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http://purl.uniprot.org/citations/8661694http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/8661694http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/8661694http://www.w3.org/2000/01/rdf-schema#comment"Short-chain acyl-CoA dehydrogenase (SCAD) is one of four straight-chain length specific enzymes involved in the first step of fatty acid beta-oxidation. To further understand the similarities between the members of this gene family, to characterize how the gene is regulated, and to determine if there is coordinate regulation between these similar genes, we have isolated genomic clones containing the mouse Acads gene. We show that Acads is a compact, single-copy gene approximately 5000 bp in size. We sequenced the entire coding portion of the gene, all of the intron/exon junctions, and an 850-bp segment upstream of the translation start site. We have determined that the gene consists of 10 exons ranging in size from 57 bp to 703 bp, and 9 introns ranging in size from 80 bp to approximately 700 bp. The 5' region of the mouse Acads gene lacks a TATA box or a CAAT box, is GC rich, and also lacks any similarity to the related gene, medium-chain acyl-CoA dehydrogenase. This is the initial report of the gene structure and 5' regulatory sequence of the short-chain acyl-CoA dehydrogenase gene in any species."xsd:string
http://purl.uniprot.org/citations/8661694http://purl.org/dc/terms/identifier"doi:10.1007/s003359900078"xsd:string
http://purl.uniprot.org/citations/8661694http://purl.org/dc/terms/identifier"doi:10.1007/s003359900078"xsd:string
http://purl.uniprot.org/citations/8661694http://purl.uniprot.org/core/author"Kelly C.L."xsd:string
http://purl.uniprot.org/citations/8661694http://purl.uniprot.org/core/author"Kelly C.L."xsd:string
http://purl.uniprot.org/citations/8661694http://purl.uniprot.org/core/author"Wood P.A."xsd:string
http://purl.uniprot.org/citations/8661694http://purl.uniprot.org/core/author"Wood P.A."xsd:string
http://purl.uniprot.org/citations/8661694http://purl.uniprot.org/core/date"1996"xsd:gYear
http://purl.uniprot.org/citations/8661694http://purl.uniprot.org/core/date"1996"xsd:gYear
http://purl.uniprot.org/citations/8661694http://purl.uniprot.org/core/name"Mamm. Genome"xsd:string
http://purl.uniprot.org/citations/8661694http://purl.uniprot.org/core/name"Mamm Genome"xsd:string
http://purl.uniprot.org/citations/8661694http://purl.uniprot.org/core/pages"262-264"xsd:string
http://purl.uniprot.org/citations/8661694http://purl.uniprot.org/core/pages"262-264"xsd:string
http://purl.uniprot.org/citations/8661694http://purl.uniprot.org/core/title"Cloning and characterization of the mouse short-chain acyl-CoA dehydrogenase gene."xsd:string
http://purl.uniprot.org/citations/8661694http://purl.uniprot.org/core/title"Cloning and characterization of the mouse short-chain acyl-CoA dehydrogenase gene."xsd:string
http://purl.uniprot.org/citations/8661694http://purl.uniprot.org/core/volume"7"xsd:string
http://purl.uniprot.org/citations/8661694http://purl.uniprot.org/core/volume"7"xsd:string
http://purl.uniprot.org/citations/8661694http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/8661694
http://purl.uniprot.org/citations/8661694http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/8661694
http://purl.uniprot.org/citations/8661694http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/8661694
http://purl.uniprot.org/citations/8661694http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/8661694
http://purl.uniprot.org/uniprot/Q6LCR2http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/8661694
http://purl.uniprot.org/uniprot/#_Q6LCR2-citation-8661694http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/8661694