@prefix this: . @prefix sub: . @prefix beldoc: . @prefix rdfs: . @prefix rdf: . @prefix xsd: . @prefix dct: . @prefix dce: . @prefix pav: . @prefix np: . @prefix belv: . @prefix prov: . @prefix chebi: . @prefix go: . @prefix Protein: . @prefix hgnc: . @prefix geneProductOf: . @prefix hasAgent: . @prefix species: . @prefix occursIn: . @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 hasAgent: sub:_2; a go:0016791 . sub:_2 geneProductOf: hgnc:13417; a Protein: . sub:_3 occursIn: species:9606; rdf:object sub:_1; rdf:predicate belv:decreases; rdf:subject chebi:7733; a rdf:Statement . sub:assertion rdfs:label "a(CHEBI:\"okadaic acid\") -| phos(p(HGNC:PPP2R3B))" . } 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:_5; pav:version "1.4" . sub:_4 prov:value "To determine whether PP2A can directly dephosphorylate the autophosphorylation sites on the Pim kinases, Pim-3 immunoprecipitates were subjected to in vitro kinase assays followed by in vitro phosphatase assays. When wild-type Pim-3 immunoprecipitates were subjected to in vitro kinase-in vitro phosphatase reactions, recombinant PP2A was able to dephosphorylate the autophosphorylation sites on Pim-3 (Fig. 2, lanes 4 and 5). This effect of PP2A was blocked by addition of okadaic acid, an inhibitor of PP2A catalytic activity, to the phosphatase reactions (Fig. 2, lanes 7 and 8)."; prov:wasQuotedFrom pubmed:12473674 . sub:_5 rdfs:label "Selventa" . sub:assertion prov:hadPrimarySource pubmed:12473674; prov:wasDerivedFrom beldoc:, sub:_4 . } sub:pubinfo { this: dct:created "2014-07-03T14:30:07.830+02:00"^^xsd:dateTime; pav:createdBy orcid:0000-0001-6818-334X, orcid:0000-0002-1267-0234 . }