RDF/XMLNTriplesTurtleShow queryShare
SubjectPredicateObject
http://purl.uniprot.org/citations/9144407http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9144407http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9144407http://www.w3.org/2000/01/rdf-schema#comment"A full-length cDNA coding for a putative intestinal carboxylesterase (iCE) was isolated from a human small intestine cDNA library. The cDNA has an open reading frame of 559 amino acids with up to 65% homology to other carboxylesterases of different mammalian species. The deduced amino-acid sequence contains many structural features, that are highly conserved among all carboxylesterase isoenzymes, like the serine esterase active site, an ER-retention signal and one Asn-Xxx-Thr site for N-linked carbohydrate addition. Northern blot analysis revealed that the corresponding mRNA is 3.4-3.6 kb in size and is preferentially expressed in human intestine with a weak signal also in liver. Analysis of cells from the gastrointestinal tract unveiled site-specific, transcriptional regulation of iCE, with higher expression in small intestine and lower expression in colon and rectum. The high expression in small intestine is attributable to a higher expression in jejunum compared to duodenum and ileum."xsd:string
http://purl.uniprot.org/citations/9144407http://purl.org/dc/terms/identifier"doi:10.1006/bbrc.1997.6413"xsd:string
http://purl.uniprot.org/citations/9144407http://purl.org/dc/terms/identifier"doi:10.1006/bbrc.1997.6413"xsd:string
http://purl.uniprot.org/citations/9144407http://purl.uniprot.org/core/author"Becker A."xsd:string
http://purl.uniprot.org/citations/9144407http://purl.uniprot.org/core/author"Becker A."xsd:string
http://purl.uniprot.org/citations/9144407http://purl.uniprot.org/core/author"Langmann T."xsd:string
http://purl.uniprot.org/citations/9144407http://purl.uniprot.org/core/author"Langmann T."xsd:string
http://purl.uniprot.org/citations/9144407http://purl.uniprot.org/core/author"Aslanidis C."xsd:string
http://purl.uniprot.org/citations/9144407http://purl.uniprot.org/core/author"Aslanidis C."xsd:string
http://purl.uniprot.org/citations/9144407http://purl.uniprot.org/core/author"Schmitz G."xsd:string
http://purl.uniprot.org/citations/9144407http://purl.uniprot.org/core/author"Schmitz G."xsd:string
http://purl.uniprot.org/citations/9144407http://purl.uniprot.org/core/author"Daig R."xsd:string
http://purl.uniprot.org/citations/9144407http://purl.uniprot.org/core/author"Daig R."xsd:string
http://purl.uniprot.org/citations/9144407http://purl.uniprot.org/core/author"Schwer H."xsd:string
http://purl.uniprot.org/citations/9144407http://purl.uniprot.org/core/author"Schwer H."xsd:string
http://purl.uniprot.org/citations/9144407http://purl.uniprot.org/core/date"1997"xsd:gYear
http://purl.uniprot.org/citations/9144407http://purl.uniprot.org/core/date"1997"xsd:gYear
http://purl.uniprot.org/citations/9144407http://purl.uniprot.org/core/name"Biochem. Biophys. Res. Commun."xsd:string
http://purl.uniprot.org/citations/9144407http://purl.uniprot.org/core/name"Biochem. Biophys. Res. Commun."xsd:string
http://purl.uniprot.org/citations/9144407http://purl.uniprot.org/core/pages"117-120"xsd:string
http://purl.uniprot.org/citations/9144407http://purl.uniprot.org/core/pages"117-120"xsd:string
http://purl.uniprot.org/citations/9144407http://purl.uniprot.org/core/title"Molecular cloning and characterization of a novel putative carboxylesterase, present in human intestine and liver."xsd:string
http://purl.uniprot.org/citations/9144407http://purl.uniprot.org/core/title"Molecular cloning and characterization of a novel putative carboxylesterase, present in human intestine and liver."xsd:string