core/title | "Human class V alcohol dehydrogenase (ADH5): A complex transcription unit generates C-terminal multiplicity."xsd:string |
| http://purl.uniprot.org/citations/11095947 | http://purl.uniprot.org/core/title | "Human class V alcohol dehydrogenase (ADH5): A complex transcription unit generates C-terminal multiplicity."xsd:string |
| http://purl.uniprot.org/citations/11095947 | http://purl.uniprot.org/core/volume | "278"xsd:string |
| http://purl.uniprot.org/citations/11095947 | http://purl.uniprot.org/core/volume | "278"xsd:string |
| http://purl.uniprot.org/citations/11095947 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/11095947 |
| http://purl.uniprot.org/citations/11095947 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/11095947 |
| http://purl.uniprot.org/citations/11095947 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/11095947 |
| http://purl.uniprot.org/citations/11095947 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/11095947 |
| http://purl.uniprot.org/uniprot/Q9H1A0 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/11095947 |
| http://purl.uniprot.org/uniprot/#_kb.Q9H1A0_up.isolatedFrom_tissue.564 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/11095947 |