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Volumn 4, Issue 5, 2003, Pages 404-409

The death effector domain protein family: Regulators of cellular homeostasis

Author keywords

[No Author keywords available]

Indexed keywords

CASPASE 10; CASPASE 8; FAS ANTIGEN; INHIBITOR OF APOPTOSIS PROTEIN; REGULATOR PROTEIN;

EID: 0038393124     PISSN: 15292908     EISSN: None     Source Type: Journal    
DOI: 10.1038/ni0503-404     Document Type: Review
Times cited : (200)

References (74)
  • 1
    • 0027281373 scopus 로고
    • A novel protein domain required for apoptosis. Mutational analysis of human Fas antigen
    • Itoh, N. & Nagata, S. A novel protein domain required for apoptosis. Mutational analysis of human Fas antigen. J. Biol. Chem. 268, 10932-10937 (1993).
    • (1993) J. Biol. Chem. , vol.268 , pp. 10932-10937
    • Itoh, N.1    Nagata, S.2
  • 2
    • 0027275490 scopus 로고
    • A novel domain within the 55 kD TNF receptor signals cell death
    • Tartaglia, L.A., Ayres, T.M., Wong, G.H. & Goeddel, D.V. A novel domain within the 55 kD TNF receptor signals cell death. Cell 74, 845-853 (1993).
    • (1993) Cell , vol.74 , pp. 845-853
    • Tartaglia, L.A.1    Ayres, T.M.2    Wong, G.H.3    Goeddel, D.V.4
  • 3
    • 0028913550 scopus 로고
    • A novel protein that interacts with the death domain of Fas/APO I contains a sequence motif related to the death domain
    • Boldin, M.P. et al. A novel protein that interacts with the death domain of Fas/APO I contains a sequence motif related to the death domain. J. Biol. Chem. 270, 7795-7798 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 7795-7798
    • Boldin, M.P.1
  • 4
    • 0029026548 scopus 로고
    • FADD, a novel death domain-containing protein, interacts with the death domain of Fas and initiates apoptosis
    • Chinnaiyan, A.M., O'Rourke, K., Tewari, M. & Dixit, V.M. FADD, a novel death domain-containing protein, interacts with the death domain of Fas and initiates apoptosis. Cell 81, 505-512 (1995).
    • (1995) Cell , vol.81 , pp. 505-512
    • Chinnaiyan, A.M.1    O'Rourke, K.2    Tewari, M.3    Dixit, V.M.4
  • 5
    • 0344053451 scopus 로고    scopus 로고
    • In vitro activation of CPP32 and Mch3 by Mch4, a novel human apoptotic cysteine protease containing two FADD-like domains
    • Fernandes-Alnemri, T. et al. In vitro activation of CPP32 and Mch3 by Mch4, a novel human apoptotic cysteine protease containing two FADD-like domains. Proc. Natl. Acad. Sci. USA 93, 7464-7469 (1996).
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 7464-7469
    • Fernandes-Alnemri, T.1
  • 7
    • 0035824635 scopus 로고    scopus 로고
    • Death receptor recruitment of endogenous caspase-10 and apoptosis initiation in the absence of caspase-8
    • Kischkel, F.C. et al. Death receptor recruitment of endogenous caspase-10 and apoptosis initiation in the absence of caspase-8. J. Biol. Chem. 276, 46639-46646 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 46639-46646
    • Kischkel, F.C.1
  • 8
    • 0032548842 scopus 로고    scopus 로고
    • Membrane oligomerization and cleavage activates the caspase-8 (FLICE/MACHα1) death signal
    • Martin, D.A., Siegel, R.M., Zheng, L. & Lenardo, M.J. Membrane oligomerization and cleavage activates the caspase-8 (FLICE/MACHα1) death signal. J. Biol. Chem. 273, 4345-4349 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 4345-4349
    • Martin, D.A.1    Siegel, R.M.2    Zheng, L.3    Lenardo, M.J.4
  • 10
    • 0030011398 scopus 로고    scopus 로고
    • Involvement of MACH, a novel MORT1/FADD-interacting protease, in Fas/Apo-1 and TNF receptor-induced cell death
    • Boldin, M.P., Goncharov, T.M., Goltsev, Y.V. & Wallach, D.I. Involvement of MACH, a novel MORT1/FADD-interacting protease, in Fas/Apo-1 and TNF receptor-induced cell death. Cell 85, 803-815 (1996).
    • (1996) Cell , vol.85 , pp. 803-815
    • Boldin, M.P.1    Goncharov, T.M.2    Goltsev, Y.V.3    Wallach, D.I.4
  • 11
    • 15844412409 scopus 로고    scopus 로고
    • FLICE, a novel FADD-homologous ICE/CED-3-like protease, is recruited to the CD95 (Fas/APO-1) death-inducing signaling complex
    • Muzio, M. et al. FLICE, a novel FADD-homologous ICE/CED-3-like protease, is recruited to the CD95 (Fas/APO-1) death-inducing signaling complex. Cell 85, 817-827 (1996).
    • (1996) Cell , vol.85 , pp. 817-827
    • Muzio, M.1
  • 12
    • 0035425256 scopus 로고    scopus 로고
    • The death domain superfamily: A tale of two interfaces?
    • Weber, C.H. & Vincenz, C. The death domain superfamily: a tale of two interfaces? Trends Biochem. Sci. 26, 475-481 (2001).
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 475-481
    • Weber, C.H.1    Vincenz, C.2
  • 13
    • 0032580153 scopus 로고    scopus 로고
    • NMR structure and mutagenesis of the FADD (MORT1) death-effector domain
    • Eberstadt, M. et al. NMR structure and mutagenesis of the FADD (MORT1) death-effector domain. Nature 392, 941-945 (1998).
    • (1998) Nature , vol.392 , pp. 941-945
    • Eberstadt, M.1
  • 14
    • 0032807406 scopus 로고    scopus 로고
    • The modular nature of apoptotic signaling proteins
    • Hofmann, K. The modular nature of apoptotic signaling proteins. Cell. Mol. Life Sci. 55, 1113-1128 (1999).
    • (1999) Cell. Mol. Life Sci. , vol.55 , pp. 1113-1128
    • Hofmann, K.1
  • 15
    • 0035916324 scopus 로고    scopus 로고
    • The pyrin domain: A possible member of the death domain family implicated in apoptosis and inflammation
    • Martinon, F., Hofman, K. & Tschopp, J. The pyrin domain: a possible member of the death domain family implicated in apoptosis and inflammation. Curr. Biol. 11, R118-R120 (2001).
    • (2001) Curr. Biol. , vol.11 , pp. R118-R120
    • Martinon, F.1    Hofman, K.2    Tschopp, J.3
  • 16
    • 0030954209 scopus 로고    scopus 로고
    • The CARD domain: A new apoptotic signalling motif
    • Hofmann, K., Bucher, P. & Tschopp, J. The CARD domain: a new apoptotic signalling motif. Trends Biochem. Sci. 22, 155-156 (1997).
    • (1997) Trends Biochem. Sci. , vol.22 , pp. 155-156
    • Hofmann, K.1    Bucher, P.2    Tschopp, J.3
  • 17
    • 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. et al. 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).
    • (2002) J. Virol. , vol.76 , pp. 697-706
    • Garvey, T.L.1
  • 18
    • 0034613376 scopus 로고    scopus 로고
    • dFADD, a novel death domain-containing adapter protein for the Drosophila caspase DREDD
    • Hu, S. & Yang, X. dFADD, a novel death domain-containing adapter protein for the Drosophila caspase DREDD. J. Biol. Chem. 275, 30761-30764 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 30761-30764
    • Hu, S.1    Yang, X.2
  • 19
    • 0034067779 scopus 로고    scopus 로고
    • Death effector domain of a mammalian apoptosis mediator, FADD, induces bacterial cell death
    • Lee, S.W., Ko, Y.G., Bang, S., Kim, K.S. & Kim, S. Death effector domain of a mammalian apoptosis mediator, FADD, induces bacterial cell death. Mol. Microbiol. 35, 1540-1549 (2000).
    • (2000) Mol. Microbiol. , vol.35 , pp. 1540-1549
    • Lee, S.W.1    Ko, Y.G.2    Bang, S.3    Kim, K.S.4    Kim, S.5
  • 20
    • 0034733584 scopus 로고    scopus 로고
    • Fas preassociation required for apoptosis signaling and dominant inhibition by pathogenic mutations
    • Siegel, R.M. et al. Fas preassociation required for apoptosis signaling and dominant inhibition by pathogenic mutations. Science 288, 2354-2357 (2000).
    • (2000) Science , vol.288 , pp. 2354-2357
    • Siegel, R.M.1
  • 21
    • 0037063338 scopus 로고    scopus 로고
    • Identification of a basic surface area of the FADD death effector domain critical for apoptotic signaling
    • Kaufmann, M. et al. Identification of a basic surface area of the FADD death effector domain critical for apoptotic signaling. FEBS Lett. 527, 250-254 (2002).
    • (2002) FEBS Lett. , vol.527 , pp. 250-254
    • Kaufmann, M.1
  • 22
    • 0035896406 scopus 로고    scopus 로고
    • A docking model of key components of the DISC complex: Death domain superfamily interactions redefined
    • Weber, C.H. & Vincent, C. A docking model of key components of the DISC complex: death domain superfamily interactions redefined. FEBS Lett. 492, 171-176 (2001).
    • (2001) FEBS Lett. , vol.492 , pp. 171-176
    • Weber, C.H.1    Vincent, C.2
  • 23
    • 0029006893 scopus 로고
    • Mutations in Fas associated with human lymphoproliferative syndrome and autoimmunity
    • Rieux-Laucat, F. et al. Mutations in Fas associated with human lymphoproliferative syndrome and autoimmunity. Science 268, 1347-1349 (1995).
    • (1995) Science , vol.268 , pp. 1347-1349
    • Rieux-Laucat, F.1
  • 24
    • 0029025441 scopus 로고
    • Dominant interfering Fas gene mutations impair apoptosis in a human autoimmune lymphoproliferative syndrome
    • Fisher, G.H. et al. Dominant interfering Fas gene mutations impair apoptosis in a human autoimmune lymphoproliferative syndrome. Cell 81, 935-946 (1995).
    • (1995) Cell , vol.81 , pp. 935-946
    • Fisher, G.H.1
  • 25
    • 0030614415 scopus 로고    scopus 로고
    • Clinical, immunologic, and genetic features of an autoimmune lymphoproliferative syndrome associated with abnormal lymphocyte apoptosis
    • Sneller, M.C. et al. Clinical, immunologic, and genetic features of an autoimmune lymphoproliferative syndrome associated with abnormal lymphocyte apoptosis. Blood 89, 1341-1348 (1997).
    • (1997) Blood , vol.89 , pp. 1341-1348
    • Sneller, M.C.1
  • 26
    • 0031615875 scopus 로고    scopus 로고
    • Autoproteolytic activation of pro-caspases by oligomerization
    • Yang, X., Chang, H.Y. & Baltimore, D. Autoproteolytic activation of pro-caspases by oligomerization. Mol. Cell 1, 319-325 (1998).
    • (1998) Mol. Cell , vol.1 , pp. 319-325
    • Yang, X.1    Chang, H.Y.2    Baltimore, D.3
  • 27
    • 0038731167 scopus 로고    scopus 로고
    • Caspase-independent cell death in T lymphocytes
    • Jaattela, M. & Tschopp, J. Caspase-independent cell death in T lymphocytes. Nat. Immunol. 4, 416-423.
    • Nat. Immunol. , vol.4 , pp. 416-423
    • Jaattela, M.1    Tschopp, J.2
  • 28
    • 5944233768 scopus 로고    scopus 로고
    • Fas triggers an alternative, caspase-8-independent cell death pathway using the kinase RIP as effector molecule
    • Holler, N. et al. Fas triggers an alternative, caspase-8-independent cell death pathway using the kinase RIP as effector molecule. Nat. Immunol. 1, 489-495 (2000).
    • (2000) Nat. Immunol. , vol.1 , pp. 489-495
    • Holler, N.1
  • 29
    • 0033861807 scopus 로고    scopus 로고
    • Induction of necrotic-like cell death by tumor necrosis factor-α and caspase inhibitors: Novel mechanism for killing virus-infected cells
    • Li, M. & Beg, A.A. Induction of necrotic-like cell death by tumor necrosis factor-α and caspase inhibitors: novel mechanism for killing virus-infected cells. J. Virol. 74, 7470-7477 (2000).
    • (2000) J. Virol. , vol.74 , pp. 7470-7477
    • Li, M.1    Beg, A.A.2
  • 30
    • 12644286556 scopus 로고    scopus 로고
    • Death effector domain-containing herpesvirus and poxvirus proteins inhibit both Fas-and TNRF1-induced apoptosis
    • Bertin, J. et al. Death effector domain-containing herpesvirus and poxvirus proteins inhibit both Fas-and TNRF1-induced apoptosis. Proc. Natl. Acad. Sci. USA 94, 1172-1176 (1997).
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 1172-1176
    • Bertin, J.1
  • 31
    • 0030950228 scopus 로고    scopus 로고
    • A novel family of viral death effector domain-containing molecules that inhibit both CD95- and tumor necrosis factor receptor-1-induced apoptosis
    • Hu, S., Vincenz, C., Buller, M. & Dixit, V.M. A novel family of viral death effector domain-containing molecules that inhibit both CD95- and tumor necrosis factor receptor-1-induced apoptosis. J. Biol. Chem. 272, 9621-9624 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 9621-9624
    • Hu, S.1    Vincenz, C.2    Buller, M.3    Dixit, V.M.4
  • 32
    • 0030970013 scopus 로고    scopus 로고
    • Viral FLICE-inhibitory proteins (FLIPs) prevent apoptosis induced by death receptors
    • Thome, M. et al. Viral FLICE-inhibitory proteins (FLIPs) prevent apoptosis induced by death receptors. Nature 386, 517-521 (1997).
    • (1997) Nature , vol.386 , pp. 517-521
    • Thome, M.1
  • 33
    • 0036389828 scopus 로고    scopus 로고
    • The death effector domains (DEDs) of the molluscum contagiosum virus MC159 v-FLIP protein are not functionally interchangeable with each other or with the DEDs of caspase-8
    • Garvey, T.L., Bertin, J., Siegel, R.M., Lenardo, M.J. & Cohen, J. The death effector domains (DEDs) of the molluscum contagiosum virus MC159 v-FLIP protein are not functionally interchangeable with each other or with the DEDs of caspase-8. Virology 300, 217-225 (2002).
    • (2002) Virology , vol.300 , pp. 217-225
    • Garvey, T.L.1    Bertin, J.2    Siegel, R.M.3    Lenardo, M.J.4    Cohen, J.5
  • 34
    • 0030800070 scopus 로고    scopus 로고
    • Inhibition of death receptor signals by cellular FLIP
    • Irmler, M. et al. Inhibition of death receptor signals by cellular FLIP. Nature 388, 190-195 (1997).
    • (1997) Nature , vol.388 , pp. 190-195
    • Irmler, M.1
  • 35
    • 0030841911 scopus 로고    scopus 로고
    • I-FLICE, a novel inhibitor of tumor necrosis factor receptor-I- and CD-95-induced apoptosis
    • Hu, S., Vincenz, C., Ni, J., Gentz, R. & Dixit, V.M. I-FLICE, a novel inhibitor of tumor necrosis factor receptor-I- and CD-95-induced apoptosis. J. Biol. Chem. 272, 17255-17257 (1997).
    • (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
  • 36
    • 0034744033 scopus 로고    scopus 로고
    • NF-κB inducers upregulate cFLIP, a cycloheximide-sensitive inhibitor of death receptor signaling
    • Kreuz, S., Siegmund, D., Scheurich, P. & Wajant, H. NF-κB inducers upregulate cFLIP, a cycloheximide-sensitive inhibitor of death receptor signaling. Mol. Cell. Biol. 21, 3964-3973 (2001).
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 3964-3973
    • Kreuz, S.1    Siegmund, D.2    Scheurich, P.3    Wajant, H.4
  • 38
    • 0036105506 scopus 로고    scopus 로고
    • Constituitive expression of c-FLIP in Hodgkin and Reed-Sternberg cells
    • Thomas, R.K. et al. Constituitive expression of c-FLIP in Hodgkin and Reed-Sternberg cells. Amer. J. of Path. 160, 1521-1528 (2002).
    • (2002) Amer. J. of Path. , vol.160 , pp. 1521-1528
    • Thomas, R.K.1
  • 39
    • 0037099678 scopus 로고    scopus 로고
    • L is a dual function regulator for caspase-8 activation and CD95-mediated apoptosis
    • L is a dual function regulator for caspase-8 activation and CD95-mediated apoptosis. EMBO J. 21, 3704-3714 (2002).
    • (2002) EMBO J. , vol.21 , pp. 3704-3714
    • Chang, D.W.1
  • 40
    • 0036310708 scopus 로고    scopus 로고
    • L modulates T-cell receptor-induced proliferation but not activation-induced cell death of lymphocytes
    • L modulates T-cell receptor-induced proliferation but not activation-induced cell death of lymphocytes. Mol. Cell. Biol. 22, 5419-5433 (2002).
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 5419-5433
    • Lens, S.1
  • 41
    • 0033527064 scopus 로고    scopus 로고
    • PED/PEA-15: An anti-apoptotic molecule that regulates FAS/TNRF1-induced apoptosis
    • Condorelli, G. et al. PED/PEA-15: an anti-apoptotic molecule that regulates FAS/TNRF1-induced apoptosis. Oncogene 18, 4409-4415 (1999).
    • (1999) Oncogene , vol.18 , pp. 4409-4415
    • Condorelli, G.1
  • 42
    • 0033216124 scopus 로고    scopus 로고
    • Knock-out of the neural death effector domain protein PEA-15 demonstrates that its expression protects astrocytes from TNFα-induced apoptosis
    • Kitsberg, D. et al. Knock-out of the neural death effector domain protein PEA-15 demonstrates that its expression protects astrocytes from TNFα-induced apoptosis. J. Neuroscience 19, 8244-8251 (1999).
    • (1999) J. Neuroscience , vol.19 , pp. 8244-8251
    • Kitsberg, D.1
  • 43
    • 0027460528 scopus 로고
    • Characterization of PEA-15, a major substrate for protein kinase C in astrocytes
    • Araujo, H., Danziger, N., Cordier, J., Glowinski, J. & Chneiweiss, H. Characterization of PEA-15, a major substrate for protein kinase C in astrocytes. J. Biol. Chem. 268, 5911-5920 (1993).
    • (1993) J. Biol. Chem. , vol.268 , pp. 5911-5920
    • Araujo, H.1    Danziger, N.2    Cordier, J.3    Glowinski, J.4    Chneiweiss, H.5
  • 44
    • 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. & Chneiweiss, H. 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).
    • (1998) J. Neurochem. , vol.71 , pp. 1307-1314
    • Kubes, M.1    Cordier, J.2    Glowinski, J.3    Girault, J.A.4    Chneiweiss, H.5
  • 45
    • 0035976906 scopus 로고    scopus 로고
    • Protein kinase C regulates FADD recruitment and death-inducing signaling complex formation in Fas/CD95-induced apoptosis
    • Gomez-Angelats, M. & Cidlowski, J.A. Protein kinase C regulates FADD recruitment and death-inducing signaling complex formation in Fas/CD95-induced apoptosis. J. Biol. Chem. 276, 44944-44952 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 44944-44952
    • Gomez-Angelats, M.1    Cidlowski, J.A.2
  • 46
    • 0037067678 scopus 로고    scopus 로고
    • Tumor necrosis factor-related apoptosis-inducing ligand-induced 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. & Hao, C. Tumor necrosis factor-related apoptosis-inducing ligand-induced death-inducing signaling complex and its modulation by c-FLIP and PED/PEA-15 in glioma cells. J. Biol. Chem. 277, 25020-25025 (2002).
    • (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
  • 47
    • 0032740020 scopus 로고    scopus 로고
    • The phosphoprotein PEA-15 inhibits Fas- but increases TNFR1 mediated caspase-8 activity and apoptosis
    • Estelles, A., Charlton, C.A. & Blau, H.M. The phosphoprotein PEA-15 inhibits Fas- but increases TNFR1 mediated caspase-8 activity and apoptosis. Dev. Biol. 216, 16-28 (1999).
    • (1999) Dev. Biol. , vol.216 , pp. 16-28
    • Estelles, A.1    Charlton, C.A.2    Blau, H.M.3
  • 48
    • 0032531817 scopus 로고    scopus 로고
    • DEDD, a novel death effector domain-containing protein, targeted to the nucleolus
    • Stegh, A.H. et al. DEDD, a novel death effector domain-containing protein, targeted to the nucleolus. EMBO J. 17, 5974-5986 (1998).
    • (1998) EMBO J. , vol.17 , pp. 5974-5986
    • Stegh, A.H.1
  • 49
    • 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. & Peter, M.E. 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, 1157-1161 (2001).
    • (2001) Cell Death Differ. , vol.8 , pp. 1157-1161
    • Schickling, O.1    Stegh, A.H.2    Byrd, J.3    Peter, M.E.4
  • 50
    • 0037119943 scopus 로고    scopus 로고
    • DEDD regulates degradation of intermediate filaments during apoptosis
    • Lee, J. et al. DEDD regulates degradation of intermediate filaments during apoptosis. J. Cell. Biol. 158, 1051-1066 (2002).
    • (2002) J. Cell. Biol. , vol.158 , pp. 1051-1066
    • Lee, J.1
  • 51
    • 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. & Reed, J.C. Identification and characterization of DEDD2, a death effector domain-containing protein. J. Biol. Chem. 277, 7501-7508 (2002).
    • (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
  • 52
    • 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. & Lenardo, M.J. The death effector domain-associated factor plays distinct regulatory roles in the nucleus and cytoplasm. J. Biol. Chem. 276, 31945-31952 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 31945-31952
    • Zheng, L.1    Schickling, O.2    Peter, M.E.3    Lenardo, M.J.4
  • 53
    • 0030705234 scopus 로고    scopus 로고
    • L and procaspase-8-associated protein in the endoplasmic reticulum
    • L and procaspase-8-associated protein in the endoplasmic reticulum. J. Cell Biol. 139, 327-338 (1997).
    • (1997) J. Cell Biol. , vol.139 , pp. 327-338
    • Ng, F.W.1
  • 54
    • 12944270500 scopus 로고    scopus 로고
    • BAR: An apoptosis regulator at the intersection of caspases and Bcl-2 family proteins
    • Zhang, H. et al. BAR: an apoptosis regulator at the intersection of caspases and Bcl-2 family proteins. Proc. Natl. Acad. Sci. USA 97, 2597-2602 (2000).
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 2597-2602
    • Zhang, H.1
  • 55
    • 0037040176 scopus 로고    scopus 로고
    • L-expressing MCF7-Fas cells: Role for bifunctional apoptosis regulator protein
    • L-expressing MCF7-Fas cells: role for bifunctional apoptosis regulator protein. J. Biol. Chem. 277, 4351-4360 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 4351-4360
    • Stegh, A.H.1
  • 56
    • 0033816610 scopus 로고    scopus 로고
    • Caspase-resistant BAF31 inhibits Fas-mediated apoptotic membrane fragmentation and release of cytochrome c from mitochondria
    • Nguyen, M., Breckenridge, D.G., Ducret, A. & Shore, G.C. Caspase-resistant BAF31 inhibits Fas-mediated apoptotic membrane fragmentation and release of cytochrome c from mitochondria. Mol. Cell. Biol. 20, 6731-6740 (2000).
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 6731-6740
    • Nguyen, M.1    Breckenridge, D.G.2    Ducret, A.3    Shore, G.C.4
  • 57
    • 0013148718 scopus 로고    scopus 로고
    • Uncleaved BAP31 in association with A4 protein at the endoplasmic reticulum is an inhibitor of Fas-initiated release of cytochrome c from mitochondria
    • advance online publication, 15 January (doi:10.1074/jbc.M209684200)
    • Wang, B. et al. Uncleaved BAP31 in association with A4 protein at the endoplasmic reticulum is an inhibitor of Fas-initiated release of cytochrome c from mitochondria. J. Biol. Chem. advance online publication, 15 January 2003 (doi:10.1074/jbc.M209684200).
    • (2003) J. Biol. Chem
    • Wang, B.1
  • 58
    • 0032101371 scopus 로고    scopus 로고
    • Death-effector filaments: Novel cytoplasmic structures that recruit caspases and trigger apoptosis
    • Siegel, R.M. et al. Death-effector filaments: novel cytoplasmic structures that recruit caspases and trigger apoptosis. J. Cell. Biol. 141, 1243-1253 (1998).
    • (1998) J. Cell. Biol. , vol.141 , pp. 1243-1253
    • Siegel, R.M.1
  • 59
    • 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. & Winoto, A. Fas-mediated apoptosis and activation-induced T-cell proliferation are defective in mice lacking FADD/Mort1. Nature 392, 296-300 (1998).
    • (1998) Nature , vol.392 , pp. 296-300
    • Zhang, J.1    Cado, D.2    Chen, A.3    Kabra, N.H.4    Winoto, A.5
  • 60
    • 0032055344 scopus 로고    scopus 로고
    • A Role for FADD in T cell activation and development
    • Walsh, C.M. et al. A Role for FADD in T cell activation and development. Immunity 8, 439-449 (1998).
    • (1998) Immunity , vol.8 , pp. 439-449
    • Walsh, C.M.1
  • 61
    • 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. & Strasser A. 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).
    • (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
  • 62
    • 0036316064 scopus 로고    scopus 로고
    • Inhibition of caspase or FADD function blocks proliferation but not MAP kinase activation and interleukin-2 production during primary stimulation of T cells
    • Mack, A. & Hacker, G. Inhibition of caspase or FADD function blocks proliferation but not MAP kinase activation and interleukin-2 production during primary stimulation of T cells. Eur. J. Immunol. 32, 1986-1992 (2002).
    • (2002) Eur. J. Immunol. , vol.32 , pp. 1986-1992
    • Mack, A.1    Hacker, G.2
  • 63
    • 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. & Sekaly, R.F. Early activation of caspases during T lymphocyte stimulation results in selective substrate cleavage in nonapoptotic cells. J. Exp. Med. 190, 1879-1890 (1999).
    • (1999) J. Exp. Med. , vol.190 , pp. 1879-1890
    • Alam, A.1    Cohen, L.Y.2    Aouad, S.3    Sekaly, R.F.4
  • 64
    • 0033386808 scopus 로고    scopus 로고
    • Caspase activation is required for T cell proliferation
    • Kennedy, N.J., Kataoka, T., Tschopp, J. & Budd, R.C. Caspase activation is required for T cell proliferation. J. Exp. Med. 190, 1891-1896 (1999).
    • (1999) J. Exp. Med. , vol.190 , pp. 1891-1896
    • Kennedy, N.J.1    Kataoka, T.2    Tschopp, J.3    Budd, R.C.4
  • 65
    • 18544383460 scopus 로고    scopus 로고
    • Pleiotropic lymphocyte activation defects due to caspase-8 mutation causes human immunodeficiency
    • Chun, H. et al. Pleiotropic lymphocyte activation defects due to caspase-8 mutation causes human immunodeficiency. Nature 419, 395-399 (2002).
    • (2002) Nature , vol.419 , pp. 395-399
    • Chun, H.1
  • 66
    • 0034648529 scopus 로고    scopus 로고
    • Activation of the NF-κB pathway by caspase 8 and its homologs
    • Chaudhary, P.M. et al. Activation of the NF-κB pathway by caspase 8 and its homologs. Oncogene 19, 4451-4460 (2000).
    • (2000) Oncogene , vol.19 , pp. 4451-4460
    • Chaudhary, P.M.1
  • 67
    • 0034646478 scopus 로고    scopus 로고
    • Activation of NF-κB by FADD, Casper, and Caspase 8
    • Hu, W.H., Johnson, H. & Shu, H.B. Activation of NF-κB by FADD, Casper, and Caspase 8. J. Biol. Chem. 275, 10838-10844 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 10838-10844
    • Hu, W.H.1    Johnson, H.2    Shu, H.B.3
  • 68
    • 0033538475 scopus 로고    scopus 로고
    • Inherited caspase 10 mutations underlie defective lymphocyte and dendritic cell apoptosis in autoimmune lymphoproliferative syndrome type II
    • Wang, J. et al. Inherited caspase 10 mutations underlie defective lymphocyte and dendritic cell apoptosis in autoimmune lymphoproliferative syndrome type II. Cell 98, 47-58 (1999).
    • (1999) Cell , vol.98 , pp. 47-58
    • Wang, J.1
  • 69
    • 18744425429 scopus 로고    scopus 로고
    • The caspase-8 inhibitor FLIP promotes activation of NF-κB and Erk signaling pathways
    • Kataoka, T et al. The caspase-8 inhibitor FLIP promotes activation of NF-κB and Erk signaling pathways. Curr. Biol. 10, 640-648 (2000).
    • (2000) Curr. Biol. , vol.10 , pp. 640-648
    • Kataoka, T.1
  • 70
    • 0027484072 scopus 로고
    • Fas transduces activation signals in normal human T lymphocytes
    • Alderson, M.R. et al. Fas transduces activation signals in normal human T lymphocytes. J. Exp. Med. 178, 1891-1896 (1993).
    • (1993) J. Exp. Med. , vol.178 , pp. 1891-1896
    • Alderson, M.R.1
  • 71
    • 0034492451 scopus 로고    scopus 로고
    • Death effector domain protein PEA-15 potentiates Ras activation of extracellular signal receptor-activated kinase by an adhesion-independent mechanism
    • Ramos, J.W. et al. Death effector domain protein PEA-15 potentiates Ras activation of extracellular signal receptor-activated kinase by an adhesion-independent mechanism. Mol. Biol. Cell 11, 2863-2872 (2000).
    • (2000) Mol. Biol. Cell , vol.11 , pp. 2863-2872
    • Ramos, J.W.1
  • 72
    • 18044405015 scopus 로고    scopus 로고
    • PEA-15 mediates cytoplasmic sequestration of ERK MAP kinase
    • Formstecher. E. et al. PEA-15 mediates cytoplasmic sequestration of ERK MAP kinase. Dev. Cell 1, 239-250 (2001).
    • (2001) Dev. Cell , vol.1 , pp. 239-250
    • Formstecher, E.1
  • 73
    • 0037130961 scopus 로고    scopus 로고
    • A stem cell molecular signature
    • Ivanova, N.B. et al. A stem cell molecular signature. Science 298, 601-604 (2002).
    • (2002) Science , vol.298 , pp. 601-604
    • Ivanova, N.B.1
  • 74
    • 0036173770 scopus 로고    scopus 로고
    • Recruitment and activation of caspase-8 by the Huntington-interacting protein Hip-I and a novel partner Hippi
    • Gervais, F.G. et al. Recruitment and activation of caspase-8 by the Huntington-interacting protein Hip-I and a novel partner Hippi. Nat. Cell Biol. 4, 95-105 (2002).
    • (2002) Nat. Cell Biol. , vol.4 , pp. 95-105
    • Gervais, F.G.1


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