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pubmed-article:8906799pubmed:abstractTextFas/APO-1 and TNF receptor 1 share a common signaling motif in their cytoplasmic tail called the "death domain." Using the death domain as bait in the yeast two-hybrid system, several death domain-containing proteins that participate in cell death signaling have been identified. Here we report the isolation of a novel protein, sentrin, which interacts with Fas/APO-1 and TNF receptor 1 but not with FADD/MORT1 or CD40. Two-hybrid interaction assays reveal that sentrin associates only with the signal-competent forms of Fas/APO-1 or TNF receptor 1 death domains. Sentrin is a novel protein of 101 amino acids with homology to ubiquitin, Nedd8, and a Saccharomyces cerevisiae protein, Smt3. When overexpressed, sentrin provides protection against both anti-Fas/APO-1 and TNF-induced cell death.lld:pubmed
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pubmed-article:8906799pubmed:articleTitleProtection against Fas/APO-1- and tumor necrosis factor-mediated cell death by a novel protein, sentrin.lld:pubmed
pubmed-article:8906799pubmed:affiliationDivision of Molecular Medicine, The University of Texas-Houston Health Science Center 77030, USA.lld:pubmed
pubmed-article:8906799pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:8906799pubmed:publicationTypeResearch Support, U.S. Gov't, P.H.S.lld:pubmed
pubmed-article:8906799pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
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