Matches in Nanopublications for { <http://www.tkuhn.ch/bel2nanopub/RAA23p2d5SpVD86b8H5njLYcUvN-E5_ccYe-NTAx8V0nU#_3> ?p ?o ?g. }
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- _3 wasQuotedFrom 18059173 provenance.
- _3 value "Here we show that two members of histone acetyltransferase complexes without enzymatic activity, hADA2a and hADA3, are required for full activity of beta-catenin. hADA2a and hADA3 physically interact with beta-catenin, and the interaction is mediated through Armadillo repeats 6 through 12 and the C-terminal transactivation domain of beta-catenin. Both hADA2a and hADA3 reside with beta-catenin at the enhancer for the Wnt target gene c-Myc." provenance.