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 …

Caspases play a crucial role in the ability of animal cells to kill themselves by apoptosis.
Caspase activity is regulated in vivo by members of three distinct protease inhibitor families …

Changes in ionic homeostasis are early events leading up to the commitment to apoptosis.
Although the direct effects of cations on caspase-3 activity have been examined …

Apoptotic caspases, such as caspase-7, are stored as inactive protease zymogens, and
when activated, lead to a fate-determining switch to induce cell death. We previously …

Caspase-2, the most evolutionarily conserved member in the human caspase family, may
play important roles in stress-induced apoptosis, cell cycle regulation, and tumor …

Cell death by apoptosis triggers the engagement of a conserved intracellular machinery of
execution, involving mainly the activation of the caspase family of cysteine proteases …

The recombinant form of the proapoptotic caspase-9 purified following expression in
Escherichia coliis processed at Asp 315, but largely inactive; however, when added to …

Caspases are cysteine proteases involved in the signalling cascades of programmed cell
death in which caspase-3 plays a central role, since it propagates death signals from …

Caspases (aspartate-specific cysteine proteases) play a critical role in the execution of the
mammalian apoptotic program. To address the regulation of human caspase activation, we …

Caspases are intracellular cysteine-class proteases with aspartate specificity that is critical
for driving processes as diverse as the innate immune response and apoptosis, exemplified …