Nanopublications

Matches in Nanopublications for { ?s ?p ?o <http://www.tkuhn.ch/bel2nanopub/RAuPatWKvZlcJBOIf4zAX9ibzD9WcX7mcw3skvevVjXn8#provenance>. }

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_9 label "Selventa" provenance.
_9 comment "support@belframework.org" provenance.
small_corpus.bel title "BEL Framework Small Corpus Document" provenance.
small_corpus.bel description "Approximately 2000 hand curated statements drawn from 57 PubMeds." provenance.
small_corpus.bel version "1.6" provenance.
small_corpus.bel authoredBy _9 provenance.
assertion wasDerivedFrom small_corpus.bel provenance.
assertion wasDerivedFrom _8 provenance.
assertion hadPrimarySource 12764228 provenance.
_8 wasQuotedFrom 12764228 provenance.
_8 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." provenance.
small_corpus.bel license "Creative Commons Attribution-Non-Commercial-ShareAlike 3.0 Unported License" provenance.