메뉴 건너뛰기




Volumn 17, Issue 6, 2005, Pages 610-616

Nonapoptotic functions of FADD-binding death receptors and their signaling molecules

Author keywords

[No Author keywords available]

Indexed keywords

ADAPTOR PROTEIN; CASPASE 8; DEATH RECEPTOR; DEATH RECEPTOR 3; DEATH RECEPTOR 4; DEATH RECEPTOR 5; FAS ANTIGEN; FAS ASSOCIATED DEATH DOMAIN PROTEIN; FAS LIGAND; FLICE INHIBITORY PROTEIN; GAMMA INTERFERON; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; MITOGEN ACTIVATED PROTEIN KINASE; PROTEIN SERINE THREONINE KINASE; T LYMPHOCYTE RECEPTOR; TUMOR NECROSIS FACTOR RECEPTOR 1; TUMOR NECROSIS FACTOR RECEPTOR ASSOCIATED FACTOR 2; UNCLASSIFIED DRUG; UROKINASE;

EID: 27544432516     PISSN: 09550674     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ceb.2005.09.010     Document Type: Review
Times cited : (118)

References (72)
  • 1
    • 17944371991 scopus 로고    scopus 로고
    • The intriguing biology of the tumour necrosis factor/tumour necrosis factor receptor superfamily: Players, rules and the games
    • T. Hehlgans, and K. Pfeffer The intriguing biology of the tumour necrosis factor/tumour necrosis factor receptor superfamily: players, rules and the games Immunology 115 2005 1 20
    • (2005) Immunology , vol.115 , pp. 1-20
    • Hehlgans, T.1    Pfeffer, K.2
  • 5
    • 0037276437 scopus 로고    scopus 로고
    • The CD95(APO-1/Fas) DISC and beyond
    • M.E. Peter, and P.H. Krammer The CD95(APO-1/Fas) DISC and beyond Cell Death Differ 10 2003 26 35
    • (2003) Cell Death Differ , vol.10 , pp. 26-35
    • Peter, M.E.1    Krammer, P.H.2
  • 9
    • 0033835065 scopus 로고    scopus 로고
    • Fas engagement accelerates liver regeneration after partial hepatectomy
    • J. Desbarats, and M.K. Newell Fas engagement accelerates liver regeneration after partial hepatectomy Nat Med 6 2000 920 923
    • (2000) Nat Med , vol.6 , pp. 920-923
    • Desbarats, J.1    Newell, M.K.2
  • 10
    • 0037321075 scopus 로고    scopus 로고
    • Fas engagement induces neurite growth through ERK activation and p35 upregulation
    • J. Desbarats, R.B. Birge, M. Mimouni-Rongy, D.E. Weinstein, J.S. Palerme, and M.K. Newell Fas engagement induces neurite growth through ERK activation and p35 upregulation Nat Cell Biol 5 2003 118 125 Stimulation of CD95 induces neurite outgrowth in sensory neurons through activation of ERK. Injection of anti-CD95 antibodies accelerates functional recovery after sciatic nerve injury in mice.
    • (2003) Nat Cell Biol , vol.5 , pp. 118-125
    • Desbarats, J.1    Birge, R.B.2    Mimouni-Rongy, M.3    Weinstein, D.E.4    Palerme, J.S.5    Newell, M.K.6
  • 11
    • 0036377840 scopus 로고    scopus 로고
    • The biological role of the Fas/FasL system during tumor formation and progression
    • E. Reichmann The biological role of the Fas/FasL system during tumor formation and progression Semin Cancer Biol 12 2002 309 315
    • (2002) Semin Cancer Biol , vol.12 , pp. 309-315
    • Reichmann, E.1
  • 12
    • 8744297444 scopus 로고    scopus 로고
    • Fas ligand induces cell-autonomous NF-κB activation and interleukin-8 production by a mechanism distinct from that of tumor necrosis factor-α
    • R. Imamura, K. Konaka, N. Matsumoto, M. Hasegawa, M. Fukui, N. Mukaida, T. Kinoshita, and T. Suda Fas ligand induces cell-autonomous NF-κB activation and interleukin-8 production by a mechanism distinct from that of tumor necrosis factor-α J Biol Chem 279 2004 46415 46423
    • (2004) J Biol Chem , vol.279 , pp. 46415-46423
    • Imamura, R.1    Konaka, K.2    Matsumoto, N.3    Hasegawa, M.4    Fukui, M.5    Mukaida, N.6    Kinoshita, T.7    Suda, T.8
  • 13
    • 0030296281 scopus 로고    scopus 로고
    • Fas-mediated stimulation induces IL-8 secretion by rheumatoid arthritis synoviocytes independently of CPP32-mediated apoptosis
    • C. Sekine, H. Yagita, T. Kobata, T. Hasunuma, K. Nishioka, and K. Okumura Fas-mediated stimulation induces IL-8 secretion by rheumatoid arthritis synoviocytes independently of CPP32-mediated apoptosis Biochem Biophys Res Commun 228 1996 14 20
    • (1996) Biochem Biophys Res Commun , vol.228 , pp. 14-20
    • Sekine, C.1    Yagita, H.2    Kobata, T.3    Hasunuma, T.4    Nishioka, K.5    Okumura, K.6
  • 16
    • 0028913463 scopus 로고
    • Fas antigen signals proliferation of normal human diploid fibroblast and its mechanism is different from tumor necrosis factor receptor
    • B.B. Aggarwal, S. Singh, R. LaPushin, and K. Totpal Fas antigen signals proliferation of normal human diploid fibroblast and its mechanism is different from tumor necrosis factor receptor FEBS Lett 364 1995 5 8
    • (1995) FEBS Lett , vol.364 , pp. 5-8
    • Aggarwal, B.B.1    Singh, S.2    Lapushin, R.3    Totpal, K.4
  • 17
    • 0027444939 scopus 로고
    • Fas/APO-1 expression and function on malignant cells of hematologic and nonhematologic origin
    • L.B. Owen-Schaub, S. Meterissian, and R.J. Ford Fas/APO-1 expression and function on malignant cells of hematologic and nonhematologic origin J Immunother 14 1993 234 241
    • (1993) J Immunother , vol.14 , pp. 234-241
    • Owen-Schaub, L.B.1    Meterissian, S.2    Ford, R.J.3
  • 18
    • 0034653734 scopus 로고    scopus 로고
    • Fas drives cell cycle progression in glioma cells via extracellular signal-regulated kinase activation
    • H. Shinohara, H. Yagita, Y. Ikawa, and N. Oyaizu Fas drives cell cycle progression in glioma cells via extracellular signal-regulated kinase activation Cancer Res 60 2000 1766 1772
    • (2000) Cancer Res , vol.60 , pp. 1766-1772
    • Shinohara, H.1    Yagita, H.2    Ikawa, Y.3    Oyaizu, N.4
  • 19
    • 0032757670 scopus 로고    scopus 로고
    • Apoptosis, proliferation and NF-κB activation induced by agonistic Fas antibodies in the human myeloma cell line OH-2: Amplification of Fas-mediated apoptosis by tumor necrosis factor
    • M. Borset, H. Hjorth-Hansen, A.C. Johnsen, C. Seidel, A. Waage, T. Espevik, and A. Sundan Apoptosis, proliferation and NF-κB activation induced by agonistic Fas antibodies in the human myeloma cell line OH-2: amplification of Fas-mediated apoptosis by tumor necrosis factor Eur J Haematol 63 1999 345 353
    • (1999) Eur J Haematol , vol.63 , pp. 345-353
    • Borset, M.1    Hjorth-Hansen, H.2    Johnsen, A.C.3    Seidel, C.4    Waage, A.5    Espevik, T.6    Sundan, A.7
  • 20
    • 3342927147 scopus 로고    scopus 로고
    • Signaling through death receptors in cancer therapy
    • S. Fulda, and K.M. Debatin Signaling through death receptors in cancer therapy Curr Opin Pharmacol 4 2004 327 332
    • (2004) Curr Opin Pharmacol , vol.4 , pp. 327-332
    • Fulda, S.1    Debatin, K.M.2
  • 21
    • 0034026719 scopus 로고    scopus 로고
    • Steering anti-cancer drugs away from the TRAIL
    • S. Nagata Steering anti-cancer drugs away from the TRAIL Nat Med 6 2000 502 503
    • (2000) Nat Med , vol.6 , pp. 502-503
    • Nagata, S.1
  • 22
    • 4143108125 scopus 로고    scopus 로고
    • CD95 ligand induces motility and invasiveness of apoptosis-resistant tumor cells
    • B.C. Barnhart, P. Legembre, E. Pietras, C. Bubici, G. Franzoso, and M.E. Peter CD95 ligand induces motility and invasiveness of apoptosis-resistant tumor cells EMBO J 23 2004 3175 3185 Stimulation of CD95 in a large number of CD95-apoptosis-resistant human tumor cell lines results in increased in vitro motility and invasiveness. CD95 stimulation causes activation of multiple non-apoptotic signaling pathways, including a pathway in which activated NF-κB causes upregulation of urokinase plasminogen activator, which contributes to the motility and invasiveness response.
    • (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
  • 23
    • 0038374723 scopus 로고    scopus 로고
    • Lack of FasL-mediated killing leads to in vivo tumor promotion in mouse Lewis lung cancer
    • J.K. Lee, T.J. Sayers, T.C. Back, J.M. Wigginton, and R.H. Wiltrout Lack of FasL-mediated killing leads to in vivo tumor promotion in mouse Lewis lung cancer Apoptosis 8 2003 151 160 Overexpression of CD95 in the CD95-apoptosis-resistant mouse Lewis lung carcinoma cell line 3LL renders the cells sensitive to CD95-mediated apoptosis in vitro. However, in vivo cells expressing CD95 grow faster as solid tumors when compared to control transfectants. In certain tumor cells CD95 can act as tumor promotor. Stimulation by endogenous CD95 ligand and the presence of a functional intracellular domain in CD95 are required for its tumor promoting activity.
    • (2003) Apoptosis , vol.8 , pp. 151-160
    • Lee, J.K.1    Sayers, T.J.2    Back, T.C.3    Wigginton, J.M.4    Wiltrout, R.H.5
  • 25
    • 8744315928 scopus 로고    scopus 로고
    • Identification of SNF1/AMP kinase-related kinase as an NF-κB-regulated anti-apoptotic kinase involved in CD95-induced motility and invasiveness
    • P. Legembre, R. Schickel, B.C. Barnhart, and M.E. Peter Identification of SNF1/AMP kinase-related kinase as an NF-κB-regulated anti-apoptotic kinase involved in CD95-induced motility and invasiveness J Biol Chem 279 2004 46742 46747
    • (2004) J Biol Chem , vol.279 , pp. 46742-46747
    • Legembre, P.1    Schickel, R.2    Barnhart, B.C.3    Peter, M.E.4
  • 26
    • 0031042972 scopus 로고    scopus 로고
    • Antitumor effect of locally produced CD95 ligand
    • K. Seino, N. Kayagaki, K. Okumura, and H. Yagita Antitumor effect of locally produced CD95 ligand Nat Med 3 1997 165 170
    • (1997) Nat Med , vol.3 , pp. 165-170
    • Seino, K.1    Kayagaki, N.2    Okumura, K.3    Yagita, H.4
  • 27
    • 0030842535 scopus 로고    scopus 로고
    • Fas ligand expression in islets of Langerhans does not confer immune privilege and instead targets them for rapid destruction
    • S.M. Kang, D.B. Schneider, Z. Lin, D. Hanahan, D.A. Dichek, P.G. Stock, and S. Baekkeskov Fas ligand expression in islets of Langerhans does not confer immune privilege and instead targets them for rapid destruction Nat Med 3 1997 738 743
    • (1997) Nat Med , vol.3 , pp. 738-743
    • Kang, S.M.1    Schneider, D.B.2    Lin, Z.3    Hanahan, D.4    Dichek, D.A.5    Stock, P.G.6    Baekkeskov, S.7
  • 28
    • 0031730436 scopus 로고    scopus 로고
    • Caspase 1-independent IL-1β release and inflammation induced by the apoptosis inducer Fas ligand
    • K. Miwa, M. Asano, R. Horai, Y. Iwakura, S. Nagata, and T. Suda Caspase 1-independent IL-1β release and inflammation induced by the apoptosis inducer Fas ligand Nat Med 4 1998 1287 1292
    • (1998) Nat Med , vol.4 , pp. 1287-1292
    • Miwa, K.1    Asano, M.2    Horai, R.3    Iwakura, Y.4    Nagata, S.5    Suda, T.6
  • 29
    • 0038618996 scopus 로고    scopus 로고
    • Fas (CD95) induces proinflammatory cytokine responses by human monocytes and monocyte-derived macrophages
    • D.R. Park, A.R. Thomsen, C.W. Frevert, U. Pham, S.J. Skerrett, P.A. Kiener, and W.C. Liles Fas (CD95) induces proinflammatory cytokine responses by human monocytes and monocyte-derived macrophages J Immunol 170 2003 6209 6216
    • (2003) J Immunol , vol.170 , pp. 6209-6216
    • Park, D.R.1    Thomsen, A.R.2    Frevert, C.W.3    Pham, U.4    Skerrett, S.J.5    Kiener, P.A.6    Liles, W.C.7
  • 30
    • 0035861624 scopus 로고    scopus 로고
    • Non-apoptotic signaling pathways activated by soluble Fas ligand in serum-starved human fibroblasts. Mitogen-activated protein kinases and NF-κB-dependent gene expression
    • J.H. Ahn, S.M. Park, H.S. Cho, M.S. Lee, J.B. Yoon, J. Vilcek, and T.H. Lee Non-apoptotic signaling pathways activated by soluble Fas ligand in serum-starved human fibroblasts. Mitogen-activated protein kinases and NF-κB-dependent gene expression J Biol Chem 276 2001 47100 47106
    • (2001) J Biol Chem , vol.276 , pp. 47100-47106
    • Ahn, J.H.1    Park, S.M.2    Cho, H.S.3    Lee, M.S.4    Yoon, J.B.5    Vilcek, J.6    Lee, T.H.7
  • 32
    • 0038320035 scopus 로고    scopus 로고
    • Apo2L/TRAIL: Apoptosis signaling, biology, and potential for cancer therapy
    • A. Almasan, and A. Ashkenazi Apo2L/TRAIL: apoptosis signaling, biology, and potential for cancer therapy Cytokine Growth Factor Rev 14 2003 337 348
    • (2003) Cytokine Growth Factor Rev , vol.14 , pp. 337-348
    • Almasan, A.1    Ashkenazi, A.2
  • 33
    • 21744448041 scopus 로고    scopus 로고
    • Taming TRAIL: The winding path to a novel form of cancer therapy
    • M.E. Peter Taming TRAIL: the winding path to a novel form of cancer therapy Cell Death Differ 12 2005 693 694
    • (2005) Cell Death Differ , vol.12 , pp. 693-694
    • Peter, M.E.1
  • 34
    • 0042844783 scopus 로고    scopus 로고
    • TRAIL-induced apoptosis and gene induction in HaCaT keratinocytes: Differential contribution of TRAIL receptors 1 and 2
    • M. Leverkus, M.R. Sprick, T. Wachter, A. Denk, E.B. Brocker, H. Walczak, and M. Neumann TRAIL-induced apoptosis and gene induction in HaCaT keratinocytes: differential contribution of TRAIL receptors 1 and 2 J Invest Dermatol 121 2003 149 155
    • (2003) J Invest Dermatol , vol.121 , pp. 149-155
    • Leverkus, M.1    Sprick, M.R.2    Wachter, T.3    Denk, A.4    Brocker, E.B.5    Walczak, H.6    Neumann, M.7
  • 35
    • 0038414629 scopus 로고    scopus 로고
    • TRAIL promotes the survival and proliferation of primary human vascular endothelial cells by activating the Akt and ERK pathways
    • P. Secchiero, A. Gonelli, E. Carnevale, D. Milani, A. Pandolfi, D. Zella, and G. Zauli TRAIL promotes the survival and proliferation of primary human vascular endothelial cells by activating the Akt and ERK pathways Circulation 107 2003 2250 2256
    • (2003) Circulation , vol.107 , pp. 2250-2256
    • Secchiero, P.1    Gonelli, A.2    Carnevale, E.3    Milani, D.4    Pandolfi, A.5    Zella, D.6    Zauli, G.7
  • 36
    • 18144416502 scopus 로고    scopus 로고
    • Tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) induces rheumatoid arthritis synovial fibroblast proliferation through mitogen-activated protein kinases and phosphatidylinositol 3-kinase/Akt
    • J. Morel, R. Audo, M. Hahne, and B. Combe Tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) induces rheumatoid arthritis synovial fibroblast proliferation through mitogen-activated protein kinases and phosphatidylinositol 3-kinase/Akt J Biol Chem 280 2005 15709 15718
    • (2005) J Biol Chem , vol.280 , pp. 15709-15718
    • Morel, J.1    Audo, R.2    Hahne, M.3    Combe, B.4
  • 38
    • 0031406386 scopus 로고    scopus 로고
    • Death receptor 5, a new member of the TNFR family, and DR4 induce FADD-dependent apoptosis and activate the NF-κB pathway
    • P.M. Chaudhary, M. Eby, A. Jasmin, A. Bookwalter, J. Murray, and L. Hood Death receptor 5, a new member of the TNFR family, and DR4 induce FADD-dependent apoptosis and activate the NF-κB pathway Immunity 7 1997 821 830
    • (1997) Immunity , vol.7 , pp. 821-830
    • Chaudhary, P.M.1    Eby, M.2    Jasmin, A.3    Bookwalter, A.4    Murray, J.5    Hood, L.6
  • 40
    • 10044232636 scopus 로고    scopus 로고
    • Induction of apoptosis and activation of NF-kappaB by CD95 require different signalling thresholds
    • P. Legembre, B.C. Barnhart, L. Zheng, S. Vijayan, S.E. Straus, J. Puck, J.K. Dale, M. Lenardo, and M.E. Peter Induction of apoptosis and activation of NF-kappaB by CD95 require different signalling thresholds EMBO Rep 5 2004 1084 1089 The CD95 death domain is essential for CD95 to induce apoptosis. By contrast, activation of non-apoptotic pathways through CD95, such as the activation of MAP kinases and NF-κB, only requires one functional CD95 allele, as found in human ALPS type Ia patients. Only when both CD95 alleles are mutated can neither apoptotic nor nonapoptotic pathways be engaged by CD95 in mouse splenocytes.
    • (2004) EMBO Rep , vol.5 , pp. 1084-1089
    • Legembre, P.1    Barnhart, B.C.2    Zheng, L.3    Vijayan, S.4    Straus, S.E.5    Puck, J.6    Dale, J.K.7    Lenardo, M.8    Peter, M.E.9
  • 42
    • 13944263937 scopus 로고    scopus 로고
    • The relevance of NF-κB for CD95 signaling in tumor cells
    • P. Legembre, B.C. Barnhart, and M.E. Peter The relevance of NF-κB for CD95 signaling in tumor cells Cell Cycle 3 2004 1235 1239
    • (2004) Cell Cycle , vol.3 , pp. 1235-1239
    • Legembre, P.1    Barnhart, B.C.2    Peter, M.E.3
  • 43
    • 0029849215 scopus 로고    scopus 로고
    • Bcl-2 prevents CD95 (Fas/APO-1)-induced degradation of lamin B and poly(ADP-ribose) polymerase and restores the NF-κB signaling pathway
    • M. Mandal, S.B. Maggirwar, N. Sharma, S.H. Kaufmann, S.C. Sun, and R. Kumar Bcl-2 prevents CD95 (Fas/APO-1)-induced degradation of lamin B and poly(ADP-ribose) polymerase and restores the NF-κB signaling pathway J Biol Chem 271 1996 30354 30359
    • (1996) J Biol Chem , vol.271 , pp. 30354-30359
    • Mandal, M.1    Maggirwar, S.B.2    Sharma, N.3    Kaufmann, S.H.4    Sun, S.C.5    Kumar, R.6
  • 44
    • 20144381544 scopus 로고    scopus 로고
    • Essential roles of Atg5 and FADD in autophagic cell death: Dissection of autophagic cell death into vacuole formation and cell death
    • J.O. Pyo, M.H. Jang, Y.K. Kwon, H.J. Lee, J.I. Jun, H.N. Woo, D.H. Cho, B. Choi, H. Lee, and J.H. Kim Essential roles of Atg5 and FADD in autophagic cell death: dissection of autophagic cell death into vacuole formation and cell death J Biol Chem 280 2005 20722 20729
    • (2005) J Biol Chem , vol.280 , pp. 20722-20729
    • Pyo, J.O.1    Jang, M.H.2    Kwon, Y.K.3    Lee, H.J.4    Jun, J.I.5    Woo, H.N.6    Cho, D.H.7    Choi, B.8    Lee, H.9    Kim, J.H.10
  • 45
    • 5044228305 scopus 로고    scopus 로고
    • Fas ligation on macrophages enhances IL-1R1-Toll-like receptor 4 signaling and promotes chronic inflammation
    • Y. Ma, H. Liu, H. Tu-Rapp, H.J. Thiesen, S.M. Ibrahim, S.M. Cole, and R.M. Pope Fas ligation on macrophages enhances IL-1R1-Toll-like receptor 4 signaling and promotes chronic inflammation Nat Immunol 5 2004 380 387
    • (2004) Nat Immunol , vol.5 , pp. 380-387
    • Ma, Y.1    Liu, H.2    Tu-Rapp, H.3    Thiesen, H.J.4    Ibrahim, S.M.5    Cole, S.M.6    Pope, R.M.7
  • 46
    • 9244236078 scopus 로고    scopus 로고
    • A FADD-dependent innate immune mechanism in mammalian cells
    • S. Balachandran, E. Thomas, and G.N. Barber A FADD-dependent innate immune mechanism in mammalian cells Nature 432 2004 401 405 FADD is important in host defense. Mammalian cells lacking FADD expression are hypersensitive to viral infection as they fail to respond to dsRNA with expression of genes such as Type I interferons. A novel signaling pathway links FADD through RIP with Tak-1 and IRF-3.
    • (2004) Nature , vol.432 , pp. 401-405
    • Balachandran, S.1    Thomas, E.2    Barber, G.N.3
  • 47
    • 0035839640 scopus 로고    scopus 로고
    • FADD-deficient T cells exhibit a disaccord in regulation of the cell cycle machinery
    • J. Zhang, N.H. Kabra, D. Cado, C. Kang, and A. Winoto FADD-deficient T cells exhibit a disaccord in regulation of the cell cycle machinery J Biol Chem 276 2001 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
  • 48
    • 0032546387 scopus 로고    scopus 로고
    • Fas-mediated apoptosis and activation-induced T-cell proliferation are defective in mice lacking FADD/Mort1
    • J. Zhang, D. Cado, A. Chen, N.H. Kabra, and A. Winoto Fas-mediated apoptosis and activation-induced T-cell proliferation are defective in mice lacking FADD/Mort1 Nature 392 1998 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
  • 49
    • 0032472916 scopus 로고    scopus 로고
    • A dominant interfering mutant of FADD/MORT1 enhances deletion of autoreactive thymocytes and inhibits proliferation of mature T lymphocytes
    • K. Newton, A.W. Harris, M.L. Bath, K.G. Smith, and A. Strasser A dominant interfering mutant of FADD/MORT1 enhances deletion of autoreactive thymocytes and inhibits proliferation of mature T lymphocytes EMBO J 17 1998 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
  • 51
    • 0032499138 scopus 로고    scopus 로고
    • P53-dependent impairment of T-cell proliferation in FADD dominant-negative transgenic mice
    • M. Zornig, A.O. Hueber, and G. Evan p53-dependent impairment of T-cell proliferation in FADD dominant-negative transgenic mice Curr Biol 8 1998 467 470
    • (1998) Curr Biol , vol.8 , pp. 467-470
    • Zornig, M.1    Hueber, A.O.2    Evan, G.3
  • 52
    • 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
    • A.O. Hueber, M. Zornig, A.M. Bernard, M. Chautan, and G. Evan 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 2000 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
  • 53
    • 0142211350 scopus 로고    scopus 로고
    • Cell cycle effects by C-FADD depend on its C-terminal phosphorylation site
    • E.C. Alappat, J. Volkland, and M.E. Peter Cell cycle effects by C-FADD depend on its C-terminal phosphorylation site J Biol Chem 278 2003 41585 41588
    • (2003) J Biol Chem , vol.278 , pp. 41585-41588
    • Alappat, E.C.1    Volkland, J.2    Peter, M.E.3
  • 54
    • 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
    • Z.C. Hua, S.J. Sohn, C. Kang, D. Cado, and A. Winoto 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 2003 513 521 T cells from FADD knockout mice reconstituted with FADD with a S191D replacement are defective in proliferation and cell cycle progression in a similar manner to T cells from mice lacking FADD expression completely, establishing the relevance of the Ser191 phosphorylation site in FADD in vivo.
    • (2003) Immunity , vol.18 , pp. 513-521
    • Hua, Z.C.1    Sohn, S.J.2    Kang, C.3    Cado, D.4    Winoto, A.5
  • 56
    • 0042467816 scopus 로고    scopus 로고
    • Caspase-8 and caspase-10 activate NF-κB through RIP, NIK and IKKα kinases
    • Y. Shikama, M. Yamada, and T. Miyashita Caspase-8 and caspase-10 activate NF-κB through RIP, NIK and IKKα kinases Eur J Immunol 33 2003 1998 2006
    • (2003) Eur J Immunol , vol.33 , pp. 1998-2006
    • Shikama, Y.1    Yamada, M.2    Miyashita, T.3
  • 57
    • 0036807323 scopus 로고    scopus 로고
    • Phosphorylation of Fas-associated death domain contributes to enhancement of etoposide-induced apoptosis in prostate cancer cells
    • K. Shimada, M. Nakamura, E. Ishida, M. Kishi, S. Yonehara, and N. Konishi Phosphorylation of Fas-associated death domain contributes to enhancement of etoposide-induced apoptosis in prostate cancer cells Jpn J Cancer Res 93 2002 1164 1174
    • (2002) Jpn J Cancer Res , vol.93 , pp. 1164-1174
    • Shimada, K.1    Nakamura, M.2    Ishida, E.3    Kishi, M.4    Yonehara, S.5    Konishi, N.6
  • 58
    • 0037380628 scopus 로고    scopus 로고
    • Essential role for caspase 8 in T-cell homeostasis and T-cell-mediated immunity
    • L. Salmena, B. Lemmers, A. Hakem, E. Matysiak-Zablocki, K. Murakami, P.Y. Au, D.M. Berry, L. Tamblyn, A. Shehabeldin, and E. Migon Essential role for caspase 8 in T-cell homeostasis and T-cell-mediated immunity Genes Dev 17 2003 883 895 Tissue-specific knock-out of caspase-8 reveals a role for caspase-8 in the activation and differentiation of peripheral T cells. Caspase-8-deficient mice are defective in mounting an immune response in response to viral infection.
    • (2003) Genes Dev , vol.17 , pp. 883-895
    • Salmena, L.1    Lemmers, B.2    Hakem, A.3    Matysiak-Zablocki, E.4    Murakami, K.5    Au, P.Y.6    Berry, D.M.7    Tamblyn, L.8    Shehabeldin, A.9    Migon, E.10
  • 62
    • 0035496099 scopus 로고    scopus 로고
    • Regulation of lymphocyte proliferation and death by FLIP
    • M. Thome, and J. Tschopp Regulation of lymphocyte proliferation and death by FLIP Nat Rev Immunol 1 2001 50 58
    • (2001) Nat Rev Immunol , vol.1 , pp. 50-58
    • Thome, M.1    Tschopp, J.2
  • 63
    • 21244449877 scopus 로고    scopus 로고
    • Cellular FLIP long form augments caspase activity and death of T cells through heterodimerization with and activation of caspase-8
    • A. Dohrman, J.Q. Russell, S. Cuenin, K. Fortner, J. Tschopp, and R.C. Budd Cellular FLIP long form augments caspase activity and death of T cells through heterodimerization with and activation of caspase-8 J Immunol 175 2005 311 318
    • (2005) J Immunol , vol.175 , pp. 311-318
    • Dohrman, A.1    Russell, J.Q.2    Cuenin, S.3    Fortner, K.4    Tschopp, J.5    Budd, R.C.6
  • 66
    • 11144224085 scopus 로고    scopus 로고
    • CFLIPL inhibits tumor necrosis factor-related apoptosis-inducing ligand-mediated NF-κB activation at the death-inducing signaling complex in human keratinocytes
    • T. Wachter, M. Sprick, D. Hausmann, A. Kerstan, K. McPherson, G. Stassi, E.B. Brocker, H. Walczak, and M. Leverkus cFLIPL inhibits tumor necrosis factor-related apoptosis-inducing ligand-mediated NF-κB activation at the death-inducing signaling complex in human keratinocytes J Biol Chem 279 2004 52824 52834
    • (2004) J Biol Chem , vol.279 , pp. 52824-52834
    • Wachter, T.1    Sprick, M.2    Hausmann, D.3    Kerstan, A.4    McPherson, K.5    Stassi, G.6    Brocker, E.B.7    Walczak, H.8    Leverkus, M.9
  • 70
    • 23944514831 scopus 로고    scopus 로고
    • FADD and caspase-8 are required for cytokine-induced proliferation of hemopoietic progenitor cells
    • M. Pellegrini, S. Bath, V.S. Marsden, D.C. Huang, D. Metcalf, A.W. Harris, and A. Strasser FADD and caspase-8 are required for cytokine-induced proliferation of hemopoietic progenitor cells Blood 106 2005 1581 1589
    • (2005) Blood , vol.106 , pp. 1581-1589
    • Pellegrini, M.1    Bath, S.2    Marsden, V.S.3    Huang, D.C.4    Metcalf, D.5    Harris, A.W.6    Strasser, A.7
  • 71
    • 23744456144 scopus 로고    scopus 로고
    • An essential role for c-FLIP in the efficient development of mature T lymphocytes
    • N. Zhang, and Y.W. He An essential role for c-FLIP in the efficient development of mature T lymphocytes J Exp Med 202 2005 395 404
    • (2005) J Exp Med , vol.202 , pp. 395-404
    • Zhang, N.1    He, Y.W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.