. . . . . . . . . . . . . . . . . . . . . . . "TextLocation" . "Results" . "tscript(complex(p(MGI:Ppargc1a),p(MGI:Mef2c))) => r(MGI:Ppargc1a)" . "Approximately 2000 hand curated statements drawn from 57 PubMeds." . "Copyright (c) 2011-2012, Selventa. All Rights Reserved." . "BEL Framework Small Corpus Document" . "Creative Commons Attribution-Non-Commercial-ShareAlike 3.0 Unported License" . . "1.6" . "To confirm that the coactivation of MEF2C by PGC-1α observed in reporter gene assays\n(Fig. 3B) was linked to direct binding of these two proteins, we tested whether\nPGC-1α directly interacts with MEF2C on this MEF-binding site. Increasing amounts\nof PGC-1α protein (amino acids 31–797) decreased the mobility of the complex\ncontaining MEF2C bound to the MEF-binding site, as visualized by a supershift\nin electrophoretic mobility-shift assays (Fig. 3D). As a control, PGC-1α protein\nthat lacks the MEF2C-interaction domain (amino acids 1–180; see ref. 7) was not\nable to bind to MEF2C. Inclusion of an MEF2- specific antibody was able to supershift\nfurther the protein–DNA complex containing MEF2C, PGC-1α, and the MEF2-binding\nsite (Fig. 3E). Neither a shift nor a supershift could be obtained when using\nthe mutated ΔMEF site. These results indicate that MEF2s bind to the PGC-1α\npromoter and that PGC-1α coactivates MEF2 proteins on the PGC-1α promoter by a\ndirect protein–protein interaction." . . "support@belframework.org" . "Selventa" . . . . "2014-07-03T14:29:34.387+02:00"^^ . . .