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• W2130703400 startingPage "1271" @default.
• W2130703400 abstract "The p55 tumor necrosis factor (TNF) receptor and Fas/APO1 induce cell death via distinct regions in their intracellular domains. Three cytoplasmic proteins that bind to these receptor regions have been identified recently. One, MORT1 (also called FADD), binds to Fas/APO1 but not to p55-R; another, TRADD, binds to the p55 TNF receptor but not to Fas/APO1; and the third, RIP, binds weakly to both receptors. The regions within these proteins that are involved in binding to the receptors and the receptor regions to which they bind share a common sequence motif, that of the death domain. This study shows that the death domain motifs in MORT1, TRADD, and RIP bind effectively to each other, a mode of binding that may allow cross-talk between the functional expression of the p55 TNF receptor and Fas/APO1." @default.
• W2130703400 created "2016-06-24" @default.
• W2130703400 creator A5010445286 @default.
• W2130703400 creator A5044639869 @default.
• W2130703400 creator A5052364035 @default.
• W2130703400 creator A5079242043 @default.
• W2130703400 date "1996-03-01" @default.
• W2130703400 modified "2023-10-11" @default.
• W2130703400 title "A potential mechanism of cross-talk between the p55 tumor necrosis factor receptor and Fas/APO1: proteins binding to the death domains of the two receptors also bind to each other." @default.
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• W2130703400 doi "https://doi.org/10.1084/jem.183.3.1271" @default.
• W2130703400 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2192337" @default.
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• W2130703400 hasPublicationYear "1996" @default.
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