메뉴 건너뛰기




Volumn 25, Issue , 2007, Pages 561-586

The death domain superfamily in intracellular signaling of apoptosis and inflammation

Author keywords

Caspase recruitment domain (CARD); Crystal structure; Death domain (DD); Death effector domain (DED); NMR structure; Pyrin domain (PYD); Tandem DED

Indexed keywords

IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; INTERLEUKIN 1BETA CONVERTING ENZYME;

EID: 34247842740     PISSN: 07320582     EISSN: None     Source Type: Book Series    
DOI: 10.1146/annurev.immunol.25.022106.141656     Document Type: Review
Times cited : (433)

References (141)
  • 1
    • 0015383455 scopus 로고
    • Apoptosis: A basic biological phenomenon with wide-ranging implications in tissue kinetics
    • Kerr JF, Wyllie AH, Currie AR. 1972. Apoptosis: a basic biological phenomenon with wide-ranging implications in tissue kinetics. Br. J. Cancer 26:239-57
    • (1972) Br. J. Cancer , vol.26 , pp. 239-257
    • Kerr, J.F.1    Wyllie, A.H.2    Currie, A.R.3
  • 3
    • 0036234468 scopus 로고    scopus 로고
    • Pathways of apoptosis in lymphocyte development, homeostasis, and disease
    • Rathmell JC, Thompson CB. 2002. Pathways of apoptosis in lymphocyte development, homeostasis, and disease. Cell 109(Suppl.):S97-107
    • (2002) Cell , vol.109 , Issue.SUPPL.
    • Rathmell, J.C.1    Thompson, C.B.2
  • 4
    • 0028943734 scopus 로고
    • Apoptosis in the pathogenesis and treatment of disease
    • Thompson CB. 1995. Apoptosis in the pathogenesis and treatment of disease. Science 267:1456-61
    • (1995) Science , vol.267 , pp. 1456-1461
    • Thompson, C.B.1
  • 5
    • 0038394624 scopus 로고    scopus 로고
    • Caspases and apoptosis
    • Salvesen GS. 2002. Caspases and apoptosis. Essays Biochem. 38:9-19
    • (2002) Essays Biochem , vol.38 , pp. 9-19
    • Salvesen, G.S.1
  • 6
    • 8444220527 scopus 로고    scopus 로고
    • Molecular mechanisms of caspase regulation during apoptosis
    • Riedl SJ, Shi Y. 2004. Molecular mechanisms of caspase regulation during apoptosis. Nat. Rev. Mol. Cell Biol. 5:897-907
    • (2004) Nat. Rev. Mol. Cell Biol , vol.5 , pp. 897-907
    • Riedl, S.J.1    Shi, Y.2
  • 7
    • 0030610362 scopus 로고    scopus 로고
    • A cytokine-responsive IκB kinase that activates the transcription factor NF-κB
    • DiDonato JA, Hayakawa M, Rothwarf DM, Zandi E, Karin M. 1997. A cytokine-responsive IκB kinase that activates the transcription factor NF-κB. Nature 388:548-54
    • (1997) Nature , vol.388 , pp. 548-554
    • DiDonato, J.A.1    Hayakawa, M.2    Rothwarf, D.M.3    Zandi, E.4    Karin, M.5
  • 8
    • 0030613551 scopus 로고    scopus 로고
    • The IκB kinase complex (IKK) contains two kinase subunits, IKKα and IKKβ, necessary for IκB phosphorylation and NF-κB activation
    • Zandi E, Rothwarf DM, Delhase M, Hayakawa M, Karin M. 1997. The IκB kinase complex (IKK) contains two kinase subunits, IKKα and IKKβ, necessary for IκB phosphorylation and NF-κB activation. Cell 91:243-52
    • (1997) Cell , vol.91 , pp. 243-252
    • Zandi, E.1    Rothwarf, D.M.2    Delhase, M.3    Hayakawa, M.4    Karin, M.5
  • 10
    • 0034703023 scopus 로고    scopus 로고
    • The IκB kinase (IKK) complex is tripartite and contains IKK gamma but not IKAP as a regular component
    • Krappmann D, Hatada EN, Tegethoff S, Li J, Hippel A, et al. 2000. The IκB kinase (IKK) complex is tripartite and contains IKK gamma but not IKAP as a regular component. J. Biol. Chem. 275:29779-87
    • (2000) J. Biol. Chem , vol.275 , pp. 29779-29787
    • Krappmann, D.1    Hatada, E.N.2    Tegethoff, S.3    Li, J.4    Hippel, A.5
  • 11
    • 0030613758 scopus 로고    scopus 로고
    • NF-kB activation: The IkB kinase revealed?
    • Stancovski I, Baltimore D. 1997. NF-kB activation: the IkB kinase revealed? Cell 91:299-302
    • (1997) Cell , vol.91 , pp. 299-302
    • Stancovski, I.1    Baltimore, D.2
  • 12
    • 0029976817 scopus 로고    scopus 로고
    • An essential role for NF-κB in preventing TNF-α-induced cell death
    • Beg AA, Baltimore D. 1996. An essential role for NF-κB in preventing TNF-α-induced cell death. Science 274:782-84
    • (1996) Science , vol.274 , pp. 782-784
    • Beg, A.A.1    Baltimore, D.2
  • 13
    • 0030298294 scopus 로고    scopus 로고
    • Dissection of TNF receptor 1 effector functions: JNK activation is not linked to apoptosis while NF-κB; activation prevents cell death
    • Liu ZG, Hsu H, Goeddel DV, Karin M. 1996. Dissection of TNF receptor 1 effector functions: JNK activation is not linked to apoptosis while NF-κB; activation prevents cell death. Cell 87:565-76
    • (1996) Cell , vol.87 , pp. 565-576
    • Liu, Z.G.1    Hsu, H.2    Goeddel, D.V.3    Karin, M.4
  • 14
    • 0030271387 scopus 로고    scopus 로고
    • NF-κ: Ten years after
    • Baeuerle PA, Baltimore D. 1996. NF-κ: ten years after. Cell 87:13-20
    • (1996) Cell , vol.87 , pp. 13-20
    • Baeuerle, P.A.1    Baltimore, D.2
  • 15
    • 2542457495 scopus 로고    scopus 로고
    • Inflammatory caspases: Linking an intracellular innate immune system to autoinflammatory diseases
    • Martinon F, Tschopp J. 2004. Inflammatory caspases: linking an intracellular innate immune system to autoinflammatory diseases. Cell 117:561-74
    • (2004) Cell , vol.117 , pp. 561-574
    • Martinon, F.1    Tschopp, J.2
  • 16
    • 19244365798 scopus 로고    scopus 로고
    • The domains of apoptosis: A genomics perspective
    • Reed JC, Doctor KS, Godzik A. 2004. The domains of apoptosis: a genomics perspective. Sci. STKE 2004:re9
    • (2004) Sci. STKE , vol.2004
    • Reed, J.C.1    Doctor, K.S.2    Godzik, A.3
  • 17
    • 11144333066 scopus 로고    scopus 로고
    • Fire and death: The pyrin domain joins the death-domain superfamily
    • Kohl A, Grutter MG. 2004. Fire and death: The pyrin domain joins the death-domain superfamily. C. R. Biol. 327:1077-86
    • (2004) C. R. Biol , vol.327 , pp. 1077-1086
    • Kohl, A.1    Grutter, M.G.2
  • 18
    • 28444491105 scopus 로고    scopus 로고
    • Mechanisms of apoptosis through structural biology
    • Yan N, Shi Y. 2005. Mechanisms of apoptosis through structural biology. Annu. Rev. Cell Dev. Biol. 21:35-56
    • (2005) Annu. Rev. Cell Dev. Biol , vol.21 , pp. 35-56
    • Yan, N.1    Shi, Y.2
  • 19
    • 8544282423 scopus 로고    scopus 로고
    • Patterns and clusters within the PSM column in TiBS, 1992-2004
    • McEntyre JR, Gibson TJ. 2004. Patterns and clusters within the PSM column in TiBS, 1992-2004. Trends Biochem. Sci. 29:627-33
    • (2004) Trends Biochem. Sci , vol.29 , pp. 627-633
    • McEntyre, J.R.1    Gibson, T.J.2
  • 20
    • 0030950228 scopus 로고    scopus 로고
    • Anovel family of viral death effector domaincontaining molecules that inhibit both CD-95- and tumor necrosis factor receptor-1-induced apoptosis
    • Hu S, Vincenz C, Buller M, Dixit VM. 1997. Anovel family of viral death effector domaincontaining molecules that inhibit both CD-95- and tumor necrosis factor receptor-1-induced apoptosis. J. Biol. Chem. 272:9621-24
    • (1997) J. Biol. Chem , vol.272 , pp. 9621-9624
    • Hu, S.1    Vincenz, C.2    Buller, M.3    Dixit, V.M.4
  • 21
    • 12644286556 scopus 로고    scopus 로고
    • Death effector domain-containing herpesvirus and poxvirus proteins inhibit both Fas- and TNFRlinduced apoptosis
    • Bertin J, Armstrong RC, Ottilie S, Martin DA, Wang Y, et al. 1997. Death effector domain-containing herpesvirus and poxvirus proteins inhibit both Fas- and TNFRlinduced apoptosis. Proc. Natl. Acad. Sci. USA 94:1172-76
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 1172-1176
    • Bertin, J.1    Armstrong, R.C.2    Ottilie, S.3    Martin, D.A.4    Wang, Y.5
  • 22
    • 0030970013 scopus 로고    scopus 로고
    • Viral FLICE-inhibitory proteins (FLIPs) prevent apoptosis induced by death receptors
    • Thome M, Schneider P, Hofmann K, Fickenscher H, Meinl E, et al. 1997. Viral FLICE-inhibitory proteins (FLIPs) prevent apoptosis induced by death receptors. Nature 386:517-21
    • (1997) Nature , vol.386 , pp. 517-521
    • Thome, M.1    Schneider, P.2    Hofmann, K.3    Fickenscher, H.4    Meinl, E.5
  • 23
    • 28844466449 scopus 로고    scopus 로고
    • A poxvirus-encoded pyrin domain protein interacts with ASC-1 to inhibit host inflammatory and apoptotic responses to infection
    • Johnston JB, Barrett JW, Nazarian SH, Goodwin M, Ricuttio D, et al. 2005. A poxvirus-encoded pyrin domain protein interacts with ASC-1 to inhibit host inflammatory and apoptotic responses to infection. Immunity 23:587-98
    • (2005) Immunity , vol.23 , pp. 587-598
    • Johnston, J.B.1    Barrett, J.W.2    Nazarian, S.H.3    Goodwin, M.4    Ricuttio, D.5
  • 25
    • 0032580153 scopus 로고    scopus 로고
    • NMR structure and mutagenesis of the FADD (Mort1) death-effector domain
    • Eberstadt M, Huang B, Chen Z, Meadows RP, Ng SC, et al. 1998. NMR structure and mutagenesis of the FADD (Mort1) death-effector domain. Nature 392:941-45
    • (1998) Nature , vol.392 , pp. 941-945
    • Eberstadt, M.1    Huang, B.2    Chen, Z.3    Meadows, R.P.4    Ng, S.C.5
  • 26
    • 0032563323 scopus 로고    scopus 로고
    • Solution structure of the RAIDD CARD and model for CARD/CARD interaction in caspase-2 and caspase-9 recruitment
    • Chou JJ, Matsuo H, Duan H, Wagner G. 1998. Solution structure of the RAIDD CARD and model for CARD/CARD interaction in caspase-2 and caspase-9 recruitment. Cell 94:171-80
    • (1998) Cell , vol.94 , pp. 171-180
    • Chou, J.J.1    Matsuo, H.2    Duan, H.3    Wagner, G.4
  • 27
    • 0141817846 scopus 로고    scopus 로고
    • NMR structure of the apoptosis- and inflammation-related NALP1 pyrin domain
    • Hiller S, Kohl A, Fiorito F, Herrmann T, Wider G, et al. 2003. NMR structure of the apoptosis- and inflammation-related NALP1 pyrin domain. Structure 11:1199-205
    • (2003) Structure , vol.11 , pp. 1199-1205
    • Hiller, S.1    Kohl, A.2    Fiorito, F.3    Herrmann, T.4    Wider, G.5
  • 28
    • 0027211704 scopus 로고
    • Crystal structure of the soluble human 55 kd TNF receptor-human TNF beta complex: Implications for TNF receptor activation
    • Banner DW, D'Arcy A, Janes W, Gentz R, Schoenfeld HJ, et al. 1993. Crystal structure of the soluble human 55 kd TNF receptor-human TNF beta complex: implications for TNF receptor activation. Cell 73:431-45
    • (1993) Cell , vol.73 , pp. 431-445
    • Banner, D.W.1    D'Arcy, A.2    Janes, W.3    Gentz, R.4    Schoenfeld, H.J.5
  • 29
    • 0028883850 scopus 로고
    • Cytotoxicity-dependent APO-1 (Fas/CD95)-associated proteins form a death-inducing signaling complex (DISC) with the receptor
    • Kischkel FC, Hellbardt S, Behrmann I, Germer M, Pawlita M, et al. 1995. Cytotoxicity-dependent APO-1 (Fas/CD95)-associated proteins form a death-inducing signaling complex (DISC) with the receptor. EMBO J. 14:5579-88
    • (1995) EMBO J , vol.14 , pp. 5579-5588
    • Kischkel, F.C.1    Hellbardt, S.2    Behrmann, I.3    Germer, M.4    Pawlita, M.5
  • 30
    • 0027275490 scopus 로고
    • A novel domain within the 55 kd TNF receptor signals cell death
    • Tartaglia LA, Ayres TM, Wong GH, Goeddel DV. 1993. A novel domain within the 55 kd TNF receptor signals cell death. Cell 74:845-53
    • (1993) Cell , vol.74 , pp. 845-853
    • Tartaglia, L.A.1    Ayres, T.M.2    Wong, G.H.3    Goeddel, D.V.4
  • 31
    • 0027281373 scopus 로고
    • A novel protein domain required for apoptosis: Mutational analysis of human Fas antigen
    • Itoh N, Nagata S. 1993. A novel protein domain required for apoptosis: mutational analysis of human Fas antigen. J. Biol. Chem. 268:10932-37
    • (1993) J. Biol. Chem , vol.268 , pp. 10932-10937
    • Itoh, N.1    Nagata, S.2
  • 32
    • 0037204952 scopus 로고    scopus 로고
    • The Fas signaling pathway: More than a paradigm
    • Wajant H. 2002. The Fas signaling pathway: more than a paradigm. Science 296:1635-36
    • (2002) Science , vol.296 , pp. 1635-1636
    • Wajant, H.1
  • 33
    • 0028985261 scopus 로고
    • Self-association of the "death domains" of the p55 tumor necrosis factor (TNF) receptor and Fas/APO1 prompts signaling for TNF and Fas/APO1 effects
    • Boldin MP, Mett IL, Varfolomeev EE, Chumakov I, Shemer-Avni Y, et al. 1995. Self-association of the "death domains" of the p55 tumor necrosis factor (TNF) receptor and Fas/APO1 prompts signaling for TNF and Fas/APO1 effects. J. Biol. Chem. 270:387-91
    • (1995) J. Biol. Chem , vol.270 , pp. 387-391
    • Boldin, M.P.1    Mett, I.L.2    Varfolomeev, E.E.3    Chumakov, I.4    Shemer-Avni, Y.5
  • 34
    • 0029026548 scopus 로고
    • FADD, a novel death domain-containing protein, interacts with the death domain of Fas and initiates apoptosis
    • Chinnaiyan AM, O'Rourke K, Tewari M, Dixit VM. 1995. FADD, a novel death domain-containing protein, interacts with the death domain of Fas and initiates apoptosis. Cell 81:505-12
    • (1995) Cell , vol.81 , pp. 505-512
    • Chinnaiyan, A.M.1    O'Rourke, K.2    Tewari, M.3    Dixit, V.M.4
  • 35
    • 15844412409 scopus 로고    scopus 로고
    • FLICE, a novel FADD-homologous ICE/CED-3-like protease, is recruited to the CD95 (Fas/APO-1) death-inducing signaling complex
    • Muzio M, Chinnaiyan AM, Kischkel FC, O'Rourke K, Shevchenko A, et al. 1996. FLICE, a novel FADD-homologous ICE/CED-3-like protease, is recruited to the CD95 (Fas/APO-1) death-inducing signaling complex. Cell 85:817-27
    • (1996) Cell , vol.85 , pp. 817-827
    • Muzio, M.1    Chinnaiyan, A.M.2    Kischkel, F.C.3    O'Rourke, K.4    Shevchenko, A.5
  • 36
    • 0030011398 scopus 로고    scopus 로고
    • Involvement of MACH, a novel MORT1/FADD-interacting protease, in Fas/APO-1- and TNF receptor-induced cell death
    • Boldin MP, Goncharov TM, Goltsev YV, Wallach D. 1996. Involvement of MACH, a novel MORT1/FADD-interacting protease, in Fas/APO-1- and TNF receptor-induced cell death. Cell 85:803-15
    • (1996) Cell , vol.85 , pp. 803-815
    • Boldin, M.P.1    Goncharov, T.M.2    Goltsev, Y.V.3    Wallach, D.4
  • 37
    • 0033613143 scopus 로고    scopus 로고
    • Caspase activation: The induced-proximity model
    • Salvesen GS, Dixit VM. 1999. Caspase activation: the induced-proximity model. Proc. Natl. Acad. Sci. USA 96:10964-67
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 10964-10967
    • Salvesen, G.S.1    Dixit, V.M.2
  • 38
    • 0030925774 scopus 로고    scopus 로고
    • FLICE is activated by association with the CD95 death-inducing signaling complex (DISC)
    • Medema JP, Scaffidi C, Kischkel FC, Shevchenko A, Mann M, et al. 1997. FLICE is activated by association with the CD95 death-inducing signaling complex (DISC). EMBO J. 16:2794-804
    • (1997) EMBO J , vol.16 , pp. 2794-2804
    • Medema, J.P.1    Scaffidi, C.2    Kischkel, F.C.3    Shevchenko, A.4    Mann, M.5
  • 39
    • 2942746419 scopus 로고    scopus 로고
    • Caspase activation: Revisiting the induced proximity model
    • Shi Y. 2004. Caspase activation: revisiting the induced proximity model. Cell 117:855-58
    • (2004) Cell , vol.117 , pp. 855-858
    • Shi, Y.1
  • 40
    • 0041853690 scopus 로고    scopus 로고
    • Induction of TNF receptor I-mediated apoptosis via two sequential signaling complexes
    • Micheau O, Tschopp J. 2003. Induction of TNF receptor I-mediated apoptosis via two sequential signaling complexes. Cell 114:181-90
    • (2003) Cell , vol.114 , pp. 181-190
    • Micheau, O.1    Tschopp, J.2
  • 41
    • 0035496099 scopus 로고    scopus 로고
    • Regulation of lymphocyte proliferation and death by FLIP
    • Thome M, Tschopp J. 2001. Regulation of lymphocyte proliferation and death by FLIP. Nat. Rev. Immunol. 1:50-58
    • (2001) Nat. Rev. Immunol , vol.1 , pp. 50-58
    • Thome, M.1    Tschopp, J.2
  • 42
    • 0030800070 scopus 로고    scopus 로고
    • Inhibition of death receptor signals by cellular FLIP
    • Irmler M, Thome M, Hahne M, Schneider P, Hofmann K, et al. 1997. Inhibition of death receptor signals by cellular FLIP. Nature 388:190-95
    • (1997) Nature , vol.388 , pp. 190-195
    • Irmler, M.1    Thome, M.2    Hahne, M.3    Schneider, P.4    Hofmann, K.5
  • 43
    • 0030746740 scopus 로고    scopus 로고
    • Casper is a FADD- and caspase-related inducer of apoptosis
    • Shu HB, Halpin DR, Goeddel DV. 1997. Casper is a FADD- and caspase-related inducer of apoptosis. Immunity 6:751-63
    • (1997) Immunity , vol.6 , pp. 751-763
    • Shu, H.B.1    Halpin, D.R.2    Goeddel, D.V.3
  • 44
    • 0030810981 scopus 로고    scopus 로고
    • FLAME-1, a novel FADD-like antiapoptotic molecule that regulates Fas/TNFR1-induced apoptosis
    • Srinivasula SM, Ahmad M, Ottilie S, Bullrich F, Banks S, et al. 1997. FLAME-1, a novel FADD-like antiapoptotic molecule that regulates Fas/TNFR1-induced apoptosis. J. Biol. Chem. 272:18542-45
    • (1997) J. Biol. Chem , vol.272 , pp. 18542-18545
    • Srinivasula, S.M.1    Ahmad, M.2    Ottilie, S.3    Bullrich, F.4    Banks, S.5
  • 45
    • 0030961084 scopus 로고    scopus 로고
    • CLARP, a death effector domain-containing protein interacts with caspase-8 and regulates apoptosis
    • Inohara N, Koseki T, Hu Y, Chen S, Nunez G. 1997. CLARP, a death effector domain-containing protein interacts with caspase-8 and regulates apoptosis. Proc. Natl. Acad. Sci. USA 94:10717-22
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 10717-10722
    • Inohara, N.1    Koseki, T.2    Hu, Y.3    Chen, S.4    Nunez, G.5
  • 47
    • 0030758315 scopus 로고    scopus 로고
    • MRIT, a novel death-effector domain-containing protein, interacts with caspases and BclXL and initiates cell death
    • Han DK, Chaudhary PM, Wright ME, Friedman C, Trask BJ, et al. 1997. MRIT, a novel death-effector domain-containing protein, interacts with caspases and BclXL and initiates cell death. Proc. Natl. Acad. Sci. USA 94:11333-38
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 11333-11338
    • Han, D.K.1    Chaudhary, P.M.2    Wright, M.E.3    Friedman, C.4    Trask, B.J.5
  • 48
    • 0030841911 scopus 로고    scopus 로고
    • I-FLICE, a novel inhibitor of tumor necrosis factor receptor-1- and CD-95-induced apoptosis
    • Hu S, Vincenz C, Ni J, Gentz R, Dixit VM. 1997. I-FLICE, a novel inhibitor of tumor necrosis factor receptor-1- and CD-95-induced apoptosis. J. Biol. Chem. 272:17255-57
    • (1997) J. Biol. Chem , vol.272 , pp. 17255-17257
    • Hu, S.1    Vincenz, C.2    Ni, J.3    Gentz, R.4    Dixit, V.M.5
  • 49
    • 7344220967 scopus 로고    scopus 로고
    • Cell death attenuation by 'Usurpin', a mammalian DED-caspase homologue that precludes caspase-8 recruitment and activation by the CD-95 (Fas, APO-1) receptor complex
    • Rasper DM, Vaillancourt JP, Hadano S, Houtzager VM, Seiden I, et al. 1998. Cell death attenuation by 'Usurpin', a mammalian DED-caspase homologue that precludes caspase-8 recruitment and activation by the CD-95 (Fas, APO-1) receptor complex. Cell Death Differ. 5:271-88
    • (1998) Cell Death Differ , vol.5 , pp. 271-288
    • Rasper, D.M.1    Vaillancourt, J.P.2    Hadano, S.3    Houtzager, V.M.4    Seiden, I.5
  • 50
    • 0036139833 scopus 로고    scopus 로고
    • Binding of FADD and caspase-8 to molluscum contagiosum virus MC159 v-FLIP is not sufficient for its antiapoptotic function
    • Garvey TL, Bertin J, Siegel RM, Wang GH, Lenardo MJ, Cohen JI. 2002. Binding of FADD and caspase-8 to molluscum contagiosum virus MC159 v-FLIP is not sufficient for its antiapoptotic function. J. Virol. 76:697-706
    • (2002) J. Virol , vol.76 , pp. 697-706
    • Garvey, T.L.1    Bertin, J.2    Siegel, R.M.3    Wang, G.H.4    Lenardo, M.J.5    Cohen, J.I.6
  • 51
    • 0035970321 scopus 로고    scopus 로고
    • Molluscum contagiosum virus inhibitors of apoptosis: The MC159 v-FLIP protein blocks Fas-induced activation of procaspases and degradation of the related MC160 protein
    • Shisler JL, Moss B. 2001. Molluscum contagiosum virus inhibitors of apoptosis: The MC159 v-FLIP protein blocks Fas-induced activation of procaspases and degradation of the related MC160 protein. Virology 282:14-25
    • (2001) Virology , vol.282 , pp. 14-25
    • Shisler, J.L.1    Moss, B.2
  • 52
    • 0032975917 scopus 로고    scopus 로고
    • Sequence and genomic analysis of a Rhesus macaque rhadinovirus with similarity to Kaposi's sarcoma-associated herpesvirus/human herpesvirus 8
    • Searles RP, Bergquam EP, Axthelm MK, Wong SW. 1999. Sequence and genomic analysis of a Rhesus macaque rhadinovirus with similarity to Kaposi's sarcoma-associated herpesvirus/human herpesvirus 8. J. Virol. 73:3040-53
    • (1999) J. Virol , vol.73 , pp. 3040-3053
    • Searles, R.P.1    Bergquam, E.P.2    Axthelm, M.K.3    Wong, S.W.4
  • 53
    • 1042280346 scopus 로고    scopus 로고
    • Development of lymphoma in autoimmune lymphoproliferative syndrome (ALPS) and its relationship to Fas gene mutations
    • Poppema S, Maggio E, van den Berg A. 2004. Development of lymphoma in autoimmune lymphoproliferative syndrome (ALPS) and its relationship to Fas gene mutations. Leuk. Lymph. 45:423-31
    • (2004) Leuk. Lymph , vol.45 , pp. 423-431
    • Poppema, S.1    Maggio, E.2    van den Berg, A.3
  • 54
    • 0037279111 scopus 로고    scopus 로고
    • Autoimmune lymphoproliferative syndromes: Genetic defects of apoptosis pathways
    • Rieux-Laucat F, Le Deist F, Fischer A. 2003. Autoimmune lymphoproliferative syndromes: genetic defects of apoptosis pathways. Cell Death Differ. 10:124-33
    • (2003) Cell Death Differ , vol.10 , pp. 124-133
    • Rieux-Laucat, F.1    Le Deist, F.2    Fischer, A.3
  • 55
    • 0029025441 scopus 로고
    • Dominant interfering Fas gene mutations impair apoptosis in a human autoimmune lyphoproliferative syndrome
    • Fisher GH, Rosenberg FJ, Straus SE, Dale JK, Middelton LA, et al. 1995. Dominant interfering Fas gene mutations impair apoptosis in a human autoimmune lyphoproliferative syndrome. Cell 81:935-46
    • (1995) Cell , vol.81 , pp. 935-946
    • Fisher, G.H.1    Rosenberg, F.J.2    Straus, S.E.3    Dale, J.K.4    Middelton, L.A.5
  • 56
    • 0030614415 scopus 로고    scopus 로고
    • Clincal, immunologic, and genetic features of an autoimmune lymphoproliferative syndrome associated with abnormal lymphocyte apoptosis
    • Sneller MC, Wang J, Dale JK, Strober W, Middelton LA, et al. 1997. Clincal, immunologic, and genetic features of an autoimmune lymphoproliferative syndrome associated with abnormal lymphocyte apoptosis. Blood 89:1341-48
    • (1997) Blood , vol.89 , pp. 1341-1348
    • Sneller, M.C.1    Wang, J.2    Dale, J.K.3    Strober, W.4    Middelton, L.A.5
  • 57
    • 0029006893 scopus 로고
    • Mutations in Fas associated with human lymphoproliferative syndrome and autoimmunity
    • Rieux-Laucat F, Le Deist F, Hivroz C, Roberts IA, Debatin KM, et al. 1995. Mutations in Fas associated with human lymphoproliferative syndrome and autoimmunity. Science 268:1347-49
    • (1995) Science , vol.268 , pp. 1347-1349
    • Rieux-Laucat, F.1    Le Deist, F.2    Hivroz, C.3    Roberts, I.A.4    Debatin, K.M.5
  • 58
    • 6844240196 scopus 로고    scopus 로고
    • Novel Fas (CD95/APO-1) mutations in infants with a lymphoproliferative disorder
    • Kasahara Y, Wada T, Niida Y, Yachie A, Seki H, et al. 1998. Novel Fas (CD95/APO-1) mutations in infants with a lymphoproliferative disorder. Int. Immunol. 10:195-202
    • (1998) Int. Immunol , vol.10 , pp. 195-202
    • Kasahara, Y.1    Wada, T.2    Niida, Y.3    Yachie, A.4    Seki, H.5
  • 59
    • 0030745646 scopus 로고    scopus 로고
    • Apaf-1, a human protein homologous to C. elegans CED-4, participates in cytochrome c-dependent activation of caspase-3
    • Zou H, Henzel WJ, Liu X, Lutschg A, Wang X. 1997. Apaf-1, a human protein homologous to C. elegans CED-4, participates in cytochrome c-dependent activation of caspase-3. Cell 90:405-13
    • (1997) Cell , vol.90 , pp. 405-413
    • Zou, H.1    Henzel, W.J.2    Liu, X.3    Lutschg, A.4    Wang, X.5
  • 60
    • 0030715323 scopus 로고    scopus 로고
    • Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade
    • Li P, Nijhawan D, Budihardjo I, Srinivasula SM, Ahmad M, et al. 1997. Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade. Cell 91:479-89
    • (1997) Cell , vol.91 , pp. 479-489
    • Li, P.1    Nijhawan, D.2    Budihardjo, I.3    Srinivasula, S.M.4    Ahmad, M.5
  • 61
    • 0036899079 scopus 로고    scopus 로고
    • Apoptosomes: Engines for caspase activation
    • Adams JM, Cory S. 2002. Apoptosomes: engines for caspase activation. Curr. Opin. Cell Biol. 14:715-20
    • (2002) Curr. Opin. Cell Biol , vol.14 , pp. 715-720
    • Adams, J.M.1    Cory, S.2
  • 62
    • 0028168593 scopus 로고
    • Ich-1, an Ice/ced-3-related gene, encodes both positive and negative regulators of programmed cell death
    • Wang L, Miura M, Bergeron L, Zhu H, Yuan J. 1994. Ich-1, an Ice/ced-3-related gene, encodes both positive and negative regulators of programmed cell death. Cell 78:739-50
    • (1994) Cell , vol.78 , pp. 739-750
    • Wang, L.1    Miura, M.2    Bergeron, L.3    Zhu, H.4    Yuan, J.5
  • 63
    • 2442453730 scopus 로고    scopus 로고
    • The PIDDosome, a protein complex implicated in activation of caspase-2 in response to genotoxic stress
    • Tinel A, Tschopp J. 2004. The PIDDosome, a protein complex implicated in activation of caspase-2 in response to genotoxic stress. Science 304:843-46
    • (2004) Science , vol.304 , pp. 843-846
    • Tinel, A.1    Tschopp, J.2
  • 64
    • 26444433872 scopus 로고    scopus 로고
    • Apoptosis caused by p53-induced protein with death domain (PIDD) depends on the death adapter protein RAIDD
    • Berube C, Boucher LM, Ma W, Wakeham A, Salmena L, et al. 2005. Apoptosis caused by p53-induced protein with death domain (PIDD) depends on the death adapter protein RAIDD. Proc. Natl. Acad. Sci. USA 102:14314-20
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 14314-14320
    • Berube, C.1    Boucher, L.M.2    Ma, W.3    Wakeham, A.4    Salmena, L.5
  • 65
    • 0033812557 scopus 로고    scopus 로고
    • Pidd, a new death-domain-containing protein, is induced by p53 and promotes apoptosis
    • Lin Y, Ma W, Benchimol S. 2000. Pidd, a new death-domain-containing protein, is induced by p53 and promotes apoptosis. Nat. Genet. 26:122-27
    • (2000) Nat. Genet , vol.26 , pp. 122-127
    • Lin, Y.1    Ma, W.2    Benchimol, S.3
  • 66
    • 0031021356 scopus 로고    scopus 로고
    • RAIDD is a new 'death' adaptor molecule
    • Duan H, Dixit VM. 1997. RAIDD is a new 'death' adaptor molecule. Nature 385:86-89
    • (1997) Nature , vol.385 , pp. 86-89
    • Duan, H.1    Dixit, V.M.2
  • 67
    • 0037162833 scopus 로고    scopus 로고
    • Requirement for caspase-2 in stress-induced apoptosis before mitochondrial permeabilization
    • Lassus P, Opitz-Araya X, Lazebnik Y. 2002. Requirement for caspase-2 in stress-induced apoptosis before mitochondrial permeabilization. Science 297:1352-54
    • (2002) Science , vol.297 , pp. 1352-1354
    • Lassus, P.1    Opitz-Araya, X.2    Lazebnik, Y.3
  • 68
    • 28944447430 scopus 로고    scopus 로고
    • PIDD mediates NF-κB activation in response to DNA damage
    • Janssens S, Tinel A, Lippens S, Tschopp J. 2005. PIDD mediates NF-κB activation in response to DNA damage. Cell 123:1079-92
    • (2005) Cell , vol.123 , pp. 1079-1092
    • Janssens, S.1    Tinel, A.2    Lippens, S.3    Tschopp, J.4
  • 69
    • 33646899303 scopus 로고    scopus 로고
    • Sorting out Toll signals
    • Fitzgerald KA, Chen ZJ. 2006. Sorting out Toll signals. Cell 125:834-36
    • (2006) Cell , vol.125 , pp. 834-836
    • Fitzgerald, K.A.1    Chen, Z.J.2
  • 70
    • 23144449789 scopus 로고    scopus 로고
    • Ubiquitin signaling in the NF-κB pathway
    • Chen ZJ. 2005. Ubiquitin signaling in the NF-κB pathway. Nat. Cell Biol. 7:758-65
    • (2005) Nat. Cell Biol , vol.7 , pp. 758-765
    • Chen, Z.J.1
  • 72
    • 0030595339 scopus 로고    scopus 로고
    • The dorsoventral regulatory gene cassette spatzle/Toll/cactus controls the potent antifungal response in Drosophila adults
    • Lemaitre B, Nicolas E, Michaut L, Reichhart JM, Hoffmann JA. 1996. The dorsoventral regulatory gene cassette spatzle/Toll/cactus controls the potent antifungal response in Drosophila adults. Cell 86:973-83
    • (1996) Cell , vol.86 , pp. 973-983
    • Lemaitre, B.1    Nicolas, E.2    Michaut, L.3    Reichhart, J.M.4    Hoffmann, J.A.5
  • 73
    • 0026030444 scopus 로고
    • Genetic and molecular characterization of tube, a Drosophila gene maternally required for embryonic dorsoventral polarity
    • Letsou A, Alexander S, Orth K, Wasserman SA. 1991. Genetic and molecular characterization of tube, a Drosophila gene maternally required for embryonic dorsoventral polarity. Proc. Natl. Acad. Sci. USA 88:810-14
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 810-814
    • Letsou, A.1    Alexander, S.2    Orth, K.3    Wasserman, S.A.4
  • 74
    • 2442612540 scopus 로고    scopus 로고
    • CARMA1, BCL-10 and MALTI in lymphocyte development and activation
    • Thome M. 2004. CARMA1, BCL-10 and MALTI in lymphocyte development and activation. Nat. Rev. Immunol. 4:348-59
    • (2004) Nat. Rev. Immunol , vol.4 , pp. 348-359
    • Thome, M.1
  • 75
    • 0035843970 scopus 로고    scopus 로고
    • Carma1, a CARD-containing binding partner of Bcl10, induces Bcl10 phosphorylation and NF-κB activation
    • Gaide O, Martinon F, Micheau O, Bonnet D, Thome M, Tschopp J. 2001. Carma1, a CARD-containing binding partner of Bcl10, induces Bcl10 phosphorylation and NF-κB activation. FEBS Lett. 496:121-27
    • (2001) FEBS Lett , vol.496 , pp. 121-127
    • Gaide, O.1    Martinon, F.2    Micheau, O.3    Bonnet, D.4    Thome, M.5    Tschopp, J.6
  • 76
    • 0036707522 scopus 로고    scopus 로고
    • CARMA1 is a critical lipid raft-associated regulator of TCR-induced NF-κ activation
    • Gaide O, Favier B, Legler DF, Bonnet D, Brissoni B, et al. 2002. CARMA1 is a critical lipid raft-associated regulator of TCR-induced NF-κ activation. Nat. Immunol. 3:836-43
    • (2002) Nat. Immunol , vol.3 , pp. 836-843
    • Gaide, O.1    Favier, B.2    Legler, D.F.3    Bonnet, D.4    Brissoni, B.5
  • 77
    • 0035374349 scopus 로고    scopus 로고
    • Bcl10 and MALT1, independent targets of chromosomal translocation in malt lymphoma, cooperate in a novel NF-κB signaling pathway
    • Lucas PC, Yonezumi M, Inohara N, McAllister-Lucas LM, Abazeed ME, et al. 2001. Bcl10 and MALT1, independent targets of chromosomal translocation in malt lymphoma, cooperate in a novel NF-κB signaling pathway. J. Biol. Chem. 276:19012-19
    • (2001) J. Biol. Chem , vol.276 , pp. 19012-19019
    • Lucas, P.C.1    Yonezumi, M.2    Inohara, N.3    McAllister-Lucas, L.M.4    Abazeed, M.E.5
  • 78
    • 0033638182 scopus 로고    scopus 로고
    • Identification of paracaspases and metacaspases: Two ancient families of caspase-like proteins, one of which plays a key role in MALT lymphoma
    • Uren AG, O'Rourke K, Aravind LA, Pisabarro MT, Seshagiri S, et al. 2000. Identification of paracaspases and metacaspases: two ancient families of caspase-like proteins, one of which plays a key role in MALT lymphoma. Mol. Cell 6:961-67
    • (2000) Mol. Cell , vol.6 , pp. 961-967
    • Uren, A.G.1    O'Rourke, K.2    Aravind, L.A.3    Pisabarro, M.T.4    Seshagiri, S.5
  • 79
    • 33344476184 scopus 로고    scopus 로고
    • cFLIP regulation of lymphocyte activation and development
    • Budd RC, Yeh WC, Tschopp J. 2006. cFLIP regulation of lymphocyte activation and development. Nat. Rev. Immunol. 6:196-204
    • (2006) Nat. Rev. Immunol , vol.6 , pp. 196-204
    • Budd, R.C.1    Yeh, W.C.2    Tschopp, J.3
  • 80
    • 2342629277 scopus 로고    scopus 로고
    • The TRAF6 ubiquitin ligase and TAK1 kinase mediate IKK activation by BCL10 and MALT1 in T lymphocytes
    • Sun L, Deng L, Ea CK, Xia ZP, Chen ZJ. 2004. The TRAF6 ubiquitin ligase and TAK1 kinase mediate IKK activation by BCL10 and MALT1 in T lymphocytes. Mol. Cell 14:289-301
    • (2004) Mol. Cell , vol.14 , pp. 289-301
    • Sun, L.1    Deng, L.2    Ea, C.K.3    Xia, Z.P.4    Chen, Z.J.5
  • 81
    • 0033591330 scopus 로고    scopus 로고
    • Nodi, an Apaf-1 -like activator of caspase-9 and nuclear factor-κB
    • Inohara N, Koseki T, del Peso L, Hu Y, Yee C, et al. 1999. Nodi, an Apaf-1 -like activator of caspase-9 and nuclear factor-κB. J. Biol. Chem. 274:14560-67
    • (1999) J. Biol. Chem , vol.274 , pp. 14560-14567
    • Inohara, N.1    Koseki, T.2    del Peso, L.3    Hu, Y.4    Yee, C.5
  • 82
    • 0032524908 scopus 로고    scopus 로고
    • RICK, a novel protein kinase containing a caspase recruitment domain, interacts with CLARP and regulates CD95 mediated apoptosis
    • Inohara N, del Peso L, Koseki T, Chen S, Nunez G. 1998. RICK, a novel protein kinase containing a caspase recruitment domain, interacts with CLARP and regulates CD95 mediated apoptosis. J. Biol. Chem. 273:12296-300
    • (1998) J. Biol. Chem , vol.273 , pp. 12296-12300
    • Inohara, N.1    del Peso, L.2    Koseki, T.3    Chen, S.4    Nunez, G.5
  • 83
    • 0034623225 scopus 로고    scopus 로고
    • An induced proximity model for NF-κ activation in the Nod1/RICK and RIP signaling pathways
    • Inohara N, Koseki T, Lin J, del Peso L, Lucas PC, et al. 2000. An induced proximity model for NF-κ activation in the Nod1/RICK and RIP signaling pathways. J. Biol. Chem. 275:27823-31
    • (2000) J. Biol. Chem , vol.275 , pp. 27823-27831
    • Inohara, N.1    Koseki, T.2    Lin, J.3    del Peso, L.4    Lucas, P.C.5
  • 84
    • 0032537836 scopus 로고    scopus 로고
    • Identification of CARDIAK, a RIP-like kinase that associates with caspase-1
    • Thome M, Hofmann K, Burns K, Martinon F, Bodmer JL, et al. 1998. Identification of CARDIAK, a RIP-like kinase that associates with caspase-1. Curr. Biol. 8:885-88
    • (1998) Curr. Biol , vol.8 , pp. 885-888
    • Thome, M.1    Hofmann, K.2    Burns, K.3    Martinon, F.4    Bodmer, J.L.5
  • 85
    • 0035895992 scopus 로고    scopus 로고
    • Nod2, a Nod1/Apaf-1 family member that is restricted to monocytes and activates NF-κB
    • Ogura Y, Inohara N, Benito A, Chen FF, Yamaoka S, Nunez G. 2001. Nod2, a Nod1/Apaf-1 family member that is restricted to monocytes and activates NF-κB. J. Biol. Chem. 276:4812-18
    • (2001) J. Biol. Chem , vol.276 , pp. 4812-4818
    • Ogura, Y.1    Inohara, N.2    Benito, A.3    Chen, F.F.4    Yamaoka, S.5    Nunez, G.6
  • 86
    • 0035978533 scopus 로고    scopus 로고
    • A frameshift mutation in NOD2 associated with susceptibility to Crohn's disease
    • Ogura Y, Bonen DK, Inohara N, Nicolae DL, Chen FF, et al. 2001. A frameshift mutation in NOD2 associated with susceptibility to Crohn's disease. Nature 411:603-6
    • (2001) Nature , vol.411 , pp. 603-606
    • Ogura, Y.1    Bonen, D.K.2    Inohara, N.3    Nicolae, D.L.4    Chen, F.F.5
  • 88
    • 0035860780 scopus 로고    scopus 로고
    • Cop, a caspase recruitment domain-containing protein and inhibitor of caspase-1 activation processing
    • Lee SH, Stehlik C, Reed JC. 2001. Cop, a caspase recruitment domain-containing protein and inhibitor of caspase-1 activation processing. J. Biol. Chem. 276:34495-500
    • (2001) J. Biol. Chem , vol.276 , pp. 34495-34500
    • Lee, S.H.1    Stehlik, C.2    Reed, J.C.3
  • 89
    • 33746028777 scopus 로고    scopus 로고
    • Intracellular pattern recognition receptors in the host response
    • Meylan E, Tschopp J, Karin M. 2006. Intracellular pattern recognition receptors in the host response. Nature 442:39-44
    • (2006) Nature , vol.442 , pp. 39-44
    • Meylan, E.1    Tschopp, J.2    Karin, M.3
  • 90
    • 24144461689 scopus 로고    scopus 로고
    • Identification and characterization of MAVS, a mitochondrial antiviral signaling protein that activates NF-κB and IRF 3
    • Seth RB, Sun L, Ea CK, Chen ZJ. 2005. Identification and characterization of MAVS, a mitochondrial antiviral signaling protein that activates NF-κB and IRF 3. Cell 122:669-82
    • (2005) Cell , vol.122 , pp. 669-682
    • Seth, R.B.1    Sun, L.2    Ea, C.K.3    Chen, Z.J.4
  • 91
    • 27144440476 scopus 로고    scopus 로고
    • Cardif is an adaptor protein in the RIG-I antiviral pathway and is targeted by hepatitis C virus
    • Meylan E, Curran J, Hofmann K, Moradpour D, Binder M, et al. 2005. Cardif is an adaptor protein in the RIG-I antiviral pathway and is targeted by hepatitis C virus. Nature 437:1167-72
    • (2005) Nature , vol.437 , pp. 1167-1172
    • Meylan, E.1    Curran, J.2    Hofmann, K.3    Moradpour, D.4    Binder, M.5
  • 92
    • 27144440523 scopus 로고    scopus 로고
    • IPS-1, an adaptor triggering RIG-I- and Mda5-mediated type I interferon induction
    • Kawai T, Takahashi K, Sato S, Coban C, Kumar H, et al. 2005. IPS-1, an adaptor triggering RIG-I- and Mda5-mediated type I interferon induction. Nat. Immunol. 6:981-88
    • (2005) Nat. Immunol , vol.6 , pp. 981-988
    • Kawai, T.1    Takahashi, K.2    Sato, S.3    Coban, C.4    Kumar, H.5
  • 93
    • 24944538819 scopus 로고    scopus 로고
    • VISA is an adapter protein required for virus-triggered IFN-β signaling
    • Xu LG, Wang YY, Han KJ, Li LY, Zhai Z, Shu HB. 2005. VISA is an adapter protein required for virus-triggered IFN-β signaling. Mol. Cell 19:727-40
    • (2005) Mol. Cell , vol.19 , pp. 727-740
    • Xu, L.G.1    Wang, Y.Y.2    Han, K.J.3    Li, L.Y.4    Zhai, Z.5    Shu, H.B.6
  • 94
    • 10344259136 scopus 로고    scopus 로고
    • The V proteins of paramyxoviruses bind the IFN-inducible RNA helicase, mda-5, and inhibit its activation of the IFN-β promoter
    • Andrejeva J, Childs KS, Young DF, Carlos TS, Stock N, et al. 2004. The V proteins of paramyxoviruses bind the IFN-inducible RNA helicase, mda-5, and inhibit its activation of the IFN-β promoter. Proc. Natl. Acad. Sci. USA 101:17264-69
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 17264-17269
    • Andrejeva, J.1    Childs, K.S.2    Young, D.F.3    Carlos, T.S.4    Stock, N.5
  • 95
    • 23844438864 scopus 로고    scopus 로고
    • Shared and unique functions of the DExD/H-box helicases RIG-I, MDA5, and LGP2 in antiviral innate immunity
    • Yoneyama M, Kikuchi M, Matsumoto K, Imaizumi T, Miyagishi M, et al. 2005. Shared and unique functions of the DExD/H-box helicases RIG-I, MDA5, and LGP2 in antiviral innate immunity. J. Immunol. 175:2851-58
    • (2005) J. Immunol , vol.175 , pp. 2851-2858
    • Yoneyama, M.1    Kikuchi, M.2    Matsumoto, K.3    Imaizumi, T.4    Miyagishi, M.5
  • 96
    • 22544455673 scopus 로고    scopus 로고
    • Cell type-specific involvement of RIG-I in antiviral response
    • Kato H, Sato S, Yoneyama M, Yamamoto M, Uematsu S, et al. 2005. Cell type-specific involvement of RIG-I in antiviral response. Immunity 23:19-28
    • (2005) Immunity , vol.23 , pp. 19-28
    • Kato, H.1    Sato, S.2    Yoneyama, M.3    Yamamoto, M.4    Uematsu, S.5
  • 97
    • 33646342149 scopus 로고    scopus 로고
    • Differential roles of MDA5 and RIG-I helicases in the recognition of RNA viruses
    • Kato H, Takeuchi O, Sato S, Yoneyama M, Yamamoto M, et al. 2006. Differential roles of MDA5 and RIG-I helicases in the recognition of RNA viruses. Nature 441:101-5
    • (2006) Nature , vol.441 , pp. 101-105
    • Kato, H.1    Takeuchi, O.2    Sato, S.3    Yoneyama, M.4    Yamamoto, M.5
  • 98
    • 26844503987 scopus 로고    scopus 로고
    • The RNA helicase Lgp2 inhibits TLR-independent sensing of viral replication by retinoic acid-inducible gene-I
    • Rothenfusser S, Goutagny N, DiPerna G, Gong M, Monks BG, et al. 2005. The RNA helicase Lgp2 inhibits TLR-independent sensing of viral replication by retinoic acid-inducible gene-I. J. Immunol. 175:5260-68
    • (2005) J. Immunol , vol.175 , pp. 5260-5268
    • Rothenfusser, S.1    Goutagny, N.2    DiPerna, G.3    Gong, M.4    Monks, B.G.5
  • 99
    • 0036671894 scopus 로고    scopus 로고
    • The inflammasome: A molecular platform triggering activation of inflammatory caspases and processing of proIL-β
    • Martinon F, Burns K, Tschopp J. 2002. The inflammasome: a molecular platform triggering activation of inflammatory caspases and processing of proIL-β. Mol. Cell 10:417-26
    • (2002) Mol. Cell , vol.10 , pp. 417-426
    • Martinon, F.1    Burns, K.2    Tschopp, J.3
  • 100
    • 0035937797 scopus 로고    scopus 로고
    • A novel enhancer of the Apaf1 apoptosome involved in cytochrome c-dependent caspase activation and apoptosis
    • Chu ZL, Pio F, Xie Z, Welsh K, Krajewska M, et al. 2001. A novel enhancer of the Apaf1 apoptosome involved in cytochrome c-dependent caspase activation and apoptosis. J. Biol. Chem. 276:9239-45
    • (2001) J. Biol. Chem , vol.276 , pp. 9239-9245
    • Chu, Z.L.1    Pio, F.2    Xie, Z.3    Welsh, K.4    Krajewska, M.5
  • 101
    • 0035937775 scopus 로고    scopus 로고
    • Molecular cloning and characterization of DEFCAP-L and -S, two isoforms of a novel member of the mammalian Ced-4 family of apoptosis proteins
    • Hlaing T, Guo RF, Dilley KA, Loussia JM, Morrish TA, et al. 2001. Molecular cloning and characterization of DEFCAP-L and -S, two isoforms of a novel member of the mammalian Ced-4 family of apoptosis proteins. J. Biol. Chem. 276:9230-38
    • (2001) J. Biol. Chem , vol.276 , pp. 9230-9238
    • Hlaing, T.1    Guo, R.F.2    Dilley, K.A.3    Loussia, J.M.4    Morrish, T.A.5
  • 102
    • 0033607768 scopus 로고    scopus 로고
    • ASC, a novel 22-kDa protein, aggregates during apoptosis of human promyelocytic leukemia HL-60 cells
    • Masumoto J, Taniguchi S, Ayukawa K, Sarvotham H, Kishino T, et al. 1999. ASC, a novel 22-kDa protein, aggregates during apoptosis of human promyelocytic leukemia HL-60 cells. J. Biol. Chem. 274:33835-38
    • (1999) J. Biol. Chem , vol.274 , pp. 33835-33838
    • Masumoto, J.1    Taniguchi, S.2    Ayukawa, K.3    Sarvotham, H.4    Kishino, T.5
  • 103
  • 104
    • 0030851905 scopus 로고    scopus 로고
    • NMR structure of the death domain of the p75 neurotrophin receptor
    • Liepinsh E, Ilag LL, Otting G, Ibanez CF. 1997. NMR structure of the death domain of the p75 neurotrophin receptor. EMBO J. 16:4999-5005
    • (1997) EMBO J , vol.16 , pp. 4999-5005
    • Liepinsh, E.1    Ilag, L.L.2    Otting, G.3    Ibanez, C.F.4
  • 105
    • 25444503240 scopus 로고    scopus 로고
    • Cutting edge: Molecular structure of the IL-1R-associated kinase-4 death domain and its implications for TLR signaling
    • Lasker MV, Gajjar MM, Nair SK. 2005. Cutting edge: molecular structure of the IL-1R-associated kinase-4 death domain and its implications for TLR signaling. J. Immunol. 175:4175-79
    • (2005) J. Immunol , vol.175 , pp. 4175-4179
    • Lasker, M.V.1    Gajjar, M.M.2    Nair, S.K.3
  • 106
    • 0033522889 scopus 로고    scopus 로고
    • The solution structure of FADD death domain: Structural basis of death domain interactions of Fas and FADD
    • Jeong EJ, Bang S, Lee TH, Park YI, Sim WS, Kim KS. 1999. The solution structure of FADD death domain: structural basis of death domain interactions of Fas and FADD. J. Biol. Chem. 274:16337-42
    • (1999) J. Biol. Chem , vol.274 , pp. 16337-16342
    • Jeong, E.J.1    Bang, S.2    Lee, T.H.3    Park, Y.I.4    Sim, W.S.5    Kim, K.S.6
  • 108
    • 33344467158 scopus 로고    scopus 로고
    • Crystal structure of RAIDD death domain implicates potential mechanism of PIDDosome assembly
    • Park HH, Wu H. 2006. Crystal structure of RAIDD death domain implicates potential mechanism of PIDDosome assembly. J. Mol. Biol. 357:358-64
    • (2006) J. Mol. Biol , vol.357 , pp. 358-364
    • Park, H.H.1    Wu, H.2
  • 109
    • 0033601077 scopus 로고    scopus 로고
    • Three-dimensional structure of a complex between the death domains of Pelle and Tube
    • Xiao T, Towb P, Wasserman SA, Sprang SR. 1999. Three-dimensional structure of a complex between the death domains of Pelle and Tube. Cell 99:545-55
    • (1999) Cell , vol.99 , pp. 545-555
    • Xiao, T.1    Towb, P.2    Wasserman, S.A.3    Sprang, S.R.4
  • 110
    • 0842307067 scopus 로고    scopus 로고
    • Regulated assembly of the Toll signaling complex drives Drosophila dorsoventral patterning
    • Sun H, Towb P, Chiem DN, Foster BA, Wasserman SA. 2004. Regulated assembly of the Toll signaling complex drives Drosophila dorsoventral patterning. EMBO J. 23:100-10
    • (2004) EMBO J , vol.23 , pp. 100-110
    • Sun, H.1    Towb, P.2    Chiem, D.N.3    Foster, B.A.4    Wasserman, S.A.5
  • 111
    • 13044282468 scopus 로고    scopus 로고
    • Defective CD95/APO-l/Fas signal complex formation in the human autoimmune lymphoproliferative syndrome, type Ia
    • Martin DA, Zheng L, Siegel RM, Huang B, Fisher GH, et al. 1999. Defective CD95/APO-l/Fas signal complex formation in the human autoimmune lymphoproliferative syndrome, type Ia. Proc. Natl. Acad. Sci. USA 96:4552-57
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 4552-4557
    • Martin, D.A.1    Zheng, L.2    Siegel, R.M.3    Huang, B.4    Fisher, G.H.5
  • 112
    • 0347723881 scopus 로고    scopus 로고
    • Identification of an expanded binding surface on the FADD death domain responsible for interaction with CD95/Fas
    • Hill JM, Morisawa G, Kim T, Huang T, Wei Y, Werner MH. 2004. Identification of an expanded binding surface on the FADD death domain responsible for interaction with CD95/Fas. J. Biol. Chem. 279:1474-81
    • (2004) J. Biol. Chem , vol.279 , pp. 1474-1481
    • Hill, J.M.1    Morisawa, G.2    Kim, T.3    Huang, T.4    Wei, Y.5    Werner, M.H.6
  • 113
    • 0029967670 scopus 로고    scopus 로고
    • Systematic mutational analysis of the death domain of the tumor necrosis factor receptor-1-associated protein TRADD
    • Park A, Baichwal VR. 1996. Systematic mutational analysis of the death domain of the tumor necrosis factor receptor-1-associated protein TRADD. J. Biol. Chem. 271:9858-62
    • (1996) J. Biol. Chem , vol.271 , pp. 9858-9862
    • Park, A.1    Baichwal, V.R.2
  • 114
    • 0034725548 scopus 로고    scopus 로고
    • Mutational analysis and NMR studies of the death domain of the tumor necrosis factor receptor-1
    • Telliez JB, Xu GY, Woronicz JD, Hsu S, Wu JL, et al. 2000. Mutational analysis and NMR studies of the death domain of the tumor necrosis factor receptor-1. J. Mol. Biol. 300:1323-33
    • (2000) J. Mol. Biol , vol.300 , pp. 1323-1333
    • Telliez, J.B.1    Xu, G.Y.2    Woronicz, J.D.3    Hsu, S.4    Wu, J.L.5
  • 115
    • 0035896406 scopus 로고    scopus 로고
    • A docking model of key components of the DISC complex: Death domain superfamily interactions redefined
    • Weber CH, Vincenz C. 2001. A docking model of key components of the DISC complex: death domain superfamily interactions redefined. FEBS Lett. 492:171-76
    • (2001) FEBS Lett , vol.492 , pp. 171-176
    • Weber, C.H.1    Vincenz, C.2
  • 116
    • 29144463250 scopus 로고    scopus 로고
    • Crystal structure of MC159 reveals molecular mechanism of DISC assembly and FLIP inhibition
    • Yang JK, Wang L, Zheng L, Wan F, Ahmed M, et al. 2005. Crystal structure of MC159 reveals molecular mechanism of DISC assembly and FLIP inhibition. Mol. Cell 20:939-49
    • (2005) Mol. Cell , vol.20 , pp. 939-949
    • Yang, J.K.1    Wang, L.2    Zheng, L.3    Wan, F.4    Ahmed, M.5
  • 117
    • 33744506980 scopus 로고    scopus 로고
    • FADD self-association is required for stable interaction with an activated death receptor
    • Sandu C, Morisawa G, Wegorzewska I, Huang T, Arechiga AF, et al. 2006. FADD self-association is required for stable interaction with an activated death receptor. Cell Death Differ. 13:2052-61
    • (2006) Cell Death Differ , vol.13 , pp. 2052-2061
    • Sandu, C.1    Morisawa, G.2    Wegorzewska, I.3    Huang, T.4    Arechiga, A.F.5
  • 118
    • 0037011120 scopus 로고    scopus 로고
    • Recognition of ERK MAP kinase by PEA-15 reveals a common docking site within the death domain and death effector domain
    • Hill JM, Vaidyanathan H, Ramos JW, Ginsberg MH, Werner MH. 2002. Recognition of ERK MAP kinase by PEA-15 reveals a common docking site within the death domain and death effector domain. EMBO J. 21:6494-504
    • (2002) EMBO J , vol.2 , Issue.1 , pp. 6494-6504
    • Hill, J.M.1    Vaidyanathan, H.2    Ramos, J.W.3    Ginsberg, M.H.4    Werner, M.H.5
  • 119
    • 33744539048 scopus 로고    scopus 로고
    • The structure of FADD and its mode of interaction with procaspase-8
    • Carrington PE, Sandu C, Wei Y, Hill JM, Morisawa G, et al. 2006. The structure of FADD and its mode of interaction with procaspase-8. Mol. Cell 22:599-610
    • (2006) Mol. Cell , vol.22 , pp. 599-610
    • Carrington, P.E.1    Sandu, C.2    Wei, Y.3    Hill, J.M.4    Morisawa, G.5
  • 120
    • 33646377433 scopus 로고    scopus 로고
    • Crystal structure of a viral FLIP: Insights into FLIP-mediated inhibition of death receptor signaling
    • Li FY, Jeffrey PD, Yu JW, Shi Y. 2006. Crystal structure of a viral FLIP: insights into FLIP-mediated inhibition of death receptor signaling. J. Biol. Chem. 281:2960-68
    • (2006) J. Biol. Chem , vol.281 , pp. 2960-2968
    • Li, F.Y.1    Jeffrey, P.D.2    Yu, J.W.3    Shi, Y.4
  • 121
    • 33744517489 scopus 로고    scopus 로고
    • 2 006. Homotypic FADD interactions through a conserved RXDLL motif are required for death receptor-induced apoptosis
    • Muppidi JR, Lobito AA, Ramaswamy M, Yang JK, Wang L, et al. 2 006. Homotypic FADD interactions through a conserved RXDLL motif are required for death receptor-induced apoptosis. Cell Death Differ. 13:1641-50
    • Cell Death Differ , vol.13 , pp. 1641-1650
    • Muppidi, J.R.1    Lobito, A.A.2    Ramaswamy, M.3    Yang, J.K.4    Wang, L.5
  • 122
    • 0032738099 scopus 로고    scopus 로고
    • Crystal structure of Apaf-1 caspase recruitment domain: An α-helical Greek key fold for apoptotic signaling
    • Vaughn DE, Rodriguez J, Lazebnik Y, Joshua-Tor L. 1999. Crystal structure of Apaf-1 caspase recruitment domain: an α-helical Greek key fold for apoptotic signaling. J. Mol. Biol. 293:439-47
    • (1999) J. Mol. Biol , vol.293 , pp. 439-447
    • Vaughn, D.E.1    Rodriguez, J.2    Lazebnik, Y.3    Joshua-Tor, L.4
  • 123
    • 17244368276 scopus 로고    scopus 로고
    • Structure of the apoptotic protease-activating factor 1 bound to ADP
    • Riedl SJ, Li W, Chao Y, Schwarzenbacher R, Shi Y. 2005. Structure of the apoptotic protease-activating factor 1 bound to ADP. Nature 434:926-33
    • (2005) Nature , vol.434 , pp. 926-933
    • Riedl, S.J.1    Li, W.2    Chao, Y.3    Schwarzenbacher, R.4    Shi, Y.5
  • 124
    • 0033542482 scopus 로고    scopus 로고
    • Structural basis of procaspase-9 recruitment by the apoptotic protease-activating factor 1
    • Qin H, Srinivasula SM, Wu G, Fernandes-Alnemri T, Alnemri ES, Shi Y. 1999. Structural basis of procaspase-9 recruitment by the apoptotic protease-activating factor 1. Nature 399:549-57
    • (1999) Nature , vol.399 , pp. 549-557
    • Qin, H.1    Srinivasula, S.M.2    Wu, G.3    Fernandes-Alnemri, T.4    Alnemri, E.S.5    Shi, Y.6
  • 125
    • 26844485563 scopus 로고    scopus 로고
    • Structure of the CED-4-CED-9 complex provides insights into programmed cell death in Caenorhabditis elegans
    • Yan N, Chai J, Lee ES, Gu L, Liu Q, et al. 2005. Structure of the CED-4-CED-9 complex provides insights into programmed cell death in Caenorhabditis elegans. Nature 43 7:831-37
    • (2005) Nature , vol.43 , Issue.7 , pp. 831-837
    • Yan, N.1    Chai, J.2    Lee, E.S.3    Gu, L.4    Liu, Q.5
  • 126
    • 27644483812 scopus 로고    scopus 로고
    • A structure of the human apoptosome at 12.8 Å resolution provides insights into this cell death platform
    • Yu X, Acehan D, Menetret JF, Booth CR, Ludtke SJ, et al. 2005. A structure of the human apoptosome at 12.8 Å resolution provides insights into this cell death platform. Structure 13:1725-35
    • (2005) Structure , vol.13 , pp. 1725-1735
    • Yu, X.1    Acehan, D.2    Menetret, J.F.3    Booth, C.R.4    Ludtke, S.J.5
  • 127
    • 0037007101 scopus 로고    scopus 로고
    • Oligomerization and activation of caspase-9, induced by Apaf-1 CARD
    • Shiozaki EN, Chai J, Shi Y. 2002. Oligomerization and activation of caspase-9, induced by Apaf-1 CARD. Proc. Natl. Acad. Sci. USA 99:4197-202
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 4197-4202
    • Shiozaki, E.N.1    Chai, J.2    Shi, Y.3
  • 128
    • 0042386425 scopus 로고    scopus 로고
    • The death-domain fold of the ASC PYRIN domain, presenting a basis for PYRIN/PYRIN recognition
    • Liepinsh E, Barbals R, Dahl E, Sharipo A, Staub E, Otting G. 2003. The death-domain fold of the ASC PYRIN domain, presenting a basis for PYRIN/PYRIN recognition. J. Mol. Biol. 332:1155-63
    • (2003) J. Mol. Biol , vol.332 , pp. 1155-1163
    • Liepinsh, E.1    Barbals, R.2    Dahl, E.3    Sharipo, A.4    Staub, E.5    Otting, G.6
  • 129
    • 0141483209 scopus 로고    scopus 로고
    • Folding pyrin into the family
    • Eliezer D. 2003. Folding pyrin into the family. Structure 11:1190-91
    • (2003) Structure , vol.11 , pp. 1190-1191
    • Eliezer, D.1
  • 130
    • 0034520137 scopus 로고    scopus 로고
    • The PYRIN domain: A novel motif found in apoptosis and inflammation proteins
    • Bertin J, DiStefano PS. 2000. The PYRIN domain: a novel motif found in apoptosis and inflammation proteins. Cell Death Differ. 7:1273-74
    • (2000) Cell Death Differ , vol.7 , pp. 1273-1274
    • Bertin, J.1    DiStefano, P.S.2
  • 131
    • 0035916324 scopus 로고    scopus 로고
    • The pyrin domain: A possible member of the death domain-fold family implicated in apoptosis and inflammation
    • Martinon F, Hofmann K, Tschopp J. 2001. The pyrin domain: a possible member of the death domain-fold family implicated in apoptosis and inflammation. Curr. Biol. 11:R118-20
    • (2001) Curr. Biol , vol.11
    • Martinon, F.1    Hofmann, K.2    Tschopp, J.3
  • 132
    • 0035253123 scopus 로고    scopus 로고
    • PAAD: A new protein domain associated with apoptosis, cancer and autoimmune diseases
    • Pawlowski K, Pio F, Chu Z, Reed JC, Godzik A. 2001. PAAD: a new protein domain associated with apoptosis, cancer and autoimmune diseases. Trends Biochem. Sci. 26:85-87
    • (2001) Trends Biochem. Sci , vol.26 , pp. 85-87
    • Pawlowski, K.1    Pio, F.2    Chu, Z.3    Reed, J.C.4    Godzik, A.5
  • 133
    • 0035425256 scopus 로고    scopus 로고
    • The death domain superfamily: A tale of two interfaces?
    • Weber CH, Vincenz C. 2001. The death domain superfamily: a tale of two interfaces? Trends Biochem. Sci. 26:475-81
    • (2001) Trends Biochem. Sci , vol.26 , pp. 475-481
    • Weber, C.H.1    Vincenz, C.2
  • 134
    • 0037063338 scopus 로고    scopus 로고
    • Identification of a basic surface area of the FADD death effector domain critical for apoptotic signaling
    • Kaufmann M, Bozic D, Briand C, Bodmer JL, Zerbe O, et al. 2002. Identification of a basic surface area of the FADD death effector domain critical for apoptotic signaling. FEBS Lett. 527:250-54
    • (2002) FEBS Lett , vol.527 , pp. 250-254
    • Kaufmann, M.1    Bozic, D.2    Briand, C.3    Bodmer, J.L.4    Zerbe, O.5
  • 135
    • 0036657283 scopus 로고    scopus 로고
    • Fire and ICE: The role of pyrin domain-containing proteins in inflammation and apoptosis
    • Gumucio DL, Diaz A, Schaner P, Richards N, Babcock C, et al. 2002. Fire and ICE: the role of pyrin domain-containing proteins in inflammation and apoptosis. Clin. Exp. Rheumatol. 20:S45-53
    • (2002) Clin. Exp. Rheumatol , vol.20
    • Gumucio, D.L.1    Diaz, A.2    Schaner, P.3    Richards, N.4    Babcock, C.5
  • 136
    • 12144284412 scopus 로고    scopus 로고
    • Role of charged and hydrophobic residues in the oligomerization of the PYRIN domain of ASC
    • Moriya M, Taniguchi S, Wu P, Liepinsh E, Otting G, Sagara J. 2005. Role of charged and hydrophobic residues in the oligomerization of the PYRIN domain of ASC. Biochemistry 44:575-83
    • (2005) Biochemistry , vol.44 , pp. 575-583
    • Moriya, M.1    Taniguchi, S.2    Wu, P.3    Liepinsh, E.4    Otting, G.5    Sagara, J.6
  • 137
    • 16944365196 scopus 로고    scopus 로고
    • A candidate gene for familial Mediterranean fever
    • Consortium TFF
    • Consortium TFF. 1997. A candidate gene for familial Mediterranean fever. Nat. Genet. 17:25-31
    • (1997) Nat. Genet , vol.17 , pp. 25-31
  • 138
    • 0035179970 scopus 로고    scopus 로고
    • 2 001. Mutation of a new gene encoding a putative pyrin-like protein causes familial cold autoinflammatory syndrome and Muckle-Wells syndrome
    • Hoffman HM, Mueller JL, Broide DH, Wanderer AA, Kolodner RD. 2 001. Mutation of a new gene encoding a putative pyrin-like protein causes familial cold autoinflammatory syndrome and Muckle-Wells syndrome. Nat. Genet. 29:301-5
    • Nat. Genet , vol.29 , pp. 301-305
    • Hoffman, H.M.1    Mueller, J.L.2    Broide, D.H.3    Wanderer, A.A.4    Kolodner, R.D.5
  • 139
    • 0035189451 scopus 로고    scopus 로고
    • A fever gene comes in from the cold
    • Kastner DL, O'Shea JJ. 2001. A fever gene comes in from the cold. Nat. Genet. 29:241-42
    • (2001) Nat. Genet , vol.29 , pp. 241-242
    • Kastner, D.L.1    O'Shea, J.J.2
  • 140
    • 33344476398 scopus 로고    scopus 로고
    • CATERPILLERs, pyrin and hereditary immunological disorders
    • Ting JP, Kastner DL, Hoffman HM. 2006. CATERPILLERs, pyrin and hereditary immunological disorders. Nat. Rev. Immunol. 6:183-95
    • (2006) Nat. Rev. Immunol , vol.6 , pp. 183-195
    • Ting, J.P.1    Kastner, D.L.2    Hoffman, H.M.3
  • 141
    • 4644354531 scopus 로고    scopus 로고
    • Inhibition of both the extrinsic and intrinsic death pathways through nonhomotypic death-fold interactions
    • Nam YJ, Mani K, Ashton AW, Peng CF, Krishnamurthy B, et al. 2004. Inhibition of both the extrinsic and intrinsic death pathways through nonhomotypic death-fold interactions. Mol. Cell 15:901-12
    • (2004) Mol. Cell , vol.15 , pp. 901-912
    • Nam, Y.J.1    Mani, K.2    Ashton, A.W.3    Peng, C.F.4    Krishnamurthy, B.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.