Apoptosis—the regulated destruction of a cell—is a complicated process. The decision to
die cannot be taken lightly, and the activity of many genes influence a cell's likelihood of …

The death morphology commonly known as apoptosis results from a post-translational
pathway driven largely by specific limited proteolysis. In the last decade the structural basis …

Caspases belong to a family of highly conserved aspartate-specific cysteine proteases and
are members of the interleukin-1β-converting enzyme family, present in multicellular …

Death receptors, such as Fas and tumor necrosis factor-related apoptosis-inducing ligand
receptors, recruit Fas-associated death domain and pro-caspase-8 homodimers, which are …

Research in apoptosis has established a central role for caspases. The recent determination
of structures of caspase-1, caspase-3 and caspase-8, together with biochemical studies, has …

The inhibitor of apoptosis proteins (IAPs) represent the only endogenous caspase inhibitors
and are characterized by the presence of baculoviral IAP repeats (BIRs). Here, we report the …

Caspase 8 is an initiator caspase that is activated by death receptors to initiate the extrinsic
pathway of apoptosis. Caspase 8 activation involves dimerization and subsequent …

The execution of apoptosis depends on the hierarchical activation of caspases. The initiator
procaspases become autoproteolytically activated through a less understood process that is …

In the death receptor induced apoptotic pathway, caspase-8 autocatalytically cleaves itself at
specific cleavage sites. To better understand the regulatory mechanisms behind caspase-8 …

Caspases are a conserved family of cysteine proteases. They play diverse roles in
inflammatory responses and apoptotic pathways. Among the caspases is a subgroup whose …