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Volumn 26, Issue 12, 2005, Pages 2086-2094

A role for caspase-8 and c-FLIPL in proliferation and cell-cycle progression of primary hepatocytes

Author keywords

[No Author keywords available]

Indexed keywords

BENZYLOXYCARBONYLASPARTYLGLUTAMYLVALYLASPARTYL FLUOROMETHYL KETONE; BENZYLOXYCARBONYLISOLEUCYLGLUTAMYLTHREONYLASPARTYL FLUOROMETHYL KETONE; CASPASE 8; EPIDERMAL GROWTH FACTOR; EPIDERMAL GROWTH FACTOR RECEPTOR; FAS ANTIGEN; FAS ASSOCIATED DEATH DOMAIN PROTEIN; FLICE INHIBITORY PROTEIN; MITOGEN ACTIVATED PROTEIN KINASE INHIBITOR; MUTANT PROTEIN; OLIGONUCLEOTIDE; SMALL INTERFERING RNA;

EID: 27944454415     PISSN: 01433334     EISSN: 14602180     Source Type: Journal    
DOI: 10.1093/carcin/bgi187     Document Type: Article
Times cited : (41)

References (60)
  • 1
    • 5044232017 scopus 로고    scopus 로고
    • Liver regeneration: From myth to mechanism
    • Taub,R. (2004) Liver regeneration: From myth to mechanism. Nat. Rev. Mol. Cell. Biol., 5, 836-847.
    • (2004) Nat. Rev. Mol. Cell. Biol. , vol.5 , pp. 836-847
    • Taub, R.1
  • 2
    • 0032795940 scopus 로고    scopus 로고
    • The mitogen-activated protein kinase kinase/extracellular signal-regulated kinase cascade activation is a key signalling pathway involved in the regulation of G(1) phase progression in proliferating hepatocytes
    • Talarmin,H., Rescan,C., Cariou,S., Glaise,D., Zanninelli,G., Bilodeau,M., Loyer,P., Guguen-Guillouzo,C. and Baffet,G. (1999) The mitogen-activated protein kinase kinase/extracellular signal-regulated kinase cascade activation is a key signalling pathway involved in the regulation of G(1) phase progression in proliferating hepatocytes. Mol. Cell. Biol., 19, 6003-6011.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 6003-6011
    • Talarmin, H.1    Rescan, C.2    Cariou, S.3    Glaise, D.4    Zanninelli, G.5    Bilodeau, M.6    Loyer, P.7    Guguen-Guillouzo, C.8    Baffet, G.9
  • 3
    • 0035159826 scopus 로고    scopus 로고
    • Mechanism in the sequential control of cell morphology and S phase entry by epidermal growth factor involves distinct MEK/ERK activations
    • Rescan,C., Coutant,A., Talarmin,H., Theret,N., Glaise,D., Guguen-Guillouzo,C. and Baffet,G. (2001) Mechanism in the sequential control of cell morphology and S phase entry by epidermal growth factor involves distinct MEK/ERK activations. Mol. Biol. Cell, 12, 725-738.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 725-738
    • Rescan, C.1    Coutant, A.2    Talarmin, H.3    Theret, N.4    Glaise, D.5    Guguen-Guillouzo, C.6    Baffet, G.7
  • 5
    • 0036287040 scopus 로고    scopus 로고
    • The EGF/ErbB receptor family and apoptosis
    • Danielsen,A.J. and Maihle,N.J. (2002) The EGF/ErbB receptor family and apoptosis. Growth Factors, 20, 1-15.
    • (2002) Growth Factors , vol.20 , pp. 1-15
    • Danielsen, A.J.1    Maihle, N.J.2
  • 8
    • 1642409200 scopus 로고    scopus 로고
    • CD95-tyrosine nitration inhibits hyperosmotic and CD95 ligand-induced CD95 activation in rat hepatocytes
    • Reinehr,R., Gorg,B., Hongen,A. and Haussinger,D. (2004) CD95-tyrosine nitration inhibits hyperosmotic and CD95 ligand-induced CD95 activation in rat hepatocytes. J. Biol. Chem., 279, 10364-10373.
    • (2004) J. Biol. Chem. , vol.279 , pp. 10364-10373
    • Reinehr, R.1    Gorg, B.2    Hongen, A.3    Haussinger, D.4
  • 9
    • 0037389392 scopus 로고    scopus 로고
    • Hyperosmolarity and CD95L trigger CD95/EGF receptor association and tyrosine phosphorylation of CD95 as prerequisites for CD95 membrane trafficking and DISC formation
    • Reinehr,R., Schliess,F. and Haussinger,D. (2003) Hyperosmolarity and CD95L trigger CD95/EGF receptor association and tyrosine phosphorylation of CD95 as prerequisites for CD95 membrane trafficking and DISC formation. FASEB J., 17, 731-733.
    • (2003) FASEB J. , vol.17 , pp. 731-733
    • Reinehr, R.1    Schliess, F.2    Haussinger, D.3
  • 11
    • 0027444939 scopus 로고
    • Fas/APO-1 expression and function on malignant cells of hematologic and nonhematologic origin
    • Owen-Schaub,L.B., Meterissian,S. and Ford,R.J. (1993) Fas/APO-1 expression and function on malignant cells of hematologic and nonhematologic origin. J. Immunother., 14, 234-241.
    • (1993) J. Immunother. , vol.14 , pp. 234-241
    • Owen-Schaub, L.B.1    Meterissian, S.2    Ford, R.J.3
  • 12
    • 0032546387 scopus 로고    scopus 로고
    • Fas-mediated apoptosis and activation-induced T-cell proliferation are defective in mice lacking FADD/Mort1
    • Zhang,J., Cado,D., Chen,A., Kabra,N.H. and Winoto,A. (1998) Fas-mediated apoptosis and activation-induced T-cell proliferation are defective in mice lacking FADD/Mort1. Nature, 392, 296-300.
    • (1998) Nature , vol.392 , pp. 296-300
    • Zhang, J.1    Cado, D.2    Chen, A.3    Kabra, N.H.4    Winoto, A.5
  • 13
    • 0037397756 scopus 로고    scopus 로고
    • A function of Fas-associated death domain protein in cell cycle progression localized to a single amino acid at its C-terminal region
    • Hua,Z.C., Sohn,S.J., Kang,C., Cado,D. and Winoto,A. (2003) A function of Fas-associated death domain protein in cell cycle progression localized to a single amino acid at its C-terminal region. Immunity, 18, 513-521.
    • (2003) Immunity , vol.18 , pp. 513-521
    • Hua, Z.C.1    Sohn, S.J.2    Kang, C.3    Cado, D.4    Winoto, A.5
  • 14
    • 0028913463 scopus 로고
    • Fas antigen signals proliferation of normal human diploid fibroblast and its mechanism is different from tumor necrosis factor receptor
    • Aggarwal,B.B., Singh,S., LaPushin,R. and Totpal,K. (1995) Fas antigen signals proliferation of normal human diploid fibroblast and its mechanism is different from tumor necrosis factor receptor. FEBS Lett., 364, 5-8.
    • (1995) FEBS Lett. , vol.364 , pp. 5-8
    • Aggarwal, B.B.1    Singh, S.2    LaPushin, R.3    Totpal, K.4
  • 16
    • 0031938485 scopus 로고    scopus 로고
    • Anti-Fas induces apoptosis and proliferation in human dermal fibroblasts: Differences between foreskin and adult fibroblasts
    • Jelaska,A. and Korn,J.H. (1998) Anti-Fas induces apoptosis and proliferation in human dermal fibroblasts: Differences between foreskin and adult fibroblasts. J. Cell Physiol., 175, 19-29.
    • (1998) J. Cell Physiol. , vol.175 , pp. 19-29
    • Jelaska, A.1    Korn, J.H.2
  • 17
    • 0033386808 scopus 로고    scopus 로고
    • Caspase activation is required for T cell proliferation
    • Kennedy,N.J., Kataoka,T., Tschopp,J. and Budd,R.C. (1999) Caspase activation is required for T cell proliferation. J. Exp. Med., 190, 1891-1896.
    • (1999) J. Exp. Med. , vol.190 , pp. 1891-1896
    • Kennedy, N.J.1    Kataoka, T.2    Tschopp, J.3    Budd, R.C.4
  • 18
    • 18544383460 scopus 로고    scopus 로고
    • Pleiotropic defects in lymphocyte activation caused by caspase-8 mutations lead to human immunodeficiency
    • Chun,H.J., Zheng,L., Ahmad,M. et al. (2002) Pleiotropic defects in lymphocyte activation caused by caspase-8 mutations lead to human immunodeficiency. Nature, 419, 395-399.
    • (2002) Nature , vol.419 , pp. 395-399
    • Chun, H.J.1    Zheng, L.2    Ahmad, M.3
  • 19
    • 0037380628 scopus 로고    scopus 로고
    • Essential role for caspase 8 in T-cell homeostasis and T-cell-mediated immunity
    • Salmena,L., Lemmers,B., Hakem,A. et al. (2003) Essential role for caspase 8 in T-cell homeostasis and T-cell-mediated immunity. Genes Dev., 17, 883-895.
    • (2003) Genes Dev. , vol.17 , pp. 883-895
    • Salmena, L.1    Lemmers, B.2    Hakem, A.3
  • 20
    • 0033662341 scopus 로고    scopus 로고
    • Requirement for Casper (c-FLIP) in regulation of death receptor-induced apoptosis and embryonic development
    • Yeh,W.C., Itie,A., Elia,A.J. et al. (2000) Requirement for Casper (c-FLIP) in regulation of death receptor-induced apoptosis and embryonic development. Immunity, 12, 633-642.
    • (2000) Immunity , vol.12 , pp. 633-642
    • Yeh, W.C.1    Itie, A.2    Elia, A.J.3
  • 21
    • 0031726359 scopus 로고    scopus 로고
    • Inhibition of fas death signals by FLIPs
    • Tschopp,J., Irmler,M. and Thome,M. (1998) Inhibition of fas death signals by FLIPs. Curr. Opin. Immunol., 10, 552-558.
    • (1998) Curr. Opin. Immunol. , vol.10 , pp. 552-558
    • Tschopp, J.1    Irmler, M.2    Thome, M.3
  • 25
    • 14644406398 scopus 로고    scopus 로고
    • The flip side of FLIP
    • Peter,M.E. (2004) The flip side of FLIP. Biochem. J., 382, e1-e3.
    • (2004) Biochem. J. , vol.382
    • Peter, M.E.1
  • 26
    • 0037470166 scopus 로고    scopus 로고
    • Calcium/calmodulin-dependent protein kinase II regulation of c-FLIP expression and phosphorylation in modulation of Fas-mediated signaling in malignant glioma cells
    • Yang,B.F., Xiao,C., Roa,W.H., Krammer,P.H. and Hao,C. (2003) Calcium/ calmodulin-dependent protein kinase II regulation of c-FLIP expression and phosphorylation in modulation of Fas-mediated signaling in malignant glioma cells. J. Biol. Chem., 278, 7043-7050.
    • (2003) J. Biol. Chem. , vol.278 , pp. 7043-7050
    • Yang, B.F.1    Xiao, C.2    Roa, W.H.3    Krammer, P.H.4    Hao, C.5
  • 28
    • 0030881603 scopus 로고    scopus 로고
    • Biochemical characteristics of caspases-3, -6, -7, and -8
    • Stennicke,H.R. and Salvesen,G.S. (1997) Biochemical characteristics of caspases-3, -6, -7, and -8. J. Biol. Chem., 272, 25719-25723.
    • (1997) J. Biol. Chem. , vol.272 , pp. 25719-25723
    • Stennicke, H.R.1    Salvesen, G.S.2
  • 29
    • 0035942736 scopus 로고    scopus 로고
    • Duplexes of 21-nucleotide RNAs mediate RNA interference in cultured mammalian cells
    • Elbashir,S.M., Harborth,J., Lendeckel,W., Yalcin,A., Weber,K. and Tuschl,T. (2001) Duplexes of 21-nucleotide RNAs mediate RNA interference in cultured mammalian cells. Nature, 411, 494-498.
    • (2001) Nature , vol.411 , pp. 494-498
    • Elbashir, S.M.1    Harborth, J.2    Lendeckel, W.3    Yalcin, A.4    Weber, K.5    Tuschl, T.6
  • 31
    • 0032539007 scopus 로고    scopus 로고
    • Mitogen-activated protein kinase kinase antagonized fas-associated death domain protein-mediated apoptosis by induced FLICE-inhibitory protein expression
    • Yeh,J.H., Hsu,S.C., Han,S.H. and Lai,M.Z. (1998) Mitogen-activated protein kinase kinase antagonized fas-associated death domain protein-mediated apoptosis by induced FLICE-inhibitory protein expression. J. Exp. Med., 188, 1795-1802.
    • (1998) J. Exp. Med. , vol.188 , pp. 1795-1802
    • Yeh, J.H.1    Hsu, S.C.2    Han, S.H.3    Lai, M.Z.4
  • 32
    • 18744425429 scopus 로고    scopus 로고
    • The caspase-8 inhibitor FLIP promotes activation of NF-kappaB and Erk signaling pathways
    • Kataoka,T., Budd,R.C., Holler,N. et al. (2000) The caspase-8 inhibitor FLIP promotes activation of NF-kappaB and Erk signaling pathways. Curr. Biol., 10, 640-648.
    • (2000) Curr. Biol. , vol.10 , pp. 640-648
    • Kataoka, T.1    Budd, R.C.2    Holler, N.3
  • 33
    • 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. and 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
  • 34
    • 0042809497 scopus 로고    scopus 로고
    • Cellular FLICE/caspase-8-inhibitory protein as a principal regulator of cell death and survival in human hepatocellular carcinoma
    • Okano,H., Shiraki,K., Inoue,H. et al. (2003) Cellular FLICE/ caspase-8-inhibitory protein as a principal regulator of cell death and survival in human hepatocellular carcinoma. Lab. Invest., 83, 1033-1043.
    • (2003) Lab. Invest. , vol.83 , pp. 1033-1043
    • Okano, H.1    Shiraki, K.2    Inoue, H.3
  • 35
    • 0033556310 scopus 로고    scopus 로고
    • The role of c-FLIP in modulation of CD95-induced apoptosis
    • Scaffidi,C., Schmitz,I., Krammer,P.H. and Peter,M.E. (1999) The role of c-FLIP in modulation of CD95-induced apoptosis. J. Biol. Chem., 274, 1541-1548.
    • (1999) J. Biol. Chem. , vol.274 , pp. 1541-1548
    • Scaffidi, C.1    Schmitz, I.2    Krammer, P.H.3    Peter, M.E.4
  • 36
    • 1642386039 scopus 로고    scopus 로고
    • N-terminal fragment of c-FLIP(L) processed by caspase 8 specifically interacts with TRAF2 and induces activation of the NF-kappaB signaling pathway
    • Kataoka,T. and Tschopp,J. (2004) N-terminal fragment of c-FLIP(L) processed by caspase 8 specifically interacts with TRAF2 and induces activation of the NF-kappaB signaling pathway. Mol. Cell. Biol., 24, 2627-36.
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 2627-2636
    • Kataoka, T.1    Tschopp, J.2
  • 37
    • 0038393124 scopus 로고    scopus 로고
    • The death effector domain protein family: Regulators of cellular homeostasis
    • Tibbetts,M.D., Zheng,L. and Lenardo,M.J. (2003) The death effector domain protein family: Regulators of cellular homeostasis. Nat. Immunol., 4, 404-409.
    • (2003) Nat. Immunol. , vol.4 , pp. 404-409
    • Tibbetts, M.D.1    Zheng, L.2    Lenardo, M.J.3
  • 39
    • 0037147199 scopus 로고    scopus 로고
    • Liver protection from apoptosis requires both blockage of initiator caspase activities and inhibition of ASK1/JNK pathway via glutathione S- transferase regulation
    • Gilot,D., Loyer,P., Corlu,A., Glaise,D., Lagadic-Gossmann,D., Atfi,A., Morel,F., Ichijo,H. and Guguen-Guillouzo,C. (2002) Liver protection from apoptosis requires both blockage of initiator caspase activities and inhibition of ASK1/JNK pathway via glutathione S- transferase regulation. J. Biol. Chem., 277, 49220-49229.
    • (2002) J. Biol. Chem. , vol.277 , pp. 49220-49229
    • Gilot, D.1    Loyer, P.2    Corlu, A.3    Glaise, D.4    Lagadic-Gossmann, D.5    Atfi, A.6    Morel, F.7    Ichijo, H.8    Guguen-Guillouzo, C.9
  • 40
    • 0031801785 scopus 로고    scopus 로고
    • Fas-mediated apoptosis in mouse hepatocytes involves the processing and activation of caspases
    • Jones,R.A., Johnson,V.L., Buck,N.R., Dobrota,M., Hinton,R.H., Chow,S.C. and Kass,G.E. (1998) Fas-mediated apoptosis in mouse hepatocytes involves the processing and activation of caspases. Hepatology, 27, 1632-1642.
    • (1998) Hepatology , vol.27 , pp. 1632-1642
    • Jones, R.A.1    Johnson, V.L.2    Buck, N.R.3    Dobrota, M.4    Hinton, R.H.5    Chow, S.C.6    Kass, G.E.7
  • 41
    • 0034674258 scopus 로고    scopus 로고
    • Synergistic induction of apoptosis in murine hepatoma Hepa1-6 cells by IFN-gamma and TNF-alpha
    • Sasagawa,T., Hlaing,M. and Akaike,T. (2000) Synergistic induction of apoptosis in murine hepatoma Hepa1-6 cells by IFN-gamma and TNF-alpha. Biochem. Biophys. Res. Commun., 272, 674-680.
    • (2000) Biochem. Biophys. Res. Commun. , vol.272 , pp. 674-680
    • Sasagawa, T.1    Hlaing, M.2    Akaike, T.3
  • 42
    • 0030961678 scopus 로고    scopus 로고
    • Processing/activation of CPP32-like proteases is involved in transforming growth factor beta1-induced apoptosis in rat hepatocytes
    • Inayat-Hussain,S.H., Couet,C., Cohen,G.M. and Cain,K. (1997) Processing/ activation of CPP32-like proteases is involved in transforming growth factor beta1-induced apoptosis in rat hepatocytes. Hepatology, 25, 1516-1526.
    • (1997) Hepatology , vol.25 , pp. 1516-1526
    • Inayat-Hussain, S.H.1    Couet, C.2    Cohen, G.M.3    Cain, K.4
  • 43
    • 0041828486 scopus 로고    scopus 로고
    • Cellular FLICE-inhibitory protein: An attractive therapeutic target?
    • Micheau,O. (2003) Cellular FLICE-inhibitory protein: An attractive therapeutic target? Expert Opin. Ther. Targets, 7, 559-573.
    • (2003) Expert Opin. Ther. Targets , vol.7 , pp. 559-573
    • Micheau, O.1
  • 44
    • 0033835065 scopus 로고    scopus 로고
    • Fas engagement accelerates liver regeneration after partial hepatectomy
    • Desbarats,J. and Newell,M.K. (2000) Fas engagement accelerates liver regeneration after partial hepatectomy. Nat. Med., 6, 920-923.
    • (2000) Nat. Med. , vol.6 , pp. 920-923
    • Desbarats, J.1    Newell, M.K.2
  • 46
    • 0033606960 scopus 로고    scopus 로고
    • Caspase-induced proteolysis of the cyclin-dependent kinase inhibitor p27Kip1 mediates its anti-apoptotic activity
    • Eymin,B., Sordet,O., Droin,N., Munsch,B., Haugg,M., Van de Craen,M., Vandenabeele,P. and Solary,E. (1999) Caspase-induced proteolysis of the cyclin-dependent kinase inhibitor p27Kip1 mediates its anti-apoptotic activity. Oncogene, 18, 4839-4847.
    • (1999) Oncogene , vol.18 , pp. 4839-4847
    • Eymin, B.1    Sordet, O.2    Droin, N.3    Munsch, B.4    Haugg, M.5    Van de Craen, M.6    Vandenabeele, P.7    Solary, E.8
  • 47
    • 15844384256 scopus 로고    scopus 로고
    • A syndrome of multiorgan hyperplasia with features of gigantism, tumorigenesis, and female sterility in p27(Kip1)-deficient mice
    • Fero,M.L., Rivkin,M., Tasch,M. et al. (1996) A syndrome of multiorgan hyperplasia with features of gigantism, tumorigenesis, and female sterility in p27(Kip1)-deficient mice. Cell, 85, 733-744.
    • (1996) Cell , vol.85 , pp. 733-744
    • Fero, M.L.1    Rivkin, M.2    Tasch, M.3
  • 48
    • 0034742547 scopus 로고    scopus 로고
    • Loss of p27(Kip1) enhances the transplantation efficiency of hepatocytes transferred into diseased livers
    • Karnezis,A.N., Dorokhov,M., Grompe,M. and Zhu,L. (2001) Loss of p27(Kip1) enhances the transplantation efficiency of hepatocytes transferred into diseased livers. J. Clin. Invest., 108, 383-390.
    • (2001) J. Clin. Invest. , vol.108 , pp. 383-390
    • Karnezis, A.N.1    Dorokhov, M.2    Grompe, M.3    Zhu, L.4
  • 49
    • 0030849093 scopus 로고    scopus 로고
    • A combinatorial approach defines specificities of members of the caspase family and granzyme B. Functional relationships established for key mediators of apoptosis
    • Thornberry,N.A., Rano,T.A., Peterson,E.P. et al. (1997) A combinatorial approach defines specificities of members of the caspase family and granzyme B. Functional relationships established for key mediators of apoptosis. J. Biol. Chem., 272, 17907-17911.
    • (1997) J. Biol. Chem. , vol.272 , pp. 17907-17911
    • Thornberry, N.A.1    Rano, T.A.2    Peterson, E.P.3
  • 50
    • 1342314180 scopus 로고    scopus 로고
    • Discovery of novel aspartyl ketone dipeptides as potent and selective caspase-3 inhibitors
    • Han,Y., Giroux,A., Grimm,E.L. et al. (2004) Discovery of novel aspartyl ketone dipeptides as potent and selective caspase-3 inhibitors. Bioorg. Med. Chem. Lett., 14, 805-808.
    • (2004) Bioorg. Med. Chem. Lett. , vol.14 , pp. 805-808
    • Han, Y.1    Giroux, A.2    Grimm, E.L.3
  • 51
    • 0034721669 scopus 로고    scopus 로고
    • Cleavage of cohesin by the CD clan protease separin triggers anaphase in yeast
    • Uhlmann,F., Wernic,D., Poupart,M.A., Koonin,E.V. and Nasmyth,K. (2000) Cleavage of cohesin by the CD clan protease separin triggers anaphase in yeast. Cell, 103, 375-386.
    • (2000) Cell , vol.103 , pp. 375-386
    • Uhlmann, F.1    Wernic, D.2    Poupart, M.A.3    Koonin, E.V.4    Nasmyth, K.5
  • 52
    • 1542390384 scopus 로고    scopus 로고
    • Separase regulation during mitosis
    • Uhlmann,F. (2003) Separase regulation during mitosis. Biochem. Soc. Symp., 243-251.
    • (2003) Biochem. Soc. Symp. , pp. 243-251
    • Uhlmann, F.1
  • 53
    • 0034944380 scopus 로고    scopus 로고
    • Raf-1 promotes cell survival by antagonizing apoptosis signal-regulating kinase 1 through a MEK-ERK independent mechanism
    • Chen,J., Fujii,K., Zhang,L., Roberts,T. and Fu,H. (2001) Raf-1 promotes cell survival by antagonizing apoptosis signal-regulating kinase 1 through a MEK-ERK independent mechanism. Proc. Natl Acad. Sci. USA, 98, 7783-7788.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 7783-7788
    • Chen, J.1    Fujii, K.2    Zhang, L.3    Roberts, T.4    Fu, H.5
  • 54
    • 0037400510 scopus 로고    scopus 로고
    • Mechanisms of regulating the Raf kinase family
    • Chong,H., Vikis,H.G. and Guan,K.L. (2003) Mechanisms of regulating the Raf kinase family. Cell Signal., 15, 463-469.
    • (2003) Cell Signal. , vol.15 , pp. 463-469
    • Chong, H.1    Vikis, H.G.2    Guan, K.L.3
  • 55
    • 0030970013 scopus 로고    scopus 로고
    • Viral FLICE-inhibitory proteins (FLIPs) prevent apoptosis induced by death receptors
    • Thome,M., Schneider,P., Hofmann,K. et al. (1997) Viral FLICE-inhibitory proteins (FLIPs) prevent apoptosis induced by death receptors. Nature, 386, 517-521.
    • (1997) Nature , vol.386 , pp. 517-521
    • Thome, M.1    Schneider, P.2    Hofmann, K.3
  • 56
    • 0030746740 scopus 로고    scopus 로고
    • Casper is a FADD- and caspase-related inducer of apoptosis
    • Shu,H.B., Halpin,D.R. and Goeddel,D.V. (1997) Casper is a FADD- and caspase-related inducer of apoptosis. Immunity, 6, 751-763.
    • (1997) Immunity , vol.6 , pp. 751-763
    • Shu, H.B.1    Halpin, D.R.2    Goeddel, D.V.3
  • 57
    • 0032524908 scopus 로고    scopus 로고
    • RICK, a novel protein kinase containing a caspase recruitment domain, interacts with CLARP and regulates CD95-mediated apoptosis
    • Inohara,N., del Peso,L., Koseki,T., Chen,S. and Nunez,G. (1998) RICK, a novel protein kinase containing a caspase recruitment domain, interacts with CLARP and regulates CD95-mediated apoptosis. J. Biol. Chem., 273, 12296-12300.
    • (1998) J. Biol. Chem. , vol.273 , pp. 12296-12300
    • Inohara, N.1    del Peso, L.2    Koseki, T.3    Chen, S.4    Nunez, G.5
  • 58
    • 27944434557 scopus 로고    scopus 로고
    • cFLIP-L inhibits p38 MAPK activation: An additional anti-apoptotic mechanism in bile acid-mediated apoptosis
    • Grambihler,A., Higuchi,H., Bronk,S.F. and Gores,G.J. (2003) cFLIP-L inhibits p38 MAPK activation: An additional anti-apoptotic mechanism in bile acid-mediated apoptosis. J. Biol. Chem., 12, 12.
    • (2003) J. Biol. Chem. , vol.12 , pp. 12
    • Grambihler, A.1    Higuchi, H.2    Bronk, S.F.3    Gores, G.J.4
  • 59
    • 0033554648 scopus 로고    scopus 로고
    • Modulation of the NF-kappa B pathway by vitally encoded death effector domains-containing proteins
    • Chaudhary,P.M., Jasmin,A., Eby,M.T. and Hood,L. (1999) Modulation of the NF-kappa B pathway by vitally encoded death effector domains-containing proteins. Oncogene, 18, 5738-5746.
    • (1999) Oncogene , vol.18 , pp. 5738-5746
    • Chaudhary, P.M.1    Jasmin, A.2    Eby, M.T.3    Hood, L.4
  • 60
    • 0344321886 scopus 로고    scopus 로고
    • Selective inhibition of FLICE-like inhibitory protein expression with small interfering RNA oligonucleotides is sufficient to sensitize tumor cells for TRAIL-induced apoptosis
    • Siegmund,D., Hadwiger,P., Pfizenmaier,K., Vornlocher,H.P. and Wajant,H. (2002) Selective inhibition of FLICE-like inhibitory protein expression with small interfering RNA oligonucleotides is sufficient to sensitize tumor cells for TRAIL-induced apoptosis. Mol. Med., 8, 725-732.
    • (2002) Mol. Med. , vol.8 , pp. 725-732
    • Siegmund, D.1    Hadwiger, P.2    Pfizenmaier, K.3    Vornlocher, H.P.4    Wajant, H.5


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