메뉴 건너뛰기




Volumn 116, Issue 2, 2004, Pages 205-219

Cell Death: Critical Control Points

Author keywords

[No Author keywords available]

Indexed keywords

APOPTOTIC PROTEASE ACTIVATING FACTOR 1; CALPAIN; CASPASE; GRANZYME A; GRANZYME B; INHIBITOR OF APOPTOSIS PROTEIN; PROTEIN BCL 2; PROTEIN MCL 1;

EID: 0842281645     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0092-8674(04)00046-7     Document Type: Review
Times cited : (4234)

References (162)
  • 1
    • 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., Akey C.W. Three-dimensional structure of the apoptosome. implications for assembly, procaspase-9 binding, and activation Mol. Cell. 9:2002;423-432.
    • (2002) Mol. 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
  • 2
    • 0035831462 scopus 로고    scopus 로고
    • Granzyme B induces BID-mediated cytochrome c release and mitochondrial permeability transition
    • Alimonti J.B., Shi L., Baijal P.K., Greenberg A.H. Granzyme B induces BID-mediated cytochrome c release and mitochondrial permeability transition. J. Biol. Chem. 276:2001;6974-6982.
    • (2001) J. Biol. Chem. , vol.276 , pp. 6974-6982
    • Alimonti, J.B.1    Shi, L.2    Baijal, P.K.3    Greenberg, A.H.4
  • 3
    • 0032575714 scopus 로고    scopus 로고
    • Death receptors: Signaling and modulation
    • Ashkenazi A., Dixit V.M. Death receptors. signaling and modulation Science. 281:1998;1305-1308.
    • (1998) Science , vol.281 , pp. 1305-1308
    • Ashkenazi, A.1    Dixit, V.M.2
  • 4
    • 0021934042 scopus 로고
    • Cloning the chromosomal breakpoint of t(14;18) human lymphomas: Clustering around JH on chromosome 14 and near a transcriptional unit on 18
    • Bakhshi A., Jensen J.P., Goldman P., Wright J.J., McBride O.W., Epstein A.L., Korsmeyer S.J. Cloning the chromosomal breakpoint of t(14;18) human lymphomas. clustering around JH on chromosome 14 and near a transcriptional unit on 18 Cell. 41:1985;899-906.
    • (1985) Cell , vol.41 , pp. 899-906
    • Bakhshi, A.1    Jensen, J.P.2    Goldman, P.3    Wright, J.J.4    Mcbride, O.W.5    Epstein, A.L.6    Korsmeyer, S.J.7
  • 6
    • 0042865992 scopus 로고    scopus 로고
    • Suppression of CED-3-independent apoptosis by mitochondrial betaNAC in Caenorhabditis elegans
    • Bloss T.A., Witze E.S., Rothman J.H. Suppression of CED-3-independent apoptosis by mitochondrial betaNAC in Caenorhabditis elegans. Nature. 424:2003;1066-1071.
    • (2003) Nature , vol.424 , pp. 1066-1071
    • Bloss, T.A.1    Witze, E.S.2    Rothman, J.H.3
  • 8
    • 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
  • 9
    • 0037417334 scopus 로고    scopus 로고
    • Caspase cleavage product of BAP31 induces mitochondrial fission through endoplasmic reticulum calcium signals, enhancing cytochrome c release to the cytosol
    • Breckenridge D.G., Stojanovic M., Marcellus R.C., Shore G.C. Caspase cleavage product of BAP31 induces mitochondrial fission through endoplasmic reticulum calcium signals, enhancing cytochrome c release to the cytosol. J. Cell Biol. 160:2003;1115-1127.
    • (2003) J. Cell Biol. , vol.160 , pp. 1115-1127
    • Breckenridge, D.G.1    Stojanovic, M.2    Marcellus, R.C.3    Shore, G.C.4
  • 10
    • 0037418839 scopus 로고    scopus 로고
    • Bantam encodes a developmentally regulated microRNA that controls cell proliferation and regulates the pro-apoptotic gene hid in Drosophila
    • Brennecke J., Hipfner D.R., Stark A., Russell R.B., Cohen S.M. bantam encodes a developmentally regulated microRNA that controls cell proliferation and regulates the pro-apoptotic gene hid in Drosophila. Cell. 113:2003;25-36.
    • (2003) Cell , vol.113 , pp. 25-36
    • Brennecke, J.1    Hipfner, D.R.2    Stark, A.3    Russell, R.B.4    Cohen, S.M.5
  • 11
    • 0016063911 scopus 로고
    • The genetics of Caenorhabditis elegans
    • Brenner S. The genetics of Caenorhabditis elegans. Genetics. 77:1974;71-94.
    • (1974) Genetics , vol.77 , pp. 71-94
    • Brenner, S.1
  • 12
    • 0034682695 scopus 로고    scopus 로고
    • Apoptosis. Mitochondria-the death signal integrators
    • Brenner C., Kroemer G. Apoptosis. Mitochondria-the death signal integrators. Science. 289:2000;1150-1151.
    • (2000) Science , vol.289 , pp. 1150-1151
    • Brenner, C.1    Kroemer, G.2
  • 13
    • 0034710649 scopus 로고    scopus 로고
    • Structural and biochemical basis of apoptotic activation by Smac/DIABLO
    • Chai J., Du C., Wu J.W., Kyin S., Wang X., Shi Y. Structural and biochemical basis of apoptotic activation by Smac/DIABLO. Nature. 406:2000;855-862.
    • (2000) Nature , vol.406 , pp. 855-862
    • Chai, J.1    Du, C.2    Wu, J.W.3    Kyin, S.4    Wang, X.5    Shi, Y.6
  • 15
    • 0029742260 scopus 로고    scopus 로고
    • Grim, a novel cell death gene in Drosophila
    • a
    • Chen P., Nordstrom W., Gish B., Abrams J.M. grim, a novel cell death gene in Drosophila. Genes Dev. 10:1996;1773-1782. a.
    • (1996) Genes Dev. , vol.10 , pp. 1773-1782
    • Chen, P.1    Nordstrom, W.2    Gish, B.3    Abrams, J.M.4
  • 16
    • 0029802591 scopus 로고    scopus 로고
    • P53 levels, functional domains, and DNA damage determine the extent of the apoptotic response of tumor cells
    • b
    • Chen X., Ko L.J., Jayaraman L., Prives C. p53 levels, functional domains, and DNA damage determine the extent of the apoptotic response of tumor cells. Genes Dev. 10:1996;2438-2451. b.
    • (1996) Genes Dev. , vol.10 , pp. 2438-2451
    • Chen, X.1    Ko, L.J.2    Jayaraman, L.3    Prives, C.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
    • 0034786019 scopus 로고    scopus 로고
    • BCL-2, BCL-X(L) sequester BH3 domain-only molecules preventing BAX- and BAK-mediated mitochondrial apoptosis
    • Cheng E.H., Wei M.C., Weiler S., Flavell R.A., Mak T.W., Lindsten T., Korsmeyer S.J. BCL-2, BCL-X(L) sequester BH3 domain-only molecules preventing BAX- and BAK-mediated mitochondrial apoptosis. Mol. Cell. 8:2001;705-711.
    • (2001) Mol. Cell , vol.8 , pp. 705-711
    • Cheng, E.H.1    Wei, M.C.2    Weiler, S.3    Flavell, R.A.4    Mak, T.W.5    Lindsten, T.6    Korsmeyer, S.J.7
  • 20
    • 0842278331 scopus 로고    scopus 로고
    • Direct activation of BAX by p53 mediates mitochondrial membrane permeabilization and apoptosis
    • Chipuk J.E., Mauer U., Green D.R., Schuler M. Direct activation of BAX by p53 mediates mitochondrial membrane permeabilization and apoptosis. Science. in press:2004.
    • (2004) Science
    • Chipuk, J.E.1    Mauer, U.2    Green, D.R.3    Schuler, M.4
  • 21
    • 0028824266 scopus 로고
    • A novel Bcl-2 related gene, Bfl-1, is overexpressed in stomach cancer and preferentially expressed in bone marrow
    • Choi S.S., Park I.C., Yun J.W., Sung Y.C., Hong S.I., Shin H.S. A novel Bcl-2 related gene, Bfl-1, is overexpressed in stomach cancer and preferentially expressed in bone marrow. Oncogene. 11:1995;1693-1698.
    • (1995) Oncogene , vol.11 , pp. 1693-1698
    • Choi, S.S.1    Park, I.C.2    Yun, J.W.3    Sung, Y.C.4    Hong, S.I.5    Shin, H.S.6
  • 23
    • 0345055662 scopus 로고
    • Nucleotide sequence of a t(14;18) chromosomal breakpoint in follicular lymphoma and demonstration of a breakpoint-cluster region near a transcriptionally active locus on chromosome 18
    • Cleary M.L., Sklar J. Nucleotide sequence of a t(14;18) chromosomal breakpoint in follicular lymphoma and demonstration of a breakpoint-cluster region near a transcriptionally active locus on chromosome 18. Proc. Natl. Acad. Sci. USA. 82:1985;7439-7443.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 7439-7443
    • Cleary, M.L.1    Sklar, J.2
  • 24
    • 0026344133 scopus 로고
    • Prevention of apoptosis by a baculovirus gene during infection of insect cells
    • Clem R.J., Fechheimer M., Miller L.K. Prevention of apoptosis by a baculovirus gene during infection of insect cells. Science. 254:1991;1388-1390.
    • (1991) Science , vol.254 , pp. 1388-1390
    • Clem, R.J.1    Fechheimer, M.2    Miller, L.K.3
  • 25
    • 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
  • 28
    • 0037107134 scopus 로고    scopus 로고
    • Exogenous smac induces competence and permits caspase activation in sympathetic neurons
    • Deshmukh M., Du C., Wang X., Johnson E.M. Jr. Exogenous smac induces competence and permits caspase activation in sympathetic neurons. J. Neurosci. 22:2002;8018-8027.
    • (2002) J. Neurosci. , vol.22 , pp. 8018-8027
    • Deshmukh, M.1    Du, C.2    Wang, X.3    Johnson, E.M.Jr.4
  • 29
    • 0030810926 scopus 로고    scopus 로고
    • X-linked IAP is a direct inhibitor of cell-death proteases
    • Deveraux Q.L., Takahashi R., Salvesen G.S., Reed J.C. X-linked IAP is a direct inhibitor of cell-death proteases. Nature. 388:1997;300-304.
    • (1997) Nature , vol.388 , pp. 300-304
    • Deveraux, Q.L.1    Takahashi, R.2    Salvesen, G.S.3    Reed, J.C.4
  • 31
    • 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
  • 32
    • 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
  • 33
    • 0026051936 scopus 로고
    • Genes required for the engulfment of cell corpses during programmed cell death in Caenorhabditis elegans
    • Ellis R.E., Jacobson D.M., Horvitz H.R. Genes required for the engulfment of cell corpses during programmed cell death in Caenorhabditis elegans. Genetics. 129:1991;79-94.
    • (1991) Genetics , vol.129 , pp. 79-94
    • Ellis, R.E.1    Jacobson, D.M.2    Horvitz, H.R.3
  • 34
    • 0031888955 scopus 로고    scopus 로고
    • A caspase-activated DNase that degrades DNA during apoptosis, and its inhibitor ICAD
    • Enari M., Sakahira H., Yokoyama H., Okawa K., Iwamatsu A., Nagata S. A caspase-activated DNase that degrades DNA during apoptosis, and its inhibitor ICAD. Nature. 391:1998;43-50.
    • (1998) Nature , vol.391 , pp. 43-50
    • Enari, M.1    Sakahira, H.2    Yokoyama, H.3    Okawa, K.4    Iwamatsu, A.5    Nagata, S.6
  • 35
    • 0034795258 scopus 로고    scopus 로고
    • Bid, a widely expressed pro-apoptotic protein of the Bcl-2 family, displays lipid transfer activity
    • Esposti M.D., Erler J.T., Hickman J.A., Dive C. Bid, a widely expressed pro-apoptotic protein of the Bcl-2 family, displays lipid transfer activity. Mol. Cell. Biol. 21:2001;7268-7276.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 7268-7276
    • Esposti, M.D.1    Erler, J.T.2    Hickman, J.A.3    Dive, C.4
  • 37
    • 0034644508 scopus 로고    scopus 로고
    • Insights into programmed cell death through structural biology
    • Fesik S.W. Insights into programmed cell death through structural biology. Cell. 103:2000;273-282.
    • (2000) Cell , vol.103 , pp. 273-282
    • Fesik, S.W.1
  • 42
    • 0033781027 scopus 로고    scopus 로고
    • The coordinate release of cytochrome c during apoptosis is rapid, complete and kinetically invariant
    • Goldstein J.C., Waterhouse N.J., Juin P., Evan G.I., Green D.R. The coordinate release of cytochrome c during apoptosis is rapid, complete and kinetically invariant. Nat. Cell Biol. 2:2000;156-162.
    • (2000) Nat. Cell Biol. , vol.2 , pp. 156-162
    • Goldstein, J.C.1    Waterhouse, N.J.2    Juin, P.3    Evan, G.I.4    Green, D.R.5
  • 43
    • 0034983918 scopus 로고    scopus 로고
    • Inhibition of early apoptotic events by Akt/PKB is dependent on the first committed step of glycolysis and mitochondrial hexokinase
    • Gottlob K., Majewski N., Kennedy S., Kandel E., Robey R.B., Hay N. Inhibition of early apoptotic events by Akt/PKB is dependent on the first committed step of glycolysis and mitochondrial hexokinase. Genes Dev. 15:2001;1406-1418.
    • (2001) Genes Dev. , vol.15 , pp. 1406-1418
    • Gottlob, K.1    Majewski, N.2    Kennedy, S.3    Kandel, E.4    Robey, R.B.5    Hay, N.6
  • 44
    • 0034651791 scopus 로고    scopus 로고
    • Induction of apoptosis by Drosophila reaper, hid and grim through inhibition of IAP function
    • Goyal L., McCall K., Agapite J., Hartwieg E., Steller H. Induction of apoptosis by Drosophila reaper, hid and grim through inhibition of IAP function. EMBO J. 19:2000;589-597.
    • (2000) EMBO J. , vol.19 , pp. 589-597
    • Goyal, L.1    Mccall, K.2    Agapite, J.3    Hartwieg, E.4    Steller, H.5
  • 47
    • 0029092356 scopus 로고
    • Induction of apoptosis in HeLa cells by trans-activation-deficient p53
    • Haupt Y., Rowan S., Shaulian E., Vousden K.H., Oren M. Induction of apoptosis in HeLa cells by trans-activation-deficient p53. Genes Dev. 9:1995;2170-2183.
    • (1995) Genes Dev. , vol.9 , pp. 2170-2183
    • Haupt, Y.1    Rowan, S.2    Shaulian, E.3    Vousden, K.H.4    Oren, M.5
  • 48
    • 0028291141 scopus 로고
    • Activation of C. elegans cell death protein CED-9 by an amino-acid substitution in a domain conserved in Bcl-2
    • a
    • 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. a.
    • (1994) Nature , vol.369 , pp. 318-320
    • Hengartner, M.O.1    Horvitz, H.R.2
  • 49
    • 0028288277 scopus 로고
    • C. elegans cell survival gene ced-9 encodes a functional homolog of the mammalian proto-oncogene bcl-2
    • b
    • 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. b.
    • (1994) Cell , vol.76 , pp. 665-676
    • Hengartner, M.O.1    Horvitz, H.R.2
  • 50
    • 0028258577 scopus 로고
    • Cytotoxic lymphocytes require granzyme B for the rapid induction of DNA fragmentation and apoptosis in allogeneic target cells
    • Heusel J.W., Wesselschmidt R.L., Shresta S., Russell J.H., Ley T.J. Cytotoxic lymphocytes require granzyme B for the rapid induction of DNA fragmentation and apoptosis in allogeneic target cells. Cell. 76:1994;977-987.
    • (1994) Cell , vol.76 , pp. 977-987
    • Heusel, J.W.1    Wesselschmidt, R.L.2    Shresta, S.3    Russell, J.H.4    Ley, T.J.5
  • 51
    • 0025204548 scopus 로고
    • Bcl-2 is an inner mitochondrial membrane protein that blocks programmed cell death
    • Hockenbery D., Nunez G., Milliman C., Schreiber R.D., Korsmeyer S.J. Bcl-2 is an inner mitochondrial membrane protein that blocks programmed cell death. Nature. 348:1990;334-336.
    • (1990) Nature , vol.348 , pp. 334-336
    • Hockenbery, D.1    Nunez, G.2    Milliman, C.3    Schreiber, R.D.4    Korsmeyer, S.J.5
  • 52
    • 0035849895 scopus 로고    scopus 로고
    • Engulfment genes cooperate with ced-3 to promote cell death in Caenorhabditis elegans
    • Hoeppner D.J., Hengartner M.O., Schnabel R. Engulfment genes cooperate with ced-3 to promote cell death in Caenorhabditis elegans. Nature. 412:2001;202-206.
    • (2001) Nature , vol.412 , pp. 202-206
    • Hoeppner, D.J.1    Hengartner, M.O.2    Schnabel, R.3
  • 53
    • 0029007855 scopus 로고
    • The TNF receptor 1-associated protein TRADD signals cell death and NF-kappa B activation
    • Hsu H., Xiong J., Goeddel D.V. The TNF receptor 1-associated protein TRADD signals cell death and NF-kappa B activation. Cell. 81:1995;495-504.
    • (1995) Cell , vol.81 , pp. 495-504
    • Hsu, H.1    Xiong, J.2    Goeddel, D.V.3
  • 54
    • 0035831022 scopus 로고    scopus 로고
    • Structural basis of caspase inhibition by XIAP: Differential roles of the linker versus the BIR domain
    • Huang Y., Park Y.C., Rich R.L., Segal D., Myszka D.G., Wu H. Structural basis of caspase inhibition by XIAP. differential roles of the linker versus the BIR domain Cell. 104:2001;781-790.
    • (2001) Cell , vol.104 , pp. 781-790
    • Huang, Y.1    Park, Y.C.2    Rich, R.L.3    Segal, D.4    Myszka, D.G.5    Wu, H.6
  • 55
    • 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. 268:1993;10932-10937.
    • (1993) J. Biol. Chem. , vol.268 , pp. 10932-10937
    • Itoh, N.1    Nagata, S.2
  • 59
    • 0033562966 scopus 로고    scopus 로고
    • Stress signaling from the lumen of the endoplasmic reticulum: Coordination of gene transcriptional and translational controls
    • Kaufman R.J. Stress signaling from the lumen of the endoplasmic reticulum. coordination of gene transcriptional and translational controls Genes Dev. 13:1999;1211-1233.
    • (1999) Genes Dev. , vol.13 , pp. 1211-1233
    • Kaufman, R.J.1
  • 60
    • 0015383455 scopus 로고
    • Apoptosis: A basic biological phenomenon with wide-ranging implications in tissue kinetics
    • Kerr J.F., Wyllie A.H., Currie A.R. Apoptosis. a basic biological phenomenon with wide-ranging implications in tissue kinetics Br. J. Cancer. 26:1972;239-257.
    • (1972) Br. J. Cancer , vol.26 , pp. 239-257
    • Kerr, J.F.1    Wyllie, A.H.2    Currie, A.R.3
  • 61
    • 0028883850 scopus 로고
    • Cytotoxicity-dependent APO-1 (Fas/CD95)-associated proteins form a death-inducing signaling complex (DISC) with the receptor
    • Kischkel F.C., Hellbardt S., Behrmann I., Germer M., Pawlita M., Krammer P.H., Peter M.E. Cytotoxicity-dependent APO-1 (Fas/CD95)-associated proteins form a death-inducing signaling complex (DISC) with the receptor. EMBO J. 14:1995;5579-5588.
    • (1995) EMBO J. , vol.14 , pp. 5579-5588
    • Kischkel, F.C.1    Hellbardt, S.2    Behrmann, I.3    Germer, M.4    Pawlita, M.5    Krammer, P.H.6    Peter, M.E.7
  • 63
    • 0034537290 scopus 로고    scopus 로고
    • Autophagy as a regulated pathway of cellular degradation
    • Klionsky D.J., Emr S.D. Autophagy as a regulated pathway of cellular degradation. Science. 290:2000;1717-1721.
    • (2000) Science , vol.290 , pp. 1717-1721
    • Klionsky, D.J.1    Emr, S.D.2
  • 65
    • 0027480450 scopus 로고
    • MCL1, a gene expressed in programmed myeloid cell differentiation, has sequence similarity to BCL2
    • Kozopas K.M., Yang T., Buchan H.L., Zhou P., Craig R.W. MCL1, a gene expressed in programmed myeloid cell differentiation, has sequence similarity to BCL2. Proc. Natl. Acad. Sci. USA. 90:1993;3516-3520.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 3516-3520
    • Kozopas, K.M.1    Yang, T.2    Buchan, H.L.3    Zhou, P.4    Craig, R.W.5
  • 66
  • 67
    • 0037162833 scopus 로고    scopus 로고
    • Requirement for caspase-2 in stress-induced apoptosis before mitochondrial permeabilization
    • Lassus P., Opitz-Araya X., Lazebnik Y. Requirement for caspase-2 in stress-induced apoptosis before mitochondrial permeabilization. Science. 297:2002;1352-1354.
    • (2002) Science , vol.297 , pp. 1352-1354
    • Lassus, P.1    Opitz-Araya, X.2    Lazebnik, Y.3
  • 69
    • 0030715323 scopus 로고    scopus 로고
    • Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade
    • Li P., Nijhawan D., Budihardjo I., Srinivasula S.M., Ahmad M., Alnemri E.S., Wang X. Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade. Cell. 91:1997;479-489.
    • (1997) Cell , vol.91 , pp. 479-489
    • Li, P.1    Nijhawan, D.2    Budihardjo, I.3    Srinivasula, S.M.4    Ahmad, M.5    Alnemri, E.S.6    Wang, X.7
  • 70
    • 0032555697 scopus 로고    scopus 로고
    • Cleavage of BID by caspase 8 mediates the mitochondrial damage in the Fas pathway of apoptosis
    • Li H., Zhu H., Xu C.J., Yuan J. Cleavage of BID by caspase 8 mediates the mitochondrial damage in the Fas pathway of apoptosis. Cell. 94:1998;491-501.
    • (1998) Cell , vol.94 , pp. 491-501
    • Li, H.1    Zhu, H.2    Xu, C.J.3    Yuan, J.4
  • 71
    • 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
  • 73
    • 0038725690 scopus 로고    scopus 로고
    • The ABCs of granule-mediated cytotoxicity: New weapons in the arsenal
    • Lieberman J. The ABCs of granule-mediated cytotoxicity. new weapons in the arsenal Nat. Rev. Immunol. 3:2003;361-370.
    • (2003) Nat. Rev. Immunol. , vol.3 , pp. 361-370
    • Lieberman, J.1
  • 75
    • 0032511234 scopus 로고    scopus 로고
    • Candidate adaptor protein CED-6 promotes the engulfment of apoptotic cells in C. elegans
    • Liu Q.A., Hengartner M.O. Candidate adaptor protein CED-6 promotes the engulfment of apoptotic cells in C. elegans. Cell. 93:1998;961-972.
    • (1998) Cell , vol.93 , pp. 961-972
    • Liu, Q.A.1    Hengartner, M.O.2
  • 76
    • 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
  • 77
    • 0030916417 scopus 로고    scopus 로고
    • DFF, a heterodimeric protein that functions downstream of caspase-3 to trigger DNA fragmentation during apoptosis
    • Liu X., Zou H., Slaughter C., Wang X. DFF, a heterodimeric protein that functions downstream of caspase-3 to trigger DNA fragmentation during apoptosis. Cell. 89:1997;175-184.
    • (1997) Cell , vol.89 , pp. 175-184
    • Liu, X.1    Zou, H.2    Slaughter, C.3    Wang, X.4
  • 79
    • 0001139444 scopus 로고
    • Programmed cell death-I. Cytology of degeneration in the intersegmental muscles of the pernyi silkmoth
    • Lockshin R.A., Williams C.M. Programmed cell death-I. Cytology of degeneration in the intersegmental muscles of the pernyi silkmoth. J. Insect Physiol. 11:1965;123-133.
    • (1965) J. Insect Physiol. , vol.11 , pp. 123-133
    • Lockshin, R.A.1    Williams, C.M.2
  • 80
    • 0032555716 scopus 로고    scopus 로고
    • Bid, a Bcl2 interacting protein, mediates cytochrome c release from mitochondria in response to activation of cell surface death receptors
    • Luo X., Budihardjo I., Zou H., Slaughter C., Wang X. Bid, a Bcl2 interacting protein, mediates cytochrome c release from mitochondria in response to activation of cell surface death receptors. Cell. 94:1998;481-490.
    • (1998) Cell , vol.94 , pp. 481-490
    • Luo, X.1    Budihardjo, I.2    Zou, H.3    Slaughter, C.4    Wang, X.5
  • 82
    • 0034329742 scopus 로고    scopus 로고
    • Apoptosis in neurodegenerative disorders
    • Mattson M.P. Apoptosis in neurodegenerative disorders. Nat. Rev. Mol. Cell Biol. 1:2000;120-129.
    • (2000) Nat. Rev. Mol. Cell Biol. , vol.1 , pp. 120-129
    • Mattson, M.P.1
  • 83
    • 0026053958 scopus 로고
    • Progression from lymphoid hyperplasia to high-grade malignant lymphoma in mice transgenic for the t(14; 18)
    • McDonnell T.J., Korsmeyer S.J. Progression from lymphoid hyperplasia to high-grade malignant lymphoma in mice transgenic for the t(14; 18). Nature. 349:1991;254-256.
    • (1991) Nature , vol.349 , pp. 254-256
    • Mcdonnell, T.J.1    Korsmeyer, S.J.2
  • 84
    • 0024521441 scopus 로고
    • Bcl-2-immunoglobulin transgenic mice demonstrate extended B cell survival and follicular lymphoproliferation
    • McDonnell T.J., Deane N., Platt F.M., Nunez G., Jaeger U., McKearn J.P., Korsmeyer S.J. bcl-2-immunoglobulin transgenic mice demonstrate extended B cell survival and follicular lymphoproliferation. Cell. 57:1989;79-88.
    • (1989) Cell , vol.57 , pp. 79-88
    • Mcdonnell, T.J.1    Deane, N.2    Platt, F.M.3    Nunez, G.4    Jaeger, U.5    Mckearn, J.P.6    Korsmeyer, S.J.7
  • 85
    • 0041853690 scopus 로고    scopus 로고
    • Induction of TNF receptor I-mediated apoptosis via two sequential signaling complexes
    • Micheau O., Tschopp J. Induction of TNF receptor I-mediated apoptosis via two sequential signaling complexes. Cell. 114:2003;181-190.
    • (2003) Cell , vol.114 , pp. 181-190
    • Micheau, O.1    Tschopp, J.2
  • 89
    • 0034610743 scopus 로고    scopus 로고
    • Caspase-12 mediates endoplasmic-reticulum-specific apoptosis and cytotoxicity by amyloid-beta
    • Nakagawa T., Zhu H., Morishima N., Li E., Xu J., Yankner B.A., Yuan J. Caspase-12 mediates endoplasmic-reticulum-specific apoptosis and cytotoxicity by amyloid-beta. Nature. 403:2000;98-103.
    • (2000) Nature , vol.403 , pp. 98-103
    • Nakagawa, T.1    Zhu, H.2    Morishima, N.3    Li, E.4    Xu, J.5    Yankner, B.A.6    Yuan, J.7
  • 90
    • 0035265686 scopus 로고    scopus 로고
    • PUMA, a novel pro-apoptotic gene, is induced by p53
    • Nakano K., Vousden K.H. PUMA, a novel pro-apoptotic gene, is induced by p53. Mol. Cell. 7:2001;683-694.
    • (2001) Mol. Cell , vol.7 , pp. 683-694
    • Nakano, K.1    Vousden, K.H.2
  • 92
    • 0030638249 scopus 로고    scopus 로고
    • Neuronal necrosis and apoptosis: Two distinct events induced by exposure to glutamate or oxidative stress
    • Nicotera P., Ankarcrona M., Bonfoco E., Orrenius S., Lipton S.A. Neuronal necrosis and apoptosis. two distinct events induced by exposure to glutamate or oxidative stress Adv. Neurol. 72:1997;95-101.
    • (1997) Adv. Neurol. , vol.72 , pp. 95-101
    • Nicotera, P.1    Ankarcrona, M.2    Bonfoco, E.3    Orrenius, S.4    Lipton, S.A.5
  • 93
    • 0038046166 scopus 로고    scopus 로고
    • Elimination of Mcl-1 is required for the initiation of apoptosis following ultraviolet irradiation
    • Nijhawan D., Fang M., Traer E., Zhong Q., Gao W., Du F., Wang X. Elimination of Mcl-1 is required for the initiation of apoptosis following ultraviolet irradiation. Genes Dev. 17:2003;1475-1486.
    • (2003) Genes Dev. , vol.17 , pp. 1475-1486
    • Nijhawan, D.1    Fang, M.2    Traer, E.3    Zhong, Q.4    Gao, W.5    Du, F.6    Wang, X.7
  • 95
    • 0037424239 scopus 로고    scopus 로고
    • Loss of OPA1 perturbates the mitochondrial inner membrane structure and integrity, leading to cytochrome c release and apoptosis
    • Olichon A., Baricault L., Gas N., Guillou E., Valette A., Belenguer P., Lenaers G. Loss of OPA1 perturbates the mitochondrial inner membrane structure and integrity, leading to cytochrome c release and apoptosis. J. Biol. Chem. 278:2003;7743-7746.
    • (2003) J. Biol. Chem. , vol.278 , pp. 7743-7746
    • Olichon, A.1    Baricault, L.2    Gas, N.3    Guillou, E.4    Valette, A.5    Belenguer, P.6    Lenaers, G.7
  • 96
    • 0027166048 scopus 로고
    • Bcl-2 heterodimerizes in vivo with a conserved homolog, Bax, that accelerates programmed cell death
    • Oltvai Z.N., Milliman C.L., Korsmeyer S.J. Bcl-2 heterodimerizes in vivo with a conserved homolog, Bax, that accelerates programmed cell death. Cell. 74:1993;609-619.
    • (1993) Cell , vol.74 , pp. 609-619
    • Oltvai, Z.N.1    Milliman, C.L.2    Korsmeyer, S.J.3
  • 97
    • 0348148880 scopus 로고    scopus 로고
    • Development and maintenance of B and T lymphocytes requires anti-apoptotic MCL-1
    • Opferman J.T., Letai A., Beard C., Sorcinelli M.D., Ong C.C., Korsmeyer S.J. Development and maintenance of B and T lymphocytes requires anti-apoptotic MCL-1. Nature. 426:2003;671-676.
    • (2003) Nature , vol.426 , pp. 671-676
    • Opferman, J.T.1    Letai, A.2    Beard, C.3    Sorcinelli, M.D.4    Ong, C.C.5    Korsmeyer, S.J.6
  • 99
    • 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
  • 100
    • 0034610995 scopus 로고    scopus 로고
    • Reduced loading of intracellular Ca(2+) stores and downregulation of capacitative Ca(2+) influx in Bcl-2-overexpressing cells
    • Pinton P., Ferrari D., Magalhaes P., Schulze-Osthoff K., Di Virgilio F., Pozzan T., Rizzuto R. Reduced loading of intracellular Ca(2+) stores and downregulation of capacitative Ca(2+) influx in Bcl-2-overexpressing cells. J. Cell Biol. 148:2000;857-862.
    • (2000) J. Cell Biol. , vol.148 , pp. 857-862
    • Pinton, P.1    Ferrari, D.2    Magalhaes, P.3    Schulze-Osthoff, K.4    Di Virgilio, F.5    Pozzan, T.6    Rizzuto, R.7
  • 101
    • 0033104996 scopus 로고    scopus 로고
    • The pro-apoptotic activity of the Bcl-2 family member Bim is regulated by interaction with the dynein motor complex
    • Puthalakath H., Huang D.C., O'Reilly L.A., King S.M., Strasser A. The pro-apoptotic activity of the Bcl-2 family member Bim is regulated by interaction with the dynein motor complex. Mol. Cell. 3:1999;287-296.
    • (1999) Mol. Cell , vol.3 , pp. 287-296
    • Puthalakath, H.1    Huang, D.C.2    O'reilly, L.A.3    King, S.M.4    Strasser, A.5
  • 102
    • 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
  • 103
    • 0026504147 scopus 로고
    • Social controls on cell survival and cell death
    • Raff M.C. Social controls on cell survival and cell death. Nature. 356:1992;397-400.
    • (1992) Nature , vol.356 , pp. 397-400
    • Raff, M.C.1
  • 104
    • 0033771902 scopus 로고    scopus 로고
    • CED-2/CrkII and CED-10/Rac control phagocytosis and cell migration in Caenorhabditis elegans
    • Reddien P.W., Horvitz H.R. CED-2/CrkII and CED-10/Rac control phagocytosis and cell migration in Caenorhabditis elegans. Nat. Cell Biol. 2:2000;131-136.
    • (2000) Nat. Cell Biol. , vol.2 , pp. 131-136
    • Reddien, P.W.1    Horvitz, H.R.2
  • 105
    • 0035849886 scopus 로고    scopus 로고
    • Phagocytosis promotes programmed cell death in C. elegans
    • Reddien P.W., Cameron S., Horvitz H.R. Phagocytosis promotes programmed cell death in C. elegans. Nature. 412:2001;198-202.
    • (2001) Nature , vol.412 , pp. 198-202
    • Reddien, P.W.1    Cameron, S.2    Horvitz, H.R.3
  • 107
    • 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
  • 109
    • 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., Yuan J. Caspase-8 is required for cell death induced by expanded polyglutamine repeats. Neuron. 22:1999;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
  • 111
    • 0034641931 scopus 로고    scopus 로고
    • Corpse clearance defines the meaning of cell death
    • Savill J., Fadok V. Corpse clearance defines the meaning of cell death. Nature. 407:2000;784-788.
    • (2000) Nature , vol.407 , pp. 784-788
    • Savill, J.1    Fadok, V.2
  • 115
    • 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
  • 116
    • 0033519705 scopus 로고    scopus 로고
    • Bcl-2 family proteins regulate the release of apoptogenic cytochrome c by the mitochondrial channel VDAC
    • Shimizu S., Narita M., Tsujimoto Y. Bcl-2 family proteins regulate the release of apoptogenic cytochrome c by the mitochondrial channel VDAC. Nature. 399:1999;483-487.
    • (1999) Nature , vol.399 , pp. 483-487
    • Shimizu, S.1    Narita, M.2    Tsujimoto, Y.3
  • 119
    • 0025251664 scopus 로고
    • Novel primitive lymphoid tumours induced in transgenic mice by cooperation between myc and bcl-2
    • Strasser A., Harris A.W., Bath M.L., Cory S. Novel primitive lymphoid tumours induced in transgenic mice by cooperation between myc and bcl-2. Nature. 348:1990;331-333.
    • (1990) Nature , vol.348 , pp. 331-333
    • Strasser, A.1    Harris, A.W.2    Bath, M.L.3    Cory, S.4
  • 120
    • 0037023693 scopus 로고    scopus 로고
    • Interaction of CED-6/GULP, an adapter protein involved in engulfment of apoptotic cells with CED-1 and CD91/low density lipoprotein receptor-related protein (LRP)
    • Su H.P., Nakada-Tsukui K., Tosello-Trampont A.C., Li Y., Bu G., Henson P.M., Ravichandran K.S. Interaction of CED-6/GULP, an adapter protein involved in engulfment of apoptotic cells with CED-1 and CD91/low density lipoprotein receptor-related protein (LRP). J. Biol. Chem. 277:2002;11772-11779.
    • (2002) J. Biol. Chem. , vol.277 , pp. 11772-11779
    • Su, H.P.1    Nakada-Tsukui, K.2    Tosello-Trampont, A.C.3    Li, Y.4    Bu, G.5    Henson, P.M.6    Ravichandran, K.S.7
  • 121
    • 0027145632 scopus 로고
    • Molecular cloning and expression of the Fas ligand, a novel member of the tumor necrosis factor family
    • Suda T., Takahashi T., Golstein P., Nagata S. Molecular cloning and expression of the Fas ligand, a novel member of the tumor necrosis factor family. Cell. 75:1993;1169-1178.
    • (1993) Cell , vol.75 , pp. 1169-1178
    • Suda, T.1    Takahashi, T.2    Golstein, P.3    Nagata, S.4
  • 122
    • 0017303612 scopus 로고
    • Post-embryonic development in the ventral cord of Caenorhabditis elegans
    • Sulston J.E. Post-embryonic development in the ventral cord of Caenorhabditis elegans. Philos. Trans. R. Soc. Lond. B Biol. Sci. 275:1976;287-297.
    • (1976) Philos. Trans. R. Soc. Lond. B Biol. Sci. , vol.275 , pp. 287-297
    • Sulston, J.E.1
  • 124
    • 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
  • 125
    • 0033713002 scopus 로고    scopus 로고
    • Structure of Bax: Coregulation of dimer formation and intracellular localization
    • Suzuki M., Youle R.J., Tjandra N. Structure of Bax. coregulation of dimer formation and intracellular localization Cell. 103:2000;645-654.
    • (2000) Cell , vol.103 , pp. 645-654
    • Suzuki, M.1    Youle, R.J.2    Tjandra, N.3
  • 126
    • 0028223847 scopus 로고
    • Generalized lymphoproliferative disease in mice, caused by a point mutation in the Fas ligand
    • Takahashi T., Tanaka M., Brannan C.I., Jenkins N.A., Copeland N.G., Suda T., Nagata S. Generalized lymphoproliferative disease in mice, caused by a point mutation in the Fas ligand. Cell. 76:1994;969-976.
    • (1994) Cell , vol.76 , pp. 969-976
    • Takahashi, T.1    Tanaka, M.2    Brannan, C.I.3    Jenkins, N.A.4    Copeland, N.G.5    Suda, T.6    Nagata, S.7
  • 127
    • 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. 74:1993;845-853.
    • (1993) Cell , vol.74 , pp. 845-853
    • Tartaglia, L.A.1    Ayres, T.M.2    Wong, G.H.3    Goeddel, D.V.4
  • 128
    • 0028990125 scopus 로고
    • Yama/CPP32 beta, a mammalian homolog of CED-3, is a CrmA-inhibitable protease that cleaves the death substrate poly(ADP-ribose) polymerase
    • Tewari M., Quan L.T., O'Rourke K., Desnoyers S., Zeng Z., Beidler D.R., Poirier G.G., Salvesen G.S., Dixit V.M. Yama/CPP32 beta, a mammalian homolog of CED-3, is a CrmA-inhibitable protease that cleaves the death substrate poly(ADP-ribose) polymerase. Cell. 81:1995;801-809.
    • (1995) Cell , vol.81 , pp. 801-809
    • Tewari, M.1    Quan, L.T.2    O'rourke, K.3    Desnoyers, S.4    Zeng, Z.5    Beidler, D.R.6    Poirier, G.G.7    Salvesen, G.S.8    Dixit, V.M.9
  • 129
    • 0032575750 scopus 로고    scopus 로고
    • Caspases: Enemies within
    • Thornberry N.A., Lazebnik Y. Caspases. enemies within Science. 281:1998;1312-1316.
    • (1998) Science , vol.281 , pp. 1312-1316
    • Thornberry, N.A.1    Lazebnik, Y.2
  • 132
    • 0021821903 scopus 로고
    • Involvement of the bcl-2 gene in human follicular lymphoma
    • Tsujimoto Y., Cossman J., Jaffe E., Croce C.M. Involvement of the bcl-2 gene in human follicular lymphoma. Science. 228:1985;1440-1443.
    • (1985) Science , vol.228 , pp. 1440-1443
    • Tsujimoto, Y.1    Cossman, J.2    Jaffe, E.3    Croce, C.M.4
  • 135
    • 0023786047 scopus 로고
    • Bcl-2 gene promotes haemopoietic cell survival and cooperates with c-myc to immortalize pre-B cells
    • Vaux D.L., Cory S., Adams J.M. Bcl-2 gene promotes haemopoietic cell survival and cooperates with c-myc to immortalize pre-B cells. Nature. 335:1988;440-442.
    • (1988) Nature , vol.335 , pp. 440-442
    • Vaux, D.L.1    Cory, S.2    Adams, J.M.3
  • 136
    • 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
  • 137
    • 0027427492 scopus 로고
    • Bcl-2-deficient mice demonstrate fulminant lymphoid apoptosis, polycystic kidneys, and hypopigmented hair
    • Veis D.J., Sorenson C.M., Shutter J.R., Korsmeyer S.J. Bcl-2-deficient mice demonstrate fulminant lymphoid apoptosis, polycystic kidneys, and hypopigmented hair. Cell. 75:1993;229-240.
    • (1993) Cell , vol.75 , pp. 229-240
    • Veis, D.J.1    Sorenson, C.M.2    Shutter, J.R.3    Korsmeyer, S.J.4
  • 139
    • 0034605121 scopus 로고    scopus 로고
    • Preservation of mitochondrial structure and function after Bid- or Bax-mediated cytochrome c release
    • von Ahsen O., Renken C., Perkins G., Kluck R.M., Bossy-Wetzel E., Newmeyer D.D. Preservation of mitochondrial structure and function after Bid- or Bax-mediated cytochrome c release. J. Cell Biol. 150:2000;1027-1036.
    • (2000) J. Cell Biol. , vol.150 , pp. 1027-1036
    • Von Ahsen, O.1    Renken, C.2    Perkins, G.3    Kluck, R.M.4    Bossy-Wetzel, E.5    Newmeyer, D.D.6
  • 141
    • 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., Lenardo M.J. Inherited human Caspase 10 mutations underlie defective lymphocyte and dendritic cell apoptosis in autoimmune lymphoproliferative syndrome type II. Cell. 98:1999;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
  • 142
    • 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
  • 143
    • 0026568919 scopus 로고
    • Lymphoproliferation disorder in mice explained by defects in Fas antigen that mediates apoptosis
    • Watanabe-Fukunaga R., Brannan C.I., Copeland N.G., Jenkins N.A., Nagata S. Lymphoproliferation disorder in mice explained by defects in Fas antigen that mediates apoptosis. Nature. 356:1992;314-317.
    • (1992) Nature , vol.356 , pp. 314-317
    • Watanabe-Fukunaga, R.1    Brannan, C.I.2    Copeland, N.G.3    Jenkins, N.A.4    Nagata, S.5
  • 147
    • 0032511145 scopus 로고    scopus 로고
    • The C. elegans cell corpse engulfment gene ced-7 encodes a protein similar to ABC transporters
    • a
    • Wu Y.C., Horvitz H.R. The C. elegans cell corpse engulfment gene ced-7 encodes a protein similar to ABC transporters. Cell. 93:1998;951-960. a.
    • (1998) Cell , vol.93 , pp. 951-960
    • Wu, Y.C.1    Horvitz, H.R.2
  • 148
    • 0032473981 scopus 로고    scopus 로고
    • C. elegans phagocytosis and cell-migration protein CED-5 is similar to human DOCK180
    • b
    • Wu Y.C., Horvitz H.R. C. elegans phagocytosis and cell-migration protein CED-5 is similar to human DOCK180. Nature. 392:1998;501-504. b.
    • (1998) Nature , vol.392 , pp. 501-504
    • Wu, Y.C.1    Horvitz, H.R.2
  • 149
    • 0034162713 scopus 로고    scopus 로고
    • NUC-1, a caenorhabditis elegans DNase II homolog, functions in an intermediate step of DNA degradation during apoptosis
    • Wu Y.C., Stanfield G.M., Horvitz H.R. NUC-1, a caenorhabditis elegans DNase II homolog, functions in an intermediate step of DNA degradation during apoptosis. Genes Dev. 14:2000;536-548.
    • (2000) Genes Dev. , vol.14 , pp. 536-548
    • Wu, Y.C.1    Stanfield, G.M.2    Horvitz, H.R.3
  • 150
    • 0035960074 scopus 로고    scopus 로고
    • Necrotic cell death in C. elegans requires the function of calreticulin and regulators of Ca(2+) release from the endoplasmic reticulum
    • Xu K., Tavernarakis N., Driscoll M. Necrotic cell death in C. elegans requires the function of calreticulin and regulators of Ca(2+) release from the endoplasmic reticulum. Neuron. 31:2001;957-971.
    • (2001) Neuron , vol.31 , pp. 957-971
    • Xu, K.1    Tavernarakis, N.2    Driscoll, M.3
  • 151
    • 0037694970 scopus 로고    scopus 로고
    • The Drosophila MicroRNA Mir-14 Suppresses Cell Death and Is Required for Normal Fat Metabolism
    • Xu P., Vernooy S.Y., Guo M., Hay B.A. The Drosophila MicroRNA Mir-14 Suppresses Cell Death and Is Required for Normal Fat Metabolism. Curr. Biol. 13:2003;790-795.
    • (2003) Curr. Biol. , vol.13 , pp. 790-795
    • Xu, P.1    Vernooy, S.Y.2    Guo, M.3    Hay, B.A.4
  • 152
    • 0029880987 scopus 로고    scopus 로고
    • The Caenorhabditis elegans cell-death protein CED-3 is a cysteine protease with substrate specificities similar to those of the human CPP32 protease
    • Xue D., Shaham S., Horvitz H.R. The Caenorhabditis elegans cell-death protein CED-3 is a cysteine protease with substrate specificities similar to those of the human CPP32 protease. Genes Dev. 10:1996;1073-1083.
    • (1996) Genes Dev. , vol.10 , pp. 1073-1083
    • Xue, D.1    Shaham, S.2    Horvitz, H.R.3
  • 153
    • 0032575723 scopus 로고    scopus 로고
    • Essential role of CED-4 oligomerization in CED-3 activation and apoptosis
    • Yang X., Chang H.Y., Baltimore D. Essential role of CED-4 oligomerization in CED-3 activation and apoptosis. Science. 281:1998;1355-1357.
    • (1998) Science , vol.281 , pp. 1355-1357
    • Yang, X.1    Chang, H.Y.2    Baltimore, D.3
  • 154
    • 0024990330 scopus 로고
    • Neurotrophic and neurotoxic effects of amyloid beta protein: Reversal by tachykinin neuropeptides
    • Yankner B.A., Duffy L.K., Kirschner D.A. Neurotrophic and neurotoxic effects of amyloid beta protein. reversal by tachykinin neuropeptides Science. 250:1990;279-282.
    • (1990) Science , vol.250 , pp. 279-282
    • Yankner, B.A.1    Duffy, L.K.2    Kirschner, D.A.3
  • 156
    • 0035265823 scopus 로고    scopus 로고
    • PUMA induces the rapid apoptosis of colorectal cancer cells
    • Yu J., Zhang L., Hwang P.M., Kinzler K.W., Vogelstein B. PUMA induces the rapid apoptosis of colorectal cancer cells. Mol. Cell. 7:2001;673-682.
    • (2001) Mol. Cell , vol.7 , pp. 673-682
    • Yu, J.1    Zhang, L.2    Hwang, P.M.3    Kinzler, K.W.4    Vogelstein, B.5
  • 158
    • 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
  • 159
    • 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
  • 160
    • 0030584088 scopus 로고    scopus 로고
    • Serine phosphorylation of death agonist BAD in response to survival factor results in binding to 14-3-3 not BCL-X(L)
    • Zha J., Harada H., Yang E., Jockel J., Korsmeyer S.J. Serine phosphorylation of death agonist BAD in response to survival factor results in binding to 14-3-3 not BCL-X(L). Cell. 87:1996;619-628.
    • (1996) Cell , vol.87 , pp. 619-628
    • Zha, J.1    Harada, H.2    Yang, E.3    Jockel, J.4    Korsmeyer, S.J.5
  • 161
    • 0035846903 scopus 로고    scopus 로고
    • CED-1 is a transmembrane receptor that mediates cell corpse engulfment in C. elegans
    • Zhou Z., Hartwieg E., Horvitz H.R. CED-1 is a transmembrane receptor that mediates cell corpse engulfment in C. elegans. Cell. 104:2001;43-56.
    • (2001) Cell , vol.104 , pp. 43-56
    • Zhou, Z.1    Hartwieg, E.2    Horvitz, H.R.3
  • 162
    • 0030745646 scopus 로고    scopus 로고
    • Apaf-1, a human protein homologous to C. elegans CED-4, participates in cytochrome c-dependent activation of caspase-3
    • Zou H., Henzel W.J., Liu X., Lutschg A., Wang X. Apaf-1, a human protein homologous to C. elegans CED-4, participates in cytochrome c-dependent activation of caspase-3. Cell. 90:1997;405-413.
    • (1997) Cell , vol.90 , pp. 405-413
    • Zou, H.1    Henzel, W.J.2    Liu, X.3    Lutschg, A.4    Wang, X.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.