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 …

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 year 2002 sees the 10th anniversary of the caspases. During the early 1990s groups at
Immunex and Merck had been following the protease responsible for the posttranslational …

▪ Abstract Apoptosis is a genetically programmed, morphologically distinct form of cell death
that can be triggered by a variety of physiological and pathological stimuli. Studies …

Caspases, a family of cysteine proteases, play a central role in apoptosis. During the last
decade, major progress has been made to further understand caspase structure and …

Caspases, which are the executioners of apoptosis, comprise two distinct classes, the
initiators and the effectors. Although general structural features are shared between the …

Background: Peptide inhibitors of caspases have helped define the role of these cysteine
proteases in biology. Structural and biochemical characterization of the caspase enzymes …

Recent studies have established that members of the caspase protease family are essential
components of a conserved cell death program. Insights into their biological roles, structure …

Caspases are proteases at the heart of networks that govern apoptosis and inflammation.
The past decade has seen huge leaps in understanding the biology and chemistry of the …

Caspases are the primary drivers of apoptotic cell death, cleaving cellular proteins that are
critical for dismantling the dying cell. Initially translated as inactive zymogenic precursors …