1995
DOI: 10.1074/jbc.270.14.7795
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Abstract: Signaling for cell death by Fas/APO1 occurs via a distinct region in its intracellular domain. This region contains a conserved sequence motif, the death domain motif, that is also found in the intracellular domains of the p55 tumor necrosis factor receptor and the low affinity nerve growth factor receptor, as well as in the regulatory domain of the ankyrins. A novel protein that specifically binds to the death domain of Fas/APO1 but not to Fas/APO1 molecules with a loss of function point mutation occurring in… Show more

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Cited by 952 publications
(649 citation statements)
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“…FADD (designated MORT-1 by Boldin et al (1995b), who simultaneously isolated the identical cDNA) is another addition to the rapidly growing list of death domain-containing proteins; the protein is appropriately named given that it shares many characteristics with TRADD. First, the 1.6 kb FADD/MORT-1 message is ubiquitously expressed (as is that of the Fas antigen).…”
Section: Fadd /Mort-1 and Ripmentioning
confidence: 99%
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“…FADD (designated MORT-1 by Boldin et al (1995b), who simultaneously isolated the identical cDNA) is another addition to the rapidly growing list of death domain-containing proteins; the protein is appropriately named given that it shares many characteristics with TRADD. First, the 1.6 kb FADD/MORT-1 message is ubiquitously expressed (as is that of the Fas antigen).…”
Section: Fadd /Mort-1 and Ripmentioning
confidence: 99%
“…Since it has been previously stated that Fas and TNF-RI can self-associate, and that this association is via the death domain, it may be that the death domain may actually be a domain which is required for protein-protein interactions (Boldin et al, 1995b;Chinnaiyan et al, 1995), thus facilitating the signal transduction pathways that lead to apoptosis. In fact, Chinnaiyan et al (1995) and others (Feinstein et al, 1995) have remarked that a death domain has been found in various other proteins such as ankyrin, a protein involved in cell adhesion and cell-cell interactions.…”
Section: Fadd /Mort-1 and Ripmentioning
confidence: 99%
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“…Alternatively, the function of other TNFR superfamily members, including TNF-R1 and Fas (CD95/APO-1), is not primarily mediated by TRAF protein binding. Instead, the effects of these receptors are mediated through association of their unique death domains with another group of molecules, including FADD/MORT1 (19,20), TRADD (21,22), RIP (23), and RAIDD/ CRADD (24). Although studies addressing the origin and clonality of Hodgkin and Reed-Sternberg (HRS) cells have shown considerable heterogeneity, the pathobiological and clinical profiles of classical Hodgkin's disease (HD) have consistently correlated with the deregulated, high-level expression of various growth promoting cytokines, transcription factors, and cell surface receptors on HRS cells (25).…”
mentioning
confidence: 99%
“…Identities between E1 and these human proteins are 30% for ankyrin 1 [11], 22% for Fas/APO1 [14], 39% for Mortl/FADD [15,16], 24% for p55 TNF-R [17,18] and 29% for NGF-R [19]. The identity to Mortl/FADD [15,16] is also the highest among two members of the DD protein family [3], whereby the O. volvulus ankyrin sequence is more identical to the DD of the human Mortl/FADD than to the DD of human ankyrins.…”
Section: A049 P E E H R H S Q H E D H E a S G A E Q H S G Q D S G T Tmentioning
confidence: 99%