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Volumn 31, Issue 18, 2011, Pages 3745-3758

Requirement of FADD, NEMO, and BAX/BAK for aberrant mitochondrial function in tumor necrosis factor alpha-induced necrosis

Author keywords

[No Author keywords available]

Indexed keywords

FAS ASSOCIATED DEATH DOMAIN PROTEIN; I KAPPA B KINASE; I KAPPA B KINASE GAMMA; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; PRONECROTIC RIP1 RIP3 KINASE; PROTEIN BAK; PROTEIN BAX; PROTEIN BCL XL; PROTEIN SERINE THREONINE KINASE; PROTEIN SUBUNIT; REACTIVE OXYGEN METABOLITE; TRANSCRIPTION FACTOR RELA; TUMOR NECROSIS FACTOR ALPHA; UNCLASSIFIED DRUG;

EID: 80052583012     PISSN: 02707306     EISSN: 10985549     Source Type: Journal    
DOI: 10.1128/MCB.05303-11     Document Type: Article
Times cited : (93)

References (72)
  • 1
    • 15844375853 scopus 로고    scopus 로고
    • Loss of cyclophilin D reveals a critical role for mitochondrial permeability transition in cell death
    • Baines, C. P., et al. 2005. Loss of cyclophilin D reveals a critical role for mitochondrial permeability transition in cell death. Nature 434:658-662.
    • (2005) Nature , vol.434 , pp. 658-662
    • Baines, C.P.1
  • 2
    • 34247895697 scopus 로고    scopus 로고
    • Voltage-dependent anion channels are dispensable for mitochondrialdependent cell death
    • Baines, C. P., R. A. Kaiser, T. Sheiko, W. J. Craigen, and J. D. Molkentin. 2007. Voltage-dependent anion channels are dispensable for mitochondrialdependent cell death. Nat. Cell Biol. 9:550-555.
    • (2007) Nat. Cell Biol. , vol.9 , pp. 550-555
    • Baines, C.P.1    Kaiser, R.A.2    Sheiko, T.3    Craigen, W.J.4    Molkentin, J.D.5
  • 3
    • 21244446551 scopus 로고    scopus 로고
    • Properties of the permeability transition pore in mitochondria devoid of cyclophilin D
    • Basso, E., et al. 2005. Properties of the permeability transition pore in mitochondria devoid of cyclophilin D. J. Biol. Chem. 280:18558-18561.
    • (2005) J. Biol. Chem. , vol.280 , pp. 18558-18561
    • Basso, E.1
  • 4
    • 55949083821 scopus 로고    scopus 로고
    • FADD and caspase-8 control the outcome of autophagic signaling in proliferating T cells
    • Bell, B. D., et al. 2008. FADD and caspase-8 control the outcome of autophagic signaling in proliferating T cells. Proc. Natl. Acad. Sci. U. S. A. 105:16677-16682.
    • (2008) Proc. Natl. Acad. Sci. U. S. A. , vol.105 , pp. 16677-16682
    • Bell, B.D.1
  • 6
    • 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., T. M. Goncharov, Y. V. Goltsev, and D. Wallach. 1996. Involvement of MACH, a novel MORT1/FADD-interacting protease, in Fas/APO-1- and TNF receptor-induced cell death. Cell 85:803-815.
    • (1996) Cell , vol.85 , pp. 803-815
    • Boldin, M.P.1    Goncharov, T.M.2    Goltsev, Y.V.3    Wallach, D.4
  • 7
    • 64849113485 scopus 로고    scopus 로고
    • Control of mitochondrial apoptosis by the Bcl-2 family
    • Brunelle, J. K., and A. Letai. 2009. Control of mitochondrial apoptosis by the Bcl-2 family. J. Cell Sci. 122:437-441.
    • (2009) J. Cell Sci. , vol.122 , pp. 437-441
    • Brunelle, J.K.1    Letai, A.2
  • 8
    • 38349070256 scopus 로고    scopus 로고
    • Mitochondria as a target for the cardioprotective effects of nitric oxide in ischemia-reperfusion injury
    • Burwell, L. S., and P. S. Brookes. 2008. Mitochondria as a target for the cardioprotective effects of nitric oxide in ischemia-reperfusion injury. Antioxid. Redox Signal. 10:579-599.
    • (2008) Antioxid. Redox Signal. , vol.10 , pp. 579-599
    • Burwell, L.S.1    Brookes, P.S.2
  • 10
    • 66449133280 scopus 로고    scopus 로고
    • Phosphorylation-driven assembly of the RIP1-RIP3 complex regulates programmed necrosis and virus-induced inflammation
    • Cho, Y. S., et al. 2009. Phosphorylation-driven assembly of the RIP1-RIP3 complex regulates programmed necrosis and virus-induced inflammation. Cell 137:1112-1123.
    • (2009) Cell , vol.137 , pp. 1112-1123
    • Cho, Y.S.1
  • 11
    • 0036794398 scopus 로고    scopus 로고
    • BAFFinduced NEMO-independent processing of NF-kappa B2 in maturing B cells
    • Claudio, E., K. Brown, S. Park, H. Wang, and U. Siebenlist. 2002. BAFFinduced NEMO-independent processing of NF-kappa B2 in maturing B cells. Nat. Immunol. 3:958-965.
    • (2002) Nat. Immunol. , vol.3 , pp. 958-965
    • Claudio, E.1    Brown, K.2    Park, S.3    Wang, H.4    Siebenlist, U.5
  • 12
    • 0029066697 scopus 로고
    • Contenders in FasL/TNF death signaling
    • Cleveland, J. L., and J. N. Ihle. 1995. Contenders in FasL/TNF death signaling. Cell 81:479-482.
    • (1995) Cell , vol.81 , pp. 479-482
    • Cleveland, J.L.1    Ihle, J.N.2
  • 13
    • 58249093873 scopus 로고    scopus 로고
    • Induction of hepatitis by JNK-mediated expression of TNF-alpha
    • Das, M., et al. 2009. Induction of hepatitis by JNK-mediated expression of TNF-alpha. Cell 136:249-260.
    • (2009) Cell , vol.136 , pp. 249-260
    • Das, M.1
  • 14
    • 72649098216 scopus 로고    scopus 로고
    • Nitration of the mitochondrial complex I subunit NDUFB8 elicits RIP1- and RIP3-mediated necrosis
    • Davis, C. W., et al. 2010. Nitration of the mitochondrial complex I subunit NDUFB8 elicits RIP1- and RIP3-mediated necrosis. Free Radic. Biol. Med. 48:306-317.
    • (2010) Free Radic. Biol. Med. , vol.48 , pp. 306-317
    • Davis, C.W.1
  • 15
    • 42249102086 scopus 로고    scopus 로고
    • Identification of RIP1 kinase as a specific cellular target of necrostatins
    • Degterev, A., et al. 2008. Identification of RIP1 kinase as a specific cellular target of necrostatins. Nat. Chem. Biol. 4:313-321.
    • (2008) Nat. Chem. Biol. , vol.4 , pp. 313-321
    • Degterev, A.1
  • 16
    • 33644840693 scopus 로고    scopus 로고
    • Chemical inhibitor of nonapoptotic cell death with therapeutic potential for ischemic brain injury
    • Degterev, A., et al. 2005. Chemical inhibitor of nonapoptotic cell death with therapeutic potential for ischemic brain injury. Nat. Chem. Biol. 1:112-119.
    • (2005) Nat. Chem. Biol. , vol.1 , pp. 112-119
    • Degterev, A.1
  • 17
    • 42449123761 scopus 로고    scopus 로고
    • Expansion and evolution of cell death programmes
    • Degterev, A., and J. Yuan. 2008. Expansion and evolution of cell death programmes. Nat. Rev. Mol. Cell Biol. 9:378-390.
    • (2008) Nat. Rev. Mol. Cell Biol. , vol.9 , pp. 378-390
    • Degterev, A.1    Yuan, J.2
  • 18
    • 77951219693 scopus 로고    scopus 로고
    • Nuclear factor kappaB- and specificity protein 1-dependent p53-mediated bi-directional regulation of the human manganese superoxide dismutase gene
    • Dhar, S. K., Y. Xu, and D. K. St. Clair. 2010. Nuclear factor kappaB- and specificity protein 1-dependent p53-mediated bi-directional regulation of the human manganese superoxide dismutase gene. J. Biol. Chem. 285:9835-9846.
    • (2010) J. Biol. Chem. , vol.285 , pp. 9835-9846
    • Dhar, S.K.1    Xu, Y.2    Clair, D.K.St.3
  • 19
    • 0036086130 scopus 로고    scopus 로고
    • Free radicals in the physiological control of cell function
    • Droge, W. 2002. Free radicals in the physiological control of cell function. Physiol. Rev. 82:47-95.
    • (2002) Physiol. Rev. , vol.82 , pp. 47-95
    • Droge, W.1
  • 20
    • 57649167477 scopus 로고    scopus 로고
    • Necroptosis: a specialized pathway of programmed necrosis
    • Galluzzi, L., and G. Kroemer. 2008. Necroptosis: a specialized pathway of programmed necrosis. Cell 135:1161-1163.
    • (2008) Cell , vol.135 , pp. 1161-1163
    • Galluzzi, L.1    Kroemer, G.2
  • 21
    • 54949147176 scopus 로고    scopus 로고
    • New regulators of NF-kappaB in inflammation
    • Ghosh, S., and M. S. Hayden. 2008. New regulators of NF-kappaB in inflammation. Nat. Rev. Immunol. 8:837-848.
    • (2008) Nat. Rev. Immunol. , vol.8 , pp. 837-848
    • Ghosh, S.1    Hayden, M.S.2
  • 22
    • 3442886811 scopus 로고    scopus 로고
    • The pathophysiology of mitochondrial cell death
    • Green, D. R., and G. Kroemer. 2004. The pathophysiology of mitochondrial cell death. Science 305:626-629.
    • (2004) Science , vol.305 , pp. 626-629
    • Green, D.R.1    Kroemer, G.2
  • 23
    • 0033179760 scopus 로고    scopus 로고
    • BCL-2 family members and the mitochondria in apoptosis
    • Gross, A., J. M. McDonnell, and S. J. Korsmeyer. 1999. BCL-2 family members and the mitochondria in apoptosis. Genes Dev. 13:1899-1911.
    • (1999) Genes Dev , vol.13 , pp. 1899-1911
    • Gross, A.1    McDonnell, J.M.2    Korsmeyer, S.J.3
  • 24
    • 33645994183 scopus 로고    scopus 로고
    • Calcium, mitochondria and reperfusion injury: a pore way to die
    • Halestrap, A. P. 2006. Calcium, mitochondria and reperfusion injury: a pore way to die. Biochem. Soc. Trans. 34:232-237.
    • (2006) Biochem. Soc. Trans. , vol.34 , pp. 232-237
    • Halestrap, A.P.1
  • 25
    • 77956186783 scopus 로고    scopus 로고
    • Mitochondrial reactive oxygen species regulate cellular signaling and dictate biological outcomes
    • Hamanaka, R. B., and N. S. Chandel. 2010. Mitochondrial reactive oxygen species regulate cellular signaling and dictate biological outcomes. Trends Biochem. Sci. 35:505-513.
    • (2010) Trends Biochem. Sci. , vol.35 , pp. 505-513
    • Hamanaka, R.B.1    Chandel, N.S.2
  • 26
    • 77955452960 scopus 로고    scopus 로고
    • S-glutathionylation activates STIM1 and alters mitochondrial homeostasis
    • Hawkins, B. J., et al. 2010. S-glutathionylation activates STIM1 and alters mitochondrial homeostasis. J. Cell Biol. 190:391-405.
    • (2010) J. Cell Biol. , vol.190 , pp. 391-405
    • Hawkins, B.J.1
  • 27
    • 35649012722 scopus 로고    scopus 로고
    • 2+-linked mitochondrial reactive oxygen species are essential for endothelial/leukocyte adherence
    • 2+-linked mitochondrial reactive oxygen species are essential for endothelial/leukocyte adherence. Mol. Cell. Biol. 27:7582-7593.
    • (2007) Mol. Cell. Biol. , vol.27 , pp. 7582-7593
    • Hawkins, B.J.1
  • 28
    • 66749183275 scopus 로고    scopus 로고
    • Receptor interacting protein kinase-3 determines cellular necrotic response to TNF-alpha
    • He, S., et al. 2009. Receptor interacting protein kinase-3 determines cellular necrotic response to TNF-alpha. Cell 137:1100-1111.
    • (2009) Cell , vol.137 , pp. 1100-1111
    • He, S.1
  • 29
    • 57649181391 scopus 로고    scopus 로고
    • Identification of a molecular signaling network that regulates a cellular necrotic cell death pathway
    • Hitomi, J., et al. 2008. Identification of a molecular signaling network that regulates a cellular necrotic cell death pathway. Cell 135:1311-1323.
    • (2008) Cell , vol.135 , pp. 1311-1323
    • Hitomi, J.1
  • 30
    • 0030692715 scopus 로고    scopus 로고
    • Tumor necrosis factor alpha and interleukin-1beta regulate the murine manganese superoxide dismutase gene through a complex intronic enhancer involving C/EBP-beta and NF-kappaB
    • Jones, P. L., D. Ping, and J. M. Boss. 1997. Tumor necrosis factor alpha and interleukin-1beta regulate the murine manganese superoxide dismutase gene through a complex intronic enhancer involving C/EBP-beta and NF-kappaB. Mol. Cell. Biol. 17:6970-6981.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 6970-6981
    • Jones, P.L.1    Ping, D.2    Boss, J.M.3
  • 31
    • 25844459154 scopus 로고    scopus 로고
    • NF-kappaB: linking inflammation and immunity to cancer development and progression
    • Karin, M., and F. R. Greten. 2005. NF-kappaB: linking inflammation and immunity to cancer development and progression. Nat. Rev. Immunol. 5:749-759.
    • (2005) Nat. Rev. Immunol. , vol.5 , pp. 749-759
    • Karin, M.1    Greten, F.R.2
  • 32
    • 0032033132 scopus 로고    scopus 로고
    • The death domain kinase RIP mediates the TNF-induced NF-kappaB signal
    • Kelliher, M. A., et al. 1998. The death domain kinase RIP mediates the TNF-induced NF-kappaB signal. Immunity 8:297-303.
    • (1998) Immunity , vol.8 , pp. 297-303
    • Kelliher, M.A.1
  • 33
    • 70449091753 scopus 로고    scopus 로고
    • Stepwise activation of BAX and BAK by tBID, BIM, and PUMA initiates mitochondrial apoptosis
    • Kim, H., et al. 2009. Stepwise activation of BAX and BAK by tBID, BIM, and PUMA initiates mitochondrial apoptosis. Mol. Cell 36:487-499.
    • (2009) Mol. Cell , vol.36 , pp. 487-499
    • Kim, H.1
  • 34
    • 34249820757 scopus 로고    scopus 로고
    • TNF-induced activation of the Nox1 NADPH oxidase and its role in the induction of necrotic cell death
    • Kim, Y. S., M. J. Morgan, S. Choksi, and Z. G. Liu. 2007. TNF-induced activation of the Nox1 NADPH oxidase and its role in the induction of necrotic cell death. Mol. Cell 26:675-687.
    • (2007) Mol. Cell , vol.26 , pp. 675-687
    • Kim, Y.S.1    Morgan, M.J.2    Choksi, S.3    Liu, Z.G.4
  • 35
    • 0036850312 scopus 로고    scopus 로고
    • Bid, Bax, and lipids cooperate to form supramolecular openings in the outer mitochondrial membrane
    • Kuwana, T., et al. 2002. Bid, Bax, and lipids cooperate to form supramolecular openings in the outer mitochondrial membrane. Cell 111:331-342.
    • (2002) Cell , vol.111 , pp. 331-342
    • Kuwana, T.1
  • 36
    • 1542406446 scopus 로고    scopus 로고
    • NOX enzymes and the biology of reactive oxygen
    • Lambeth, J. D. 2004. NOX enzymes and the biology of reactive oxygen. Nat. Rev. Immunol. 4:181-189.
    • (2004) Nat. Rev. Immunol. , vol.4 , pp. 181-189
    • Lambeth, J.D.1
  • 38
    • 0032555697 scopus 로고    scopus 로고
    • Cleavage of BID by caspase 8 mediates the mitochondrial damage in the Fas pathway of apoptosis
    • Li, H., H. Zhu, C. J. Xu, and J. Yuan. 1998. Cleavage of BID by caspase 8 mediates the mitochondrial damage in the Fas pathway of apoptosis. Cell 94:491-501.
    • (1998) Cell , vol.94 , pp. 491-501
    • Li, H.1    Zhu, H.2    Xu, C.J.3    Yuan, J.4
  • 39
    • 1642299768 scopus 로고    scopus 로고
    • Tumor necrosis factor-induced nonapoptotic cell death requires receptor-interacting protein-mediated cellular reactive oxygen species accumulation
    • Lin, Y., et al. 2004. Tumor necrosis factor-induced nonapoptotic cell death requires receptor-interacting protein-mediated cellular reactive oxygen species accumulation. J. Biol. Chem. 279:10822-10828.
    • (2004) J. Biol. Chem. , vol.279 , pp. 10822-10828
    • Lin, Y.1
  • 40
    • 0033214236 scopus 로고    scopus 로고
    • Cleavage of the death domain kinase RIP by caspase-8 prompts TNF-induced apoptosis
    • Lin, Y., A. Devin, Y. Rodriguez, and Z. G. Liu. 1999. Cleavage of the death domain kinase RIP by caspase-8 prompts TNF-induced apoptosis. Genes Dev. 13:2514-2526.
    • (1999) Genes Dev , vol.13 , pp. 2514-2526
    • Lin, Y.1    Devin, A.2    Rodriguez, Y.3    Liu, Z.G.4
  • 41
    • 0034508217 scopus 로고    scopus 로고
    • The combined functions of proapoptotic Bcl-2 family members bak and bax are essential for normal development of multiple tissues
    • Lindsten, T., et al. 2000. The combined functions of proapoptotic Bcl-2 family members bak and bax are essential for normal development of multiple tissues. Mol. Cell 6:1389-1399.
    • (2000) Mol. Cell , vol.6 , pp. 1389-1399
    • Lindsten, T.1
  • 42
    • 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., I. Budihardjo, H. Zou, C. Slaughter, and X. Wang. 1998. Bid, a Bcl2 interacting protein, mediates cytochrome c release from mitochondria in response to activation of cell surface death receptors. Cell 94:481-490.
    • (1998) Cell , vol.94 , pp. 481-490
    • Luo, X.1    Budihardjo, I.2    Zou, H.3    Slaughter, C.4    Wang, X.5
  • 43
    • 0037085380 scopus 로고    scopus 로고
    • Rapid kinetics of tBid-induced cytochrome c and Smac/DIABLO release and mitochondrial depolarization
    • Madesh, M., B. Antonsson, S. M. Srinivasula, E. S. Alnemri, and G. Hajnoczky. 2002. Rapid kinetics of tBid-induced cytochrome c and Smac/DIABLO release and mitochondrial depolarization. J. Biol. Chem. 277:5651-5659.
    • (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
  • 44
    • 0035842896 scopus 로고    scopus 로고
    • VDAC-dependent permeabilization of the outer mitochondrial membrane by superoxide induces rapid and massive cytochrome c release
    • Madesh, M., and G. Hajnoczky. 2001. VDAC-dependent permeabilization of the outer mitochondrial membrane by superoxide induces rapid and massive cytochrome c release. J. Cell Biol. 155:1003-1015.
    • (2001) J. Cell Biol. , vol.155 , pp. 1003-1015
    • Madesh, M.1    Hajnoczky, G.2
  • 45
    • 25444525139 scopus 로고    scopus 로고
    • Selective role for superoxide in InsP3 receptormediated mitochondrial dysfunction and endothelial apoptosis
    • Madesh, M., et al. 2005. Selective role for superoxide in InsP3 receptormediated mitochondrial dysfunction and endothelial apoptosis. J. Cell Biol. 170:1079-1090.
    • (2005) J. Cell Biol. , vol.170 , pp. 1079-1090
    • Madesh, M.1
  • 46
    • 0030971084 scopus 로고    scopus 로고
    • Phospholipase D activity in the intestinal mitochondria: activation by oxygen free radicals
    • Madesh, M., S. A. Ibrahim, and K. A. Balasubramanian. 1997. Phospholipase D activity in the intestinal mitochondria: activation by oxygen free radicals. Free Radic. Biol. Med. 23:271-277.
    • (1997) Free Radic. Biol. Med. , vol.23 , pp. 271-277
    • Madesh, M.1    Ibrahim, S.A.2    Balasubramanian, K.A.3
  • 47
    • 66349101019 scopus 로고    scopus 로고
    • Execution of superoxide-induced cell death by the proapoptotic Bcl-2-related proteins Bid and Bak
    • Madesh, M., et al. 2009. Execution of superoxide-induced cell death by the proapoptotic Bcl-2-related proteins Bid and Bak. Mol. Cell. Biol. 29:3099-3112.
    • (2009) Mol. Cell. Biol. , vol.29 , pp. 3099-3112
    • Madesh, M.1
  • 48
    • 0033634663 scopus 로고    scopus 로고
    • Female mice heterozygous for IKK gamma/NEMO deficiencies develop a dermatopathy similar to the human X-linked disorder incontinentia pigmenti
    • Makris, C., et al. 2000. Female mice heterozygous for IKK gamma/NEMO deficiencies develop a dermatopathy similar to the human X-linked disorder incontinentia pigmenti. Mol. Cell 5:969-979.
    • (2000) Mol. Cell , vol.5 , pp. 969-979
    • Makris, C.1
  • 49
    • 0026012078 scopus 로고
    • Lipopolysaccharide, tumor necrosis factor-alpha, and IL-1 beta prevent programmed cell death (apoptosis) in human peripheral blood monocytes
    • Mangan, D. F., G. R. Welch, and S. M. Wahl. 1991. Lipopolysaccharide, tumor necrosis factor-alpha, and IL-1 beta prevent programmed cell death (apoptosis) in human peripheral blood monocytes. J. Immunol. 146:1541-1546.
    • (1991) J. Immunol. , vol.146 , pp. 1541-1546
    • Mangan, D.F.1    Welch, G.R.2    Wahl, S.M.3
  • 50
    • 14744299357 scopus 로고    scopus 로고
    • The RIP kinases: crucial integrators of cellular stress
    • Meylan, E., and J. Tschopp. 2005. The RIP kinases: crucial integrators of cellular stress. Trends Biochem. Sci. 30:151-159.
    • (2005) Trends Biochem. Sci. , vol.30 , pp. 151-159
    • Meylan, E.1    Tschopp, J.2
  • 51
    • 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., 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 85:817-827.
    • (1996) Cell , vol.85 , pp. 817-827
    • Muzio, M.1
  • 52
    • 15844407874 scopus 로고    scopus 로고
    • Cyclophilin D-dependent mitochondrial permeability transition regulates some necrotic but not apoptotic cell death
    • Nakagawa, T., et al. 2005. Cyclophilin D-dependent mitochondrial permeability transition regulates some necrotic but not apoptotic cell death. Nature 434:652-658.
    • (2005) Nature , vol.434 , pp. 652-658
    • Nakagawa, T.1
  • 53
    • 0037459081 scopus 로고    scopus 로고
    • Mitochondria: releasing power for life and unleashing the machineries of death
    • Newmeyer, D. D., and S. Ferguson-Miller. 2003. Mitochondria: releasing power for life and unleashing the machineries of death. Cell 112:481-490.
    • (2003) Cell , vol.112 , pp. 481-490
    • Newmeyer, D.D.1    Ferguson-Miller, S.2
  • 54
    • 0842304221 scopus 로고    scopus 로고
    • Kinase RIP3 is dispensable for normal NF-kappa Bs, signaling by the B-cell and T-cell receptors, tumor necrosis factor receptor 1, and Toll-like receptors 2 and 4
    • Newton, K., X. Sun, and V. M. Dixit. 2004. Kinase RIP3 is dispensable for normal NF-kappa Bs, signaling by the B-cell and T-cell receptors, tumor necrosis factor receptor 1, and Toll-like receptors 2 and 4. Mol. Cell. Biol. 24:1464-1469.
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 1464-1469
    • Newton, K.1    Sun, X.2    Dixit, V.M.3
  • 55
    • 77954227734 scopus 로고    scopus 로고
    • Bid agonist regulates murine hepatocyte proliferation by controlling endoplasmic reticulum calcium homeostasis
    • Ni, H. M., et al. 2010. Bid agonist regulates murine hepatocyte proliferation by controlling endoplasmic reticulum calcium homeostasis. Hepatology 52: 338-348.
    • (2010) Hepatology , vol.52 , pp. 338-348
    • Ni, H.M.1
  • 57
    • 77955609495 scopus 로고    scopus 로고
    • Fas-associated death domain (FADD) is a negative regulator of T-cell receptor-mediated necroptosis
    • Osborn, S. L., et al. 2010. Fas-associated death domain (FADD) is a negative regulator of T-cell receptor-mediated necroptosis. Proc. Natl. Acad. Sci. U. S. A. 107:13034-13039.
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , pp. 13034-13039
    • Osborn, S.L.1
  • 58
    • 62549155321 scopus 로고    scopus 로고
    • Specific recognition of linear ubiquitin chains by NEMO is important for NF-kappaB activation
    • Rahighi, S., et al. 2009. Specific recognition of linear ubiquitin chains by NEMO is important for NF-kappaB activation. Cell 136:1098-1109.
    • (2009) Cell , vol.136 , pp. 1098-1109
    • Rahighi, S.1
  • 59
    • 24744460273 scopus 로고    scopus 로고
    • Cyclophilin D is a component of mitochondrial permeability transition and mediates neuronal cell death after focal cerebral ischemia
    • Schinzel, A. C., et al. 2005. Cyclophilin D is a component of mitochondrial permeability transition and mediates neuronal cell death after focal cerebral ischemia. Proc. Natl. Acad. Sci. U. S. A. 102:12005-12010.
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 12005-12010
    • Schinzel, A.C.1
  • 60
    • 0037418843 scopus 로고    scopus 로고
    • 2+: a control point for apoptosis
    • 2+: a control point for apoptosis. Science 300:135-139.
    • (2003) Science , vol.300 , pp. 135-139
    • Scorrano, L.1
  • 61
    • 15244341289 scopus 로고    scopus 로고
    • A novel NF-kappaB inhibitor, IMD-0354, suppresses neoplastic proliferation of human mast cells with constitutively activated c-kit receptors
    • Tanaka, A., et al. 2005. A novel NF-kappaB inhibitor, IMD-0354, suppresses neoplastic proliferation of human mast cells with constitutively activated c-kit receptors. Blood 105:2324-2331.
    • (2005) Blood , vol.105 , pp. 2324-2331
    • Tanaka, A.1
  • 62
    • 33644763298 scopus 로고    scopus 로고
    • Inhibition of ADP/ATP exchange in receptor-interacting protein-mediated necrosis
    • Temkin, V., Q. Huang, H. Liu, H. Osada, and R. M. Pope. 2006. Inhibition of ADP/ATP exchange in receptor-interacting protein-mediated necrosis. Mol. Cell. Biol. 26:2215-2225.
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 2215-2225
    • Temkin, V.1    Huang, Q.2    Liu, H.3    Osada, H.4    Pope, R.M.5
  • 66
    • 0032482169 scopus 로고    scopus 로고
    • Inhibition of caspases increases the sensitivity of L929 cells to necrosis mediated by tumor necrosis factor
    • Vercammen, D., et al. 1998. Inhibition of caspases increases the sensitivity of L929 cells to necrosis mediated by tumor necrosis factor. J. Exp. Med. 187:1477-1485.
    • (1998) J. Exp. Med. , vol.187 , pp. 1477-1485
    • Vercammen, D.1
  • 67
    • 0032494143 scopus 로고    scopus 로고
    • Dual signaling of the Fas receptor: initiation of both apoptotic and necrotic cell death pathways
    • Vercammen, D., et al. 1998. Dual signaling of the Fas receptor: initiation of both apoptotic and necrotic cell death pathways. J. Exp. Med. 188:919-930.
    • (1998) J. Exp. Med. , vol.188 , pp. 919-930
    • Vercammen, D.1
  • 68
    • 43049152912 scopus 로고    scopus 로고
    • TNF-alpha induces two distinct caspase-8 activation pathways
    • Wang, L., F. Du, and X. Wang. 2008. TNF-alpha induces two distinct caspase-8 activation pathways. Cell 133:693-703.
    • (2008) Cell , vol.133 , pp. 693-703
    • Wang, L.1    Du, F.2    Wang, X.3
  • 69
    • 0035890085 scopus 로고    scopus 로고
    • The expanding role of mitochondria in apoptosis
    • Wang, X. 2001. The expanding role of mitochondria in apoptosis. Genes Dev. 15:2922-2933.
    • (2001) Genes Dev. , vol.15 , pp. 2922-2933
    • Wang, X.1
  • 70
    • 27144487808 scopus 로고    scopus 로고
    • The endoplasmic reticulum gateway to apoptosis by Bcl-X(L) modulation of the InsP3R
    • White, C., et al. 2005. The endoplasmic reticulum gateway to apoptosis by Bcl-X(L) modulation of the InsP3R. Nat. Cell Biol. 7:1021-1028.
    • (2005) Nat. Cell Biol. , vol.7 , pp. 1021-1028
    • White, C.1
  • 71
    • 37549048249 scopus 로고    scopus 로고
    • The BCL-2 protein family: opposing activities that mediate cell death
    • Youle, R. J., and A. Strasser. 2008. The BCL-2 protein family: opposing activities that mediate cell death. Nat. Rev. Mol. Cell Biol. 9:47-59.
    • (2008) Nat. Rev. Mol. Cell Biol. , vol.9 , pp. 47-59
    • Youle, R.J.1    Strasser, A.2
  • 72
    • 67650812332 scopus 로고    scopus 로고
    • RIP3, an energy metabolism regulator that switches TNF-induced cell death from apoptosis to necrosis
    • Zhang, D. W., et al. 2009. RIP3, an energy metabolism regulator that switches TNF-induced cell death from apoptosis to necrosis. Science 325: 332-336.
    • (2009) Science , vol.325 , pp. 332-336
    • Zhang, D.W.1


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