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- W577235718 abstract "Fas-associated death domain protein (FADD) recruits and activates procaspase-8 through interactions between the death effector domains of these two proteins. Cellular FLICE-inhibitory protein (c-FLIP) was identified as a molecule with sequence homology to caspase-8. It has been postulated that c-FLIP prevents formation of the competent death-inducing signaling complex in a ligand-dependent manner, through its interaction with FADD and/or caspase-8. However, the interaction of FADD and <TEX>$c-FLIP_s$</TEX> (short form) in apoptosis signaling has been controversially discussed. We show the purification and the characterization of human full-length FADD and <TEX>$c-FLIP_s$</TEX> expressed in Escherichia coli. The purified FADD and <TEX>$c-FLIP_s$</TEX> are shown as homogeneity, respectively, in SDS-PAGE analysis and light-scattering measurements. The folding properties of the <TEX>$alpha$</TEX>-helical structure of FADD and the super-secondary structure of <TEX>$c-FLIP_s$</TEX> proteins were characterized by circular dichroism spectroscopy. Furthermore, we report here a series of biochemical and biophysical data for FADD-<TEX>$c-FLIP_s$</TEX> binding in vitro. The binding of both FADD and <TEX>$c-FLIP_s$</TEX> proteins was detected by BIAcore biosensor, fluorescence measurement, and size-exclusion column (SEC)." @default.
- W577235718 created "2016-06-24" @default.
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- W577235718 date "2006-01-20" @default.
- W577235718 modified "2023-10-16" @default.
- W577235718 title "Full-length Fas-associated Death Domain Protein Interacts with Short Form of Cellular FLICE Inhibitory Protein" @default.
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- W577235718 doi "https://doi.org/10.5012/bkcs.2006.27.1.087" @default.
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