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- W2165280313 abstract "Using the cytoplasmic domain of Fas in the yeast two-hybrid system, we have identified a novel interacting protein, FADD, which binds Fas and Fas-FD5, a mutant of Fas possessing enhanced killing activity, but not the functionally inactive mutants Fas-LPR and Fas-FD8. FADD contains a death domain homologous to the death domains of Fas and TNFR-1. A point mutation in FADD, analogous to the Ipr mutation of Fas, abolishes its ability to bind Fas, suggesting a death domain to death domain interaction. Overexpression of FADD in MCF7 and BJAB cells induces apoptosis, which, like Fas-induced apoptosis, is blocked by CrmA, a specific inhibitor of the interieukin-lβ-converting enzyme. These findings suggest that FADD may play an important role in the proximal signal transduction of Fas." @default.
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- W2165280313 date "2003-09-01" @default.
- W2165280313 modified "2023-09-27" @default.
- W2165280313 title "709 Outcome and patterns of failure in solitary plasmacytoma: a multicenter rare cancer network study on 258 patients" @default.
- W2165280313 doi "https://doi.org/10.1016/s1359-6349(03)90740-3" @default.
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