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http://purl.uniprot.org/citations/9559670http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9559670http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9559670http://www.w3.org/2000/01/rdf-schema#comment"The interaction of the adrenoleukodystrophy protein (ALDP), mutated in the peroxisomal disorder X-linked adrenoleukodystrophy, and the very long-chain acyl-CoA synthetase (VLACS), the enzyme whose function is missing in this disease, remains obscure. As a first step to studying this interaction in wild type versus ALDP-deficient mice, we have cloned a VLACS cDNA from mouse liver. The 1860 bp open reading frame encodes a 620 amino acid protein with a predicted molecular mass of 70.3 kDa. By Northern blot analysis, a 2.6 kbp VLACS mRNA was highly abundant in liver and kidney and present at low levels in brain and testes. By RT-PCR VLACS mRNA was also detected in heart and lung but remained undetectable in skeletal muscle and spleen. In contrast to the peroxisomal beta-oxidation marker acyl-CoA oxidase, whose mRNA level steadily increases during brain development, the VLACS transcript was found at a constant low level from embryo through adulthood, suggesting that additional isoforms may exist in brain."xsd:string
http://purl.uniprot.org/citations/9559670http://purl.org/dc/terms/identifier"doi:10.1016/s0014-5793(98)00255-5"xsd:string
http://purl.uniprot.org/citations/9559670http://purl.org/dc/terms/identifier"doi:10.1016/s0014-5793(98)00255-5"xsd:string
http://purl.uniprot.org/citations/9559670http://purl.uniprot.org/core/author"Berger J."xsd:string
http://purl.uniprot.org/citations/9559670http://purl.uniprot.org/core/author"Berger J."xsd:string
http://purl.uniprot.org/citations/9559670http://purl.uniprot.org/core/author"Neumann H."xsd:string
http://purl.uniprot.org/citations/9559670http://purl.uniprot.org/core/author"Neumann H."xsd:string
http://purl.uniprot.org/citations/9559670http://purl.uniprot.org/core/author"Forss-Petter S."xsd:string
http://purl.uniprot.org/citations/9559670http://purl.uniprot.org/core/author"Forss-Petter S."xsd:string
http://purl.uniprot.org/citations/9559670http://purl.uniprot.org/core/author"Truppe C."xsd:string
http://purl.uniprot.org/citations/9559670http://purl.uniprot.org/core/author"Truppe C."xsd:string
http://purl.uniprot.org/citations/9559670http://purl.uniprot.org/core/date"1998"xsd:gYear
http://purl.uniprot.org/citations/9559670http://purl.uniprot.org/core/date"1998"xsd:gYear
http://purl.uniprot.org/citations/9559670http://purl.uniprot.org/core/name"FEBS Lett."xsd:string
http://purl.uniprot.org/citations/9559670http://purl.uniprot.org/core/name"FEBS Lett."xsd:string
http://purl.uniprot.org/citations/9559670http://purl.uniprot.org/core/pages"305-309"xsd:string
http://purl.uniprot.org/citations/9559670http://purl.uniprot.org/core/pages"305-309"xsd:string
http://purl.uniprot.org/citations/9559670http://purl.uniprot.org/core/title"cDNA cloning and mRNA distribution of a mouse very long-chain acyl-CoA synthetase."xsd:string
http://purl.uniprot.org/citations/9559670http://purl.uniprot.org/core/title"cDNA cloning and mRNA distribution of a mouse very long-chain acyl-CoA synthetase."xsd:string
http://purl.uniprot.org/citations/9559670http://purl.uniprot.org/core/volume"425"xsd:string
http://purl.uniprot.org/citations/9559670http://purl.uniprot.org/core/volume"425"xsd:string
http://purl.uniprot.org/citations/9559670http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/9559670
http://purl.uniprot.org/citations/9559670http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/9559670