During apoptosis, initiator caspases (8, 9 and 10) activate downstream executioner
caspases (3, 6 and 7) by cleaving the IDC (interdomain connector) at two sites. Here, we …

Caspases are central to apoptosis, and the principal executioner caspases, caspase-3 and-
7, were reported to be similar in activity, primary structure, and three-dimensional structure …

A unified model for initiator caspase activation has previously been proposed based on the
biochemical analysis of caspase-8 and-9. Caspase-2 is structurally related to caspase-9, but …

Caspase-7 is an obligate dimer of catalytic domains, with generation of activity requiring
limited proteolysis within a region that separates the large and small chains of each domain …

Our recent characterization of porcine caspase-15 suggested that the amino terminus of the
small catalytic subunit is formed by proteolytic processing between the consecutive …

Caspase activation is the'point of no return'commitment to cell death. Synthesized as
inactive zymogens, it is essential that the caspases remain inactive until the death signal is …

Various apoptotic signals can activate caspases 3 and 7 by triggering the L2 loop cleavage
of their proenzymes. These two enzymes have highly similar structures and functions, and …

Dimeric effectors caspase 3 and caspase 7 are activated by initiator caspase processing. In
this study, we report the crystal structures of effector caspase 6 (CASP6) zymogen and N …

Apoptosis is primarily executed by active caspases, which are derived from the inactive
procaspase zymogens through proteolytic cleavage. Here we report the crystal structures of …

Studying the interactions between a protease and its protein substrates at a molecular level
is crucial for identifying the factors facilitating selection of particular proteolytic substrates …