@prefix dcterms: . @prefix this: . @prefix sub: . @prefix beldoc: . @prefix rdfs: . @prefix rdf: . @prefix xsd: . @prefix dce: . @prefix pav: . @prefix np: . @prefix belv: . @prefix prov: . @prefix chebi: . @prefix RNA: . @prefix rgd: . @prefix geneProductOf: . @prefix mesh: . @prefix occursIn: . @prefix species: . @prefix pubmed: . @prefix orcid: . sub:Head { this: np:hasAssertion sub:assertion; np:hasProvenance sub:provenance; np:hasPublicationInfo sub:pubinfo; a np:Nanopublication . } sub:assertion { sub:_1 geneProductOf: rgd:2303; a RNA: . sub:_2 occursIn: mesh:D009130, species:10116; rdf:object sub:_1; rdf:predicate belv:increases; rdf:subject chebi:23965; a rdf:Statement . sub:assertion rdfs:label "a(CHEBI:estradiol) -> r(RGD:Cd38)" . } sub:provenance { beldoc: dce:description "Approximately 61,000 statements."; dce:rights "Copyright (c) 2011-2012, Selventa. All rights reserved."; dce:title "BEL Framework Large Corpus Document"; pav:authoredBy sub:_4; pav:version "1.4" . sub:_3 prov:value "A cell surface glycoprotein, CD38, catalyzes the synthesis and breakdown of cADPR and thus possesses bifunctional enzymatic activity. The results demonstrate that cyclase and hydrolase activities are associated with a single protein fraction, similar to CD38 in uteri from both ovariectomized and estradiol-treated rats, and estradiol-17 beta causes 1) increased CD38 mRNA and protein expression and 2) significantly enhanced cyclase but not hydrolase activity."; prov:wasQuotedFrom pubmed:11870063 . sub:_4 rdfs:label "Selventa" . sub:assertion prov:hadPrimarySource pubmed:11870063; prov:wasDerivedFrom beldoc:, sub:_3 . } sub:pubinfo { this: dcterms:created "2014-07-03T14:30:01.385+02:00"^^xsd:dateTime; pav:createdBy orcid:0000-0001-6818-334X, orcid:0000-0002-1267-0234 . }