@prefix dc: .
@prefix this: .
@prefix sub: .
@prefix beldoc: .
@prefix rdfs: .
@prefix rdf: .
@prefix xsd: .
@prefix dce: .
@prefix pav: .
@prefix np: .
@prefix belv: .
@prefix prov: .
@prefix go: .
@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:D008099, mesh:D018482, species:10090;
hasAnnotation: sub:_7;
rdf:object sub:_5;
rdf:predicate belv:directlyIncreases;
rdf:subject sub:_1;
a rdf:Statement .
sub:_7 dc: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";
dc:license "Creative Commons Attribution-Non-Commercial-ShareAlike 3.0 Unported License";
pav:authoredBy sub:_9;
pav:version "1.6" .
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: dc:created "2014-07-03T14:29:34.387+02:00"^^xsd:dateTime;
pav:createdBy orcid:0000-0001-6818-334X, orcid:0000-0002-1267-0234 .
}