@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 schem: . @prefix hgnc: . @prefix proteinModification: . @prefix psimod: . @prefix hasAnnotation: . @prefix atcc: . @prefix occursIn: . @prefix species: . @prefix mesh: . @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 belv:variantOf hgnc:4616; a proteinModification:, psimod:00696 . sub:_2 occursIn: mesh:D002460, mesh:D007668, atcc:CRL-2210.aspx, species:10116; hasAnnotation: sub:_3; rdf:object sub:_1; rdf:predicate belv:increases; rdf:subject schem:Isoproterenol; a rdf:Statement . sub:_3 dct:subject "TextLocation"; rdf:value "Results" . sub:assertion rdfs:label "a(SCHEM:Isoproterenol) -> p(HGNC:GSK3A,pmod(P,S,21))" . } sub:provenance { beldoc: dce:description "Approximately 2000 hand curated statements drawn from 57 PubMeds."; dce:rights "Copyright (c) 2011-2012, Selventa. All Rights Reserved."; dce:title "BEL Framework Small Corpus Document"; dct:license "Creative Commons Attribution-Non-Commercial-ShareAlike 3.0 Unported License"; pav:authoredBy sub:_5; pav:version "1.6" . sub:_4 prov:value """In Rat1, NIH 3T3, and HEK293 cells, increases in the intracellular levels of cAMP stimulate phosphorylation of GSK-3α and -β, as demonstrated by immunoblotting with GSK-3 phosphorylation-specific antibodies. As shown in Fig. 1, the cell-permeable cAMP analogue 8-Br-cAMP induced a marked increase in phosphorylation of GSK-3α and - β at serine 21 and 9, respectively, whereas the structurally related cGMP analogue 8-Br-cGMP had little effect. Forskolin, which activates adenyl cyclase thus raising intracellular cAMP levels (15), triggered a similar elevation in GSK-3 phosphorylation at serine 21 and 9. In Rat1 cells, isoproterenol, which activates the b-adrenergic receptor stimulating adenylate cyclase and increasing endogenous cAMP levels (16, 17), also efficiently stimulated GSK-3 phosphorylation at these serine sites. In NIH 3T3 cells that contain few of the β-adrenergic receptors, stimulation with other G-protein-coupled receptor agonists, such as lysophosphatidic acid. also led to GSK-3 phosphorylation (data not shown)"""; prov:wasQuotedFrom pubmed:11035810 . sub:_5 rdfs:comment "support@belframework.org"; rdfs:label "Selventa" . sub:assertion prov:hadPrimarySource pubmed:11035810; prov:wasDerivedFrom beldoc:, sub:_4 . } sub:pubinfo { this: dct:created "2014-07-03T14:29:34.657+02:00"^^xsd:dateTime; pav:createdBy orcid:0000-0001-6818-334X, orcid:0000-0002-1267-0234 . }