The activation of caspase-3 represents a critical step in the pathways leading to the
biochemical and morphological changes that underlie apoptosis. Upon induction of …

The caspase-3 zymogen has essentially zero activity until it is cleaved by initiator caspases
during apoptosis. However, a mutation of V266E in the dimer interface activates the …

Caspases form a family of proteinases required for the initiation and execution phases of
apoptosis. Distinct proapoptotic stimuli lead to activation of the initiator caspases-8 and-9 …

Central to the execution phase of apoptosis are the two closely related caspase-3 and-7.
They share common substrate specificity and structure, but differ completely in the sequence …

Although significant efforts have been made to understand the mechanisms of caspase
activation during apoptosis, many questions remain regarding how and when executioner …

Members of the caspase family of cysteine proteases coordinate the highly disparate
processes of apoptosis and inflammation. However, although hundreds of substrates for the …

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-8 is an apoptotic protease that is activated at the cytosolic face of the cell
membrane. Activation relies on adaptor-induced dimerization of monomeric caspase-8 and …

Apoptosis is primarily executed by active caspases, which are derived from the inactive
zymogens. Structural and biochemical studies of caspases-1,-3,-7,-8 and-9 have greatly …

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 …