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The TNF receptor 1-associated protein TRADD signals cell death and NF-kappa B activation
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FADD, a novel death domain-containing protein, interacts with the death domain of Fas and initiates apoptosis
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Chinnaiyan AM, O'Rourke K, Tewari M, Dixit VM: FADD, a novel death domain-containing protein, interacts with the death domain of Fas and initiates apoptosis. Cell 1995, 81:505-512. The authors of this paper identified FADD as a critical mediator of CD95-induced apoptosis.
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Chinnaiyan, A.M.1
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0028913550
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A novel protein that interacts with the death domain of Fas/AP01 contains a sequence motif related to the death domain
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Boldin MP, Varfolomeev EE, Pancer Z, Mett IL, Camonis JH, Wallach D: A novel protein that interacts with the death domain of Fas/AP01 contains a sequence motif related to the death domain. J Biol Chem 1995, 270:7795-7798. This paper identified MACH, a novel MORT1/FADD-interacting ICE-like protease with homology to FADD/MORT1.
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Boldin, M.P.1
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Cytotoxicity-dependent APO-1 (Fas/CD95)-associated proteins form a death-inducing signaling complex (DISC) with the receptor
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Kischkel FC, Hellbardt S, Behrmann I, Germer M, Pawlita M, Krammer PH, Peter ME: Cytotoxicity-dependent APO-1 (Fas/CD95)-associated proteins form a death-inducing signaling complex (DISC) with the receptor. EMBO J 1995, 14:5579-5588. Instantaneous association of the components, CAP1-4, of a death-inducing signaling complex (DISC) upon cross-linking of CD95 was detected by two-dimensional electrophoresis.
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Kischkel, F.C.1
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0029965280
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FADD/MORT1 is a common mediator of CD95 (Fas/APO-1) and tumor necrosis factor receptor-induced apoptosis
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Chinnaiyan AM, Tepper CG, Seldin MF, O'Rourke K, Kischkel FC, Hellbardt S, Krammer PH, Peter ME, Dixit VM: FADD/MORT1 is a common mediator of CD95 (Fas/APO-1) and tumor necrosis factor receptor-induced apoptosis. J Biol Chem 1996, 271:4961-4965. Using a FADD mutant, this work demonstrated that FADD is involved in both CD95- and TNF-mediated signaling.
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Chinnaiyan, A.M.1
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FLICE, a novel FADD-homologous ICE/CED-3-like protease, is recruited to the CD95 (Fas/APO-1) death-inducing signaling complex
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Muzio M, Chinnaiyan AM, Kischkel FC, O'Rourke K, Shevchenko A, Ni J, Scaffidi C, Bretz JD, Zhang M, Gentz R et al.: FLICE, a novel FADD-homologous ICE/CED-3-like protease, is recruited to the CD95 (Fas/APO-1) death-inducing signaling complex. Cell 1996, 85:817-827 See annotation [17••].
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Involvement of MACH, a novel MORT1/FADD-interacting protease, in Fas/APO-1- and TNF receptor-induced cell death
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Boldin, M.P.1
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0029054725
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RIP: A novel protein containing a death domain that interacts with Fas/APO-1 (CD95) in yeast and causes cell death
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Stanger BZ, Leder P, Lee TH, Kim E, Seed B: RIP: a novel protein containing a death domain that interacts with Fas/APO-1 (CD95) in yeast and causes cell death. Cell 1995, 81:513-523. This work identified RIP as a death domain containing kinase that interacts with CD95.
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Peter ME, Kischkel FC, Hellbardt S, Chinnaiyan AM, Krammer PH, Dixit VM: CD95 (APO-1/Fas)-associating signalling proteins. Cell Death Differ 1996, 3:161-170.
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Hsu H, Huang J, Shu HB, Baichwal V, Goeddel DV: TNF-dependent recruitment of the protein kinase RIP to the TNF receptor-1 signaling complex. Immunity 1996, 4:387-396. This work showed that RIP may be a component of the TNF-R complex.
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RIP mediates tumor necrosis factor receptor 1 activation of NF-κB but not Fas/APO-1-initiated apoptosis
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Ting AT, Pimentel-Muinos FX, Seed B: RIP mediates tumor necrosis factor receptor 1 activation of NF-κB but not Fas/APO-1-initiated apoptosis. EMBO J 1996, 15:6189-6196.
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A novel family of putative signal transducers associated with the cytoplasmic domain of the 75 kDa tumor necrosis factor receptor
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Involvement of CRAF1, a relative of TRAF, in CD40 signaling
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Presence of a new conserved domain in CART1, a novel member of the tumor necrosis factor receptor-associated protein family, which is expressed in breast carcinoma
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Cloning and expression of apoptosis inhibitory protein homologs that function to inhibit apoptosis and/or bind tumor necrosis factor receptor-associated factors
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