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   <subfield code="a">P45 Forms a Complex with FADD and Promotes Neuronal Cell Survival Following Spinal Cord Injury</subfield>
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   <subfield code="c">[Tsung-Chang Sung, Zhijiang Chen Chen, Sandrine Thuret, Marçal Vilar, Fred H. Gage, Roland Riek, Kuo-Fen Lee]</subfield>
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   <subfield code="a">Fas-associated death domain (DD) adaptor (FADD), a member of the DD superfamily, contains both a DD and a death effector domain (DED) that are important in mediating FAS ligand-induced apoptotic signaling. P45 is a unique member of the DD superfamily in that it has a domain with sequence and structural characteristics of both DD and DED. We show that p45 forms a complex with FADD and diminishes Fas-FADD mediated death signaling. The DED of FADD is required for the complex formation with p45. Following spinal cord injury, transgenic mice over-expressing p45 exhibit increased neuronal survival, decreased retraction of corticospinal tract fibers and improved functional recovery. Understanding p45-mediated cellular and molecular mechanisms may provide insights into facilitating nerve regeneration in humans.</subfield>
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