Key result
CrmA selectively inhibits caspases, showing high affinity for interleukin-1beta-converting enzyme and FLICE (Ki = 0.95 nM), suggesting FLICE is a key target during Fas-mediated apoptosis.
Population
In vitro biochemical assay of five proteases (caspases) that may play a role in apoptosis
Design
Preclinical
Authors
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Supports FLICE as key apoptosis target; hypothesis-generating for caspase inhibitors, pending mammalian validation.
Effect estimate: Ki = 0.95 nM
CrmA selectively inhibits specific caspases, particularly FLICE, supporting the hypothesis that FLICE catalyzes a crucial step in Fas-mediated apoptosis.
Zhou et al. (1997) studied Apoptosis. CrmA vs. Five proteases (caspases) was evaluated on Kinetics of interaction of CrmA with five proteases (Ki = 0.95 nM). CrmA selectively inhibits caspases, showing high affinity for interleukin-1beta-converting enzyme and FLICE (Ki = 0.95 nM), suggesting FLICE is a key target during Fas-mediated apoptosis.
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