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Volumn 89, Issue 6, 2011, Pages 917-926

The involvement of β-actin in the signaling of transmembrane TNF-α-mediated cytotoxicity

Author keywords

Apoptosis; Cytoskeleton; Tnfr; Tnfr2; Tumor

Indexed keywords

BETA ACTIN; CASPASE 8; CYTOCHALASIN D; FLICE INHIBITORY PROTEIN; I KAPPA B; OSTEOCLAST DIFFERENTIATION FACTOR; TUMOR NECROSIS FACTOR ALPHA; TUMOR NECROSIS FACTOR RECEPTOR 2; TUMOR NECROSIS FACTOR RECEPTOR ASSOCIATED FACTOR 2;

EID: 79957837396     PISSN: 07415400     EISSN: None     Source Type: Journal    
DOI: 10.1189/jlb.1209812     Document Type: Article
Times cited : (14)

References (57)
  • 1
    • 0027333425 scopus 로고
    • Tumor necrosis factor, other cytokines and disease
    • Tracey, K. J., Cerami, A. (1993) Tumor necrosis factor, other cytokines and disease. Annu. Rev. Cell Biol. 9, 317-343.
    • (1993) Annu. Rev. Cell Biol , vol.9 , pp. 317-343
    • Tracey, K.J.1    Cerami, A.2
  • 3
    • 0024828372 scopus 로고
    • Evidence for the existence of two forms of membrane tumor necrosis factor: An integral protein and a molecule attached to its receptor
    • Luettig, B., Decker, T., Lohmann-Matthes, M. L. (1989) Evidence for the existence of two forms of membrane tumor necrosis factor: an integral protein and a molecule attached to its receptor. J. Immunol. 143, 4034-4038.
    • (1989) J. Immunol , vol.143 , pp. 4034-4038
    • Luettig, B.1    Decker, T.2    Lohmann-Matthes, M.L.3
  • 4
    • 0027322559 scopus 로고
    • The 26-kD transmembrane form of tumor necrosis factor a on activated CD4+ T cell clones provides a costimulatory signal for human B cell activation
    • Aversa, G., Punnonen, J., de Vries, J. E. (1993) The 26-kD transmembrane form of tumor necrosis factor a on activated CD4+ T cell clones provides a costimulatory signal for human B cell activation. J. Exp. Med. 177, 1575-1585.
    • (1993) J. Exp. Med , vol.177 , pp. 1575-1585
    • Aversa, G.1    Punnonen, J.2    de Vries, J.E.3
  • 5
    • 0031569583 scopus 로고    scopus 로고
    • Contact with T cells modulates monocyte IL-10 production: Role of T cell membrane TNF-α
    • Parry, S. L., Sebbag, M., Feldmann, M., Brennan, F. M. (1997) Contact with T cells modulates monocyte IL-10 production: role of T cell membrane TNF-α. J. Immunol. 158, 3673-3681.
    • (1997) J. Immunol , vol.158 , pp. 3673-3681
    • Parry, S.L.1    Sebbag, M.2    Feldmann, M.3    Brennan, F.M.4
  • 6
    • 0030956179 scopus 로고    scopus 로고
    • Both soluble and membrane-associated TNF activate brain microvascular endothelium: Relevance to multiple sclerosis
    • Burger, D., Lou, J., Dayer, J. M., Grau, G. E. (1997) Both soluble and membrane-associated TNF activate brain microvascular endothelium: relevance to multiple sclerosis. Mol. Psychiatry 2, 113-116.
    • (1997) Mol. Psychiatry , vol.2 , pp. 113-116
    • Burger, D.1    Lou, J.2    Dayer, J.M.3    Grau, G.E.4
  • 7
    • 0024360816 scopus 로고
    • Cell surface tumor necrosis factor (TNF) accounts for monocyte- and lymphocyte-mediated killing of TNF-resistant target cells
    • Peck, R., Brockhaus, M., Frey, J. R. (1989) Cell surface tumor necrosis factor (TNF) accounts for monocyte- and lymphocyte-mediated killing of TNF-resistant target cells. Cell. Immunol. 122, 1-10.
    • (1989) Cell. Immunol , vol.122 , pp. 1-10
    • Peck, R.1    Brockhaus, M.2    Frey, J.R.3
  • 8
    • 0346964820 scopus 로고    scopus 로고
    • Comparison of the cytocidal effect induced by transmembrane and secreted TNF-α
    • Shi, W., Li, Z., Gong, F. (1998) Comparison of the cytocidal effect induced by transmembrane and secreted TNF-α. Chin. J. Microbiol. Immunol. 18, 499 -504.
    • (1998) Chin. J. Microbiol. Immunol , vol.18 , pp. 499-504
    • Shi, W.1    Li, Z.2    Gong, F.3
  • 9
    • 0026751717 scopus 로고
    • The p70 tumor necrosis factor receptor mediates cytotoxicity
    • Heller, R. A., Song, K, Fan, N., Chang, D.J. (1992) The p70 tumor necrosis factor receptor mediates cytotoxicity. Cell 70, 47-56.
    • (1992) Cell , vol.70 , pp. 47-56
    • Heller, R.A.1    Song, K.2    Fan, N.3    Chang, D.J.4
  • 10
    • 0028588613 scopus 로고
    • Mechanisms of tumor necrosis factor cytotoxicity and the cytotoxic signals transduced by the p75-tumor necrosis factor receptor
    • Reid, T., Louie, P., Heller, R A. (1994) Mechanisms of tumor necrosis factor cytotoxicity and the cytotoxic signals transduced by the p75-tumor necrosis factor receptor. Circ. Shock 44, 84-90.
    • (1994) Circ. Shock , vol.44 , pp. 84-90
    • Reid, T.1    Louie, P.2    Heller, R.A.3
  • 12
    • 0035523359 scopus 로고    scopus 로고
    • Actin' up: RhoB in cancer and apoptosis
    • Prendergast, G. C. (2001) Actin' up: RhoB in cancer and apoptosis. Nat. Rev. Cancer 1, 162-168.
    • (2001) Nat. Rev. Cancer , vol.1 , pp. 162-168
    • Prendergast, G.C.1
  • 13
    • 0036165995 scopus 로고    scopus 로고
    • Shear stress and material surface effects on adherent human monocyte apoptosis
    • Shive, M. S., Brodbeck, W. G., Colton, E., Anderson, J. M. (2002) Shear stress and material surface effects on adherent human monocyte apoptosis. J. Biomed. Mater. Res. 60, 148-158.
    • (2002) J. Biomed. Mater. Res , vol.60 , pp. 148-158
    • Shive, M.S.1    Brodbeck, W.G.2    Colton, E.3    Anderson, J.M.4
  • 14
    • 0029610432 scopus 로고
    • Identification of actin as a substrate of ICE and an ICE-like protease and involvement of an ICE-like protease but not ICE in VP-16-induced U937 apoptosis
    • Mashima, T., Naito, M., Fujita, N., Noguchi, K, Tsuruo, T. (1995) Identification of actin as a substrate of ICE and an ICE-like protease and involvement of an ICE-like protease but not ICE in VP-16-induced U937 apoptosis. Biochem. Biophys. Res. Commun. 217, 1185-1192.
    • (1995) Biochem. Biophys. Res. Commun , vol.217 , pp. 1185-1192
    • Mashima, T.1    Naito, M.2    Fujita, N.3    Noguchi, K.4    Tsuruo, T.5
  • 15
    • 1542283580 scopus 로고    scopus 로고
    • Cytoskeletal disruption is the key factor that triggers apoptosis in okadaic acid-treated neuroblastoma cells
    • Cabado, A. G., Leira, F., Vieytes, M. R, Vieites, J. M., Botana, L. M. (2004) Cytoskeletal disruption is the key factor that triggers apoptosis in okadaic acid-treated neuroblastoma cells. Arch. Toxicol. 78, 74-85.
    • (2004) Arch. Toxicol , vol.78 , pp. 74-85
    • Cabado, A.G.1    Leira, F.2    Vieytes, M.R.3    Vieites, J.M.4    Botana, L.M.5
  • 16
    • 0034597013 scopus 로고    scopus 로고
    • CD95 (APO-1/Fas) linkage to the actin cytoskeleton through ezrin in human T lymphocytes: A novel regulatory mechanism of the CD95 apoptotic pathway
    • Parlato, S., Giammarioli, A M., Logozzi, M., Lozupone, F., Matarrese, P., Lu-ciani, F., Falchi, M., Malorni, W., Fais, S. (2000) CD95 (APO-1/Fas) linkage to the actin cytoskeleton through ezrin in human T lymphocytes: a novel regulatory mechanism of the CD95 apoptotic pathway. EMBOJ. 19, 5123-5134.
    • (2000) EMBOJ , vol.19 , pp. 5123-5134
    • Parlato, S.1    Giammarioli, A.M.2    Logozzi, M.3    Lozupone, F.4    Matarrese, P.5    Lu-Ciani, F.6    Falchi, M.7    Malorni, W.8    Fais, S.9
  • 18
    • 0036628903 scopus 로고    scopus 로고
    • Effects of the inhibitors of dynamics of cytoskeletal structures on the development of apoptosis induced by the tumor necrosis factor
    • Domnina, L. V., Ivanova, O. Y., Cherniak, B. V., Skulachev, V. P., Vasiliev, J. M. (2002) Effects of the inhibitors of dynamics of cytoskeletal structures on the development of apoptosis induced by the tumor necrosis factor. Biochemistry (Mosc.) 67, 737-746.
    • (2002) Biochemistry (Mosc.) , vol.67 , pp. 737-746
    • Domnina, L.V.1    Ivanova, O.Y.2    Cherniak, B.V.3    Skulachev, V.P.4    Vasiliev, J.M.5
  • 19
    • 7244242456 scopus 로고    scopus 로고
    • β-Actin is required for mitochondria clustering and ROS generation in TNF-induced, caspase-inde-pendent cell death
    • Li, J., Li, Q., Xie, C, Zhou, H., Wang, Y., Zhang, N., Shao, H., Chan, S. C., Peng, X., Lin, S. C, Han, J. (2004) β-Actin is required for mitochondria clustering and ROS generation in TNF-induced, caspase-inde-pendent cell death. J. Cell Sci. 117, 4673-4680.
    • (2004) J. Cell Sci , vol.117 , pp. 4673-4680
    • Li, J.1    Li, Q.2    Xie, C.3    Zhou, H.4    Wang, Y.5    Zhang, N.6    Shao, H.7    Chan, S.C.8    Peng, X.9    Lin, S.C.10    Han, J.11
  • 20
    • 0026099731 scopus 로고
    • The principal tumor necrosis factor receptor in monocyte cytotoxicity is on the effector cell, not on the target cell
    • Peck, R., Brockhaus, M., Frey, J. R (1991) The principal tumor necrosis factor receptor in monocyte cytotoxicity is on the effector cell, not on the target cell. Cell. Immunol. 132, 308-318.
    • (1991) Cell. Immunol , vol.132 , pp. 308-318
    • Peck, R.1    Brockhaus, M.2    Frey, J.R.3
  • 22
    • 0037186342 scopus 로고    scopus 로고
    • Flow cytometric estimation of the plasma membrane diversity of bone marrow cells in mice treated with WR-2721 and cyclophosphamide
    • Mazur, L., Augustynek, A, Bochenek, M. (2002) Flow cytometric estimation of the plasma membrane diversity of bone marrow cells in mice treated with WR-2721 and cyclophosphamide. Toxicology 171, 63-72.
    • (2002) Toxicology , vol.171 , pp. 63-72
    • Mazur, L.1    Augustynek, A.2    Bochenek, M.3
  • 23
    • 78650204901 scopus 로고    scopus 로고
    • The expression and activity of human soluble TNF receptor I by E. coli and appraisement of its activity
    • Ye, F., Li, Z., Yin, B., Gong, F., Jiang, X., Feng, W., Xu, Y, Xiong, P. (2002) The expression and activity of human soluble TNF receptor I by E. coli and appraisement of its activity. Chin. J. Immunol. 18, 743-746.
    • (2002) Chin. J. Immunol , vol.18 , pp. 743-746
    • Ye, F.1    Li, Z.2    Yin, B.3    Gong, F.4    Jiang, X.5    Feng, W.6    Xu, Y.7    Xiong, P.8
  • 24
    • 79957843718 scopus 로고    scopus 로고
    • Cloning and expression of human soluble tumor necrosis factor receptor II by E. coli and appraisement of its activity
    • Liang, H., Li, Q., Chen, Q., Jiang, X., Feng, W., Li, Z. (2005) Cloning and expression of human soluble tumor necrosis factor receptor II by E. coli and appraisement of its activity. J. Huazhong Univ. Sci. Technolog. Med. Sci. 34, 536-538.
    • (2005) J. Huazhong Univ. Sci. Technolog. Med. Sci , vol.34 , pp. 536-538
    • Liang, H.1    Li, Q.2    Chen, Q.3    Jiang, X.4    Feng, W.5    Li, Z.6
  • 26
    • 0025287304 scopus 로고
    • Actin gene expression in murine eryth-roleukemia cells treated with cytochalasin D
    • Sympson, C. J., Geoghegan, T E. (1990) Actin gene expression in murine eryth-roleukemia cells treated with cytochalasin D. Exp. Cell Res. 189, 28-32.
    • (1990) Exp. Cell Res , vol.189 , pp. 28-32
    • Sympson, C.J.1    Geoghegan, T.E.2
  • 27
    • 24744440776 scopus 로고    scopus 로고
    • Tumor necrosis factor receptor 2 (TNFR2) signaling is negatively regulated by a novel, carboxyl-terminal TNFR-associated factor 2 (TRAF2)-binding site
    • Grech, A. P., Gardam, S., Chan, T., Quinn, R, Gonzales, R, Basten, A, Brink, R (2005) Tumor necrosis factor receptor 2 (TNFR2) signaling is negatively regulated by a novel, carboxyl-terminal TNFR-associated factor 2 (TRAF2)-binding site. J. Biol. Chem. 280, 31572-31581.
    • (2005) J. Biol. Chem , vol.280 , pp. 31572-31581
    • Grech, A.P.1    Gardam, S.2    Chan, T.3    Quinn, R.4    Gonzales, R.5    Basten, A.6    Brink, R.7
  • 28
    • 0033725155 scopus 로고    scopus 로고
    • The distinct roles of TRAF2 and RIP in IKK activation by TNF-R1: TRAF2 recruits IKK to TNF-R1 while RIP mediates IKK activation
    • Devin, A, Cook, A, Lin, Y, Rodriguez, Y, Kelliher, M., Liu, Z. (2000) The distinct roles of TRAF2 and RIP in IKK activation by TNF-R1: TRAF2 recruits IKK to TNF-R1 while RIP mediates IKK activation. Immunity 12, 419-429.
    • (2000) Immunity , vol.12 , pp. 419-429
    • Devin, A.1    Cook, A.2    Lin, Y.3    Rodriguez, Y.4    Kelliher, M.5    Liu, Z.6
  • 29
    • 0029786304 scopus 로고    scopus 로고
    • Anatomy of TRAF2. Distinct domains for nuclear factor-KB activation and association with tumor necrosis factor signaling proteins
    • Takeuchi, M., Rothe, M., Goeddel, D. V. (1996) Anatomy of TRAF2. Distinct domains for nuclear factor-KB activation and association with tumor necrosis factor signaling proteins. J. Biol. Chem. 271, 19935-19942.
    • (1996) J. Biol. Chem , vol.271 , pp. 19935-19942
    • Takeuchi, M.1    Rothe, M.2    Goeddel, D.V.3
  • 30
    • 0035021123 scopus 로고    scopus 로고
    • The a and β subunits of IkB 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. (2001) The a and β subunits of IkB kinase (IKK) mediate TRAF2-dependent IKK recruitment to tumor necrosis factor (TNF) receptor 1 in response to TNF. Mol. Cell. Biol. 21, 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.6
  • 31
    • 0033864476 scopus 로고    scopus 로고
    • Multiple regulation of constitutive and induced interleukin 8 secretion in human myelomono-cytic cell lines
    • Steube, K. G., Meyer, C, Drexler, H. G. (2000) Multiple regulation of constitutive and induced interleukin 8 secretion in human myelomono-cytic cell lines. Cytokine 12, 1236-1239.
    • (2000) Cytokine , vol.12 , pp. 1236-1239
    • Steube, K.G.1    Meyer, C.2    Drexler, H.G.3
  • 32
    • 0033214236 scopus 로고    scopus 로고
    • Cleavage of the death domain kinase RIP by caspase-8 prompts TNF-induced apoptosis
    • Lin, Y, Devin, A., Rodriguez, Y, Liu, Z. G. (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
  • 33
    • 0029812554 scopus 로고    scopus 로고
    • Effect of tumor necrosis factor a on rabbit corneal endothelial permeability
    • Watsky, M. A, Guan, Z., Ragsdale, D. N. (1996) Effect of tumor necrosis factor a on rabbit corneal endothelial permeability. Invest. Ophthalmol. Vis. Sci. 37, 1924-1929.
    • (1996) Invest. Ophthalmol. Vis. Sci , vol.37 , pp. 1924-1929
    • Watsky, M.A.1    Guan, Z.2    Ragsdale, D.N.3
  • 36
    • 0348049699 scopus 로고    scopus 로고
    • Podocyte cytoskeleton is connected to the integral membrane protein podocalyxin through Na+/H+-exchanger regulatory factor 2 and ezrin
    • Takeda, T. (2003) Podocyte cytoskeleton is connected to the integral membrane protein podocalyxin through Na+/H+-exchanger regulatory factor 2 and ezrin. Clin. Exp. Nephrol. 7, 260-269.
    • (2003) Clin. Exp. Nephrol , vol.7 , pp. 260-269
    • Takeda, T.1
  • 37
    • 33748068089 scopus 로고    scopus 로고
    • New concepts regarding focal adhesion kinase promotion of cell migration and proliferation
    • Cox, B. D., Natarajan, M., Stettner, M. R, Gladson, C. L. (2006) New concepts regarding focal adhesion kinase promotion of cell migration and proliferation. J. Cell. Biochem. 99, 35-52.
    • (2006) J. Cell. Biochem , vol.99 , pp. 35-52
    • Cox, B.D.1    Natarajan, M.2    Stettner, M.R.3    Gladson, C.L.4
  • 38
    • 34147096542 scopus 로고    scopus 로고
    • Essential role of the TNF-TNFR2 cognate interaction in mouse dendritic cell-natural killer cell crosstalk
    • Xu, J., Chakrabarti, A. K, Tan, J. L., Ge, L., Gambotto, A, Vujanovic, N. L. (2007) Essential role of the TNF-TNFR2 cognate interaction in mouse dendritic cell-natural killer cell crosstalk. Blood 109, 3333-3341.
    • (2007) Blood , vol.109 , pp. 3333-3341
    • Xu, J.1    Chakrabarti, A.K.2    Tan, J.L.3    Ge, L.4    Gambotto, A.5    Vujanovic, N.L.6
  • 39
    • 79957849384 scopus 로고    scopus 로고
    • A comparison between the effects of transmembrane and secretory tumor necrosis factor-a on tumor necrosis factor receptors
    • Shi, W., Li, Z., Gong, F. (1998) A comparison between the effects of transmembrane and secretory tumor necrosis factor-a on tumor necrosis factor receptors. Chin. J. Immunol. 14, 243-246.
    • (1998) Chin. J. Immunol , vol.14 , pp. 243-246
    • Shi, W.1    Li, Z.2    Gong, F.3
  • 40
    • 0033538073 scopus 로고    scopus 로고
    • Inhibition of receptor internalization by monodansylcadaverine selectively blocks p55 tumor necrosis factor receptor death domain signaling
    • Schutze, S., Machleidt, T., Adam, D., Schwandner, R, Wiegmann, K, Kruse, M. L., Heinrich, M., Wickel, M., Kronke, M. (1999) Inhibition of receptor internalization by monodansylcadaverine selectively blocks p55 tumor necrosis factor receptor death domain signaling. J. Biol. Chem. 274, 10203-10212.
    • (1999) J. Biol. Chem , vol.274 , pp. 10203-10212
    • Schutze, S.1    Machleidt, T.2    Adam, D.3    Schwandner, R.4    Wiegmann, K.5    Kruse, M.L.6    Heinrich, M.7    Wickel, M.8    Kronke, M.9
  • 41
    • 0028124428 scopus 로고
    • A novel family of putative signal transducers associated with the cytoplasmic domain of the 75 kDa tumor necrosis factor receptor
    • Rothe, M., Wong, S. C, Henzel, W. J., Goeddel, D. V. (1994) A novel family of putative signal transducers associated with the cytoplasmic domain of the 75 kDa tumor necrosis factor receptor. Cell 78, 681-692.
    • (1994) Cell , vol.78 , pp. 681-692
    • Rothe, M.1    Wong, S.C.2    Henzel, W.J.3    Goeddel, D.V.4
  • 42
    • 0033452005 scopus 로고    scopus 로고
    • Regulated commitment of TNF receptor signaling: A molecular switch for death or activation
    • Pimentel-Muiños, F. X., Seed, B. (1999) Regulated commitment of TNF receptor signaling: a molecular switch for death or activation. Immunity 11, 783-793.
    • (1999) Immunity , vol.11 , pp. 783-793
    • Pimentel-Muiños, F.X.1    Seed, B.2
  • 43
    • 50849093241 scopus 로고    scopus 로고
    • Transmembrane TNF-α mediates forward and reverse signaling, inducing cell death or survival via the NF-kB pathway in Raji Burkitt lymphoma cells
    • Zhang, H., Yan, D., Shi, X., Liang, H., Pang, Y, Qin, N., Chen, H., Wang, J., Yin, B., Jiang, X., Feng, W., Zhang, W., Zhou, M., Li, Z. (2008) Transmembrane TNF-α mediates forward and reverse signaling, inducing cell death or survival via the NF-kB pathway in Raji Burkitt lymphoma cells. J. Leukoc. Biol. 84, 789-797.
    • (2008) J. Leukoc. Biol , vol.84 , pp. 789-797
    • Zhang, H.1    Yan, D.2    Shi, X.3    Liang, H.4    Pang, Y.5    Qin, N.6    Chen, H.7    Wang, J.8    Yin, B.9    Jiang, X.10    Feng, W.11    Zhang, W.12    Zhou, M.13    Li, Z.14
  • 44
    • 0030271387 scopus 로고    scopus 로고
    • NF-k B: Ten years after
    • Baeuerle, P. A, Baltimore, D. (1996) NF-k B: ten years after. Cell 87, 13-20.
    • (1996) Cell , vol.87 , pp. 13-20
    • Baeuerle, P.A.1    Baltimore, D.2
  • 45
    • 0029874138 scopus 로고    scopus 로고
    • The NF-k B and IkB proteins: New discoveries and insights
    • Baldwin Jr., A. S. (1996) The NF-k B and IkB proteins: new discoveries and insights. Annu. Rev. Immunol. 14, 649-683.
    • (1996) Annu. Rev. Immunol , vol.14 , pp. 649-683
    • Baldwin, A.S.1
  • 46
    • 0033625022 scopus 로고    scopus 로고
    • Involvement of NF-kB in the protection of cell death by tumor necrosis factor in L929 derived TNF resistant C12 cells
    • Kitahara, J., Sakamoto, H., Tsujimoto, M., Nakagawa, Y (2000) Involvement of NF-kB in the protection of cell death by tumor necrosis factor in L929 derived TNF resistant C12 cells. Biol. Pharm. Bull. 23, 397-401.
    • (2000) Biol. Pharm. Bull , vol.23 , pp. 397-401
    • Kitahara, J.1    Sakamoto, H.2    Tsujimoto, M.3    Nakagawa, Y.4
  • 47
    • 54249085295 scopus 로고    scopus 로고
    • Actin cytoskeleton differentially modulates NF-KB-mediated IL-8 expression in myelomonocytic cells
    • Kustermans, G, El Mjiyad, N, Horion, J., Jacobs, N, Piette, J., Legrand-Poels, S. (2008) Actin cytoskeleton differentially modulates NF-KB-mediated IL-8 expression in myelomonocytic cells. Biochem. Pharmacol 76, 1214-1228.
    • (2008) Biochem. Pharmacol , vol.76 , pp. 1214-1228
    • Kustermans, G.1    El-Mjiyad, N.2    Horion, J.3    Jacobs, N.4    Piette, J.5    Legrand-Poels, S.6
  • 48
    • 1542283796 scopus 로고    scopus 로고
    • Tumor necrosis factor-a promotes survival of opossum kidney cells via Cdc42-induced phospholipase C-71 activation and actin filament redistribution
    • Papakonstanti, E. A, Stournaras, C. (2004) Tumor necrosis factor-a promotes survival of opossum kidney cells via Cdc42-induced phospholipase C-71 activation and actin filament redistribution. Mol. Biol. Cell 15, 1273-1286.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 1273-1286
    • Papakonstanti, E.A.1    Stournaras, C.2
  • 49
    • 0028978626 scopus 로고
    • TRAF2-mediated activation of NF-k B by TNF receptor 2 and CD40
    • Rothe, M., Sarma, V., Dixit, V. M., Goeddel, D. V. (1995) TRAF2-mediated activation of NF-k B by TNF receptor 2 and CD40. Science 269, 1424-1427.
    • (1995) Science , vol.269 , pp. 1424-1427
    • Rothe, M.1    Sarma, V.2    Dixit, V.M.3    Goeddel, D.V.4
  • 50
    • 0033563101 scopus 로고    scopus 로고
    • Signaling by proinflammatory cytokines: Oligomerization of TRAF2 and TRAF6 is sufficient for JNK and IKK activation and target gene induction via an amino-terminal effector domain
    • Baud, V., Liu, Z. G., Bennett, B., Suzuki, N., Xia, Y, Karin, M. (1999) Signaling by proinflammatory cytokines: oligomerization of TRAF2 and TRAF6 is sufficient for JNK and IKK activation and target gene induction via an amino-terminal effector domain. Genes Dev. 13, 1297-1308.
    • (1999) Genes Dev , vol.13 , pp. 1297-1308
    • Baud, V.1    Liu, Z.G.2    Bennett, B.3    Suzuki, N.4    Xia, Y.5    Karin, M.6
  • 51
    • 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. (1996) TNF-dependent recruitment of the protein kinase RIP to the TNF receptor-1 signaling complex. Immunity 4, 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
  • 52
  • 53
    • 4043136609 scopus 로고    scopus 로고
    • The kinase activity of Rip1 is not required for tumor necrosis factor-a-induced IkB kinase or p38 MAP kinase activation or for the ubiquitination of Rip1 by Traf2
    • Lee, T. H., Shank, J., Cusson, N., Kelliher, M. A. (2004) The kinase activity of Rip1 is not required for tumor necrosis factor-a-induced IkB kinase or p38 MAP kinase activation or for the ubiquitination of Rip1 by Traf2. J. Biol. Chem. 279, 33185-33191.
    • (2004) J. Biol. Chem , vol.279 , pp. 33185-33191
    • Lee, T.H.1    Shank, J.2    Cusson, N.3    Kelliher, M.A.4
  • 54
    • 33744951304 scopus 로고    scopus 로고
    • Ubiquitination of RIP is required for tumor necrosis factor a-induced NF-kB activation
    • Li, H., Kobayashi, M., Blonska, M., You, Y, Lin, X. (2006) Ubiquitination of RIP is required for tumor necrosis factor a-induced NF-kB activation. J. Biol. Chem. 281, 13636-13643.
    • (2006) J. Biol. Chem , vol.281 , pp. 13636-13643
    • Li, H.1    Kobayashi, M.2    Blonska, M.3    You, Y.4    Lin, X.5
  • 55
    • 0035930905 scopus 로고    scopus 로고
    • Alternative splicing variants of c-FLIP transduce the differential signal through the Raf or TRAF2 in TNF-induced cell proliferation
    • Park, S. J., Kim, Y Y, Ju, J. W., Han, B. G., Park, S. I., Park, B. J. (2001) Alternative splicing variants of c-FLIP transduce the differential signal through the Raf or TRAF2 in TNF-induced cell proliferation. Biochem. Biophys. Res. Commun. 289, 1205-1210.
    • (2001) Biochem. Biophys. Res. Commun , vol.289 , pp. 1205-1210
    • Park, S.J.1    Kim, Y.Y.2    Ju, J.W.3    Han, B.G.4    Park, S.I.5    Park, B.J.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.