@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 go: . @prefix RNA: . @prefix hgnc: . @prefix geneProductOf: . @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 geneProductOf: hgnc:9283; a RNA: . sub:_2 occursIn: species:9606; rdf:object sub:_1; rdf:predicate belv:decreases; rdf:subject go:0001666; a rdf:Statement . sub:assertion rdfs:label "bp(GO:\"response to hypoxia\") -| r(HGNC:PPP1CC)" . } 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 "The importance of PP1 as a CREB phosphatase is illustrated by the finding that brain-targetted genetic inhibition of PP1 in mice correlated with an enhanced learning capability that involved the hyperphosphorylation of a number of proteins, including CREB (145) (see also sect. VIIIC). In normal conditions, two additional serines that control the stability of CREB are kept dephosphorylated by PP1 (359). However, the decreased expression of PP1-gamma following hypoxia results in the hyperphosphorylation and subsequent ubiquitin-mediated degradation of CREB."; prov:wasQuotedFrom pubmed:14715909 . sub:_4 rdfs:label "Selventa" . sub:assertion prov:hadPrimarySource pubmed:14715909; prov:wasDerivedFrom beldoc:, sub:_3 . } sub:pubinfo { this: dct:created "2014-07-03T14:30:19.667+02:00"^^xsd:dateTime; pav:createdBy orcid:0000-0001-6818-334X, orcid:0000-0002-1267-0234 . }