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All rights reserved. http://resource.belframework.org/belframework/20131211/knowledge/large_corpus.bel http://purl.org/dc/elements/1.1/title BEL Framework Large Corpus Document http://resource.belframework.org/belframework/20131211/knowledge/large_corpus.bel http://purl.org/pav/authoredBy http://www.tkuhn.ch/bel2nanopub/RAy1wyUbUWLc9gb1I1RC6IFAkY30HSVBynGcUJpFerlBM#_7 http://resource.belframework.org/belframework/20131211/knowledge/large_corpus.bel http://purl.org/pav/version 20131211 http://www.tkuhn.ch/bel2nanopub/RAy1wyUbUWLc9gb1I1RC6IFAkY30HSVBynGcUJpFerlBM#_6 http://www.w3.org/ns/prov#value cells were left untreated or treated with H202 and formaldehyde followed by incubation with the profluorescent Z-DEVD-rhodamine 110 substrate. The catalytic activity of the two effectors, caspase-3 and caspase-7, was determined by measuring the fluorescence of the cleavage product. In the presence of 100 Amol/L H2O2, the caspase-3/7 activity was 8- to 11-fold elevated in parental, mock, and Wt K-ras–transfected cells in comparison with the untreated cells, whereas the enzymatic activity was only 2- to 3-fold enhanced in the two K-ras mutants (Fig. 5D). 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