메뉴 건너뛰기




Volumn 27, Issue 2, 2003, Pages 199-214

Apoptotic signaling cascades

Author keywords

Apoptosis; Bcl 2 proteins; Caspases; Death receptor; Mitochondria; Signal transduction

Indexed keywords

CASPASE; FAS ANTIGEN; PROTEIN BCL 2; TUMOR NECROSIS FACTOR;

EID: 0037376285     PISSN: 02785846     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0278-5846(03)00016-2     Document Type: Article
Times cited : (158)

References (194)
  • 1
    • 0031045588 scopus 로고    scopus 로고
    • CRADD, a novel human apoptotic adaptor molecule for caspase-2, and FasL/tumor necrosis factor receptor-interacting protein RIP
    • Ahmad M., Srinivasula S.M., Wang L., Talanian R.V., Litwack G., Fernandes-Alnemri T., Alnemri E.S. CRADD, a novel human apoptotic adaptor molecule for caspase-2, and FasL/tumor necrosis factor receptor-interacting protein RIP. Cancer Res. 57:1997;615-619.
    • (1997) Cancer Res. , vol.57 , pp. 615-619
    • Ahmad, M.1    Srinivasula, S.M.2    Wang, L.3    Talanian, R.V.4    Litwack, G.5    Fernandes-Alnemri, T.6    Alnemri, E.S.7
  • 3
    • 0034650523 scopus 로고    scopus 로고
    • Bax oligomerization is required for channel-forming activity in liposomes and to trigger cytochrome c release from mitochondria
    • Antonsson B., Montessuit S., Lauper S., Eskes R., Martinou J.C. Bax oligomerization is required for channel-forming activity in liposomes and to trigger cytochrome c release from mitochondria. Biochem. J. 345:2000;271-278.
    • (2000) Biochem. J. , vol.345 , pp. 271-278
    • Antonsson, B.1    Montessuit, S.2    Lauper, S.3    Eskes, R.4    Martinou, J.C.5
  • 4
    • 0032575714 scopus 로고    scopus 로고
    • Death receptors: Signaling and modulation
    • Ashkenazi A., Dixit V.M. Death receptors: signaling and modulation. Science. 281:1998;1305-1308.
    • (1998) Science , vol.281 , pp. 1305-1308
    • Ashkenazi, A.1    Dixit, V.M.2
  • 5
    • 0032910169 scopus 로고    scopus 로고
    • Apoptosis control by death and decoy receptors
    • Ashkenazi A., Dixit V.M. Apoptosis control by death and decoy receptors. Curr. Opin. Cell Biol. 11:1999;255-260.
    • (1999) Curr. Opin. Cell Biol. , vol.11 , pp. 255-260
    • Ashkenazi, A.1    Dixit, V.M.2
  • 7
    • 0026783210 scopus 로고
    • I-κB interacts with the nuclear localization sequences of the subunits of NF-κB: A mechanism for cytoplasmic retention
    • Beg A.A., Ruben S.M., Scheinman R.I., Haskill S., Rosen C.A., Baldwin A.S. Jr. I-κB interacts with the nuclear localization sequences of the subunits of NF-κB: a mechanism for cytoplasmic retention. Genes Dev. 6:1992;1899-1913.
    • (1992) Genes Dev. , vol.6 , pp. 1899-1913
    • Beg, A.A.1    Ruben, S.M.2    Scheinman, R.I.3    Haskill, S.4    Rosen, C.A.5    Baldwin, A.S.6
  • 8
  • 9
    • 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 M.P., Goncharov T.M., Goltsev Y.V., Wallach D. Involvement of MACH, a novel MORT1/FADD-interacting protease, in Fas/APO-1- and TNF receptor-induced cell death. Cell. 85:1996;803-815.
    • (1996) Cell , vol.85 , pp. 803-815
    • Boldin, M.P.1    Goncharov, T.M.2    Goltsev, Y.V.3    Wallach, D.4
  • 10
    • 0035368563 scopus 로고    scopus 로고
    • Apoptotic death sensor: An organelle's alter ego?
    • Bratton S.B., Cohen G.M. Apoptotic death sensor: an organelle's alter ego? Trends Pharmacol. Sci. 22:2001;306-315.
    • (2001) Trends Pharmacol. Sci. , vol.22 , pp. 306-315
    • Bratton, S.B.1    Cohen, G.M.2
  • 11
    • 0030755579 scopus 로고    scopus 로고
    • The regulation of anoikis: MEKK-1 activation requires cleavage by caspases
    • Cardone M.H., Salvesen G.S., Widmann C., Johnson G., Frisch S.M. The regulation of anoikis: MEKK-1 activation requires cleavage by caspases. Cell. 90:1997;315-323.
    • (1997) Cell , vol.90 , pp. 315-323
    • Cardone, M.H.1    Salvesen, G.S.2    Widmann, C.3    Johnson, G.4    Frisch, S.M.5
  • 12
    • 0033213973 scopus 로고    scopus 로고
    • Caspase and calpain substrates: Roles in synaptic plasticity and cell death
    • Chan S.L., Mattson M.P. Caspase and calpain substrates: roles in synaptic plasticity and cell death. J. Neurosci. Res. 58:1999;167-190.
    • (1999) J. Neurosci. Res. , vol.58 , pp. 167-190
    • Chan, S.L.1    Mattson, M.P.2
  • 13
    • 0034733682 scopus 로고    scopus 로고
    • A domain in TNF receptors that mediates ligand-independent receptor assembly and signaling
    • Chan F.K.-M., Chun H.J., Zheng L., Siegel R.M., Bui K.L., Lenardo M.J. A domain in TNF receptors that mediates ligand-independent receptor assembly and signaling. Science. 288:2000;2351-2354.
    • (2000) Science , vol.288 , pp. 2351-2354
    • Chan, F.K.-M.1    Chun, H.J.2    Zheng, L.3    Siegel, R.M.4    Bui, K.L.5    Lenardo, M.J.6
  • 14
    • 0034440818 scopus 로고    scopus 로고
    • Proteases for cell suicide: Functions and regulation of caspases
    • Chang H.Y., Yang X. Proteases for cell suicide: functions and regulation of caspases. Microbiol. Mol. Biol. Rev. 64:2000;821-846.
    • (2000) Microbiol. Mol. Biol. Rev. , vol.64 , pp. 821-846
    • Chang, H.Y.1    Yang, X.2
  • 15
    • 0032544309 scopus 로고    scopus 로고
    • Activation of apoptosis signal-regulating kinase 1 (ASK1) by the adapter protein Daxx
    • Chang H.Y., Nishitoh H., Yang X., Ichijo H., Baltimore D. Activation of apoptosis signal-regulating kinase 1 (ASK1) by the adapter protein Daxx. Science. 281:1998;1860-1863.
    • (1998) Science , vol.281 , pp. 1860-1863
    • Chang, H.Y.1    Nishitoh, H.2    Yang, X.3    Ichijo, H.4    Baltimore, D.5
  • 16
    • 0031406386 scopus 로고    scopus 로고
    • Death receptor 5, a new member of the TNFR family, and DR4 induce FADD- dependent apoptosis and activate the NF-κB pathway
    • Chaudhary P.M., Eby M., Jasmin A., Bookwalter A., Murray J., Hood L. Death receptor 5, a new member of the TNFR family, and DR4 induce FADD- dependent apoptosis and activate the NF-κB pathway. Immunity. 7:1997;821-830.
    • (1997) Immunity , vol.7 , pp. 821-830
    • Chaudhary, P.M.1    Eby, M.2    Jasmin, A.3    Bookwalter, A.4    Murray, J.5    Hood, L.6
  • 17
    • 0037204948 scopus 로고    scopus 로고
    • TNF-R1 signaling: A beautiful pathway
    • Chen G., Goeddel D.V. TNF-R1 signaling: a beautiful pathway. Science. 296:2002;1634-1635.
    • (2002) Science , vol.296 , pp. 1634-1635
    • Chen, G.1    Goeddel, D.V.2
  • 22
    • 0030931876 scopus 로고    scopus 로고
    • Caspases: The executioners of apoptosis
    • Cohen G.M. Caspases: the executioners of apoptosis. Biochem. J. 326:1997;1-16.
    • (1997) Biochem. J. , vol.326 , pp. 1-16
    • Cohen, G.M.1
  • 23
    • 0036716281 scopus 로고    scopus 로고
    • The Bcl2 family: Regulators of the cellular life-or-death switch
    • Cory S., Adams J.M. The Bcl2 family: regulators of the cellular life-or-death switch. Nat. Rev., Cancer. 2:2002;647-656.
    • (2002) Nat. Rev., Cancer , vol.2 , pp. 647-656
    • Cory, S.1    Adams, J.M.2
  • 24
    • 0023106245 scopus 로고
    • Cell-associated tumor necrosis factor (TNF) as a killing mechanism of activated cytotoxic macrophages
    • Decker T., Lohmann-Matthes M.L., Gifford G.E. Cell-associated tumor necrosis factor (TNF) as a killing mechanism of activated cytotoxic macrophages. J. Immunol. 138:1987;957-962.
    • (1987) J. Immunol. , vol.138 , pp. 957-962
    • Decker, T.1    Lohmann-Matthes, M.L.2    Gifford, G.E.3
  • 25
    • 0036141029 scopus 로고    scopus 로고
    • TRAIL-induced apoptosis requires Bax-dependent mitochondrial release of Smac/DIABLO
    • Deng Y., Lin Y., Wu X. TRAIL-induced apoptosis requires Bax-dependent mitochondrial release of Smac/DIABLO. Genes Dev. 16:2002;33-45.
    • (2002) Genes Dev. , vol.16 , pp. 33-45
    • Deng, Y.1    Lin, Y.2    Wu, X.3
  • 26
    • 0035021123 scopus 로고    scopus 로고
    • The α and β subunits of IκB kinase (IKK) mediate TRAF2-dependent IKK recruitment to tumor necrosis factor (TNF) receptor 1 in response to TNF
    • Devin A., Lin Y., Yamaoka S., Li Z., Karin M., Liu Z.-G. The α and β subunits of IκB kinase (IKK) mediate TRAF2-dependent IKK recruitment to tumor necrosis factor (TNF) receptor 1 in response to TNF. Mol. Cell. Biol. 21:2001;3986-3994.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 3986-3994
    • Devin, A.1    Lin, Y.2    Yamaoka, S.3    Li, Z.4    Karin, M.5    Liu, Z.-G.6
  • 27
    • 0029670083 scopus 로고    scopus 로고
    • Mapping of the inducible IκB phosphorylation sites that signal its ubiquitination and degradation
    • DiDonato J., Mercurio F., Rosette C., Wu-Li J., Suyang H., Ghosh S., Karin M. Mapping of the inducible IκB phosphorylation sites that signal its ubiquitination and degradation. Mol. Cell. Biol. 16:1996;1295-1304.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 1295-1304
    • DiDonato, J.1    Mercurio, F.2    Rosette, C.3    Wu-Li, J.4    Suyang, H.5    Ghosh, S.6    Karin, M.7
  • 28
    • 0030610362 scopus 로고    scopus 로고
    • A cytokine-responsive IκB kinase that activates the transcription factor NF-κB
    • DiDonato J.A., Hayakawa M., Rothwarf D.M., Zandi E., Karin M. A cytokine-responsive IκB kinase that activates the transcription factor NF-κB. Nature. 388:1997;548-554.
    • (1997) Nature , vol.388 , pp. 548-554
    • DiDonato, J.A.1    Hayakawa, M.2    Rothwarf, D.M.3    Zandi, E.4    Karin, M.5
  • 30
    • 0034616945 scopus 로고    scopus 로고
    • Smac, a mitochondrial protein that promotes cytochrome c-dependent caspase activation by eliminating IAP inhibition
    • Du C., Fang M., Li Y., Li L., Wang X. Smac, a mitochondrial protein that promotes cytochrome c-dependent caspase activation by eliminating IAP inhibition. Cell. 102:2000;33-42.
    • (2000) Cell , vol.102 , pp. 33-42
    • Du, C.1    Fang, M.2    Li, Y.3    Li, L.4    Wang, X.5
  • 31
    • 0031021356 scopus 로고    scopus 로고
    • RAIDD is a new 'death' adaptor molecule
    • Duan H., Dixit V.M. RAIDD is a new 'death' adaptor molecule. Nature. 385:1997;86-89.
    • (1997) Nature , vol.385 , pp. 86-89
    • Duan, H.1    Dixit, V.M.2
  • 33
    • 0031888955 scopus 로고    scopus 로고
    • A caspase-activated DNase that degrades DNA during apoptosis, and its inhibitor ICAD
    • Enari M., Sakahira H., Yokoyama H., Okawa K., Iwamatsu A., Nagata S. A caspase-activated DNase that degrades DNA during apoptosis, and its inhibitor ICAD. Nature. 391:1998;43-50.
    • (1998) Nature , vol.391 , pp. 43-50
    • Enari, M.1    Sakahira, H.2    Yokoyama, H.3    Okawa, K.4    Iwamatsu, A.5    Nagata, S.6
  • 34
    • 0033968517 scopus 로고    scopus 로고
    • Fas/CD95/APO-1 can function as a death receptor for neuronal cells in vitro and in vivo and is upregulated following cerebral hypoxic-ischemic injury to the developing rat brain
    • Felderhoff-Mueser U., Taylor D.L., Greenwood K., Kozma M., Stibenz D., Joashi U.C., Edwards A.D., Mehmet H. Fas/CD95/APO-1 can function as a death receptor for neuronal cells in vitro and in vivo and is upregulated following cerebral hypoxic-ischemic injury to the developing rat brain. Brain Pathol. 10:2000;17-29.
    • (2000) Brain Pathol. , vol.10 , pp. 17-29
    • Felderhoff-Mueser, U.1    Taylor, D.L.2    Greenwood, K.3    Kozma, M.4    Stibenz, D.5    Joashi, U.C.6    Edwards, A.D.7    Mehmet, H.8
  • 35
    • 0035736259 scopus 로고    scopus 로고
    • Organelle-specific initiation of cell death pathways
    • Ferri K.F., Kroemer G. Organelle-specific initiation of cell death pathways. Nat. Cell Biol. 3:2001;E255-E263.
    • (2001) Nat. Cell Biol. , vol.3 , pp. 255-E263
    • Ferri, K.F.1    Kroemer, G.2
  • 38
    • 0030871457 scopus 로고    scopus 로고
    • P53-Dependent DNA damage-induced apoptosis requires Fas/APO-1-independent activation of CPP32β
    • Fuchs E.J., McKenna K.A., Bedi A. p53-Dependent DNA damage-induced apoptosis requires Fas/APO-1-independent activation of CPP32β Cancer Res. 57:1997;2550-2554.
    • (1997) Cancer Res. , vol.57 , pp. 2550-2554
    • Fuchs, E.J.1    McKenna, K.A.2    Bedi, A.3
  • 40
    • 0036463405 scopus 로고    scopus 로고
    • A matter of life and death
    • Green D.R., Evan G.I. A matter of life and death. Cancer Cells. 1:2002;19-30.
    • (2002) Cancer Cells , vol.1 , pp. 19-30
    • Green, D.R.1    Evan, G.I.2
  • 42
    • 0035008833 scopus 로고    scopus 로고
    • Evidence that the death receptor DR4 is a DNA damage-inducible, p53-regulated gene
    • Guan B., Yue P., Clayman G.L., Sun S.Y. Evidence that the death receptor DR4 is a DNA damage-inducible, p53-regulated gene. J. Cell Physiol. 188:2001;98-105.
    • (2001) J. Cell Physiol. , vol.188 , pp. 98-105
    • Guan, B.1    Yue, P.2    Clayman, G.L.3    Sun, S.Y.4
  • 46
    • 0033605376 scopus 로고    scopus 로고
    • Mitochondrial depolarization accompanies cytochrome c release during apoptosis in PC6 cells
    • Heiskanen K.M., Bhat M.B., Wang H.W., Ma J., Nieminen A.L. Mitochondrial depolarization accompanies cytochrome c release during apoptosis in PC6 cells. J. Biol. Chem. 274:1999;5654-5658.
    • (1999) J. Biol. Chem. , vol.274 , pp. 5654-5658
    • Heiskanen, K.M.1    Bhat, M.B.2    Wang, H.W.3    Ma, J.4    Nieminen, A.L.5
  • 48
    • 0033554554 scopus 로고    scopus 로고
    • Mediation of TNF receptor-associated factor effector functions by apoptosis signal-regulating kinase-1 (ASK1)
    • Hoeflich K.P., Yeh W.C., Yao Z., Mak T.W., Woodgett J.R. Mediation of TNF receptor-associated factor effector functions by apoptosis signal-regulating kinase-1 (ASK1). Oncogene. 18:1999;5814-5820.
    • (1999) Oncogene , vol.18 , pp. 5814-5820
    • Hoeflich, K.P.1    Yeh, W.C.2    Yao, Z.3    Mak, T.W.4    Woodgett, J.R.5
  • 49
    • 0029007855 scopus 로고
    • The TNF receptor 1-associated protein TRADD signals cell death and NF-κB activation
    • Hsu H., Xiong J., Goeddel D.V. The TNF receptor 1-associated protein TRADD signals cell death and NF-κB activation. Cell. 81:1995;495-504.
    • (1995) Cell , vol.81 , pp. 495-504
    • Hsu, H.1    Xiong, J.2    Goeddel, D.V.3
  • 50
    • 0029949257 scopus 로고    scopus 로고
    • TNF-dependent recruitment of the protein kinase RIP to the TNF receptor-1 signaling complex
    • Hsu H., Huang J., Shu H.B., Baichwal V., Goeddel D.V. TNF-dependent recruitment of the protein kinase RIP to the TNF receptor-1 signaling complex. Immunity. 4:1996;387-396.
    • (1996) Immunity , vol.4 , pp. 387-396
    • Hsu, H.1    Huang, J.2    Shu, H.B.3    Baichwal, V.4    Goeddel, D.V.5
  • 51
    • 0030032106 scopus 로고    scopus 로고
    • TRADD-TRAF2 and TRADD-FADD interactions define two distinct TNF receptor 1 signal transduction pathways
    • Hsu H., Shu H.B., Pan M.G., Goeddel D.V. TRADD-TRAF2 and TRADD-FADD interactions define two distinct TNF receptor 1 signal transduction pathways. Cell. 84:1996;299-308.
    • (1996) Cell , vol.84 , pp. 299-308
    • Hsu, H.1    Shu, H.B.2    Pan, M.G.3    Goeddel, D.V.4
  • 52
    • 0032509354 scopus 로고    scopus 로고
    • WD-40 repeat region regulates Apaf-1 self-association and procaspase-9 activation
    • Hu Y., Ding L., Spencer D.M., Nunez G. WD-40 repeat region regulates Apaf-1 self-association and procaspase-9 activation. J. Biol. Chem. 273:1998;33489-33494.
    • (1998) J. Biol. Chem. , vol.273 , pp. 33489-33494
    • Hu, Y.1    Ding, L.2    Spencer, D.M.3    Nunez, G.4
  • 53
    • 0030465072 scopus 로고    scopus 로고
    • NMR structure and mutagenesis of the Fas (APO-1/CD95) death domain
    • Huang B., Eberstadt M., Olejniczak E.T., Meadows R.P., Fesik S.W. NMR structure and mutagenesis of the Fas (APO-1/CD95) death domain. Nature. 384:1996;638-641.
    • (1996) Nature , vol.384 , pp. 638-641
    • Huang, B.1    Eberstadt, M.2    Olejniczak, E.T.3    Meadows, R.P.4    Fesik, S.W.5
  • 56
    • 0033593655 scopus 로고    scopus 로고
    • Prevention of constitutive TNF receptor 1 signaling by silencer of death domains
    • Jiang Y., Woronicz J.D., Liu W., Goeddel D.V. Prevention of constitutive TNF receptor 1 signaling by silencer of death domains. Science. 283:1999;543-546.
    • (1999) Science , vol.283 , pp. 543-546
    • Jiang, Y.1    Woronicz, J.D.2    Liu, W.3    Goeddel, D.V.4
  • 57
    • 0034612885 scopus 로고    scopus 로고
    • L inhibits cytochrome c release but not mitochondrial depolarization during the activation of multiple death pathways by tumor necrosis factor-α
    • L inhibits cytochrome c release but not mitochondrial depolarization during the activation of multiple death pathways by tumor necrosis factor-α J. Biol. Chem. 275:2000;31546-31553.
    • (2000) J. Biol. Chem. , vol.275 , pp. 31546-31553
    • Johnson, B.W.1    Cepero, E.2    Boise, L.H.3
  • 59
    • 85047700229 scopus 로고    scopus 로고
    • Tumor necrosis factor-α induces the expression of DR6, a member of the TNF receptor family, through activation of NF-κB
    • Kasof G.M., Lu J.J., Liu D., Speer B., Mongan K.N., Gomes B.C., Lorenzi M.V. Tumor necrosis factor-α induces the expression of DR6, a member of the TNF receptor family, through activation of NF-κB. Oncogene. 20:2001;7965-7975.
    • (2001) Oncogene , vol.20 , pp. 7965-7975
    • Kasof, G.M.1    Lu, J.J.2    Liu, D.3    Speer, B.4    Mongan, K.N.5    Gomes, B.C.6    Lorenzi, M.V.7
  • 60
    • 0035575679 scopus 로고    scopus 로고
    • Programmed cell death: Alive and well in the new millennium
    • Kaufmann S.H., Hengartner M.O. Programmed cell death: alive and well in the new millennium. Trends Cell Biol. 11:2001;526-534.
    • (2001) Trends Cell Biol. , vol.11 , pp. 526-534
    • Kaufmann, S.H.1    Hengartner, M.O.2
  • 61
    • 0015383455 scopus 로고
    • Apoptosis: A basic biological phenomenon with wide-ranging implications in tissue kinetics
    • Kerr J.F., Wyllie A.H., Currie A.R. Apoptosis: a basic biological phenomenon with wide-ranging implications in tissue kinetics. Br. J. Cancer. 26:1972;239-257.
    • (1972) Br. J. Cancer , vol.26 , pp. 239-257
    • Kerr, J.F.1    Wyllie, A.H.2    Currie, A.R.3
  • 62
    • 0033974084 scopus 로고    scopus 로고
    • Molecular determinants of response to TRAIL in killing of normal and cancer cells
    • Kim K., Fisher M.J., Xu S.-Q., El-Deiry W.S. Molecular determinants of response to TRAIL in killing of normal and cancer cells. Clin. Cancer Res. 6:2000;335-346.
    • (2000) Clin. Cancer Res. , vol.6 , pp. 335-346
    • Kim, K.1    Fisher, M.J.2    Xu, S.-Q.3    El-Deiry, W.S.4
  • 63
    • 0035258615 scopus 로고    scopus 로고
    • Enhanced TRAIL sensitivity by p53 overexpression in human cancer but not normal cell lines
    • Kim K., Takimoto R., Dicker D.T., Chen Y., Gazitt Y., El-Deiry W.S. Enhanced TRAIL sensitivity by p53 overexpression in human cancer but not normal cell lines. Int. J. Oncol. 18:2001;241-247.
    • (2001) Int. J. Oncol. , vol.18 , pp. 241-247
    • Kim, K.1    Takimoto, R.2    Dicker, D.T.3    Chen, Y.4    Gazitt, Y.5    El-Deiry, W.S.6
  • 64
    • 0028883850 scopus 로고
    • Cytotoxicity-dependent APO-1 (Fas/CD95)-associated proteins form a death-inducing signaling complex (DISC) with the receptor
    • Kischkel F.C., Hellbardt S., Behrmann I., Germer M., Pawlita M., Krammer P.H., Peter M.E. Cytotoxicity-dependent APO-1 (Fas/CD95)-associated proteins form a death-inducing signaling complex (DISC) with the receptor. EMBO J. 14:1995;5579-5588.
    • (1995) EMBO J. , vol.14 , pp. 5579-5588
    • Kischkel, F.C.1    Hellbardt, S.2    Behrmann, I.3    Germer, M.4    Pawlita, M.5    Krammer, P.H.6    Peter, M.E.7
  • 65
    • 0033662433 scopus 로고    scopus 로고
    • Apo2L/TRAIL-dependent recruitment of endogenous FADD and caspase-8 to death receptors 4 and 5
    • Kischkel F.C., Lawrence D.A., Chuntharapai A., Schow P., Kim K.J., Ashkenazi A. Apo2L/TRAIL-dependent recruitment of endogenous FADD and caspase-8 to death receptors 4 and 5. Immunity. 12:2000;611-620.
    • (2000) Immunity , vol.12 , pp. 611-620
    • Kischkel, F.C.1    Lawrence, D.A.2    Chuntharapai, A.3    Schow, P.4    Kim, K.J.5    Ashkenazi, A.6
  • 67
    • 0031037897 scopus 로고    scopus 로고
    • The release of cytochrome c from mitochondria: A primary site for Bcl-2 regulation of apoptosis
    • Kluck R.M., Bossy-Wetzel E., Green D.R., Newmeyer D.D. The release of cytochrome c from mitochondria: a primary site for Bcl-2 regulation of apoptosis. Science. 275:1997;1132-1136.
    • (1997) Science , vol.275 , pp. 1132-1136
    • Kluck, R.M.1    Bossy-Wetzel, E.2    Green, D.R.3    Newmeyer, D.D.4
  • 69
    • 0033198273 scopus 로고    scopus 로고
    • Mitochondrial depolarization is not required for neuronal apoptosis
    • Krohn A.J., Wahlbrink T., Prehn J.H. Mitochondrial depolarization is not required for neuronal apoptosis. J. Neurosci. 19:1999;7394-7404.
    • (1999) J. Neurosci. , vol.19 , pp. 7394-7404
    • Krohn, A.J.1    Wahlbrink, T.2    Prehn, J.H.3
  • 70
    • 0034682802 scopus 로고    scopus 로고
    • FADD is required for DR4- and DR5-mediated apoptosis. Lack of TRAIL-induced apoptosis in FADD-deficient mouse embryonic fibroblasts
    • Kuang A.A., Diehl G.E., Zhang J., Winoto A. FADD is required for DR4- and DR5-mediated apoptosis. Lack of TRAIL-induced apoptosis in FADD-deficient mouse embryonic fibroblasts. J. Biol. Chem. 275:2000;25065-25068.
    • (2000) J. Biol. Chem. , vol.275 , pp. 25065-25068
    • Kuang, A.A.1    Diehl, G.E.2    Zhang, J.3    Winoto, A.4
  • 71
    • 0033815948 scopus 로고    scopus 로고
    • Neuronal apoptosis as a therapeutic target in neurodegenerative disease
    • Larner A.J. Neuronal apoptosis as a therapeutic target in neurodegenerative disease. Expert Opin. Ther. Pat. 10:2000;1493-1518.
    • (2000) Expert Opin. Ther. Pat. , vol.10 , pp. 1493-1518
    • Larner, A.J.1
  • 72
    • 0028102478 scopus 로고
    • Cleavage of Poly(ADP-ribose) polymerase by a proteinase with properties like ICE
    • Lazebnik Y., Kaufmann S.H., Desnoyers S., Poirier G.G., Earnshaw W.C. Cleavage of Poly(ADP-ribose) polymerase by a proteinase with properties like ICE. Nature. 371:1994;346-347.
    • (1994) Nature , vol.371 , pp. 346-347
    • Lazebnik, Y.1    Kaufmann, S.H.2    Desnoyers, S.3    Poirier, G.G.4    Earnshaw, W.C.5
  • 76
    • 0036009909 scopus 로고    scopus 로고
    • NF-κB-dependent signaling pathways
    • Li X., Stark G.R. NF-κB-dependent signaling pathways. Exp. Hematol. 30:2002;285-296.
    • (2002) Exp. Hematol. , vol.30 , pp. 285-296
    • Li, X.1    Stark, G.R.2
  • 77
    • 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 S.M., Ahmad M., Alnemri E.S., Wang X. Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade. Cell. 91:1997;479-489.
    • (1997) Cell , vol.91 , pp. 479-489
    • Li, P.1    Nijhawan, D.2    Budihardjo, I.3    Srinivasula, S.M.4    Ahmad, M.5    Alnemri, E.S.6    Wang, X.7
  • 78
    • 0032555697 scopus 로고    scopus 로고
    • Cleavage of Bid by caspase 8 mediates the mitochondrial damage in the Fas pathway of apoptosis
    • Li H., Zhu H., Xu C.J., Yuan J. Cleavage of Bid by caspase 8 mediates the mitochondrial damage in the Fas pathway of apoptosis. Cell. 94:1998;491-501.
    • (1998) Cell , vol.94 , pp. 491-501
    • Li, H.1    Zhu, H.2    Xu, C.J.3    Yuan, J.4
  • 79
    • 0033821215 scopus 로고    scopus 로고
    • The death domain kinase RIP is essential for TRAIL (Apo2L)-induced activation of IκB kinase and c-Jun N-terminal kinase
    • Lin Y., Devin A., Cook A., Keane M.M., Kelliher M., Lipkowitz S., Liu Z.-G. The death domain kinase RIP is essential for TRAIL (Apo2L)-induced activation of IκB kinase and c-Jun N-terminal kinase. Mol. Cell. Biol. 20:2000;6638-6645.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 6638-6645
    • Lin, Y.1    Devin, A.2    Cook, A.3    Keane, M.M.4    Kelliher, M.5    Lipkowitz, S.6    Liu, Z.-G.7
  • 80
    • 0036677061 scopus 로고    scopus 로고
    • Tissue-specific regulation of Fas/APO-1/CD95 expression by p53
    • Lin P., Bush J.A., Cheung K.J. Jr., Li G. Tissue-specific regulation of Fas/APO-1/CD95 expression by p53. Int. J. Oncol. 21:2002;261-264.
    • (2002) Int. J. Oncol. , vol.21 , pp. 261-264
    • Lin, P.1    Bush, J.A.2    Cheung, K.J.3    Li, G.4
  • 82
    • 0030581151 scopus 로고    scopus 로고
    • Induction of apoptotic program in cell-free extracts: Requirement for dATP and cytochrome c
    • Liu X., Kim C.N., Yang J., Jemmerson R., Wang X. Induction of apoptotic program in cell-free extracts: requirement for dATP and cytochrome c. Cell. 86:1996;147-157.
    • (1996) Cell , vol.86 , pp. 147-157
    • Liu, X.1    Kim, C.N.2    Yang, J.3    Jemmerson, R.4    Wang, X.5
  • 83
    • 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 Z.G., Hsu H., Goeddel D.V., Karin M. Dissection of TNF receptor 1 effector functions: JNK activation is not linked to apoptosis while NF-κB activation prevents cell death. Cell. 87:1996;565-576.
    • (1996) Cell , vol.87 , pp. 565-576
    • Liu, Z.G.1    Hsu, H.2    Goeddel, D.V.3    Karin, M.4
  • 84
    • 0034001070 scopus 로고    scopus 로고
    • Activation of apoptosis signal-regulating kinase 1 (ASK1) by tumor necrosis factor receptor-associated factor 2 requires prior dissociation of the ASK1 inhibitor thioredoxin
    • Liu H., Nishitoh H., Ichijo H., Kyriakis J.M. Activation of apoptosis signal-regulating kinase 1 (ASK1) by tumor necrosis factor receptor-associated factor 2 requires prior dissociation of the ASK1 inhibitor thioredoxin. Mol. Cell. Biol. 20:2000;2198-2208.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 2198-2208
    • Liu, H.1    Nishitoh, H.2    Ichijo, H.3    Kyriakis, J.M.4
  • 85
    • 0033010612 scopus 로고    scopus 로고
    • Apoptosis inducing factor (AIF): A phylogenetically old, caspase-independent effector of cell death
    • Lorenzo H.K., Susin S.A., Penninger J., Kroemer G. Apoptosis inducing factor (AIF): a phylogenetically old, caspase-independent effector of cell death. Cell Death Differ. 6:1999;516-524.
    • (1999) Cell Death Differ. , vol.6 , pp. 516-524
    • Lorenzo, H.K.1    Susin, S.A.2    Penninger, J.3    Kroemer, G.4
  • 87
    • 0032555716 scopus 로고    scopus 로고
    • Bid, a Bcl2 interacting protein, mediates cytochrome c release from mitochondria in response to activation of cell surface death receptors
    • Luo X., Budihardjo I., Zou H., Slaughter C., Wang X. Bid, a Bcl2 interacting protein, mediates cytochrome c release from mitochondria in response to activation of cell surface death receptors. Cell. 94:1998;481-490.
    • (1998) Cell , vol.94 , pp. 481-490
    • Luo, X.1    Budihardjo, I.2    Zou, H.3    Slaughter, C.4    Wang, X.5
  • 88
    • 0037085380 scopus 로고    scopus 로고
    • Rapid kinetics of tBid-induced cytochrome c and Smac/DIABLO release and mitochondrial depolarization
    • Madesh M., Antonsson B., Srinivasula S.M., Alnemri E.S., Hajnoczky G. Rapid kinetics of tBid-induced cytochrome c and Smac/DIABLO release and mitochondrial depolarization. J. Biol. Chem. 277:2002;5651-5659.
    • (2002) J. Biol. Chem. , vol.277 , pp. 5651-5659
    • Madesh, M.1    Antonsson, B.2    Srinivasula, S.M.3    Alnemri, E.S.4    Hajnoczky, G.5
  • 89
    • 0031017618 scopus 로고    scopus 로고
    • MAP3K-related kinase involved in NF-κB induction by TNF, CD95 and IL-1
    • Malinin N.L., Boldin M.P., Kovalenko A.V., Wallach D. MAP3K-related kinase involved in NF-κB induction by TNF, CD95 and IL-1. Nature. 385:1997;540-544.
    • (1997) Nature , vol.385 , pp. 540-544
    • Malinin, N.L.1    Boldin, M.P.2    Kovalenko, A.V.3    Wallach, D.4
  • 90
  • 93
    • 0033562658 scopus 로고    scopus 로고
    • CD95 ligand (Fas-L/APO-1L) and tumor necrosis factor-related apoptosis-inducing ligand mediate ischemia-induced apoptosis in neurons
    • Martin-Villalba A., Herr I., Jeremias I., Hahne M., Brandt R., Vogel J., Schenkel J., Herdegen T., Debatin K.M. CD95 ligand (Fas-L/APO-1L) and tumor necrosis factor-related apoptosis-inducing ligand mediate ischemia-induced apoptosis in neurons. J. Neurosci. 19:1999;3809-3817.
    • (1999) J. Neurosci. , vol.19 , pp. 3809-3817
    • Martin-Villalba, A.1    Herr, I.2    Jeremias, I.3    Hahne, M.4    Brandt, R.5    Vogel, J.6    Schenkel, J.7    Herdegen, T.8    Debatin, K.M.9
  • 95
    • 0034136792 scopus 로고    scopus 로고
    • The TRAIL decoy receptor TRUNDD (DcR2, TRAIL-R4) is induced by adenovirus-p53 overexpression and can delay TRAIL-, p53-, and KILLER/DR5-dependent colon cancer apoptosis
    • Meng R.D., McDonald E.R. III, Sheikh M.S., Fornace A.J. Jr., El-Deiry W.S. The TRAIL decoy receptor TRUNDD (DcR2, TRAIL-R4) is induced by adenovirus-p53 overexpression and can delay TRAIL-, p53-, and KILLER/DR5-dependent colon cancer apoptosis. Molec. Ther. 1:2000;130-144.
    • (2000) Molec. Ther. , vol.1 , pp. 130-144
    • Meng, R.D.1    McDonald E.R. III2    Sheikh, M.S.3    Fornace, A.J.4    El-Deiry, W.S.5
  • 97
    • 0028883179 scopus 로고
    • Tumor suppressor p53 is a direct transcriptional activator of the human bax gene
    • Miyashita T., Reed J.C. Tumor suppressor p53 is a direct transcriptional activator of the human bax gene. Cell. 80:1995;293-299.
    • (1995) Cell , vol.80 , pp. 293-299
    • Miyashita, T.1    Reed, J.C.2
  • 98
    • 0035478618 scopus 로고    scopus 로고
    • β-Amyloid induces neuronal apoptosis via a mechanism that involves the c-Jun N-terminal kinase pathway and the induction of Fas ligand
    • Morishima Y., Gotoh Y., Zieg J., Barrett T., Takano H., Flavell R., Davis R.J., Shirasaki Y., Greenberg M.E. β-Amyloid induces neuronal apoptosis via a mechanism that involves the c-Jun N-terminal kinase pathway and the induction of Fas ligand. J. Neurosci. 21:2001;7551-7560.
    • (2001) J. Neurosci. , vol.21 , pp. 7551-7560
    • Morishima, Y.1    Gotoh, Y.2    Zieg, J.3    Barrett, T.4    Takano, H.5    Flavell, R.6    Davis, R.J.7    Shirasaki, Y.8    Greenberg, M.E.9
  • 103
    • 0034635373 scopus 로고    scopus 로고
    • Human and mouse Fas (APO-1/CD95) death receptor genes each contain a p53-responsive element that is activated by p53 mutants unable to induce apoptosis
    • Munsch D., Watanabe-Fukunaga R., Bourdon J.C., Nagata S., May E., Yonish-Rouach E., Reisdorf P. Human and mouse Fas (APO-1/CD95) death receptor genes each contain a p53-responsive element that is activated by p53 mutants unable to induce apoptosis. J. Biol. Chem. 275:2000;3867-3872.
    • (2000) J. Biol. Chem. , vol.275 , pp. 3867-3872
    • Munsch, D.1    Watanabe-Fukunaga, R.2    Bourdon, J.C.3    Nagata, S.4    May, E.5    Yonish-Rouach, E.6    Reisdorf, P.7
  • 105
    • 0031018914 scopus 로고    scopus 로고
    • FLICE induced apoptosis in a cell-free system. Cleavage of caspase zymogens
    • Muzio M., Salvesen G.S., Dixit V.M. FLICE induced apoptosis in a cell-free system. Cleavage of caspase zymogens. J. Biol. Chem. 272:1997;2952-2956.
    • (1997) J. Biol. Chem. , vol.272 , pp. 2952-2956
    • Muzio, M.1    Salvesen, G.S.2    Dixit, V.M.3
  • 106
    • 0030892234 scopus 로고    scopus 로고
    • Apoptosis by death factor
    • Nagata S. Apoptosis by death factor. Cell. 88:1997;355-365.
    • (1997) Cell , vol.88 , pp. 355-365
    • Nagata, S.1
  • 107
    • 0034610743 scopus 로고    scopus 로고
    • Caspase-12 mediates endoplasmic reticulum-specific apoptosis and cytotoxicity by amyloid-β
    • Nakagawa T., Zhu H., Morishima N., Li E., Xu J., Yankner B.A., Yuan J. Caspase-12 mediates endoplasmic reticulum-specific apoptosis and cytotoxicity by amyloid-β Nature. 403:2000;98-103.
    • (2000) Nature , vol.403 , pp. 98-103
    • Nakagawa, T.1    Zhu, H.2    Morishima, N.3    Li, E.4    Xu, J.5    Yankner, B.A.6    Yuan, J.7
  • 108
    • 0035265686 scopus 로고    scopus 로고
    • PUMA, a novel proapoptotic gene, is induced by p53
    • Nakano K., Vousden K.H. PUMA, a novel proapoptotic gene, is induced by p53. Mol. Cell. 7:2001;683-694.
    • (2001) Mol. Cell , vol.7 , pp. 683-694
    • Nakano, K.1    Vousden, K.H.2
  • 110
    • 0030666194 scopus 로고    scopus 로고
    • Tumor necrosis factor (TNF) receptor 1 signaling downstream of TNF receptor-associated factor 2. Nuclear factor κB (NFκB)-inducing kinase requirement for activation of activating protein 1 and NF-κB but not of c-Jun N-terminal kinase/stress-activated protein kinase
    • Natoli G., Costanzo A., Moretti F., Fulco M., Balsano C., Levrero M. Tumor necrosis factor (TNF) receptor 1 signaling downstream of TNF receptor-associated factor 2. Nuclear factor κB (NFκB)-inducing kinase requirement for activation of activating protein 1 and NF-κB but not of c-Jun N-terminal kinase/stress-activated protein kinase. J. Biol. Chem. 272:1997;26079-26082.
    • (1997) J. Biol. Chem. , vol.272 , pp. 26079-26082
    • Natoli, G.1    Costanzo, A.2    Moretti, F.3    Fulco, M.4    Balsano, C.5    Levrero, M.6
  • 111
    • 0033971898 scopus 로고    scopus 로고
    • Mitochondria and neuronal survival
    • Nicholls D.G., Budd S.L. Mitochondria and neuronal survival. Physiol. Rev. 80:2000;315-360.
    • (2000) Physiol. Rev. , vol.80 , pp. 315-360
    • Nicholls, D.G.1    Budd, S.L.2
  • 112
    • 0032785021 scopus 로고    scopus 로고
    • Caspase structure, proteolytic substrates, and function during apoptotic cell death
    • Nicholson D.W. Caspase structure, proteolytic substrates, and function during apoptotic cell death. Cell Death Differ. 6:1999;1028-1042.
    • (1999) Cell Death Differ. , vol.6 , pp. 1028-1042
    • Nicholson, D.W.1
  • 115
    • 0031452639 scopus 로고    scopus 로고
    • Separate domains of the human Fas ligand dictate self-association and receptor binding
    • Orlinick J.R., Elkon K.B., Chao M.V. Separate domains of the human Fas ligand dictate self-association and receptor binding. J. Biol. Chem. 272:1997;32221-32229.
    • (1997) J. Biol. Chem. , vol.272 , pp. 32221-32229
    • Orlinick, J.R.1    Elkon, K.B.2    Chao, M.V.3
  • 116
    • 0030762815 scopus 로고    scopus 로고
    • An antagonist decoy receptor and a death domain-containing receptor for TRAIL
    • Pan G., Ni J., Wei Y.-F., Yu G.-I., Gentz R., Dixit V.M. An antagonist decoy receptor and a death domain-containing receptor for TRAIL. Science. 277:1997;815-818.
    • (1997) Science , vol.277 , pp. 815-818
    • Pan, G.1    Ni, J.2    Wei, Y.-F.3    Yu, G.-I.4    Gentz, R.5    Dixit, V.M.6
  • 121
    • 17544367410 scopus 로고    scopus 로고
    • Induction of apoptosis by Apo-2 ligand, a new member of the tumor necrosis factor cytokine family
    • Pitti R.M., Marsters S.A., Ruppert S., Donahue C.J., Moore A., Ashkenazi A. Induction of apoptosis by Apo-2 ligand, a new member of the tumor necrosis factor cytokine family. J. Biol. Chem. 271:1996;12687-12690.
    • (1996) J. Biol. Chem. , vol.271 , pp. 12687-12690
    • Pitti, R.M.1    Marsters, S.A.2    Ruppert, S.3    Donahue, C.J.4    Moore, A.5    Ashkenazi, A.6
  • 125
    • 0033198217 scopus 로고    scopus 로고
    • Bax translocation is a critical event in neuronal apoptosis: Regulation by neuroprotectants, Bcl-2, and caspases
    • Putcha G.V., Deshmukh M., Johnson E.M. Jr. Bax translocation is a critical event in neuronal apoptosis: regulation by neuroprotectants, Bcl-2, and caspases. J. Neurosci. 19:1999;7476-7485.
    • (1999) J. Neurosci. , vol.19 , pp. 7476-7485
    • Putcha, G.V.1    Deshmukh, M.2    Johnson, E.M.3
  • 128
    • 0033957236 scopus 로고    scopus 로고
    • Active killing of neurons during development and following stress: A role for p75(NTR) and Fas?
    • Raoul C., Pettmann B., Henderson C.E. Active killing of neurons during development and following stress: a role for p75(NTR) and Fas? Curr. Opin. Neurobiol. 10:2000;111-117.
    • (2000) Curr. Opin. Neurobiol. , vol.10 , pp. 111-117
    • Raoul, C.1    Pettmann, B.2    Henderson, C.E.3
  • 129
    • 0036308059 scopus 로고    scopus 로고
    • Mitochondria, the killer organelles and their weapons
    • Ravagnan L., Roumier T., Kroemer G. Mitochondria, the killer organelles and their weapons. J. Cell Physiol. 192:2002;131-137.
    • (2002) J. Cell Physiol. , vol.192 , pp. 131-137
    • Ravagnan, L.1    Roumier, T.2    Kroemer, G.3
  • 130
    • 0031048067 scopus 로고    scopus 로고
    • Tumor necrosis factor α-induced activation of c-Jun N-terminal kinase is mediated by TRAF2
    • Reinhard C., Shamoon B., Shyamala V., Williams L.T. Tumor necrosis factor α-induced activation of c-Jun N-terminal kinase is mediated by TRAF2. EMBO J. 16:1997;1080-1092.
    • (1997) EMBO J. , vol.16 , pp. 1080-1092
    • Reinhard, C.1    Shamoon, B.2    Shyamala, V.3    Williams, L.T.4
  • 132
    • 0028978626 scopus 로고
    • TRAF2-mediated activation of NF-κB by TNF receptor 2 and CD40
    • Rothe M., Sarma V., Dixit V.M., Goeddel D.V. TRAF2-mediated activation of NF-κB by TNF receptor 2 and CD40. Science. 269:1995;1424-1427.
    • (1995) Science , vol.269 , pp. 1424-1427
    • Rothe, M.1    Sarma, V.2    Dixit, V.M.3    Goeddel, D.V.4
  • 133
    • 0030918572 scopus 로고    scopus 로고
    • Membrane and morphological changes in apoptotic cells regulated by caspase-mediated activation of PAK2
    • Rudel T., Bokoch G.M. Membrane and morphological changes in apoptotic cells regulated by caspase-mediated activation of PAK2. Science. 276:1997;1571-1574.
    • (1997) Science , vol.276 , pp. 1571-1574
    • Rudel, T.1    Bokoch, G.M.2
  • 134
    • 0033539067 scopus 로고    scopus 로고
    • Acinus is a caspase-3-activated protein required for apoptotic chromatin condensation
    • Sahara S., Aoto M., Eguchi Y., Imamoto N., Yoneda Y., Tsujimoto Y. Acinus is a caspase-3-activated protein required for apoptotic chromatin condensation. Nature. 401:1999;168-173.
    • (1999) Nature , vol.401 , pp. 168-173
    • Sahara, S.1    Aoto, M.2    Eguchi, Y.3    Imamoto, N.4    Yoneda, Y.5    Tsujimoto, Y.6
  • 135
    • 0034253592 scopus 로고    scopus 로고
    • Bax-dependent transport of cytochrome c reconstituted in pure liposomes
    • Saito M., Korsmeyer S.J., Schlesinger P.H. Bax-dependent transport of cytochrome c reconstituted in pure liposomes. Nat. Cell Biol. 2:2000;553-555.
    • (2000) Nat. Cell Biol. , vol.2 , pp. 553-555
    • Saito, M.1    Korsmeyer, S.J.2    Schlesinger, P.H.3
  • 136
    • 0031889132 scopus 로고    scopus 로고
    • Cleavage of CAD inhibitor in CAD activation and DNA degradation during apoptosis
    • Sakahira H., Enari M., Nagata S. Cleavage of CAD inhibitor in CAD activation and DNA degradation during apoptosis. Nature. 391:1998;96-99.
    • (1998) Nature , vol.391 , pp. 96-99
    • Sakahira, H.1    Enari, M.2    Nagata, S.3
  • 138
    • 0035825488 scopus 로고    scopus 로고
    • Molecular mechanisms of death-receptor-mediated apoptosis
    • Sartorius U., Schmitz I., Krammer P.H. Molecular mechanisms of death-receptor-mediated apoptosis. ChemBioChem. 2:2001;20-29.
    • (2001) ChemBioChem , vol.2 , pp. 20-29
    • Sartorius, U.1    Schmitz, I.2    Krammer, P.H.3
  • 142
    • 0034097347 scopus 로고    scopus 로고
    • Subcellular localization and CARD-dependent oligomerization of the death adaptor RAIDD
    • Shearwin-Whyatt L.M., Harvey N.L., Kumar S. Subcellular localization and CARD-dependent oligomerization of the death adaptor RAIDD. Cell Death Differ. 7:2000;155-165.
    • (2000) Cell Death Differ. , vol.7 , pp. 155-165
    • Shearwin-Whyatt, L.M.1    Harvey, N.L.2    Kumar, S.3
  • 144
    • 0036205587 scopus 로고    scopus 로고
    • Mechanisms of caspase activation and inhibition during apoptosis
    • Shi Y. Mechanisms of caspase activation and inhibition during apoptosis. Mol. Cell. 9:2002;459-470.
    • (2002) Mol. Cell , vol.9 , pp. 459-470
    • Shi, Y.1
  • 146
    • 12644272789 scopus 로고    scopus 로고
    • Tumor necrosis factor (TNF)-mediated kinase cascades: Bifurcation of nuclear factor-κB and c-Jun N-terminal kinase (JNK/SAPK) pathways at TNF receptor-associated factor 2
    • Song H.Y., Regnier C.H., Kirschning C.J., Goeddel D.V., Rothe M. Tumor necrosis factor (TNF)-mediated kinase cascades: bifurcation of nuclear factor-κB and c-Jun N-terminal kinase (JNK/SAPK) pathways at TNF receptor-associated factor 2. Proc. Natl. Acad. Sci. U. S. A. 94:1997;9792-9796.
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 9792-9796
    • Song, H.Y.1    Regnier, C.H.2    Kirschning, C.J.3    Goeddel, D.V.4    Rothe, M.5
  • 147
    • 0033667778 scopus 로고    scopus 로고
    • FADD/MORT1 and caspase-8 are recruited to TRAIL receptors 1 and 2 and are essential for apoptosis mediated by TRAIL receptor 2
    • Sprick M.R., Weigand M.A., Rieser E., Rauch C.T., Juo P., Blenis J., Krammer P.H., Walczak H. FADD/MORT1 and caspase-8 are recruited to TRAIL receptors 1 and 2 and are essential for apoptosis mediated by TRAIL receptor 2. Immunity. 12:2000;599-609.
    • (2000) Immunity , vol.12 , pp. 599-609
    • Sprick, M.R.1    Weigand, M.A.2    Rieser, E.3    Rauch, C.T.4    Juo, P.5    Blenis, J.6    Krammer, P.H.7    Walczak, H.8
  • 148
    • 0037009370 scopus 로고    scopus 로고
    • Caspase-10 is recruited to and activated at the native TRAIL and CD95 death-inducing signalling complexes in a FADD-dependent manner but cannot functionally substitute caspase-8
    • Sprick M.R., Rieser E., Stahl H., Grosse-Wilde A., Weigand M.A., Walczak H. Caspase-10 is recruited to and activated at the native TRAIL and CD95 death-inducing signalling complexes in a FADD-dependent manner but cannot functionally substitute caspase-8. EMBO J. 21:2002;4520-4530.
    • (2002) EMBO J. , vol.21 , pp. 4520-4530
    • Sprick, M.R.1    Rieser, E.2    Stahl, H.3    Grosse-Wilde, A.4    Weigand, M.A.5    Walczak, H.6
  • 150
    • 0029905073 scopus 로고    scopus 로고
    • Molecular ordering of the Fas-apoptotic pathway: The Fas/APO-1 protease Mch5 is a CrmA-inhibitable protease that activates multiple Ced-3/ICE-like cysteine proteases
    • Srinivasula S.M., Ahmad M., Fernandes-Alnemri T., Litwack G., Alnemri E.S. Molecular ordering of the Fas-apoptotic pathway: the Fas/APO-1 protease Mch5 is a CrmA-inhibitable protease that activates multiple Ced-3/ICE-like cysteine proteases. Proc. Natl. Acad. Sci. U. S. A. 93:1996;14486-14491.
    • (1996) Proc. Natl. Acad. Sci. U. S. A. , vol.93 , pp. 14486-14491
    • Srinivasula, S.M.1    Ahmad, M.2    Fernandes-Alnemri, T.3    Litwack, G.4    Alnemri, E.S.5
  • 151
    • 0034680876 scopus 로고    scopus 로고
    • Molecular determinants of the caspase-promoting activity of Smac/DIABLO and its role in the death receptor pathway
    • Srinivasula S.M., Datta P., Fan X.-J., Fernandes-Alnemri T., Huang Z., Alnemri E.S. Molecular determinants of the caspase-promoting activity of Smac/DIABLO and its role in the death receptor pathway. J. Biol. Chem. 275:2000;36152-36157.
    • (2000) J. Biol. Chem. , vol.275 , pp. 36152-36157
    • Srinivasula, S.M.1    Datta, P.2    Fan, X.-J.3    Fernandes-Alnemri, T.4    Huang, Z.5    Alnemri, E.S.6
  • 153
    • 0032416062 scopus 로고    scopus 로고
    • Death by a thousand cuts: An ever increasing list of caspase substrates
    • Stroh C., Schulze-Osthoff K. Death by a thousand cuts: an ever increasing list of caspase substrates. Cell Death Differ. 5:1998;997-1000.
    • (1998) Cell Death Differ. , vol.5 , pp. 997-1000
    • Stroh, C.1    Schulze-Osthoff, K.2
  • 154
    • 0027145632 scopus 로고
    • Molecular cloning and expression of the Fas ligand, a novel member of the tumor necrosis factor family
    • Suda T., Takahashi T., Golstein P., Nagata S. Molecular cloning and expression of the Fas ligand, a novel member of the tumor necrosis factor family. Cell. 75:1993;1169-1178.
    • (1993) Cell , vol.75 , pp. 1169-1178
    • Suda, T.1    Takahashi, T.2    Golstein, P.3    Nagata, S.4
  • 155
    • 0037192790 scopus 로고    scopus 로고
    • L inhibit CD95-mediated apoptosis by preventing mitochondrial release of Smac/DIABLO and subsequent inactivation of X-linked inhibitor-of-apoptosis protein
    • L inhibit CD95-mediated apoptosis by preventing mitochondrial release of Smac/DIABLO and subsequent inactivation of X-linked inhibitor-of-apoptosis protein. J. Biol. Chem. 277:2002;11345-11351.
    • (2002) J. Biol. Chem. , vol.277 , pp. 11345-11351
    • Sun, X.M.1    Bratton, S.B.2    Butterworth, M.3    MacFarlane, M.4    Cohen, G.M.5
  • 159
    • 0035800225 scopus 로고    scopus 로고
    • Increased expression of Fas (CD95/APO-1) in adult rat brain after kainate-induced seizures
    • Tan Z., Levid J., Schreiber S.S. Increased expression of Fas (CD95/APO-1) in adult rat brain after kainate-induced seizures. NeuroReport. 12:2001;1979-1982.
    • (2001) NeuroReport , vol.12 , pp. 1979-1982
    • Tan, Z.1    Levid, J.2    Schreiber, S.S.3
  • 162
    • 0027275490 scopus 로고
    • A novel domain within the 55 kd TNF receptor signals cell death
    • Tartaglia L.A., Ayres T.M., Wong G.H., Goeddel D.V. A novel domain within the 55 kd TNF receptor signals cell death. Cell. 74:1993;845-853.
    • (1993) Cell. , vol.74 , pp. 845-853
    • Tartaglia, L.A.1    Ayres, T.M.2    Wong, G.H.3    Goeddel, D.V.4
  • 163
    • 0027301244 scopus 로고
    • Ligand passing: The 75-kDa tumor necrosis factor (TNF) receptor recruits TNF for signaling by the 55-kDa TNF receptor
    • Tartaglia L.A., Pennica D., Goeddel D.V. Ligand passing: the 75-kDa tumor necrosis factor (TNF) receptor recruits TNF for signaling by the 55-kDa TNF receptor. J. Biol. Chem. 268:1993;18542-18548.
    • (1993) J. Biol. Chem. , vol.268 , pp. 18542-18548
    • Tartaglia, L.A.1    Pennica, D.2    Goeddel, D.V.3
  • 166
    • 0033971901 scopus 로고    scopus 로고
    • Bcl-2 family: Life-or-death switch
    • Tsujimoto Y., Shimizu S. Bcl-2 family: life-or-death switch. FEBS Lett. 466:2000;6-10.
    • (2000) FEBS Lett. , vol.466 , pp. 6-10
    • Tsujimoto, Y.1    Shimizu, S.2
  • 167
    • 0023621203 scopus 로고
    • Human T cells from autoimmune and normal individuals can produce tumor necrosis factor
    • Turner M., Londei M., Feldmann M. Human T cells from autoimmune and normal individuals can produce tumor necrosis factor. Eur. J. Immunol. 17:1987;1807-1814.
    • (1987) Eur. J. Immunol. , vol.17 , pp. 1807-1814
    • Turner, M.1    Londei, M.2    Feldmann, M.3
  • 170
    • 0031890109 scopus 로고    scopus 로고
    • Mitochondrial membrane potential and nuclear changes in apoptosis caused by serum and nerve growth factor withdrawal: Time course and modification by (-)-deprenyl
    • Wadia J.S., Chalmers-Redman R.M., Ju W.J., Carlile G.W., Phillips J.L., Fraser A.D., Tatton W.G. Mitochondrial membrane potential and nuclear changes in apoptosis caused by serum and nerve growth factor withdrawal: time course and modification by (-)-deprenyl. J. Neurosci. 18:1998;932-947.
    • (1998) J. Neurosci. , vol.18 , pp. 932-947
    • Wadia, J.S.1    Chalmers-Redman, R.M.2    Ju, W.J.3    Carlile, G.W.4    Phillips, J.L.5    Fraser, A.D.6    Tatton, W.G.7
  • 171
    • 0037204952 scopus 로고    scopus 로고
    • The Fas signaling pathway: More than a paradigm
    • Wajant H. The Fas signaling pathway: more than a paradigm. Science. 296:2002;1635-1636.
    • (2002) Science , vol.296 , pp. 1635-1636
    • Wajant, H.1
  • 172
    • 0037377189 scopus 로고    scopus 로고
    • Prospects for anti-apoptotic drug therapy of neurodegenerative diseases
    • (this issue)
    • Waldmeier P.C. Prospects for anti-apoptotic drug therapy of neurodegenerative diseases. Prog. Neuro-Psychopharmacol. Biol. Psychiatry. 27:2003;303-321. (this issue).
    • (2003) Prog. Neuro-Psychopharmacol. Biol. Psychiatry , vol.27 , pp. 303-321
    • Waldmeier, P.C.1
  • 174
    • 0032508414 scopus 로고    scopus 로고
    • NF-κB antiapoptosis: Induction of TRAF1 and TRAF2 and c-IAP1 and c-IAP2 to suppress caspase-8 activation
    • Wang C.-Y., Mayo M.W., Korneluk R.G., Goeddel D.V., Baldwin A.S. Jr. NF-κB antiapoptosis: induction of TRAF1 and TRAF2 and c-IAP1 and c-IAP2 to suppress caspase-8 activation. Science. 281:1998;1680-1683.
    • (1998) Science , vol.281 , pp. 1680-1683
    • Wang, C.-Y.1    Mayo, M.W.2    Korneluk, R.G.3    Goeddel, D.V.4    Baldwin, A.S.5
  • 176
    • 0037174864 scopus 로고    scopus 로고
    • TRAIL-receptor and CD95 signal to mitochondria via FADD, caspase-8/10, Bid and Bax, but differentially regulate events downstream from truncated Bid
    • Werner A.B., de Vries E., Tait S.W.G., Bontjer I., Borst J. TRAIL-receptor and CD95 signal to mitochondria via FADD, caspase-8/10, Bid and Bax, but differentially regulate events downstream from truncated Bid. J. Biol. Chem. 277:2002;40760-40767.
    • (2002) J. Biol. Chem. , vol.277 , pp. 40760-40767
    • Werner, A.B.1    De Vries, E.2    Tait, S.W.G.3    Bontjer, I.4    Borst, J.5
  • 177
    • 0032549670 scopus 로고    scopus 로고
    • Caspase-dependent cleavage of signaling proteins during apoptosis. A turn-off mechanism for anti-apoptotic signals
    • Widmann C., Gibson S., Johnson G.L. Caspase-dependent cleavage of signaling proteins during apoptosis. A turn-off mechanism for anti-apoptotic signals. J. Biol. Chem. 273:1998;7141-7147.
    • (1998) J. Biol. Chem. , vol.273 , pp. 7141-7147
    • Widmann, C.1    Gibson, S.2    Johnson, G.L.3
  • 179
    • 0033575255 scopus 로고    scopus 로고
    • Suicidal tendencies: Apoptotic cell death by caspase family proteinases
    • Wolf B.B., Green D.R. Suicidal tendencies: apoptotic cell death by caspase family proteinases. J. Biol. Chem. 274:1999;20049-20052.
    • (1999) J. Biol. Chem. , vol.274 , pp. 20049-20052
    • Wolf, B.B.1    Green, D.R.2
  • 181
    • 0029086989 scopus 로고
    • The role of free radicals and p53 in neuron apoptosis in vivo
    • Wood K.A., Youle R.J. The role of free radicals and p53 in neuron apoptosis in vivo. J. Neurosci. 15:1995;5851-5857.
    • (1995) J. Neurosci. , vol.15 , pp. 5851-5857
    • Wood, K.A.1    Youle, R.J.2
  • 183
    • 0035691186 scopus 로고    scopus 로고
    • Caspase-dependent apoptotic pathways in CNS injury
    • Yakovlev A.G., Faden A.I. Caspase-dependent apoptotic pathways in CNS injury. Mol. Neurobiol. 24:2001;131-144.
    • (2001) Mol. Neurobiol. , vol.24 , pp. 131-144
    • Yakovlev, A.G.1    Faden, A.I.2
  • 184
    • 0033499801 scopus 로고    scopus 로고
    • Bcl-2 is phosphorylated and inactivated by an ASK1/Jun N-terminal protein kinase pathway normally activated at G2/M
    • Yamamoto K., Ichijo H., Korsmeyer S.J. Bcl-2 is phosphorylated and inactivated by an ASK1/Jun N-terminal protein kinase pathway normally activated at G2/M. Mol. Cell. Biol. 19:1999;8469-8478.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 8469-8478
    • Yamamoto, K.1    Ichijo, H.2    Korsmeyer, S.J.3
  • 186
    • 0031587883 scopus 로고    scopus 로고
    • Daxx, a novel Fas-binding protein that activates JNK and apoptosis
    • Yang X., Khosravi-Far R., Chang H.Y., Baltimore D. Daxx, a novel Fas-binding protein that activates JNK and apoptosis. Cell. 89:1997;1067-1076.
    • (1997) Cell , vol.89 , pp. 1067-1076
    • Yang, X.1    Khosravi-Far, R.2    Chang, H.Y.3    Baltimore, D.4
  • 187
    • 0036830353 scopus 로고    scopus 로고
    • Bid-mediated mitochondrial pathway is critical to ischemic neuronal apoptosis and focal cerebral ischemia
    • Yin X.-M., Luo Y., Cao G., Bai L., Pei W., Kuharsky D.K., Chen J. Bid-mediated mitochondrial pathway is critical to ischemic neuronal apoptosis and focal cerebral ischemia. J. Biol. Chem. 277(44):2002;42074-42081.
    • (2002) J. Biol. Chem. , vol.277 , Issue.44 , pp. 42074-42081
    • Yin, X.-M.1    Luo, Y.2    Cao, G.3    Bai, L.4    Pei, W.5    Kuharsky, D.K.6    Chen, J.7
  • 190
    • 0033712615 scopus 로고    scopus 로고
    • Recruitment of the IKK signalosome to the p55 TNF receptor: RIP and A20 bind to NEMO (IKKγ) upon receptor stimulation
    • Zhang S.Q., Kovalenko A., Cantarella G., Wallach D. Recruitment of the IKK signalosome to the p55 TNF receptor: RIP and A20 bind to NEMO (IKKγ) upon receptor stimulation. Immunity. 12:2000;301-311.
    • (2000) Immunity , vol.12 , pp. 301-311
    • Zhang, S.Q.1    Kovalenko, A.2    Cantarella, G.3    Wallach, D.4
  • 191
    • 0032499702 scopus 로고    scopus 로고
    • Caspase-dependent activation of cyclin-dependent kinases during Fas-induced apoptosis in Jurkat cells
    • Zhou B.B., Li H., Yuan J., Kirschner M.W. Caspase-dependent activation of cyclin-dependent kinases during Fas-induced apoptosis in Jurkat cells. Proc. Natl. Acad. Sci. U. S. A. 95:1998;6785-6790.
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 6785-6790
    • Zhou, B.B.1    Li, H.2    Yuan, J.3    Kirschner, M.W.4
  • 193
    • 0035876483 scopus 로고    scopus 로고
    • BH3-only proteins that bind pro-survival Bcl-2 family members fail to induce apoptosis in the absence of Bax and Bak
    • Zong W.-X., Lindsten T., Ross A.J., MacGregor G.R., Thompson C.B. BH3-only proteins that bind pro-survival Bcl-2 family members fail to induce apoptosis in the absence of Bax and Bak. Genes Dev. 15:2001;1481-1486.
    • (2001) Genes Dev. , vol.15 , pp. 1481-1486
    • Zong, W.-X.1    Lindsten, T.2    Ross, A.J.3    MacGregor, G.R.4    Thompson, C.B.5
  • 194
    • 0033596980 scopus 로고    scopus 로고
    • An APAF-1·cytochrome c multimeric complex is a functional apoptosome that activates procaspase-9
    • Zou H., Li Y., Liu X., Wang X. An APAF-1·cytochrome c multimeric complex is a functional apoptosome that activates procaspase-9. J. Biol. Chem. 274:1999;11549-11556.
    • (1999) J. Biol. Chem. , vol.274 , pp. 11549-11556
    • Zou, H.1    Li, Y.2    Liu, X.3    Wang, X.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.