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http://purl.uniprot.org/citations/9565681http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9565681http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9565681http://www.w3.org/2000/01/rdf-schema#comment"Carboxylesterases (EC 3.1.1.1) comprise a group of serine hydrolases with at least 20 genetically distinct loci in mice. Here, we describe differential display PCR-based cloning of a cDNA, encoding a novel murine carboxylesterase termed ES-x, which was expressed predominantly in liver but also in kidney and lung. The cDNA of ES-x spanned a 2249-bp sequence with an open reading frame encoding 565 amino acids, including an N-terminal hydrophobic signal peptide which directs the synthesis into microsomal lumen and a C-terminal HVEL consensus sequence for retaining the protein in the lumen of the endoplasmic reticulum. The predicted amino acid sequence of ES-x exhibited 75% identity with rat liver pI 6.1 esterase. We further demonstrate that feeding mice with diets containing cholestyramine or sodium cholate increases mRNA-expression of ES-x in liver 2.5- to 3-fold."xsd:string
http://purl.uniprot.org/citations/9565681http://purl.org/dc/terms/identifier"doi:10.1016/s0167-4781(98)00023-2"xsd:string
http://purl.uniprot.org/citations/9565681http://purl.org/dc/terms/identifier"doi:10.1016/s0167-4781(98)00023-2"xsd:string
http://purl.uniprot.org/citations/9565681http://purl.uniprot.org/core/author"Assmann G."xsd:string
http://purl.uniprot.org/citations/9565681http://purl.uniprot.org/core/author"Assmann G."xsd:string
http://purl.uniprot.org/citations/9565681http://purl.uniprot.org/core/author"Seedorf U."xsd:string
http://purl.uniprot.org/citations/9565681http://purl.uniprot.org/core/author"Seedorf U."xsd:string
http://purl.uniprot.org/citations/9565681http://purl.uniprot.org/core/author"Ellinghaus P."xsd:string
http://purl.uniprot.org/citations/9565681http://purl.uniprot.org/core/author"Ellinghaus P."xsd:string
http://purl.uniprot.org/citations/9565681http://purl.uniprot.org/core/date"1998"xsd:gYear
http://purl.uniprot.org/citations/9565681http://purl.uniprot.org/core/date"1998"xsd:gYear
http://purl.uniprot.org/citations/9565681http://purl.uniprot.org/core/name"Biochim. Biophys. Acta"xsd:string
http://purl.uniprot.org/citations/9565681http://purl.uniprot.org/core/name"Biochim. Biophys. Acta"xsd:string
http://purl.uniprot.org/citations/9565681http://purl.uniprot.org/core/pages"175-179"xsd:string
http://purl.uniprot.org/citations/9565681http://purl.uniprot.org/core/pages"175-179"xsd:string
http://purl.uniprot.org/citations/9565681http://purl.uniprot.org/core/title"Cloning and sequencing of a novel murine liver carboxylesterase cDNA."xsd:string
http://purl.uniprot.org/citations/9565681http://purl.uniprot.org/core/title"Cloning and sequencing of a novel murine liver carboxylesterase cDNA."xsd:string
http://purl.uniprot.org/citations/9565681http://purl.uniprot.org/core/volume"1397"xsd:string
http://purl.uniprot.org/citations/9565681http://purl.uniprot.org/core/volume"1397"xsd:string
http://purl.uniprot.org/citations/9565681http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/9565681
http://purl.uniprot.org/citations/9565681http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/9565681
http://purl.uniprot.org/citations/9565681http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/9565681
http://purl.uniprot.org/citations/9565681http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/9565681