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Volumn 1644, Issue 2-3, 2004, Pages 73-81

Role of Bcl-2 family members in invertebrates

Author keywords

Apoptosis; Bcl 2 family; Caenorhabditis elegans; Cell death; Drosophila; Mitochondrion

Indexed keywords

APOPTOTIC PROTEASE ACTIVATING FACTOR 1; BH3 PROTEIN; CASPASE; INTERLEUKIN 1BETA CONVERTING ENZYME; PROTEIN; PROTEIN BCL 2; PROTEIN CED 3; PROTEIN CED 4; PROTEIN CED 9; PROTEIN DROB 1; PROTEIN EGL 1; UNCLASSIFIED DRUG;

EID: 1442310961     PISSN: 01674889     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamcr.2003.09.007     Document Type: Review
Times cited : (48)

References (76)
  • 1
    • 0022497852 scopus 로고
    • Genetic control of programmed cell death in the nematode C. elegans
    • Ellis H.M., Horvitz H.R. Genetic control of programmed cell death in the nematode C. elegans. Cell. 44:1986;817-829.
    • (1986) Cell , vol.44 , pp. 817-829
    • Ellis, H.M.1    Horvitz, H.R.2
  • 2
    • 0026582702 scopus 로고
    • Caenorhabditis elegans gene ced-9 protects cells from programmed cell death
    • Hengartner M.O., Ellis R.E., Horvitz H.R. Caenorhabditis elegans gene ced-9 protects cells from programmed cell death. Nature. 356:1992;494-499.
    • (1992) Nature , vol.356 , pp. 494-499
    • Hengartner, M.O.1    Ellis, R.E.2    Horvitz, H.R.3
  • 3
    • 0032524885 scopus 로고    scopus 로고
    • The C. elegans protein EGL-1 is required for programmed cell death and interacts with the Bcl-2-like protein CED-9
    • Conradt B., Horvitz H.R. The C. elegans protein EGL-1 is required for programmed cell death and interacts with the Bcl-2-like protein CED-9. Cell. 93:1998;519-529.
    • (1998) Cell , vol.93 , pp. 519-529
    • Conradt, B.1    Horvitz, H.R.2
  • 4
    • 0026448963 scopus 로고
    • The Caenorhabditis elegans cell death gene ced-4 encodes a novel protein and is expressed during the period of extensive programmed cell death
    • Yuan J., Horvitz H.R. The Caenorhabditis elegans cell death gene ced-4 encodes a novel protein and is expressed during the period of extensive programmed cell death. Development. 116:1992;309-320.
    • (1992) Development , vol.116 , pp. 309-320
    • Yuan, J.1    Horvitz, H.R.2
  • 5
    • 0027525104 scopus 로고
    • The C. elegans cell death gene ced-3 encodes a protein similar to mammalian interleukin-1 beta-converting enzyme
    • Yuan J., Shaham S., Ledoux S., Ellis H.M., Horvitz H.R. The C. elegans cell death gene ced-3 encodes a protein similar to mammalian interleukin-1 beta-converting enzyme. Cell. 75:1993;641-652.
    • (1993) Cell , vol.75 , pp. 641-652
    • Yuan, J.1    Shaham, S.2    Ledoux, S.3    Ellis, H.M.4    Horvitz, H.R.5
  • 6
    • 0028288277 scopus 로고
    • C. elegans cell survival gene ced-9 encodes a functional homolog of the mammalian proto-oncogene bcl-2
    • Hengartner M.O., Horvitz H.R. C. elegans cell survival gene ced-9 encodes a functional homolog of the mammalian proto-oncogene bcl-2. Cell. 76:1994;665-676.
    • (1994) Cell , vol.76 , pp. 665-676
    • Hengartner, M.O.1    Horvitz, H.R.2
  • 7
    • 0027050145 scopus 로고
    • Prevention of programmed cell death in Caenorhabditis elegans by human bcl-2
    • Vaux D.L., Weissman I.L., Kim S.K. Prevention of programmed cell death in Caenorhabditis elegans by human bcl-2. Science. 258:1992;1955-1957.
    • (1992) Science , vol.258 , pp. 1955-1957
    • Vaux, D.L.1    Weissman, I.L.2    Kim, S.K.3
  • 8
    • 0027449187 scopus 로고
    • Induction of apoptosis in fibroblasts by IL-1 beta-converting enzyme, a mammalian homolog of the C. elegans cell death gene ced-3
    • Miura M., Zhu H., Rotello R., Hartwieg E.A., Yuan J. Induction of apoptosis in fibroblasts by IL-1 beta-converting enzyme, a mammalian homolog of the C. elegans cell death gene ced-3. Cell. 75:1993;653-660.
    • (1993) Cell , vol.75 , pp. 653-660
    • Miura, M.1    Zhu, H.2    Rotello, R.3    Hartwieg, E.A.4    Yuan, J.5
  • 9
    • 0030012008 scopus 로고    scopus 로고
    • Developing Caenorhabditis elegans neurons may contain both cell-death protective and killer activities
    • Shaham S., Horvitz H.R. Developing Caenorhabditis elegans neurons may contain both cell-death protective and killer activities. Genes Dev. 10:1996;578-591.
    • (1996) Genes Dev. , vol.10 , pp. 578-591
    • Shaham, S.1    Horvitz, H.R.2
  • 10
    • 0030776157 scopus 로고    scopus 로고
    • Caenorhabditis elegans CED-9 protein is a bifunctional cell-death inhibitor
    • Xue D., Horvitz H.R. Caenorhabditis elegans CED-9 protein is a bifunctional cell-death inhibitor. Nature. 390:1997;305-308.
    • (1997) Nature , vol.390 , pp. 305-308
    • Xue, D.1    Horvitz, H.R.2
  • 11
    • 0031020227 scopus 로고    scopus 로고
    • Interaction and regulation of subcellular localization of CED-4 by CED-9
    • Wu D., Wallen H.D., Nunez G. Interaction and regulation of subcellular localization of CED-4 by CED-9. Science. 275:1997;1126-1129.
    • (1997) Science , vol.275 , pp. 1126-1129
    • Wu, D.1    Wallen, H.D.2    Nunez, G.3
  • 12
    • 0031034997 scopus 로고    scopus 로고
    • Interaction of CED-4 with CED-3 and CED-9: A molecular framework for cell death
    • Chinnaiyan A.M., O'Rourke K., Lane B.R., Dixit V.M. Interaction of CED-4 with CED-3 and CED-9: a molecular framework for cell death. Science. 275:1997;1122-1126.
    • (1997) Science , vol.275 , pp. 1122-1126
    • Chinnaiyan, A.M.1    O'Rourke, K.2    Lane, B.R.3    Dixit, V.M.4
  • 13
    • 0030826436 scopus 로고    scopus 로고
    • Interaction and regulation of the Caenorhabditis elegans death protease CED-3 by CED-4 and CED-9
    • Wu D., Wallen H.D., Inohara N., Nunez G. Interaction and regulation of the Caenorhabditis elegans death protease CED-3 by CED-4 and CED-9. J. Biol. Chem. 272:1997;21449-21454.
    • (1997) J. Biol. Chem. , vol.272 , pp. 21449-21454
    • Wu, D.1    Wallen, H.D.2    Inohara, N.3    Nunez, G.4
  • 14
    • 0031582671 scopus 로고    scopus 로고
    • Apoptosis. CED-4 is a stranger no more
    • Hengartner M.O. Apoptosis. CED-4 is a stranger no more. Nature. 388:1997;714-715.
    • (1997) Nature , vol.388 , pp. 714-715
    • Hengartner, M.O.1
  • 15
    • 0034282926 scopus 로고    scopus 로고
    • Disruption of the CED-9/CED-4 complex by EGL-1 is a critical step for programmed cell death in Caenorhabditis elegans
    • del P.L., Gonzalez V.M., Inohara N., Ellis R.E., Nunez G. Disruption of the CED-9/CED-4 complex by EGL-1 is a critical step for programmed cell death in Caenorhabditis elegans. J. Biol. Chem. 275:2000;27205-27211.
    • (2000) J. Biol. Chem. , vol.275 , pp. 27205-27211
    • Del, P.L.1    Gonzalez, V.M.2    Inohara, N.3    Ellis, R.E.4    Nunez, G.5
  • 16
    • 0034710971 scopus 로고    scopus 로고
    • Demonstration of the in vivo interaction of key cell death regulators by structure-based design of second-site suppressors
    • Parrish J., Metters H., Chen L., Xue D. Demonstration of the in vivo interaction of key cell death regulators by structure-based design of second-site suppressors. Proc. Natl. Acad. Sci. U. S. A. 97:2000;11916-11921.
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 11916-11921
    • Parrish, J.1    Metters, H.2    Chen, L.3    Xue, D.4
  • 17
    • 0034712042 scopus 로고    scopus 로고
    • Translocation of C. elegans CED-4 to nuclear membranes during programmed cell death
    • Chen F., Hersh B.M., Conradt B., Zhou Z., Riemer D., Gruenbaum Y., Horvitz H.R. Translocation of C. elegans CED-4 to nuclear membranes during programmed cell death. Science. 287:2000;1485-1489.
    • (2000) Science , vol.287 , pp. 1485-1489
    • Chen, F.1    Hersh, B.M.2    Conradt, B.3    Zhou, Z.4    Riemer, D.5    Gruenbaum, Y.6    Horvitz, H.R.7
  • 18
    • 0034641980 scopus 로고    scopus 로고
    • Apoptosis in development
    • Meier P., Finch A., Evan G. Apoptosis in development. Nature. 407:2000;796-801.
    • (2000) Nature , vol.407 , pp. 796-801
    • Meier, P.1    Finch, A.2    Evan, G.3
  • 20
    • 0033193863 scopus 로고    scopus 로고
    • Dark is a Drosophila homologue of Apaf-1/CED-4 and functions in an evolutionarily conserved death pathway
    • Rodriguez A., Oliver H., Zou H., Chen P., Wang X., Abrams J.M. Dark is a Drosophila homologue of Apaf-1/CED-4 and functions in an evolutionarily conserved death pathway. Nat. Cell Biol. 1:1999;272-279.
    • (1999) Nat. Cell Biol. , vol.1 , pp. 272-279
    • Rodriguez, A.1    Oliver, H.2    Zou, H.3    Chen, P.4    Wang, X.5    Abrams, J.M.6
  • 21
    • 0033231614 scopus 로고    scopus 로고
    • Control of the cell death pathway by Dapaf-1, a Drosophila Apaf-1/CED-4-related caspase activator
    • Kanuka H., Sawamoto K., Inohara N., Matsuno K., Okano H., Miura M. Control of the cell death pathway by Dapaf-1, a Drosophila Apaf-1/CED-4-related caspase activator. Mol. Cell. 4:1999;757-769.
    • (1999) Mol. Cell , vol.4 , pp. 757-769
    • Kanuka, H.1    Sawamoto, K.2    Inohara, N.3    Matsuno, K.4    Okano, H.5    Miura, M.6
  • 22
    • 0033231548 scopus 로고    scopus 로고
    • HAC-1, a Drosophila homolog of APAF-1 and CED-4 functions in developmental and radiation-induced apoptosis
    • Zhou L., Song Z., Tittel J., Steller H. HAC-1, a Drosophila homolog of APAF-1 and CED-4 functions in developmental and radiation-induced apoptosis. Mol. Cell. 4:1999;745-755.
    • (1999) Mol. Cell , vol.4 , pp. 745-755
    • Zhou, L.1    Song, Z.2    Tittel, J.3    Steller, H.4
  • 23
    • 0031023782 scopus 로고    scopus 로고
    • DCP-1, a Drosophila cell death protease essential for development
    • Song Z., McCall K., Steller H. DCP-1, a Drosophila cell death protease essential for development. Science. 275:1997;536-540.
    • (1997) Science , vol.275 , pp. 536-540
    • Song, Z.1    McCall, K.2    Steller, H.3
  • 24
    • 0031001092 scopus 로고    scopus 로고
    • Identification of a Drosophila melanogaster ICE/CED-3-related protease, drICE
    • Fraser A.G., Evan G.I. Identification of a Drosophila melanogaster ICE/CED-3-related protease, drICE. EMBO J. 16:1997;2805-2813.
    • (1997) EMBO J. , vol.16 , pp. 2805-2813
    • Fraser, A.G.1    Evan, G.I.2
  • 25
    • 0032530359 scopus 로고    scopus 로고
    • Dredd, a novel effector of the apoptosis activators reaper, grim, and hid in Drosophila
    • Chen P., Rodriguez A., Erskine R., Thach T., Abrams J.M. Dredd, a novel effector of the apoptosis activators reaper, grim, and hid in Drosophila. Dev. Biol. 201:1998;202-216.
    • (1998) Dev. Biol. , vol.201 , pp. 202-216
    • Chen, P.1    Rodriguez, A.2    Erskine, R.3    Thach, T.4    Abrams, J.M.5
  • 27
    • 0032718887 scopus 로고    scopus 로고
    • DECAY, a novel Drosophila caspase related to mammalian caspase-3 and caspase-7
    • Dorstyn L., Read S.H., Quinn L.M., Richardson H., Kumar S. DECAY, a novel Drosophila caspase related to mammalian caspase-3 and caspase-7. J. Biol. Chem. 274:1999;30778-30783.
    • (1999) J. Biol. Chem. , vol.274 , pp. 30778-30783
    • Dorstyn, L.1    Read, S.H.2    Quinn, L.M.3    Richardson, H.4    Kumar, S.5
  • 29
    • 0035037628 scopus 로고    scopus 로고
    • STRICA, a novel Drosophila melanogaster caspase with an unusual serine/threonine-rich prodomain, interacts with DIAP1 and DIAP2
    • Doumanis J., Quinn L., Richardson H., Kumar S. STRICA, a novel Drosophila melanogaster caspase with an unusual serine/threonine-rich prodomain, interacts with DIAP1 and DIAP2. Cell Death Differ. 8:2001;387-394.
    • (2001) Cell Death Differ. , vol.8 , pp. 387-394
    • Doumanis, J.1    Quinn, L.2    Richardson, H.3    Kumar, S.4
  • 31
    • 0034695914 scopus 로고    scopus 로고
    • Debcl, a proapoptotic Bcl-2 homologue, is a component of the Drosophila melanogaster cell death machinery
    • Colussi P.A., Quinn L.M., Huang D.C., Coombe M., Read S.H., Richardson H., Kumar S. Debcl, a proapoptotic Bcl-2 homologue, is a component of the Drosophila melanogaster cell death machinery. J. Cell Biol. 148:2000;703-714.
    • (2000) J. Cell Biol. , vol.148 , pp. 703-714
    • Colussi, P.A.1    Quinn, L.M.2    Huang, D.C.3    Coombe, M.4    Read, S.H.5    Richardson, H.6    Kumar, S.7
  • 32
    • 0034193520 scopus 로고    scopus 로고
    • The Drosophila bcl-2 family member dBorg-1 functions in the apoptotic response to UV-irradiation
    • Brachmann C.B., Jassim O.W., Wachsmuth B.D., Cagan R.L. The Drosophila bcl-2 family member dBorg-1 functions in the apoptotic response to UV-irradiation. Curr. Biol. 10:2000;547-550.
    • (2000) Curr. Biol. , vol.10 , pp. 547-550
    • Brachmann, C.B.1    Jassim, O.W.2    Wachsmuth, B.D.3    Cagan, R.L.4
  • 33
    • 0034282917 scopus 로고    scopus 로고
    • Drosophila pro-apoptotic Bcl-2/Bax homologue reveals evolutionary conservation of cell death mechanisms
    • Zhang H., Huang Q., Ke N., Matsuyama S., Hammock B., Godzik A., Reed J.C. Drosophila pro-apoptotic Bcl-2/Bax homologue reveals evolutionary conservation of cell death mechanisms. J. Biol. Chem. 275:2000;27303-27306.
    • (2000) J. Biol. Chem. , vol.275 , pp. 27303-27306
    • Zhang, H.1    Huang, Q.2    Ke, N.3    Matsuyama, S.4    Hammock, B.5    Godzik, A.6    Reed, J.C.7
  • 35
    • 0029161958 scopus 로고
    • The head involution defective gene of Drosophila melanogaster functions in programmed cell death
    • Grether M.E., Abrams J.M., Agapite J., White K., Steller H. The head involution defective gene of Drosophila melanogaster functions in programmed cell death. Genes Dev. 9:1995;1694-1708.
    • (1995) Genes Dev. , vol.9 , pp. 1694-1708
    • Grether, M.E.1    Abrams, J.M.2    Agapite, J.3    White, K.4    Steller, H.5
  • 36
    • 0029742260 scopus 로고    scopus 로고
    • Grim, a novel cell death gene in Drosophila
    • Chen P., Nordstrom W., Gish B., Abrams J.M. Grim, a novel cell death gene in Drosophila. Genes Dev. 10:1996;1773-1782.
    • (1996) Genes Dev. , vol.10 , pp. 1773-1782
    • Chen, P.1    Nordstrom, W.2    Gish, B.3    Abrams, J.M.4
  • 37
    • 0032582793 scopus 로고    scopus 로고
    • Ras promotes cell survival in Drosophila by downregulating hid expression
    • Kurada P., White K. Ras promotes cell survival in Drosophila by downregulating hid expression. Cell. 95:1998;319-329.
    • (1998) Cell , vol.95 , pp. 319-329
    • Kurada, P.1    White, K.2
  • 38
    • 0032582662 scopus 로고    scopus 로고
    • The Drosophila gene hid is a direct molecular target of Ras-dependent survival signaling
    • Bergmann A., Agapite J., McCall K., Steller H. The Drosophila gene hid is a direct molecular target of Ras-dependent survival signaling. Cell. 95:1998;331-341.
    • (1998) Cell , vol.95 , pp. 331-341
    • Bergmann, A.1    Agapite, J.2    McCall, K.3    Steller, H.4
  • 39
    • 0033588273 scopus 로고    scopus 로고
    • The Drosophila caspase inhibitor DIAP1 is essential for cell survival and is negatively regulated by HID
    • Wang S.L., Hawkins C.J., Yoo S.J., Muller H.A., Hay B.A. The Drosophila caspase inhibitor DIAP1 is essential for cell survival and is negatively regulated by HID. Cell. 98:1999;453-463.
    • (1999) Cell , vol.98 , pp. 453-463
    • Wang, S.L.1    Hawkins, C.J.2    Yoo, S.J.3    Muller, H.A.4    Hay, B.A.5
  • 41
    • 0036307854 scopus 로고    scopus 로고
    • Morgue mediates apoptosis in the Drosophila melanogaster retina by promoting degradation of DIAP1
    • Hays R., Wickline L., Cagan R. Morgue mediates apoptosis in the Drosophila melanogaster retina by promoting degradation of DIAP1. Nat. Cell Biol. 4:2002;425-431.
    • (2002) Nat. Cell Biol. , vol.4 , pp. 425-431
    • Hays, R.1    Wickline, L.2    Cagan, R.3
  • 42
    • 0036300083 scopus 로고    scopus 로고
    • Regulation of Drosophila IAP1 degradation and apoptosis by reaper and ubcD1
    • Ryoo H.D., Bergmann A., Gonen H., Ciechanover A., Steller H. Regulation of Drosophila IAP1 degradation and apoptosis by reaper and ubcD1. Nat. Cell Biol. 4:2002;432-438.
    • (2002) Nat. Cell Biol. , vol.4 , pp. 432-438
    • Ryoo, H.D.1    Bergmann, A.2    Gonen, H.3    Ciechanover, A.4    Steller, H.5
  • 45
    • 0036303143 scopus 로고    scopus 로고
    • Reaper eliminates IAP proteins through stimulated IAP degradation and generalized translational inhibition
    • Holley C.L., Olson M.R., Colon R.D., Kornbluth S. Reaper eliminates IAP proteins through stimulated IAP degradation and generalized translational inhibition. Nat. Cell Biol. 4:2002;439-444.
    • (2002) Nat. Cell Biol. , vol.4 , pp. 439-444
    • Holley, C.L.1    Olson, M.R.2    Colon, R.D.3    Kornbluth, S.4
  • 46
    • 0036712650 scopus 로고    scopus 로고
    • Reaper-mediated inhibition of DIAP1-induced DTRAF1 degradation results in activation of JNK in Drosophila
    • Kuranaga E., Kanuka H., Igaki T., Sawamoto K., Ichijo H., Okano H., Miura M. Reaper-mediated inhibition of DIAP1-induced DTRAF1 degradation results in activation of JNK in Drosophila. Nat. Cell Biol. 4:2002;705-710.
    • (2002) Nat. Cell Biol. , vol.4 , pp. 705-710
    • Kuranaga, E.1    Kanuka, H.2    Igaki, T.3    Sawamoto, K.4    Ichijo, H.5    Okano, H.6    Miura, M.7
  • 49
    • 0037154014 scopus 로고    scopus 로고
    • The damage-responsive Drosophila gene sickle encodes a novel IAP binding protein similar to but distinct from reaper, grim, and hid
    • Christich A., Kauppila S., Chen P., Sogame N., Ho S.I., Abrams J.M. The damage-responsive Drosophila gene sickle encodes a novel IAP binding protein similar to but distinct from reaper, grim, and hid. Curr. Biol. 12:2002;137-140.
    • (2002) Curr. Biol. , vol.12 , pp. 137-140
    • Christich, A.1    Kauppila, S.2    Chen, P.3    Sogame, N.4    Ho, S.I.5    Abrams, J.M.6
  • 51
    • 0037162294 scopus 로고    scopus 로고
    • Evolution of TNF signaling mechanisms: JNK-dependent apoptosis triggered by Eiger, the Drosophila homolog of the TNF superfamily
    • Moreno E., Yan M., Basler K. Evolution of TNF signaling mechanisms: JNK-dependent apoptosis triggered by Eiger, the Drosophila homolog of the TNF superfamily. Curr. Biol. 12:2002;1263-1268.
    • (2002) Curr. Biol. , vol.12 , pp. 1263-1268
    • Moreno, E.1    Yan, M.2    Basler, K.3
  • 53
    • 0037047362 scopus 로고    scopus 로고
    • Wengen, a member of the Drosophila tumor necrosis factor receptor superfamily, is required for Eiger signaling
    • Kanda H., Igaki T., Kanuka H., Yagi T., Miura M. Wengen, a member of the Drosophila tumor necrosis factor receptor superfamily, is required for Eiger signaling. J. Biol. Chem. 277:2002;28372-28375.
    • (2002) J. Biol. Chem. , vol.277 , pp. 28372-28375
    • Kanda, H.1    Igaki, T.2    Kanuka, H.3    Yagi, T.4    Miura, M.5
  • 54
    • 0029906828 scopus 로고    scopus 로고
    • BAX-induced cell death may not require interleukin 1 beta-converting enzyme-like proteases
    • Xiang J., Chao D.T., Korsmeyer S.J. BAX-induced cell death may not require interleukin 1 beta-converting enzyme-like proteases. Proc. Natl. Acad. Sci. U. S. A. 93:1996;14559-14563.
    • (1996) Proc. Natl. Acad. Sci. U. S. A. , vol.93 , pp. 14559-14563
    • Xiang, J.1    Chao, D.T.2    Korsmeyer, S.J.3
  • 55
    • 0031033274 scopus 로고    scopus 로고
    • Inhibition of Ced-3/ICE-related proteases does not prevent cell death induced by oncogenes, DNA damage, or the Bcl-2 homologue Bak
    • McCarthy N.J., Whyte M.K., Gilbert C.S., Evan G.I. Inhibition of Ced-3/ICE-related proteases does not prevent cell death induced by oncogenes, DNA damage, or the Bcl-2 homologue Bak. J. Cell Biol. 136:1997;215-227.
    • (1997) J. Cell Biol. , vol.136 , pp. 215-227
    • McCarthy, N.J.1    Whyte, M.K.2    Gilbert, C.S.3    Evan, G.I.4
  • 56
    • 0041813273 scopus 로고    scopus 로고
    • Buffy, a Drosophila Bcl-2 protein, has anti-apoptotic and cell cycle inhibitory functions
    • Quinn L., Coombe M., Mills K., Daish T., Colussi P., Kumar S., Richardson H. Buffy, a Drosophila Bcl-2 protein, has anti-apoptotic and cell cycle inhibitory functions. EMBO J. 22:2003;3568-3579.
    • (2003) EMBO J. , vol.22 , pp. 3568-3579
    • Quinn, L.1    Coombe, M.2    Mills, K.3    Daish, T.4    Colussi, P.5    Kumar, S.6    Richardson, H.7
  • 57
    • 0030581151 scopus 로고    scopus 로고
    • Induction of apoptotic program in cell-free extracts: Requirement for dATP and cytochrome c
    • Liu X., Kim C.N., Yang J., Jemmerson R., Wang X. Induction of apoptotic program in cell-free extracts: requirement for dATP and cytochrome c. Cell. 86:1996;147-157.
    • (1996) Cell , vol.86 , pp. 147-157
    • Liu, X.1    Kim, C.N.2    Yang, J.3    Jemmerson, R.4    Wang, X.5
  • 58
    • 0034616945 scopus 로고    scopus 로고
    • Smac, a mitochondrial protein that promotes cytochrome c-dependent caspase activation by eliminating IAP inhibition
    • Du C., Fang M., Li Y., Li L., Wang X. Smac, a mitochondrial protein that promotes cytochrome c-dependent caspase activation by eliminating IAP inhibition. Cell. 102:2000;33-42.
    • (2000) Cell , vol.102 , pp. 33-42
    • Du, C.1    Fang, M.2    Li, Y.3    Li, L.4    Wang, X.5
  • 60
    • 0034785591 scopus 로고    scopus 로고
    • A serine protease, HtrA2, is released from the mitochondria and interacts with XIAP, inducing cell death
    • Suzuki Y., Imai Y., Nakayama H., Takahashi K., Takio K., Takahashi R. A serine protease, HtrA2, is released from the mitochondria and interacts with XIAP, inducing cell death. Mol. Cell. 8:2001;613-621.
    • (2001) Mol. Cell , vol.8 , pp. 613-621
    • Suzuki, Y.1    Imai, Y.2    Nakayama, H.3    Takahashi, K.4    Takio, K.5    Takahashi, R.6
  • 66
    • 0035811511 scopus 로고    scopus 로고
    • Mitochondrial endonuclease G is important for apoptosis in C. elegans
    • Parrish J., Li L., Klotz K., Ledwich D., Wang X., Xue D. Mitochondrial endonuclease G is important for apoptosis in C. elegans. Nature. 412:2001;90-94.
    • (2001) Nature , vol.412 , pp. 90-94
    • Parrish, J.1    Li, L.2    Klotz, K.3    Ledwich, D.4    Wang, X.5    Xue, D.6
  • 67
    • 0035811496 scopus 로고    scopus 로고
    • Endonuclease G is an apoptotic DNase when released from mitochondria
    • Li L.Y., Luo X., Wang X. Endonuclease G is an apoptotic DNase when released from mitochondria. Nature. 412:2001;95-99.
    • (2001) Nature , vol.412 , pp. 95-99
    • Li, L.Y.1    Luo, X.2    Wang, X.3
  • 68
    • 0037159784 scopus 로고    scopus 로고
    • Mechanisms of AIF-mediated apoptotic DNA degradation in Caenorhabditis elegans
    • Wang X., Yang C., Chai J., Shi Y., Xue D. Mechanisms of AIF-mediated apoptotic DNA degradation in Caenorhabditis elegans. Science. 298:2002;1587-1592.
    • (2002) Science , vol.298 , pp. 1587-1592
    • Wang, X.1    Yang, C.2    Chai, J.3    Shi, Y.4    Xue, D.5
  • 69
    • 0033593791 scopus 로고    scopus 로고
    • Altered cytochrome c display precedes apoptotic cell death in Drosophila
    • Varkey J., Chen P., Jemmerson R., Abrams J.M. Altered cytochrome c display precedes apoptotic cell death in Drosophila. J. Cell Biol. 144:1999;701-710.
    • (1999) J. Cell Biol. , vol.144 , pp. 701-710
    • Varkey, J.1    Chen, P.2    Jemmerson, R.3    Abrams, J.M.4
  • 70
    • 0037128924 scopus 로고    scopus 로고
    • The role of cytochrome c in caspase activation in Drosophila melanogaster cells
    • Dorstyn L., Read S., Cakouros D., Huh J.R., Hay B.A., Kumar S. The role of cytochrome c in caspase activation in Drosophila melanogaster cells. J. Cell Biol. 156:2002;1089-1098.
    • (2002) J. Cell Biol. , vol.156 , pp. 1089-1098
    • Dorstyn, L.1    Read, S.2    Cakouros, D.3    Huh, J.R.4    Hay, B.A.5    Kumar, S.6
  • 71
    • 0037654554 scopus 로고    scopus 로고
    • Caspase activity and a specific cytochrome C are required for sperm differentiation in Drosophila
    • Arama E., Agapite J., Steller H. Caspase activity and a specific cytochrome C are required for sperm differentiation in Drosophila. Dev. Cell Biol. 4:2003;687-697.
    • (2003) Dev. Cell Biol. , vol.4 , pp. 687-697
    • Arama, E.1    Agapite, J.2    Steller, H.3
  • 72
    • 0037128923 scopus 로고    scopus 로고
    • The role of ARK in stress-induced apoptosis in Drosophila cells
    • Zimmermann K.C., Ricci J.E., Droin N.M., Green D.R. The role of ARK in stress-induced apoptosis in Drosophila cells. J. Cell Biol. 156:2002;1077-1087.
    • (2002) J. Cell Biol. , vol.156 , pp. 1077-1087
    • Zimmermann, K.C.1    Ricci, J.E.2    Droin, N.M.3    Green, D.R.4
  • 74
    • 0028291141 scopus 로고
    • Activation of C. elegans cell death protein CED-9 by an amino acid substitution in a domain conserved in Bcl-2
    • Hengartner M.O., Horvitz H.R. Activation of C. elegans cell death protein CED-9 by an amino acid substitution in a domain conserved in Bcl-2. Nature. 369:1994;318-320.
    • (1994) Nature , vol.369 , pp. 318-320
    • Hengartner, M.O.1    Horvitz, H.R.2
  • 75
    • 0037189566 scopus 로고    scopus 로고
    • Down-regulation of DIAP1 triggers a novel Drosophila cell death pathway mediated by Dark and DRONC
    • Igaki T., Yamamoto-Goto Y., Tokushige N., Kanda H., Miura M. Down-regulation of DIAP1 triggers a novel Drosophila cell death pathway mediated by Dark and DRONC. J. Biol. Chem. 277:2002;23103-23106.
    • (2002) J. Biol. Chem. , vol.277 , pp. 23103-23106
    • Igaki, T.1    Yamamoto-Goto, Y.2    Tokushige, N.3    Kanda, H.4    Miura, M.5
  • 76
    • 0346668315 scopus 로고    scopus 로고
    • The Drosophila DIAP1 protein is required to prevent accumulation of a continuously generated, processed form of the apical caspase DRONC
    • Muro I., Hay B.A., Clem R.J. The Drosophila DIAP1 protein is required to prevent accumulation of a continuously generated, processed form of the apical caspase DRONC. J. Biol. Chem. 277:2002;49644-49650.
    • (2002) J. Biol. Chem. , vol.277 , pp. 49644-49650
    • Muro, I.1    Hay, B.A.2    Clem, R.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.