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http://purl.uniprot.org/citations/1317175http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/1317175http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/1317175http://www.w3.org/2000/01/rdf-schema#comment"A genomic clone of glucocerebrosidase (D-glucosyl-N-acyl-sphingosine glucohydrolase; E.C. 3.2.1.45) purified from a genomic library derived from a Balb/c mouse was analyzed by restriction mapping and nucleotide sequencing of its promoter and protein coding regions. Promoter activity was functionally assessed by ligation of a 2 kb glucocerebrosidase fragment to the protein coding segment of a bacterial neomycin resistance gene. Smaller segments of the 5' flanking sequence were then analyzed for their ability to initiate transcription of the chloramphenicol acetyltransferase reporter gene. A 319 bp Eco RI-Bgl II fragment (containing 259 bp upstream of the cDNA 5' limit) ligated to the chloramphenicol acetyltransferase open reading frame produced considerable activity."xsd:string
http://purl.uniprot.org/citations/1317175http://purl.org/dc/terms/identifier"doi:10.1016/s0006-291x(05)80049-x"xsd:string
http://purl.uniprot.org/citations/1317175http://purl.org/dc/terms/identifier"doi:10.1016/s0006-291x(05)80049-x"xsd:string
http://purl.uniprot.org/citations/1317175http://purl.uniprot.org/core/author"Murray G.J."xsd:string
http://purl.uniprot.org/citations/1317175http://purl.uniprot.org/core/author"Murray G.J."xsd:string
http://purl.uniprot.org/citations/1317175http://purl.uniprot.org/core/author"O'Neill R.R."xsd:string
http://purl.uniprot.org/citations/1317175http://purl.uniprot.org/core/author"O'Neill R.R."xsd:string
http://purl.uniprot.org/citations/1317175http://purl.uniprot.org/core/author"Carstea E.D."xsd:string
http://purl.uniprot.org/citations/1317175http://purl.uniprot.org/core/author"Carstea E.D."xsd:string
http://purl.uniprot.org/citations/1317175http://purl.uniprot.org/core/date"1992"xsd:gYear
http://purl.uniprot.org/citations/1317175http://purl.uniprot.org/core/date"1992"xsd:gYear
http://purl.uniprot.org/citations/1317175http://purl.uniprot.org/core/name"Biochem. Biophys. Res. Commun."xsd:string
http://purl.uniprot.org/citations/1317175http://purl.uniprot.org/core/name"Biochem. Biophys. Res. Commun."xsd:string
http://purl.uniprot.org/citations/1317175http://purl.uniprot.org/core/pages"1477-1483"xsd:string
http://purl.uniprot.org/citations/1317175http://purl.uniprot.org/core/pages"1477-1483"xsd:string
http://purl.uniprot.org/citations/1317175http://purl.uniprot.org/core/title"Molecular and functional characterization of the murine glucocerebrosidase gene."xsd:string
http://purl.uniprot.org/citations/1317175http://purl.uniprot.org/core/title"Molecular and functional characterization of the murine glucocerebrosidase gene."xsd:string
http://purl.uniprot.org/citations/1317175http://purl.uniprot.org/core/volume"184"xsd:string
http://purl.uniprot.org/citations/1317175http://purl.uniprot.org/core/volume"184"xsd:string
http://purl.uniprot.org/citations/1317175http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/1317175
http://purl.uniprot.org/citations/1317175http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/1317175
http://purl.uniprot.org/citations/1317175http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/1317175
http://purl.uniprot.org/citations/1317175http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/1317175