Caspases are a family of cysteine proteases related to interleukin-1 converting enzyme
(ICE) and represent the effector arm of the cell death pathway. The zymogen form of all …

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 …

Abstract Caspase-3 and-7 represent executioner/effector caspases that directly cause
apoptotic morphological changes by cleaving various death substrates. The substrates for …

Caspases, a family of cysteine proteases, have been recognized as the central executors of
programmed cell death. Nonetheless, the information on the caspase family has been …

Procaspase-2 is one of the aspartate-specific cysteine proteases that are activated in
response to various apoptotic stimuli. Two isoforms of human procaspase-2 have been …

Caspase-7 was considered to be redundant with caspase-3 because these related cysteine
proteases share an optimal peptide recognition sequence and have several endogenous …

OBJECTIVE: The preferred amino acids in the proteolytic sites have been considered to be
similar between caspase-1 and caspase-9, which do not support their differential functions …

Caspases play a key role during apoptotic execution. In an attempt to elucidate the specific
role of caspase-7 we generated a chicken DT40 cell line in which both alleles of the gene …

The complex sequence of events leading to apoptotic cell death is governed by an elaborate
regulatory scheme involving the actions of both initiator and executioner proteases. Among …

The caspase family of cysteine proteases is composed of at least 14 mammalian family
members. Phylogenetically they can be divided into two distinct subgroups having markedly …