@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 obo: . @prefix Protein: . @prefix mgi: . @prefix geneProductOf: . @prefix hasPart: . @prefix ProteinComplex: . @prefix hasAgent: . @prefix RNA: . @prefix mesh: . @prefix occursIn: . @prefix hasAnnotation: . @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 hasAgent: sub:_2; a go:0042789 . sub:_2 hasPart: sub:_3, sub:_4; a ProteinComplex: . sub:_3 geneProductOf: mgi:1342774; a Protein: . sub:_4 geneProductOf: mgi:99458; a Protein: . sub:_5 geneProductOf: mgi:1342774; a RNA: . sub:_6 occursIn: mesh:D018482, obo:UBERON_0002107, species:10090; hasAnnotation: sub:_7; rdf:object sub:_5; rdf:predicate belv:directlyIncreases; rdf:subject sub:_1; a rdf:Statement . sub:_7 dct:subject "TextLocation"; rdf:value "Results" . sub:assertion rdfs:label "tscript(complex(p(MGI:Ppargc1a),p(MGI:Mef2c))) => r(MGI:Ppargc1a)" . } 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:_9; pav:version "20131211" . sub:_8 prov:value """To confirm that the coactivation of MEF2C by PGC-1α observed in reporter gene assays (Fig. 3B) was linked to direct binding of these two proteins, we tested whether PGC-1α directly interacts with MEF2C on this MEF-binding site. Increasing amounts of PGC-1α protein (amino acids 31–797) decreased the mobility of the complex containing MEF2C bound to the MEF-binding site, as visualized by a supershift in electrophoretic mobility-shift assays (Fig. 3D). As a control, PGC-1α protein that lacks the MEF2C-interaction domain (amino acids 1–180; see ref. 7) was not able to bind to MEF2C. Inclusion of an MEF2- specific antibody was able to supershift further the protein–DNA complex containing MEF2C, PGC-1α, and the MEF2-binding site (Fig. 3E). Neither a shift nor a supershift could be obtained when using the mutated ΔMEF site. These results indicate that MEF2s bind to the PGC-1α promoter and that PGC-1α coactivates MEF2 proteins on the PGC-1α promoter by a direct protein–protein interaction."""; prov:wasQuotedFrom pubmed:12764228 . sub:_9 rdfs:comment "support@belframework.org"; rdfs:label "Selventa" . sub:assertion prov:hadPrimarySource pubmed:12764228; prov:wasDerivedFrom beldoc:, sub:_8 . } sub:pubinfo { this: dct:created "2014-07-03T14:31:18.172+02:00"^^xsd:dateTime; pav:createdBy orcid:0000-0001-6818-334X, orcid:0000-0002-1267-0234 . }