executioner caspases, such as caspase-3, -6 or –7, were activated by proteolytic cleavage by initiator caspases such as caspase-2, -8, -9 or –10
active dimer fragments capable in turn to process various substrates as the PARP (Poly-ADP-Ribose-Polymerase)
dimerization alone was sufficient to induce initiator caspase activation
full p20 caspase-3 fragment processing is required for TRAIL-mediated apoptosis execution in a Bax-dependent fashion
IAPs, have been shown to bind to and inhibit caspases downstream mitochondria.
XIAP inhibits caspase-3 via its BIR2 domain
exogenous cytochrome c enabled caspase-3 activation
Smac-induced cytochrome c release has been shown to be independent of Bax in human carcinoma cells