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- W4310367131 abstract "Inflammatory caspases are effector caspases that execute proinflammatory cell death by pyroptosis as well as maturation of proinflammatory cytokines IL-1β and IL-18. Caspase-1 is activated in canonical inflammasomes, while caspase-4 and caspase-5 in humans as well as caspase-11 in mice are activated by bacterial lipopolysaccharide (LPS). All inflammatory caspases are activated by proximity-induced dimerization of the large and small catalytic domains from two caspase molecules, which is facilitated by clustering or oligomerization of the N-terminal caspase recruitment domain (CARD). This chapter summarizes the mechanism of caspase-1 activation that relies on CARD oligomerization, caspase dimerization, and autoproteolytic processing. It will illuminate substrate specificity mediated by the cleavage site as well as independent interactions between caspase and substrate. Lastly, this chapter will discuss the regulation of caspases at the level of cooperative assembly of caspase-1CARD filaments." @default.
- W4310367131 created "2022-12-09" @default.
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- W4310367131 date "2023-01-01" @default.
- W4310367131 modified "2023-09-27" @default.
- W4310367131 title "Inflammatory caspases" @default.
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- W4310367131 doi "https://doi.org/10.1016/b978-0-323-91802-2.00018-9" @default.
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