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:_7 ;
    pav:version "1.6" .
  sub:_6 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:_7 rdfs:comment "support@belframework.org" ;
    rdfs:label "Selventa" .
  sub:assertion prov:hadPrimarySource pubmed:12764228 ;
    prov:wasDerivedFrom beldoc: , sub:_6 .
}