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Volumn 66, Issue 5, 2009, Pages 814-830

Death effector domain-containing proteins

Author keywords

Apoptosis; Caspase; Death effector domain; FADD; Migration; Proliferation; Signal transduction

Indexed keywords

CASPASE 10; CASPASE 8; DEATH EFFECTOR DOMAIN CONTAINING DNA BINDING PROTEIN; DEATH EFFECTOR DOMAIN CONTAINING DNA BINDING PROTEIN 2; FAS ASSOCIATED DEATH DOMAIN PROTEIN; FLICE INHIBITORY PROTEIN; PHOSPHOPROTEIN; PROTEIN DERIVATIVE; UNCLASSIFIED DRUG; DEATH DOMAIN RECEPTOR SIGNALING ADAPTOR PROTEIN; ISOPROTEIN;

EID: 63049089877     PISSN: 1420682X     EISSN: 15691632     Source Type: Journal    
DOI: 10.1007/s00018-008-8489-0     Document Type: Review
Times cited : (95)

References (165)
  • 2
    • 42449123761 scopus 로고    scopus 로고
    • Expansion and evolution of cell death programmes
    • Degterev A. and Yuan J. (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
  • 3
    • 33344476184 scopus 로고    scopus 로고
    • cFLIP regulation of lymphocyte activation and development
    • Budd R. C., Yeh W. C., and Tschopp J. (2006) cFLIP regulation of lymphocyte activation and development. Nat. Rev. Immunol. 6, 196-204.
    • (2006) Nat. Rev. Immunol , vol.6 , pp. 196-204
    • Budd, R.C.1    Yeh, W.C.2    Tschopp, J.3
  • 4
    • 0033216124 scopus 로고    scopus 로고
    • Knock-out of the neural death effector domain protein PEA-15 demonstrates that its expression protects astrocytes from TNFalpha-induced apoptosis
    • Kitsberg D., Formstecher E., Fauquet M., Kubes M., Cordier J., Canton B., Pan G., Rolli M., Glowinski J., and Chneiweiss H. (1999) Knock-out of the neural death effector domain protein PEA-15 demonstrates that its expression protects astrocytes from TNFalpha-induced apoptosis. J. Neurosci. 19, 8244-8251.
    • (1999) J. Neurosci , vol.19 , pp. 8244-8251
    • Kitsberg, D.1    Formstecher, E.2    Fauquet, M.3    Kubes, M.4    Cordier, J.5    Canton, B.6    Pan, G.7    Rolli, M.8    Glowinski, J.9    Chneiweiss, H.10
  • 6
    • 27544432516 scopus 로고    scopus 로고
    • Nonapoptotic functions of FADD-binding death receptors and their signaling molecules
    • Park S. M., Schickel R., and Peter M. E. (2005) Nonapoptotic functions of FADD-binding death receptors and their signaling molecules. Curr. Opin. Cell Biol. 17, 610-616.
    • (2005) Curr. Opin. Cell Biol , vol.17 , pp. 610-616
    • Park, S.M.1    Schickel, R.2    Peter, M.E.3
  • 10
    • 49649096191 scopus 로고    scopus 로고
    • Caspase-8: Fly or die
    • Frisch S. M. (2008) Caspase-8: fly or die. Cancer Res. 68, 4491 -4493.
    • (2008) Cancer Res , vol.68 , pp. 4491-4493
    • Frisch, S.M.1
  • 11
  • 12
    • 0036187036 scopus 로고    scopus 로고
    • Three-Dimensional Structure of the Apoptosome: Implications for Assembly, Procaspase-9 Binding, and Activation
    • Acehan D., Jiang X., Morgan D. G., Heuser J. E., Wang X., and Akey C. W. (2002) Three-Dimensional Structure of the Apoptosome: Implications for Assembly, Procaspase-9 Binding, and Activation. Molecular Cell 9, 423-432.
    • (2002) Molecular Cell , vol.9 , pp. 423-432
    • Acehan, D.1    Jiang, X.2    Morgan, D.G.3    Heuser, J.E.4    Wang, X.5    Akey, C.W.6
  • 13
    • 0035425256 scopus 로고    scopus 로고
    • The death domain superfamily: A tale of two interfaces?
    • Weber C. H. and Vincenz C. (2001) The death domain superfamily: a tale of two interfaces? Trends in Biochemical Sciences 26, 475-481.
    • (2001) Trends in Biochemical Sciences , vol.26 , pp. 475-481
    • Weber, C.H.1    Vincenz, C.2
  • 15
    • 0035425256 scopus 로고    scopus 로고
    • The death domain superfamily: A tale of two interfaces?
    • Weber C. H. and Vincenz C. (2001) The death domain superfamily: a tale of two interfaces? Trends in Biochemical Sciences, 26, 475-481.
    • (2001) Trends in Biochemical Sciences , vol.26 , pp. 475-481
    • Weber, C.H.1    Vincenz, C.2
  • 16
    • 0033542482 scopus 로고    scopus 로고
    • Structural basis of procaspase-9 recruitment by the apoptotic protease-activat-ing factor 1
    • Qin H., Srinivasula S. M., Wu G., Fernandes-Alnemri T., Alnemri E. S., and Shi Y. (1999) Structural basis of procaspase-9 recruitment by the apoptotic protease-activat-ing factor 1. Nature 399, 549-557.
    • (1999) Nature , vol.399 , pp. 549-557
    • Qin, H.1    Srinivasula, S.M.2    Wu, G.3    Fernandes-Alnemri, T.4    Alnemri, E.S.5    Shi, Y.6
  • 17
    • 0033601077 scopus 로고    scopus 로고
    • Three-Dimensional Structure of a Complex between the Death Domains of Pelle and Tube
    • Xiao T., Towb P., Wasserman S. A., and Sprang S. R. (1999) Three-Dimensional Structure of a Complex between the Death Domains of Pelle and Tube. Cell 99, 545-555.
    • (1999) Cell , vol.99 , pp. 545-555
    • Xiao, T.1    Towb, P.2    Wasserman, S.A.3    Sprang, S.R.4
  • 19
    • 0037063338 scopus 로고    scopus 로고
    • Identification of a basic surface area of the FADD death effector domain critical for apoptotic signaling
    • Kaufmann M., Bozic D., Briand C., Bodmer J. L., Zerbe O., Kohl A., Tschopp J., and Grutter M. G. (2002) Identification of a basic surface area of the FADD death effector domain critical for apoptotic signaling. FEBS Lett. 527, 250-254.
    • (2002) FEBS Lett , vol.527 , pp. 250-254
    • Kaufmann, M.1    Bozic, D.2    Briand, C.3    Bodmer, J.L.4    Zerbe, O.5    Kohl, A.6    Tschopp, J.7    Grutter, M.G.8
  • 21
    • 33646377433 scopus 로고    scopus 로고
    • Crystal structure of a viral FLIP: Insights into FLIP-mediated inhibition of death receptor signaling
    • Li F. Y., Jeffrey P. D., Yu J. W., and Shi Y. (2006) Crystal structure of a viral FLIP: insights into FLIP-mediated inhibition of death receptor signaling. J. Biol. Chem. 281, 2960-2968.
    • (2006) J. Biol. Chem , vol.281 , pp. 2960-2968
    • Li, F.Y.1    Jeffrey, P.D.2    Yu, J.W.3    Shi, Y.4
  • 22
    • 0036139833 scopus 로고    scopus 로고
    • Binding of FADD and caspase-8 to molluscum contagiosum virus MC159 v-FLIP is not sufficient for its antiapoptotic function
    • Garvey T. L., Bertin J., Siegel R. M., Wang G. H., Lenardo M. J., and Cohen J. I. (2002) Binding of FADD and caspase-8 to molluscum contagiosum virus MC159 v-FLIP is not sufficient for its antiapoptotic function. J. Virol. 76, 697-706.
    • (2002) J. Virol , vol.76 , pp. 697-706
    • Garvey, T.L.1    Bertin, J.2    Siegel, R.M.3    Wang, G.H.4    Lenardo, M.J.5    Cohen, J.I.6
  • 23
    • 33744517489 scopus 로고    scopus 로고
    • Homotypic FADD interactions through a conserved RXDLL motif are required for death receptor-induced apoptosis
    • Muppidi J. R., Lobito A. A., Ramaswamy M., Yang J. K., Wang L., Wu H., and Siegel R. M. (2006) Homotypic FADD interactions through a conserved RXDLL motif are required for death receptor-induced apoptosis. Cell Death Differ. 13, 1641-1650.
    • (2006) Cell Death Differ , vol.13 , pp. 1641-1650
    • Muppidi, J.R.1    Lobito, A.A.2    Ramaswamy, M.3    Yang, J.K.4    Wang, L.5    Wu, H.6    Siegel, R.M.7
  • 24
    • 0347723881 scopus 로고    scopus 로고
    • Identification of an expanded binding surface on the FADD death domain responsible for interaction with CD95/Fas
    • Hill J. M., Morisawa G., Kim T., Huang T., Wei Y., Wei Y., and Werner M. H. (2004) Identification of an expanded binding surface on the FADD death domain responsible for interaction with CD95/Fas. J. Biol. Chem. 279, 1474-1481.
    • (2004) J. Biol. Chem , vol.279 , pp. 1474-1481
    • Hill, J.M.1    Morisawa, G.2    Kim, T.3    Huang, T.4    Wei, Y.5    Wei, Y.6    Werner, M.H.7
  • 25
    • 29144463250 scopus 로고    scopus 로고
    • Crystal structure of MC159 reveals molecular mechanism of DISC assembly and FLIP inhibition
    • Yang J. K., Wang L., Zheng L., Wan F., Ahmed M., Lenardo M. J., and Wu H. (2005) Crystal structure of MC159 reveals molecular mechanism of DISC assembly and FLIP inhibition. Mol. Cell 20, 939-949.
    • (2005) Mol. Cell , vol.20 , pp. 939-949
    • Yang, J.K.1    Wang, L.2    Zheng, L.3    Wan, F.4    Ahmed, M.5    Lenardo, M.J.6    Wu, H.7
  • 27
    • 40949149811 scopus 로고    scopus 로고
    • Mutational analyses of c-FLIPR., the only murine short FLIP isoform, reveal requirements for DISC recruitment
    • Ueffing N., Keil E., Freund C., Kuhne R., Schulze-Osthoff K., and Schmitz I. (2008) Mutational analyses of c-FLIPR., the only murine short FLIP isoform, reveal requirements for DISC recruitment. Cell Death Differ. 15,773-782.
    • (2008) Cell Death Differ , vol.15 , pp. 773-782
    • Ueffing, N.1    Keil, E.2    Freund, C.3    Kuhne, R.4    Schulze-Osthoff, K.5    Schmitz, I.6
  • 28
    • 0035895540 scopus 로고    scopus 로고
    • Apoptotic molecular machinery: Vastly increased complexity in vertebrates revealed by genome comparisons
    • Aravind L., Dixit V. M., and Koonin E. V. (2001) Apoptotic molecular machinery: vastly increased complexity in vertebrates revealed by genome comparisons. Science 291, 1279-1284.
    • (2001) Science , vol.291 , pp. 1279-1284
    • Aravind, L.1    Dixit, V.M.2    Koonin, E.V.3
  • 29
    • 0030954209 scopus 로고    scopus 로고
    • The CARD domain: A new apoptotic signalling motif
    • Hofmann K., Bucher P., and Tschopp J. (1997) The CARD domain: a new apoptotic signalling motif. Trends Biochem. Sci. 22, 155-156.
    • (1997) Trends Biochem. Sci , vol.22 , pp. 155-156
    • Hofmann, K.1    Bucher, P.2    Tschopp, J.3
  • 30
    • 10644283823 scopus 로고    scopus 로고
    • Sequence and comparative analysis of the chicken genome provide unique perspectives on vertebrate evolution. Nature 432, 695 -716
    • (2004) Sequence and comparative analysis of the chicken genome provide unique perspectives on vertebrate evolution. Nature 432, 695 -716.
  • 33
    • 0037072933 scopus 로고    scopus 로고
    • Regulation of Fas-associated death domain interactions by the death effector domain identified by a modified reverse two-hybrid screen
    • Thomas L. R., Stillman D. J., and Thorburn A. (2002) Regulation of Fas-associated death domain interactions by the death effector domain identified by a modified reverse two-hybrid screen. J. Biol. Chem. 277, 34343-34348.
    • (2002) J. Biol. Chem , vol.277 , pp. 34343-34348
    • Thomas, L.R.1    Stillman, D.J.2    Thorburn, A.3
  • 35
    • 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-kappaB pathway
    • Chaudhary P. M., Eby M., Jasmin A., Bookwalter A., Murray J., and Hood L. (1997) Death receptor 5, a new member of the TNFR family, and DR4 induce FADD-dependent apoptosis and activate the NF-kappaB pathway. Immunity 7, 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
  • 36
    • 9444268061 scopus 로고    scopus 로고
    • SPOTS: Signaling protein oligomeric transduction structures are early mediators of death receptor-induced apoptosis at the plasma membrane
    • Siegel R. M., Muppidi J. R., Sarker M., Lobito A., Jen M., Martin D., Straus S. E., and Lenardo M. J. (2004) SPOTS: signaling protein oligomeric transduction structures are early mediators of death receptor-induced apoptosis at the plasma membrane. J. Cell Biol. 167, 735-744.
    • (2004) J. Cell Biol , vol.167 , pp. 735-744
    • Siegel, R.M.1    Muppidi, J.R.2    Sarker, M.3    Lobito, A.4    Jen, M.5    Martin, D.6    Straus, S.E.7    Lenardo, M.J.8
  • 38
    • 27744477444 scopus 로고    scopus 로고
    • Mammalian initiator apoptotic caspases
    • Ho P. K. and Hawkins C. J. (2005) Mammalian initiator apoptotic caspases. FEBS J. 272, 5436-5453.
    • (2005) FEBS J , vol.272 , pp. 5436-5453
    • Ho, P.K.1    Hawkins, C.J.2
  • 40
    • 0036510367 scopus 로고    scopus 로고
    • Identification and characterization of DEDD2, a death effector domain-containing protein
    • Roth W., Stenner-Liewen F., Pawlowski K., Godzik A., and Reed J. C. (2002) Identification and characterization of DEDD2, a death effector domain-containing protein. J. Biol. Chem. 277, 7501 -7508.
    • (2002) J. Biol. Chem , vol.277 , pp. 7501-7508
    • Roth, W.1    Stenner-Liewen, F.2    Pawlowski, K.3    Godzik, A.4    Reed, J.C.5
  • 42
    • 0035678257 scopus 로고    scopus 로고
    • Nuclear localization of DEDD leads to caspase-6 activation through its death effector domain and inhibition of RNA polymerase I dependent transcription
    • Schickling O., Stegh A. H., Byrd J., and Peter M. E. (2001) Nuclear localization of DEDD leads to caspase-6 activation through its death effector domain and inhibition of RNA polymerase I dependent transcription. Cell Death Differ. 8, 1157-1168.
    • (2001) Cell Death Differ , vol.8 , pp. 1157-1168
    • Schickling, O.1    Stegh, A.H.2    Byrd, J.3    Peter, M.E.4
  • 43
    • 0035943632 scopus 로고    scopus 로고
    • The death effector domain-associated factor plays distinct regulatory roles in the nucleus and cytoplasm
    • Zheng L., Schickling O., Peter M. E., and Lenardo M. J. (2001) The death effector domain-associated factor plays distinct regulatory roles in the nucleus and cytoplasm. J. Biol. Chem. 276,31945 -31952.
    • (2001) J. Biol. Chem , vol.276 , pp. 31945-31952
    • Zheng, L.1    Schickling, O.2    Peter, M.E.3    Lenardo, M.J.4
  • 45
    • 0037448684 scopus 로고    scopus 로고
    • DEDD and DEDD2 associate with caspase-8/10 and signal cell death
    • Alcivar A., Hu S., Tang J., and Yang X. (2003) DEDD and DEDD2 associate with caspase-8/10 and signal cell death. Oncogene 22, 291 -297.
    • (2003) Oncogene , vol.22 , pp. 291-297
    • Alcivar, A.1    Hu, S.2    Tang, J.3    Yang, X.4
  • 47
    • 0030841911 scopus 로고    scopus 로고
    • I- FLICE., a novel inhibitor of tumor necrosis factor receptor-1- and CD-95-induced apoptosis
    • Hu S., Vincenz C., Ni J., Gentz R., and Dixit V. M. (1997) I- FLICE., a novel inhibitor of tumor necrosis factor receptor-1- and CD-95-induced apoptosis. J. Biol. Chem. 272, 17255-17257.
    • (1997) J. Biol. Chem , vol.272 , pp. 17255-17257
    • Hu, S.1    Vincenz, C.2    Ni, J.3    Gentz, R.4    Dixit, V.M.5
  • 48
    • 0030950228 scopus 로고    scopus 로고
    • A novel family of viral death effector domain-containing molecules that inhibit both CD-95- and tumor necrosis factor receptor-1- induced apoptosis
    • Hu S., Vincenz C., Buller M., and Dixit V. M. (1997) A novel family of viral death effector domain-containing molecules that inhibit both CD-95- and tumor necrosis factor receptor-1- induced apoptosis. J. Biol. Chem. 272, 9621 -9624.
    • (1997) J. Biol. Chem , vol.272 , pp. 9621-9624
    • Hu, S.1    Vincenz, C.2    Buller, M.3    Dixit, V.M.4
  • 51
    • 0037067678 scopus 로고    scopus 로고
    • TRAIL-induced death-inducing signaling complex (DISC) and its modulation by c-FLIP and PED/PEA-15 in glioma cells
    • Xiao C., Yang B. F., Asadi N., Beguinot F., and Hao C. (2002) TRAIL-induced death-inducing signaling complex (DISC) and its modulation by c-FLIP and PED/PEA-15 in glioma cells. J. Biol. Chem. 277, 25020-25025.
    • (2002) J. Biol. Chem , vol.277 , pp. 25020-25025
    • Xiao, C.1    Yang, B.F.2    Asadi, N.3    Beguinot, F.4    Hao, C.5
  • 52
    • 25844522837 scopus 로고    scopus 로고
    • Phosphorylation of PEA-15 switches its binding specificity from ERK/MAPK to FADD
    • Renganathan H., Vaidyanathan H., Knapinska A., and Ramos J. W. (2005) Phosphorylation of PEA-15 switches its binding specificity from ERK/MAPK to FADD. Biochem. J. 390,729-735.
    • (2005) Biochem. J , vol.390 , pp. 729-735
    • Renganathan, H.1    Vaidyanathan, H.2    Knapinska, A.3    Ramos, J.W.4
  • 54
    • 0031819445 scopus 로고    scopus 로고
    • Endothelin induces a calcium-dependent phosphorylation of PEA-15 in intact astrocytes: Identification of Ser104 and Ser116 phosphorylated, respectively, by protein kinase C and calcium/calmodulin kinase II in vitro
    • Kubes M., Cordier J., Glowinski J., Girault J. A., and Chneiweiss H. (1998) Endothelin induces a calcium-dependent phosphorylation of PEA-15 in intact astrocytes: identification of Ser104 and Ser116 phosphorylated, respectively, by protein kinase C and calcium/calmodulin kinase II in vitro. J. Neurochem. 71,1307-1314.
    • (1998) J. Neurochem , vol.71 , pp. 1307-1314
    • Kubes, M.1    Cordier, J.2    Glowinski, J.3    Girault, J.A.4    Chneiweiss, H.5
  • 55
    • 0027460528 scopus 로고
    • Characterization of PEA-15, a major substrate for protein kinase C in astrocytes
    • Araujo H., Danziger N., Cordier J., Glowinski J., and Chneiweiss H. (1993) Characterization of PEA-15, a major substrate for protein kinase C in astrocytes. J. Biol. Chem. 268, 5911 -5920.
    • (1993) J. Biol. Chem , vol.268 , pp. 5911-5920
    • Araujo, H.1    Danziger, N.2    Cordier, J.3    Glowinski, J.4    Chneiweiss, H.5
  • 56
    • 0032101371 scopus 로고    scopus 로고
    • Death-effector filaments: Novel cytoplasmic structures that recruit caspases and trigger apoptosis
    • Siegel R. M., Martin D. A., Zheng L., Ng S. Y., Bertin J., Cohen J., and Lenardo M. J. (1998) Death-effector filaments: novel cytoplasmic structures that recruit caspases and trigger apoptosis. J. Cell Biol. 141, 1243-1253.
    • (1998) J. Cell Biol , vol.141 , pp. 1243-1253
    • Siegel, R.M.1    Martin, D.A.2    Zheng, L.3    Ng, S.Y.4    Bertin, J.5    Cohen, J.6    Lenardo, M.J.7
  • 57
    • 0032472916 scopus 로고    scopus 로고
    • A dominant interfering mutant of FADD/ MORT1 enhances deletion of autoreactive thymocytes and inhibits proliferation of mature T lymphocytes
    • Newton K., Harris A. W., Bath M. L., Smith K. G., and Strasser A. (1998) A dominant interfering mutant of FADD/ MORT1 enhances deletion of autoreactive thymocytes and inhibits proliferation of mature T lymphocytes. EMBO J. 17, 706-718.
    • (1998) EMBO J , vol.17 , pp. 706-718
    • Newton, K.1    Harris, A.W.2    Bath, M.L.3    Smith, K.G.4    Strasser, A.5
  • 59
    • 0035839640 scopus 로고    scopus 로고
    • FADD-deficient T cells exhibit a disaccord in regulation of the cell cycle machinery
    • Zhang J., Kabra N. H., Cado D., Kang C., and Winoto A. (2001) FADD-deficient T cells exhibit a disaccord in regulation of the cell cycle machinery. J. Biol. Chem. 276, 29815-29818.
    • (2001) J. Biol. Chem , vol.276 , pp. 29815-29818
    • Zhang, J.1    Kabra, N.H.2    Cado, D.3    Kang, C.4    Winoto, A.5
  • 60
    • 0040189996 scopus 로고    scopus 로고
    • A dominant negative Fas-associated death domain protein mutant inhibits proliferation and leads to impaired calcium mobilization in both T-cells and fibroblasts
    • Hueber A. O., Zornig M., Bernard A. M., Chautan M., and Evan G. (2000) A dominant negative Fas-associated death domain protein mutant inhibits proliferation and leads to impaired calcium mobilization in both T-cells and fibroblasts. J. Biol. Chem. 275,10453-10462.
    • (2000) J. Biol. Chem , vol.275 , pp. 10453-10462
    • Hueber, A.O.1    Zornig, M.2    Bernard, A.M.3    Chautan, M.4    Evan, G.5
  • 61
    • 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
  • 63
    • 0032505751 scopus 로고    scopus 로고
    • Caspase-3-like activity is necessary for IL-2 release in activated Jurkat T-cells
    • Posmantur R., Wang K. K., and Gilbertsen R. B. (1998) Caspase-3-like activity is necessary for IL-2 release in activated Jurkat T-cells. Exp. Cell Res. 244, 302-309.
    • (1998) Exp. Cell Res , vol.244 , pp. 302-309
    • Posmantur, R.1    Wang, K.K.2    Gilbertsen, R.B.3
  • 64
    • 0033378016 scopus 로고    scopus 로고
    • Early activation of caspases during T lymphocyte stimulation results in selective substrate cleavage in nonapoptotic cells
    • Alam A., Cohen L. Y., Aouad S., and Sekaly R. P. (1999) Early activation of caspases during T lymphocyte stimulation results in selective substrate cleavage in nonapoptotic cells. J. Exp. Med. 190, 1879-1890.
    • (1999) J. Exp. Med , vol.190 , pp. 1879-1890
    • Alam, A.1    Cohen, L.Y.2    Aouad, S.3    Sekaly, R.P.4
  • 67
    • 48349125069 scopus 로고    scopus 로고
    • The paracaspase MALT1 controls caspase-8 activation during lymphocyte proliferation
    • Kawadler H., Gantz M. A., Riley J. L., and Yang X. (2008) The paracaspase MALT1 controls caspase-8 activation during lymphocyte proliferation. Mol. Cell 31, 415-421.
    • (2008) Mol. Cell , vol.31 , pp. 415-421
    • Kawadler, H.1    Gantz, M.A.2    Riley, J.L.3    Yang, X.4
  • 69
    • 17844361968 scopus 로고    scopus 로고
    • Cellular FLIP (long form) regulates CD8+ T cell activation through caspase-8-dependent NF- kappa B activation
    • Dohrman A., Kataoka T., Cuenin S., Russell J. Q., Tschopp J., and Budd R. C. (2005) Cellular FLIP (long form) regulates CD8+ T cell activation through caspase-8-dependent NF- kappa B activation. J. Immunol. 174, 5270-5278.
    • (2005) J. Immunol , vol.174 , pp. 5270-5278
    • Dohrman, A.1    Kataoka, T.2    Cuenin, S.3    Russell, J.Q.4    Tschopp, J.5    Budd, R.C.6
  • 73
    • 0034142374 scopus 로고    scopus 로고
    • Phosphorylation of FADD/MORT1 at serine 194 and association with a 70-kDa cell cycle- regulated protein kinase
    • Scaffidi C., Volkland J., Blomberg I., Hoffmann I., Krammer P. H., and Peter M. E. (2000) Phosphorylation of FADD/MORT1 at serine 194 and association with a 70-kDa cell cycle- regulated protein kinase. J. Immunol. 164,1236-1242.
    • (2000) J. Immunol , vol.164 , pp. 1236-1242
    • Scaffidi, C.1    Volkland, J.2    Blomberg, I.3    Hoffmann, I.4    Krammer, P.H.5    Peter, M.E.6
  • 74
    • 33344457562 scopus 로고    scopus 로고
    • FADD phosphorylation is critical for cell cycle regulation in breast cancer cells
    • Matsuyoshi S., Shimada K., Nakamura M., Ishida E., and Konishi N. (2006) FADD phosphorylation is critical for cell cycle regulation in breast cancer cells. Br. J. Cancer 94, 532-539.
    • (2006) Br. J. Cancer , vol.94 , pp. 532-539
    • Matsuyoshi, S.1    Shimada, K.2    Nakamura, M.3    Ishida, E.4    Konishi, N.5
  • 75
    • 9444233897 scopus 로고    scopus 로고
    • FADD and its phosphorylation
    • Zhang J., Zhang D., and Hua Z. (2004) FADD and its phosphorylation. IUBMB. Life, 56, 395 - 401.
    • (2004) IUBMB. Life , vol.56 , pp. 395-401
    • Zhang, J.1    Zhang, D.2    Hua, Z.3
  • 76
    • 0142211350 scopus 로고    scopus 로고
    • Cell cycle effects by C-FADD depend on its C-terminal phosphorylation site
    • Alappat E. C., Volkland J., and Peter M. E. (2003) Cell cycle effects by C-FADD depend on its C-terminal phosphorylation site. J. Biol. Chem. 278, 41585-41588.
    • (2003) J. Biol. Chem , vol.278 , pp. 41585-41588
    • Alappat, E.C.1    Volkland, J.2    Peter, M.E.3
  • 77
    • 0034675849 scopus 로고    scopus 로고
    • FIST/HIPK3: A Fas/FADD- interacting serine/threonine kinase that induces FADD phosphorylation and inhibits fas-mediated Jun NH(2)-termi- nal kinase activation
    • Rochat-Steiner V., Becker K., Micheau O., Schneider P., Burns K., and Tschopp J. (2000) FIST/HIPK3: a Fas/FADD- interacting serine/threonine kinase that induces FADD phosphorylation and inhibits fas-mediated Jun NH(2)-termi- nal kinase activation. J. Exp. Med. 192,1165-1174.
    • (2000) J. Exp. Med , vol.192 , pp. 1165-1174
    • Rochat-Steiner, V.1    Becker, K.2    Micheau, O.3    Schneider, P.4    Burns, K.5    Tschopp, J.6
  • 79
    • 38349161010 scopus 로고    scopus 로고
    • Two distinctcontrolsofmitotic cdk1/cyclin B1 activity requisite for cell growth prior to cell division
    • and AraiS
    • Miyazaki T. and AraiS. (2007) Two distinctcontrolsofmitotic cdk1/cyclin B1 activity requisite for cell growth prior to cell division. Cell Cycle 6, 1419-1425.
    • (2007) Cell Cycle , vol.6 , pp. 1419-1425
    • Miyazaki, T.1
  • 81
    • 0346220291 scopus 로고    scopus 로고
    • Activation of caspases is required for osteoblastic differentiation
    • Mogi M. and Togari A. (2003) Activation of caspases is required for osteoblastic differentiation. J. Biol. Chem. 278, 47477-47482.
    • (2003) J. Biol. Chem , vol.278 , pp. 47477-47482
    • Mogi, M.1    Togari, A.2
  • 83
    • 0042858127 scopus 로고    scopus 로고
    • RSK2 activity is regulated by its interaction with PEA-15
    • Vaidyanathan H. and Ramos J. W. (2003) RSK2 activity is regulated by its interaction with PEA-15. J. Biol. Chem. 278, 32367-32372.
    • (2003) J. Biol. Chem , vol.278 , pp. 32367-32372
    • Vaidyanathan, H.1    Ramos, J.W.2
  • 84
    • 33748320817 scopus 로고    scopus 로고
    • RSK and MSK in MAP kinase signalling
    • Hauge C. and Frodin M. (2006) RSK and MSK in MAP kinase signalling. J. Cell Sci. 119, 3021-3023.
    • (2006) J. Cell Sci , vol.119 , pp. 3021-3023
    • Hauge, C.1    Frodin, M.2
  • 85
    • 47749089820 scopus 로고    scopus 로고
    • Regulation of TNFR1 and CD95 signalling by receptor compartmentalization
    • Schutze S., Tchikov V., and Schneider-Brachert W. (2008) Regulation of TNFR1 and CD95 signalling by receptor compartmentalization. Nat. Rev Mol. Cell Biol. 9, 655 -662.
    • (2008) Nat. Rev Mol. Cell Biol , vol.9 , pp. 655-662
    • Schutze, S.1    Tchikov, V.2    Schneider-Brachert, W.3
  • 88
    • 0032545497 scopus 로고    scopus 로고
    • The death effector domain of PEA-15 is involved in its regulation of integrin activation
    • Ramos J. W., Kojima T. K., Hughes P. E., Fenczik C. A., and Ginsberg M. H. (1998) The death effector domain of PEA-15 is involved in its regulation of integrin activation. J. Biol. Chem. 273, 33897-33900.
    • (1998) J. Biol. Chem , vol.273 , pp. 33897-33900
    • Ramos, J.W.1    Kojima, T.K.2    Hughes, P.E.3    Fenczik, C.A.4    Ginsberg, M.H.5
  • 89
    • 0030909050 scopus 로고    scopus 로고
    • Suppression of integrin activation: A novel function of a Ras/Raf- initiated MAP kinase pathway
    • Hughes P. E., Renshaw M. W., Pfaff M., Forsyth J., Keivens V. M., Schwartz M. A., and Ginsberg M. H. (1997) Suppression of integrin activation: a novel function of a Ras/Raf- initiated MAP kinase pathway. Cell 88, 521 -530.
    • (1997) Cell , vol.88 , pp. 521-530
    • Hughes, P.E.1    Renshaw, M.W.2    Pfaff, M.3    Forsyth, J.4    Keivens, V.M.5    Schwartz, M.A.6    Ginsberg, M.H.7
  • 90
    • 67349098322 scopus 로고    scopus 로고
    • Renault-Mihara F., Beuvon F., Iturrioz X., Canton B., De B. S., Leonard N., Mouhamad S., Sharif A., Ramos J. W., Junier M. P., and Chneiweiss H. (2006) PEA-15 Expression Inhibits Astrocyte Migration by a PKC Delta-Dependent Mechanism. Mol. Biol. Cell.
    • Renault-Mihara F., Beuvon F., Iturrioz X., Canton B., De B. S., Leonard N., Mouhamad S., Sharif A., Ramos J. W., Junier M. P., and Chneiweiss H. (2006) PEA-15 Expression Inhibits Astrocyte Migration by a PKC Delta-Dependent Mechanism. Mol. Biol. Cell.
  • 91
    • 33847759815 scopus 로고    scopus 로고
    • PEA-15 inhibits tumor cell invasion by binding to extracellular signal-regulated kinase 1/2
    • Glading A., Koziol J. A., Krueger J., and Ginsberg M. H. (2007) PEA-15 inhibits tumor cell invasion by binding to extracellular signal-regulated kinase 1/2. Cancer Res. 67, 1536-1544.
    • (2007) Cancer Res , vol.67 , pp. 1536-1544
    • Glading, A.1    Koziol, J.A.2    Krueger, J.3    Ginsberg, M.H.4
  • 94
    • 33748286819 scopus 로고    scopus 로고
    • Integrin-regulated FAK-Src signaling in normal and cancer cells
    • Mitra S. K. and Schlaepfer D. D. (2006) Integrin-regulated FAK-Src signaling in normal and cancer cells. Curr. Opin. Cell Biol. 18, 516-523.
    • (2006) Curr. Opin. Cell Biol , vol.18 , pp. 516-523
    • Mitra, S.K.1    Schlaepfer, D.D.2
  • 95
    • 37549062115 scopus 로고    scopus 로고
    • Caspase-8 interacts with the p85 subunit of phosphatidylinositol 3-kinase to regulate cell adhesion and motility
    • Senft J., Helfer B., and Frisch S. M. (2007) Caspase-8 interacts with the p85 subunit of phosphatidylinositol 3-kinase to regulate cell adhesion and motility. Cancer Res. 67, 11505-11509.
    • (2007) Cancer Res , vol.67 , pp. 11505-11509
    • Senft, J.1    Helfer, B.2    Frisch, S.M.3
  • 96
    • 45149096045 scopus 로고    scopus 로고
    • Identification of a critical tyrosine residue in caspase 8 that promotes cell migration
    • Barbero S., Barila D., Mielgo A., Stagni V., Clair K., and Stupack D. (2008) Identification of a critical tyrosine residue in caspase 8 that promotes cell migration. J. Biol. Chem. 283, 13031-13034.
    • (2008) J. Biol. Chem , vol.283 , pp. 13031-13034
    • Barbero, S.1    Barila, D.2    Mielgo, A.3    Stagni, V.4    Clair, K.5    Stupack, D.6
  • 97
    • 37549060944 scopus 로고    scopus 로고
    • Novel noncatalytic role for caspase-8 in promoting SRC-mediated adhesion and Erk signaling in neuroblastoma cells
    • Finlay D. and Vuori K. (2007) Novel noncatalytic role for caspase-8 in promoting SRC-mediated adhesion and Erk signaling in neuroblastoma cells. Cancer Res. 67, 11704-11711.
    • (2007) Cancer Res , vol.67 , pp. 11704-11711
    • Finlay, D.1    Vuori, K.2
  • 98
    • 44949199303 scopus 로고    scopus 로고
    • C-FLIP promotes the motility of cancer cells by activating FAK and ERK., and increasing MMP-9 expression
    • Park D., Shim E., Kim Y., Kim Y. M., Lee H., Choe J., Kang D., Lee Y. S., and Jeoung D. (2008) C-FLIP promotes the motility of cancer cells by activating FAK and ERK., and increasing MMP-9 expression. Mol. Cells, 25, 184-195.
    • (2008) Mol. Cells , vol.25 , pp. 184-195
    • Park, D.1    Shim, E.2    Kim, Y.3    Kim, Y.M.4    Lee, H.5    Choe, J.6    Kang, D.7    Lee, Y.S.8    Jeoung, D.9
  • 99
    • 4143108125 scopus 로고    scopus 로고
    • CD95 ligand induces motility and invasiveness of apoptosis-resistant tumor cells
    • Barnhart B. C., Legembre P., Pietras E., Bubici C., Franzoso G., and Peter M. E. (2004) CD95 ligand induces motility and invasiveness of apoptosis-resistant tumor cells. EMBO J. 23, 3175-3185.
    • (2004) EMBO J , vol.23 , pp. 3175-3185
    • Barnhart, B.C.1    Legembre, P.2    Pietras, E.3    Bubici, C.4    Franzoso, G.5    Peter, M.E.6
  • 102
    • 0032143986 scopus 로고    scopus 로고
    • Varfolomeev E. E., Schuchmann M., Luria V., Chiannilkul- chai N., Beckmann J. S., Mett I. L., Rebrikov D., Brodianski V. M., Kemper O. C., Kollet O., Lapidot T., Soffer D., Sobe T., Avraham K. B., Goncharov T., Holtmann H., Lonai P., and WallachD. (1998) Targeted disruption of the mouse Caspase8 gene ablates cell death induction by the TNF receptors, Fas/ Apo1, and DR3 and is lethal prenatally. Immunity 9,267 - 276.
    • Varfolomeev E. E., Schuchmann M., Luria V., Chiannilkul- chai N., Beckmann J. S., Mett I. L., Rebrikov D., Brodianski V. M., Kemper O. C., Kollet O., Lapidot T., Soffer D., Sobe T., Avraham K. B., Goncharov T., Holtmann H., Lonai P., and WallachD. (1998) Targeted disruption of the mouse Caspase8 gene ablates cell death induction by the TNF receptors, Fas/ Apo1, and DR3 and is lethal prenatally. Immunity 9,267 - 276.
  • 103
    • 0034077189 scopus 로고    scopus 로고
    • Roles of caspases in apoptosis, development, and cytokine maturation revealed by homozygous gene deficiencies
    • Wang J. and Lenardo M. J. (2000) Roles of caspases in apoptosis, development, and cytokine maturation revealed by homozygous gene deficiencies. J. Cell Sci. 113 (Pt 5), 753 -757.
    • (2000) J. Cell Sci , vol.113 , Issue.PART 5 , pp. 753-757
    • Wang, J.1    Lenardo, M.J.2
  • 104
    • 0035203050 scopus 로고    scopus 로고
    • Apoptosis by pan- caspase inhibitors in lipopolysaccharide-activated macro-phages
    • Kim S. O., Ono K., and Han J. (2001) Apoptosis by pan- caspase inhibitors in lipopolysaccharide-activated macro-phages. Am. J. Physiol Lung Cell Mol. Physiol 281, L1095- L1105.
    • (2001) Am. J. Physiol Lung Cell Mol. Physiol , vol.281
    • Kim, S.O.1    Ono, K.2    Han, J.3
  • 107
    • 0033103523 scopus 로고    scopus 로고
    • Caspase-8 is required for cell death induced by expanded polyglutamine repeats
    • Sanchez I., Xu C. J., Juo P., Kakizaka A., Blenis J., and Yuan J. (1999) Caspase-8 is required for cell death induced by expanded polyglutamine repeats. Neuron 22, 623-633.
    • (1999) Neuron , vol.22 , pp. 623-633
    • Sanchez, I.1    Xu, C.J.2    Juo, P.3    Kakizaka, A.4    Blenis, J.5    Yuan, J.6
  • 110
    • 42049109891 scopus 로고    scopus 로고
    • Genetic defects of apoptosis and primary immunodeficiency
    • ix
    • Su H. C. and Lenardo M. J. (2008) Genetic defects of apoptosis and primary immunodeficiency. Immunol. Allergy Clin. North Am. 28, 329-51, ix.
    • (2008) Immunol. Allergy Clin. North Am , vol.28 , pp. 329-351
    • Su, H.C.1    Lenardo, M.J.2
  • 111
    • 0033007321 scopus 로고    scopus 로고
    • Mature T lymphocyte apoptosis-immune regulation in a dynamic and unpredictable antigenic environment
    • Lenardo M., Chan K. M., Hornung F., McFarland H., Siegel R., Wang J., and Zheng L. (1999) Mature T lymphocyte apoptosis-immune regulation in a dynamic and unpredictable antigenic environment. Annu. Rev. Immunol. 17, 221 -253.
    • (1999) Annu. Rev. Immunol , vol.17 , pp. 221-253
    • Lenardo, M.1    Chan, K.M.2    Hornung, F.3    McFarland, H.4    Siegel, R.5    Wang, J.6    Zheng, L.7
  • 112
    • 0345059209 scopus 로고    scopus 로고
    • An inherited disorder of lymphocyte apoptosis: The autoimmune lymphoproliferative syndrome
    • Straus S. E., Sneller M., Lenardo M. J., Puck J. M., and Strober W. (1999) An inherited disorder of lymphocyte apoptosis: the autoimmune lymphoproliferative syndrome. Ann. Intern. Med. 130, 591 -601.
    • (1999) Ann. Intern. Med , vol.130 , pp. 591-601
    • Straus, S.E.1    Sneller, M.2    Lenardo, M.J.3    Puck, J.M.4    Strober, W.5
  • 113
    • 0033538475 scopus 로고    scopus 로고
    • Inherited human Caspase 10 mutations underlie defective lymphocyte and dendritic cell apoptosis in autoimmune lymphoproliferative syndrome type II
    • Wang J., Zheng L., Lobito A., Chan F. K., Dale J., Sneller M., Yao X., Puck J. M., Straus S. E., and Lenardo M. J. (1999) Inherited human Caspase 10 mutations underlie defective lymphocyte and dendritic cell apoptosis in autoimmune lymphoproliferative syndrome type II. Cell 98, 47-58.
    • (1999) Cell , vol.98 , pp. 47-58
    • Wang, J.1    Zheng, L.2    Lobito, A.3    Chan, F.K.4    Dale, J.5    Sneller, M.6    Yao, X.7    Puck, J.M.8    Straus, S.E.9    Lenardo, M.J.10
  • 116
    • 0033567436 scopus 로고    scopus 로고
    • Involvement of nitric oxide and biopterin in proinflammatory cytokine-induced apoptotic cell death in mouse osteoblastic cell line MC3T3-E1
    • Mogi M., Kinpara K., Kondo A., and Togari A. (1999) Involvement of nitric oxide and biopterin in proinflammatory cytokine-induced apoptotic cell death in mouse osteoblastic cell line MC3T3-E1. Biochem. Pharmacol. 58, 649-654.
    • (1999) Biochem. Pharmacol , vol.58 , pp. 649-654
    • Mogi, M.1    Kinpara, K.2    Kondo, A.3    Togari, A.4
  • 117
    • 0033278035 scopus 로고    scopus 로고
    • Extracts of Actinobacillus actino- mycetemcomitans induce apoptotic cell death in human osteoblastic MG63 cells
    • Morimoto Y., Morimoto H., Murata T., Kobayashi S., Ohba T., and Haneji T. (1999) Extracts of Actinobacillus actino- mycetemcomitans induce apoptotic cell death in human osteoblastic MG63 cells. J. Dent. Res. 78, 735-742.
    • (1999) J. Dent. Res , vol.78 , pp. 735-742
    • Morimoto, Y.1    Morimoto, H.2    Murata, T.3    Kobayashi, S.4    Ohba, T.5    Haneji, T.6
  • 119
    • 0035871631 scopus 로고    scopus 로고
    • Impaired Fas signaling pathway is involved in defective T cell apoptosis in autoimmune murine arthritis
    • Zhang J., Bardos T., Mikecz K., Finnegan A., and Glant T. T. (2001) Impaired Fas signaling pathway is involved in defective T cell apoptosis in autoimmune murine arthritis. J. Immunol. 166, 4981-4986.
    • (2001) J. Immunol , vol.166 , pp. 4981-4986
    • Zhang, J.1    Bardos, T.2    Mikecz, K.3    Finnegan, A.4    Glant, T.T.5
  • 120
    • 0032528419 scopus 로고    scopus 로고
    • Resistance to apoptosis and elevated expression of Bcl-2 in clonally expanded CD4+
    • Schirmer M., Vallejo A. N., Weyand C. M., and Goronzy J. J. (1998) Resistance to apoptosis and elevated expression of Bcl-2 in clonally expanded CD4+. J. Immunol. 161, 1018-1025.
    • (1998) J. Immunol , vol.161 , pp. 1018-1025
    • Schirmer, M.1    Vallejo, A.N.2    Weyand, C.M.3    Goronzy, J.J.4
  • 121
    • 0029126857 scopus 로고
    • Apoptosis in rheumatoid arthritis synovium
    • Firestein G. S., Yeo M., and Zvaifler N. J. (1995) Apoptosis in rheumatoid arthritis synovium. J. Clin. Invest, 96, 1631 -1638.
    • (1995) J. Clin. Invest , vol.96 , pp. 1631-1638
    • Firestein, G.S.1    Yeo, M.2    Zvaifler, N.J.3
  • 122
    • 0036786268 scopus 로고    scopus 로고
    • Low levels of apoptosis and high FLIP expression in early rheumatoid arthritis synovium
    • Catrina A. I., Ulfgren A. K., Lindblad S., Grondal L., and Klareskog L. (2002) Low levels of apoptosis and high FLIP expression in early rheumatoid arthritis synovium. Ann. Rheum. Dis. 61, 934-936.
    • (2002) Ann. Rheum. Dis , vol.61 , pp. 934-936
    • Catrina, A.I.1    Ulfgren, A.K.2    Lindblad, S.3    Grondal, L.4    Klareskog, L.5
  • 123
    • 4444292431 scopus 로고    scopus 로고
    • Down-regulation of FLIP sensitizes rheumatoid synovial fibroblasts to Fas-mediated apoptosis
    • Palao G., Santiago B., Galindo M., Paya M., Ramirez J. C., and Pablos J. L. (2004) Down-regulation of FLIP sensitizes rheumatoid synovial fibroblasts to Fas-mediated apoptosis. Arthritis Rheum. 50, 2803 - 2810.
    • (2004) Arthritis Rheum , vol.50 , pp. 2803-2810
    • Palao, G.1    Santiago, B.2    Galindo, M.3    Paya, M.4    Ramirez, J.C.5    Pablos, J.L.6
  • 124
    • 33646468506 scopus 로고    scopus 로고
    • Fas activation of a proinflammatory program in rheumatoid synoviocytes and its regulation by FLIP and caspase 8 signaling
    • Palao G., Santiago B., Galindo M. A., Rullas J. N., Alcami J., Ramirez J. C., and Pablos J. L. (2006) Fas activation of a proinflammatory program in rheumatoid synoviocytes and its regulation by FLIP and caspase 8 signaling. Arthritis Rheum. 54, 1473-1481.
    • (2006) Arthritis Rheum , vol.54 , pp. 1473-1481
    • Palao, G.1    Santiago, B.2    Galindo, M.A.3    Rullas, J.N.4    Alcami, J.5    Ramirez, J.C.6    Pablos, J.L.7
  • 125
    • 0030589302 scopus 로고    scopus 로고
    • Genomic structure and mapping of human FADD., an intracellular mediator of lymphocyte apoptosis
    • Kim P. K., Dutra A. S., Chandrasekharappa S. C., and Puck J. M. (1996) Genomic structure and mapping of human FADD., an intracellular mediator of lymphocyte apoptosis. J. Immunol. 157, 5461-5466.
    • (1996) J. Immunol , vol.157 , pp. 5461-5466
    • Kim, P.K.1    Dutra, A.S.2    Chandrasekharappa, S.C.3    Puck, J.M.4
  • 126
    • 0034161282 scopus 로고    scopus 로고
    • FADD/ MORT1 regulates the pre-TCR checkpoint and can function as a tumour suppressor
    • Newton K., Harris A. W., and Strasser A. (2000) FADD/ MORT1 regulates the pre-TCR checkpoint and can function as a tumour suppressor. EMBO J. 19, 931-941.
    • (2000) EMBO J , vol.19 , pp. 931-941
    • Newton, K.1    Harris, A.W.2    Strasser, A.3
  • 128
    • 0037616595 scopus 로고    scopus 로고
    • Loss of FADD protein expression results in a biased Fas-signaling pathway and correlates with the development of tumoral status in thyroid follicular cells
    • Tourneur L., Mistou S., Michiels F. M., Devauchelle V., Renia L., Feunteun J., and Chiocchia G. (2003) Loss of FADD protein expression results in a biased Fas-signaling pathway and correlates with the development of tumoral status in thyroid follicular cells. Oncogene 22, 2795-2804.
    • (2003) Oncogene , vol.22 , pp. 2795-2804
    • Tourneur, L.1    Mistou, S.2    Michiels, F.M.3    Devauchelle, V.4    Renia, L.5    Feunteun, J.6    Chiocchia, G.7
  • 129
    • 0038494553 scopus 로고    scopus 로고
    • Molecular evidence for the nuclear localization of FADD
    • Gomez-Angelats M. and Cidlowski J. A. (2003) Molecular evidence for the nuclear localization of FADD. Cell Death Differ. 10, 791-797.
    • (2003) Cell Death Differ , vol.10 , pp. 791-797
    • Gomez-Angelats, M.1    Cidlowski, J.A.2
  • 130
    • 0037965916 scopus 로고    scopus 로고
    • Fas-associated death domain protein interacts with methyl- CpG binding domain protein 4: A potential link between genome surveillance and apoptosis
    • Screaton R. A., Kiessling S., Sansom O. J., Millar C. B., Maddison K., Bird A., Clarke A. R., and Frisch S. M. (2003) Fas-associated death domain protein interacts with methyl- CpG binding domain protein 4: a potential link between genome surveillance and apoptosis. Proc. Natl. Acad. Sci. USA 100, 5211 -5216.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 5211-5216
    • Screaton, R.A.1    Kiessling, S.2    Sansom, O.J.3    Millar, C.B.4    Maddison, K.5    Bird, A.6    Clarke, A.R.7    Frisch, S.M.8
  • 131
    • 0034704985 scopus 로고    scopus 로고
    • LRDD., a novel leucine rich repeat and death domain containing protein
    • Telliez J. B., Bean K. M., and Lin L. L. (2000) LRDD., a novel leucine rich repeat and death domain containing protein. Biochim. Biophys. Acta 1478, 280-288.
    • (2000) Biochim. Biophys. Acta , vol.1478 , pp. 280-288
    • Telliez, J.B.1    Bean, K.M.2    Lin, L.L.3
  • 132
    • 67349249038 scopus 로고    scopus 로고
    • SheikhM.S. andHuangY. (2003) The FADD is going nuclear. Cell Cycle 2, 346-347.
    • SheikhM.S. andHuangY. (2003) The FADD is going nuclear. Cell Cycle 2, 346-347.
  • 133
    • 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
  • 135
    • 0034662625 scopus 로고    scopus 로고
    • Loss of caspase-8 expression in highly malignant human neuroblas- toma cells correlates with resistance to tumor necrosis factor- related apoptosis-inducing ligand-induced apoptosis
    • Hopkins-Donaldson S., Bodmer J. L., Bourloud K. B., Brognara C. B., Tschopp J., and Gross N. (2000) Loss of caspase-8 expression in highly malignant human neuroblas- toma cells correlates with resistance to tumor necrosis factor- related apoptosis-inducing ligand-induced apoptosis. Cancer Res. 60, 4315-4319.
    • (2000) Cancer Res , vol.60 , pp. 4315-4319
    • Hopkins-Donaldson, S.1    Bodmer, J.L.2    Bourloud, K.B.3    Brognara, C.B.4    Tschopp, J.5    Gross, N.6
  • 138
    • 33749244622 scopus 로고    scopus 로고
    • Targeting caspase 8 to reduce the formation of metastases in neuroblastoma
    • McKee A. E. and Thiele C. J. (2006) Targeting caspase 8 to reduce the formation of metastases in neuroblastoma. Expert. Opin. Ther. Targets. 10, 703-708.
    • (2006) Expert. Opin. Ther. Targets , vol.10 , pp. 703-708
    • McKee, A.E.1    Thiele, C.J.2
  • 139
    • 33745714272 scopus 로고    scopus 로고
    • Does integrin- mediated cell death confer tissue tropism in metastasis?
    • Lahti J. M., Teitz T., and Stupack D. G. (2006) Does integrin- mediated cell death confer tissue tropism in metastasis? Cancer Res. 66, 5981 -5984.
    • (2006) Cancer Res , vol.66 , pp. 5981-5984
    • Lahti, J.M.1    Teitz, T.2    Stupack, D.G.3
  • 142
    • 0037067678 scopus 로고    scopus 로고
    • Tumor necrosis factor-related apoptosis-inducing ligand-in- duced death-inducing signaling complex and its modulation by c-FLIP and PED/PEA-15 in glioma cells
    • Xiao C., Yang B. F., Asadi N., Beguinot F., and Hao C. (2002) Tumor necrosis factor-related apoptosis-inducing ligand-in- duced death-inducing signaling complex and its modulation by c-FLIP and PED/PEA-15 in glioma cells. J. Biol. Chem. 277, 25020-25025.
    • (2002) J. Biol. Chem , vol.277 , pp. 25020-25025
    • Xiao, C.1    Yang, B.F.2    Asadi, N.3    Beguinot, F.4    Hao, C.5
  • 143
    • 0035117038 scopus 로고    scopus 로고
    • Induction and intracellular regulation of tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) mediated apotosis in human malignant glioma cells
    • Hao C., Beguinot F., Condorelli G., Trencia A., Van Meir E. G., Yong V. W., Parney I. F., Roa W. H., and Petruk K. C. (2001) Induction and intracellular regulation of tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) mediated apotosis in human malignant glioma cells. Cancer Res. 61, 1162-1170.
    • (2001) Cancer Res , vol.61 , pp. 1162-1170
    • Hao, C.1    Beguinot, F.2    Condorelli, G.3    Trencia, A.4    Van Meir, E.G.5    Yong, V.W.6    Parney, I.F.7    Roa, W.H.8    Petruk, K.C.9
  • 144
    • 55549124430 scopus 로고    scopus 로고
    • Zanca C., Garofalo M., Quintavalle C., Romano G., Acunzo M., Ragno P., Montuori N., Incoronato M. R., Tornillo L., Baumhoer D., Briguori C., Terracciano L., and Condorelli G. (2008) PED is overexpressed and mediates TRAIL resistance in human non-small cell lung cancer. J. Cell Mol. Med.[Epub ahead of print] doi: 10.1111/j.1582-4934.2008.00283.x.
    • Zanca C., Garofalo M., Quintavalle C., Romano G., Acunzo M., Ragno P., Montuori N., Incoronato M. R., Tornillo L., Baumhoer D., Briguori C., Terracciano L., and Condorelli G. (2008) PED is overexpressed and mediates TRAIL resistance in human non-small cell lung cancer. J. Cell Mol. Med.[Epub ahead of print] doi: 10.1111/j.1582-4934.2008.00283.x.
  • 145
    • 33846968457 scopus 로고    scopus 로고
    • Selective inhibition of PED protein expression sensitizes B-cell chronic lymphocytic leukaemia cells to TRAIL-induced apoptosis
    • Garofalo M., Romano G., Quintavalle C., Romano M. F., Chiurazzi F., Zanca C., and Condorelli G. (2007) Selective inhibition of PED protein expression sensitizes B-cell chronic lymphocytic leukaemia cells to TRAIL-induced apoptosis. Int. J. Cancer 120, 1215-1222.
    • (2007) Int. J. Cancer , vol.120 , pp. 1215-1222
    • Garofalo, M.1    Romano, G.2    Quintavalle, C.3    Romano, M.F.4    Chiurazzi, F.5    Zanca, C.6    Condorelli, G.7
  • 149
    • 30044450499 scopus 로고    scopus 로고
    • Antitumor effect of E1A in ovarian cancer by cytoplasmic sequestration of activated ERK by PEA15
    • Bartholomeusz C., Itamochi H., Nitta M., Saya H., Ginsberg M. H., and Ueno N. T. (2006) Antitumor effect of E1A in ovarian cancer by cytoplasmic sequestration of activated ERK by PEA15. Oncogene 25, 79-90.
    • (2006) Oncogene , vol.25 , pp. 79-90
    • Bartholomeusz, C.1    Itamochi, H.2    Nitta, M.3    Saya, H.4    Ginsberg, M.H.5    Ueno, N.T.6
  • 150
    • 8744314046 scopus 로고    scopus 로고
    • PEA-15 is inhibited by adenovirus E1A and plays a role in ERK nuclear export and Ras-induced senescence
    • Gaumont-Leclerc M. F., Mukhopadhyay U. K., Goumard S., and Ferbeyre G. (2004) PEA-15 is inhibited by adenovirus E1A and plays a role in ERK nuclear export and Ras-induced senescence. J. Biol. Chem. 279, 46802-46809.
    • (2004) J. Biol. Chem , vol.279 , pp. 46802-46809
    • Gaumont-Leclerc, M.F.1    Mukhopadhyay, U.K.2    Goumard, S.3    Ferbeyre, G.4
  • 151
    • 0035970321 scopus 로고    scopus 로고
    • Molluscum contagiosum virus inhibitors of apoptosis: The MC159 v-FLIP protein blocks Fas-induced activation of procaspases and degradation of the related MC160 protein
    • Shisler J. L. and Moss B. (2001) Molluscum contagiosum virus inhibitors of apoptosis: The MC159 v-FLIP protein blocks Fas-induced activation of procaspases and degradation of the related MC160 protein. Virology 282, 14-25.
    • (2001) Virology , vol.282 , pp. 14-25
    • Shisler, J.L.1    Moss, B.2
  • 152
    • 30344457034 scopus 로고    scopus 로고
    • The MC160 protein expressed by the dermatotropic poxvirus molluscum conta- giosum virus prevents tumor necrosis factor alpha-induced NF-kappaB activation via inhibition of I kappa kinase complex formation
    • Nichols D. B. and Shisler J. L. (2006) The MC160 protein expressed by the dermatotropic poxvirus molluscum conta- giosum virus prevents tumor necrosis factor alpha-induced NF-kappaB activation via inhibition of I kappa kinase complex formation. J. Virol. 80, 578-586.
    • (2006) J. Virol , vol.80 , pp. 578-586
    • Nichols, D.B.1    Shisler, J.L.2
  • 153
    • 0033554648 scopus 로고    scopus 로고
    • Modulation of the NF-kappa B pathway by virally 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 virally 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
  • 154
    • 33744531931 scopus 로고    scopus 로고
    • The TRAF3-binding site of human molluscipox virus FLIP molecule MC159 is critical for its capacity to inhibit Fas-induced apoptosis
    • Thurau M., Everett H., Tapernoux M., Tschopp J., and Thome M. (2006) The TRAF3-binding site of human molluscipox virus FLIP molecule MC159 is critical for its capacity to inhibit Fas-induced apoptosis. Cell Death Differ. 13, 1577-1585.
    • (2006) Cell Death Differ , vol.13 , pp. 1577-1585
    • Thurau, M.1    Everett, H.2    Tapernoux, M.3    Tschopp, J.4    Thome, M.5
  • 155
    • 0035127174 scopus 로고    scopus 로고
    • Kaposi's sarcoma-associated herpesvirus: A new DNA tumor virus
    • Boshoff C. and Chang Y. (2001) Kaposi's sarcoma-associated herpesvirus: a new DNA tumor virus. Annu. Rev. Med. 52, 453-470.
    • (2001) Annu. Rev. Med , vol.52 , pp. 453-470
    • Boshoff, C.1    Chang, Y.2
  • 156
    • 0038653408 scopus 로고    scopus 로고
    • Molecular genetics of Kaposi's sarcoma-associated herpesvirus (human herpesvirus-8) epidemiology and pathogenesis
    • table
    • Dourmishev L. A., Dourmishev A. L., Palmeri D., Schwartz R. A., and Lukac D. M. (2003) Molecular genetics of Kaposi's sarcoma-associated herpesvirus (human herpesvirus-8) epidemiology and pathogenesis. Microbiol. Mol. Biol. Rev. 67, 175-212, table.
    • (2003) Microbiol. Mol. Biol. Rev , vol.67 , pp. 175-212
    • Dourmishev, L.A.1    Dourmishev, A.L.2    Palmeri, D.3    Schwartz, R.A.4    Lukac, D.M.5
  • 157
    • 0035234040 scopus 로고    scopus 로고
    • The biology of Kaposi's sarcoma
    • Herndier B. and Ganem D. (2001) The biology of Kaposi's sarcoma. Cancer Treat. Res. 104, 89-126.
    • (2001) Cancer Treat. Res , vol.104 , pp. 89-126
    • Herndier, B.1    Ganem, D.2
  • 158
    • 0033523684 scopus 로고    scopus 로고
    • The inhibitor of death receptor signaling, FLICE-inhibitory protein defines a new class of tumor progression factors
    • Djerbi M., Screpanti V., Catrina A. I., Bogen B., Biberfeld P., and Grandien A. (1999) The inhibitor of death receptor signaling, FLICE-inhibitory protein defines a new class of tumor progression factors. J. Exp. Med. 190,1025-1032.
    • (1999) J. Exp. Med , vol.190 , pp. 1025-1032
    • Djerbi, M.1    Screpanti, V.2    Catrina, A.I.3    Bogen, B.4    Biberfeld, P.5    Grandien, A.6
  • 159
    • 33947114420 scopus 로고    scopus 로고
    • Induction of spindle cell morphology in human vascular endothelial cells by human herpesvirus 8-encoded viral FLICE inhibitory protein K13
    • Matta H., Surabhi R. M., Zhao J., PunjV., Sun Q., Schamus S., Mazzacurati L., and Chaudhary P. M. (2007) Induction of spindle cell morphology in human vascular endothelial cells by human herpesvirus 8-encoded viral FLICE inhibitory protein K13. Oncogene 26,1656-1660.
    • (2007) Oncogene , vol.26 , pp. 1656-1660
    • Matta, H.1    Surabhi, R.M.2    Zhao, J.3    PunjV4    Sun, Q.5    Schamus, S.6    Mazzacurati, L.7    Chaudhary, P.M.8
  • 160
    • 33646579583 scopus 로고    scopus 로고
    • Induction of IL-8 expression by human herpesvirus 8 encoded vFLIP K13 via NF-kappaB activation
    • Sun Q., Matta H., Lu G., and Chaudhary P. M. (2006) Induction of IL-8 expression by human herpesvirus 8 encoded vFLIP K13 via NF-kappaB activation. Oncogene 25, 2717-2726.
    • (2006) Oncogene , vol.25 , pp. 2717-2726
    • Sun, Q.1    Matta, H.2    Lu, G.3    Chaudhary, P.M.4
  • 161
    • 24644491664 scopus 로고    scopus 로고
    • Constitutive NF-kappaB activation, normal Fas-induced apoptosis, and increased incidence of lymphoma in human herpes virus 8 K13 transgenic mice
    • Chugh P., Matta H., Schamus S., Zachariah S., Kumar A., Richardson J. A., Smith A. L., and Chaudhary P. M. (2005) Constitutive NF-kappaB activation, normal Fas-induced apoptosis, and increased incidence of lymphoma in human herpes virus 8 K13 transgenic mice. Proc. Natl. Acad. Sci. USA 102,12885-12890.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 12885-12890
    • Chugh, P.1    Matta, H.2    Schamus, S.3    Zachariah, S.4    Kumar, A.5    Richardson, J.A.6    Smith, A.L.7    Chaudhary, P.M.8
  • 162
    • 18144378467 scopus 로고    scopus 로고
    • Sun Q., Matta H., and Chaudhary P. M. (2005) Kaposi's sarcoma associated herpes virus-encoded viral FLICE inhibitory protein activates transcription from HIV-1 Long Terminal Repeat via the classical NF-kappaB pathway and functionally cooperates with Tat. Retrovirology 2, 9.
    • Sun Q., Matta H., and Chaudhary P. M. (2005) Kaposi's sarcoma associated herpes virus-encoded viral FLICE inhibitory protein activates transcription from HIV-1 Long Terminal Repeat via the classical NF-kappaB pathway and functionally cooperates with Tat. Retrovirology 2, 9.
  • 163
    • 34548364068 scopus 로고    scopus 로고
    • Kaposi's sarcoma-associated herpes- virus (KSHV) oncoprotein K13 bypasses TRAFs and directly interacts with the IkappaB kinase complex to selectively activate NF-kappaB without JNK activation
    • Matta H., Mazzacurati L., Schamus S., Yang T., Sun Q., and Chaudhary P. M. (2007) Kaposi's sarcoma-associated herpes- virus (KSHV) oncoprotein K13 bypasses TRAFs and directly interacts with the IkappaB kinase complex to selectively activate NF-kappaB without JNK activation. J. Biol. Chem. 282, 24858-24865.
    • (2007) J. Biol. Chem , vol.282 , pp. 24858-24865
    • Matta, H.1    Mazzacurati, L.2    Schamus, S.3    Yang, T.4    Sun, Q.5    Chaudhary, P.M.6
  • 164
    • 51349159558 scopus 로고    scopus 로고
    • A nuclear role for Kaposi's sarcoma-associated herpesvirus-encoded K13 protein in gene regulation
    • Matta H., PunjV., Schamus S., Mazzacurati L., Chen A. M., Song R., Yang T., and Chaudhary P. M. (2008) A nuclear role for Kaposi's sarcoma-associated herpesvirus-encoded K13 protein in gene regulation. Oncogene 27, 5243 - 5253.
    • (2008) Oncogene , vol.27 , pp. 5243-5253
    • Matta, H.1    PunjV2    Schamus, S.3    Mazzacurati, L.4    Chen, A.M.5    Song, R.6    Yang, T.7    Chaudhary, P.M.8
  • 165
    • 0037011120 scopus 로고    scopus 로고
    • Recognition of ERK MAP kinase by PEA-15 reveals a common docking site within the death domain and death effector domain
    • Hill J. M., Vaidyanathan H., Ramos J. W., Ginsberg M. H., and Werner M. H. (2002) Recognition of ERK MAP kinase by PEA-15 reveals a common docking site within the death domain and death effector domain. EMBO J. 21, 6494-6504.
    • (2002) EMBO J , vol.21 , pp. 6494-6504
    • Hill, J.M.1    Vaidyanathan, H.2    Ramos, J.W.3    Ginsberg, M.H.4    Werner, M.H.5


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