Granzyme B (GrB) is predicted to trigger apoptosis by activating preferred caspases, but the
zymogens that are directly processed by the granzyme and the requirements for these …

The caspases are a unique family of cysteine proteases, which cleave proteins next to an
aspartate residue. Among all known mammalian proteases, only the serine protease …

Members of the caspase family of proteases are evolutionarily conserved cysteine proteases
that play a crucial role as the central executioners of the apoptotic pathway. Since the …

Caspase-8 is a cysteine protease activated by membrane-bound receptors at the cytosolic
face of the cell membrane, initiating the extrinsic pathway of apoptosis. Caspase-8 activation …

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 …

Structural studies of caspase-1 reveal that the dimeric thiol protease can exist in two states:
in an on-state, when the active site is occupied, or in an off-state, when the active site is …

Caspases are cysteine proteases that play a critical role in the initiation and regulation of
apoptosis. These enzymes act in a cascade to promote cell death through proteolytic …

Proteases constitute the largest enzyme family, yet their biological roles are obscured by our
rudimentary understanding of their cellular substrates. There are 12 human caspases that …

Caspase-13 was reported to be a member of the human caspase family of proteases
(Humke, E., et al., J. Biol. Chem. 273, 15702–15707, 1998). By contrast, a recent study (Lin …

Intracellular cysteine proteinases (caspases) play key roles in inflammation and apoptosis.
Recombinant caspases are typically produced inEscherichia coliexpression systems with …