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All rights reserved. http://resource.belframework.org/belframework/1.0/knowledge/large_corpus.bel http://purl.org/dc/elements/1.1/title BEL Framework Large Corpus Document http://resource.belframework.org/belframework/1.0/knowledge/large_corpus.bel http://purl.org/pav/authoredBy http://www.tkuhn.ch/bel2nanopub/RAGyqcWgQnim1e8xgzxHT0a9_es2gyPnuKE4hmrY7E4zU#_6 http://resource.belframework.org/belframework/1.0/knowledge/large_corpus.bel http://purl.org/pav/version 1.4 http://www.tkuhn.ch/bel2nanopub/RAGyqcWgQnim1e8xgzxHT0a9_es2gyPnuKE4hmrY7E4zU#_5 http://www.w3.org/ns/prov#value These findings suggest that Par-4, Daxx, and ZIPK may form a ternary complex, though further work is required to verify this hypothesis. ZIPK, Daxx, and Par-4 collaborate in caspase activation and apoptosis induction. Cells transfected individually with plasmids encoding ZIPK, Par-4, or Daxx did not exhibit an increase in apoptosis at the concentrations of plasmid DNA used here (Fig. 6A). In contrast, the percentage of apoptotic cells was increased two- to threefold in cultures of cells coexpressing ZIPK with either Par-4 or Daxx (Fig. 6A). Similarly, coexpressing Daxx with Par-4 elevated the percentage of apoptotic cells by two to threefold compared to the percentage due to expression of either Daxx or Par-4 alone (Fig. 6A). The most striking increase in apoptosis, however, was achieved by expressing all three proteins together. 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