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- W1997789120 endingPage "6227" @default.
- W1997789120 startingPage "6216" @default.
- W1997789120 abstract "Death effector domains (DEDs) are protein interaction modules found in a number of proteins known to regulate apoptosis from death receptors. The core DED family members that orchestrate programmed cell death from death receptors include the adaptor protein FADD, the initiator caspases procaspases-8 and -10 and the regulatory protein c-FLIP. Through homotypic DED interactions, these proteins assemble into the death-inducing signaling complex (DISC) to regulate initiator caspase activation and launch the apoptotic proteolytic cascade. A considerable body of evidence, however, is revealing that the same core group of DED-containing proteins also paradoxically promotes survival and proliferation in lymphocytes and possibly other cell types. This review delves into recent findings regarding these two opposing functional aspects of the core DED proteins. We discuss the current effort expanding our structural and biochemical view of how DED proteins assemble into the DISC to fully activate initiator caspases and execute cell death, and finally we examine details linking the same proteins to proliferation and describe how this outcome might be achieved through restricted activation of initiator caspases." @default.
- W1997789120 created "2016-06-24" @default.
- W1997789120 creator A5012059549 @default.
- W1997789120 creator A5019260221 @default.
- W1997789120 date "2008-10-20" @default.
- W1997789120 modified "2023-10-17" @default.
- W1997789120 title "FLIP and the death effector domain family" @default.
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