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Yeast two-hybrid analysis revealed that E8 protein interacted with the caspase-8 prodomain whereas MC159 protein interacted with FADD. Furthermore, expression of either E8 protein or MC159 protein protected cells from Fas- and TNFR1-induced apoptosis indicating that certain herpesviruses and poxviruses use DED-mediated interactions to interfere with apoptotic signaling pathways. These findings identify a novel control point exploited by viruses to regulate Fas- and TNFR1-mediated apoptosis.<\/jats:p>","DOI":"10.1073\/pnas.94.4.1172","type":"journal-article","created":{"date-parts":[[2002,7,26]],"date-time":"2002-07-26T10:40:52Z","timestamp":1027680052000},"page":"1172-1176","update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":357,"title":["Death effector domain-containing herpesvirus and poxvirus proteins inhibit both Fas- and TNFR1-induced\u2009apoptosis"],"prefix":"10.1073","volume":"94","author":[{"given":"John","family":"Bertin","sequence":"first","affiliation":[{"name":"Laboratory of Clinical Investigation, Laboratory of Immunology, and Laboratory of Viral Diseases, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892; IDUN Pharmaceuticals Inc., La Jolla, CA 92037; and Center for Apoptosis Research and the Kimmel Cancer Institute, Jefferson Medical 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