c‐FLIPL is a dual function regulator for caspase‐8 activation and CD95‐mediated apoptosis
By D. W. Chang, Zheng Xing, Yi Pan, A. Algeciras-Schimnich, B. Barnhart, S. Yaish-Ohad, Marcus E. Peter, Xiaolu Yang. EMBO Journal, 2002
620 citations recorded by the source corpus.
Subfields: Molecular Biology, Oncology
View Paper: https://www.semanticscholar.org/paper/efd273c5909bf140510844cf92075186776f844f
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In Molecular Biology
- Alexandru Almasan
- Peter Vandenabeele
- T. Vanden Berghe
- M. Lamkanfi
- A. Ashkenazi
- Guido Kroemer
- T. Kanneganti
Citations in the corpus
- Cellular mechanisms controlling caspase activation and function. (2013, result): “In contrast to the studies above, which characterized FLIPL as an inhibitor of caspase activation, some studies have shown that FLIPL can, in fact, facilitate caspase activation (Chang et al. 2002; Micheau et al. 2002).”
- Caspases in cell survival, proliferation and differentiation (2007, background): “At high concentrations of c-FLIPL, recruitment of caspase-8 to the DISC is strongly prevented and caspase-8 processing is impeded, thus blocking the induction of cell death while promoting FLIPL-mediated NF-kB activation (Figure 1c).(34,49)”
- Life and death by death receptors (2009, neutral): “cellular levels relative to caspase 8 (19).”
- Apoptosis and cancer: mutations within caspase genes (2009, background): “At high concentrations of c-FLIPL, procaspase-8 recruitment is blocked, and c-FLIPL cleavage is ensured by basal caspase-8 activity, and subsequently NF-kB is activated.(70) 71 In fact, besides function in”
- Apo2L/TRAIL: apoptosis signaling, biology, and potential for cancer therapy. (2003, background): “Moreover, recent work suggests that FLIP can actually promote caspase-8 activation in response to Fas engagement [68,69].”