@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 scomp: . @prefix ProteinComplex: . @prefix hasAgent: . @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 { scomp:AP-1%20Complex a ProteinComplex: . sub:_1 hasAgent: scomp:AP-1%20Complex; a go:0042789 . sub:_2 geneProductOf: hgnc:7155; a RNA: . sub:_3 occursIn: species:9606; rdf:object sub:_2; rdf:predicate belv:directlyIncreases; rdf:subject sub:_1; a rdf:Statement . sub:assertion rdfs:label "tscript(complex(SCOMP:\"AP-1 Complex\")) => r(HGNC:MMP1)" . } 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 "20131211" . sub:_4 prov:value "In gel shift assays however, the Erg protein bound little or not to the collagenase1 promoter, whereas it bound to the stromelysin1 promoter. By site-specific mutagenesis, we identified one major site at -88 that abolished collagenase1 promoter activation by Erg. Surprisingly, mutation of the collagenase1 AP1 site at -73 also abolished the activation by Erg suggesting that Erg cooperates with Fos/Jun in collagenase1 promoter regulation."; prov:wasQuotedFrom pubmed:8957070 . sub:_5 rdfs:label "Selventa" . sub:assertion prov:hadPrimarySource pubmed:8957070; prov:wasDerivedFrom beldoc:, sub:_4 . } sub:pubinfo { this: dct:created "2014-07-03T14:33:55.460+02:00"^^xsd:dateTime; pav:createdBy orcid:0000-0001-6818-334X, orcid:0000-0002-1267-0234 . }