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Volumn 2, Issue 9, 2002, Pages 647-656

The BCL2 family: Regulators of the cellular life-or-death switch

Author keywords

[No Author keywords available]

Indexed keywords

CASPASE; CASPASE 9; CELL PROTEIN; CYTOCHROME C; OUTER MEMBRANE PROTEIN; PROTEIN BAK; PROTEIN BAX; PROTEIN BCL 2; PROTEIN P53;

EID: 0036716281     PISSN: 1474175X     EISSN: None     Source Type: Journal    
DOI: 10.1038/nrc883     Document Type: Review
Times cited : (3517)

References (154)
  • 1
    • 0015383455 scopus 로고
    • Apoptosis: A basic biological phenomenon with wide-ranging implications in tissue kinetics
    • Kerr, J. F. R., Wyllie, A. H. & Currie, A. R. Apoptosis: a basic biological phenomenon with wide-ranging implications in tissue kinetics. Br. J. Cancer 26, 239-257 (1972). Cell death recognized to be an intrinsic cellular programme that plays a complementary role to mitosis in regulating tissue homeostasis.
    • (1972) Br. J. Cancer , vol.26 , pp. 239-257
    • Kerr, J.F.R.1    Wyllie, A.H.2    Currie, A.R.3
  • 2
    • 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, 440-442 (1988). Discovery that Bcl2 promotes cell survival. First recognition that cell survival is controlled separately from cell proliferation and that inhibition of apoptosis is a central step in tumour development. The first demonstration of cooperativity of Bcl2 and Myc in transformation.
    • (1988) Nature , vol.335 , pp. 440-442
    • Vaux, D.L.1    Cory, S.2    Adams, J.M.3
  • 3
    • 0033118755 scopus 로고    scopus 로고
    • Insights from Bcl2 and Myc: Malignancy involves abrogation of apoptosis as well as sustained proliferation
    • Cory, S., Vaux, D. L., Strasser A., Harris, A. W. & Adams, J. M. Insights from Bcl2 and Myc: malignancy involves abrogation of apoptosis as well as sustained proliferation. Cancer Res. 59, S1685-S1692 (1999).
    • (1999) Cancer Res. , vol.59
    • Cory, S.1    Vaux, D.L.2    Strasser, A.3    Harris, A.W.4    Adams, J.M.5
  • 4
    • 0034614637 scopus 로고    scopus 로고
    • The hallmarks of cancer
    • Hanahan, D. & Weinberg, R. A. The hallmarks of cancer. Cell 100, 57-70 (2000).
    • (2000) Cell , vol.100 , pp. 57-70
    • Hanahan, D.1    Weinberg, R.A.2
  • 5
    • 0036463405 scopus 로고    scopus 로고
    • A matter of life and death
    • Green, D. R. & Evan, G. I. A matter of life and death. Cancer Cell 1, 19-30 (2002).
    • (2002) Cancer Cell , vol.1 , pp. 19-30
    • Green, D.R.1    Evan, G.I.2
  • 6
    • 0037169358 scopus 로고    scopus 로고
    • Apoptosis: A link between cancer genetics and chemotherapy
    • Johnstone, R. W., Ruefli, A. A. & Lowe, S. W. Apoptosis: a link between cancer genetics and chemotherapy. Cell 108, 153-164 (2002).
    • (2002) Cell , vol.108 , pp. 153-164
    • Johnstone, R.W.1    Ruefli, A.A.2    Lowe, S.W.3
  • 7
    • 0028025563 scopus 로고
    • Apoptosis in cancer therapy: Crossing the threshold
    • Fisher, D. E. Apoptosis in cancer therapy: crossing the threshold. Cell 78, 539-542 (1994).
    • (1994) Cell , vol.78 , pp. 539-542
    • Fisher, D.E.1
  • 8
    • 0032575688 scopus 로고    scopus 로고
    • The BCl-2 protein family: Arbiters of cell survival
    • Adams, J. M. & Cory, S. The BCl-2 protein family: arbiters of cell survival. Science 281, 1322-1326 (1998).
    • (1998) Science , vol.281 , pp. 1322-1326
    • Adams, J.M.1    Cory, S.2
  • 9
    • 0032575752 scopus 로고    scopus 로고
    • Mitochondria and apoptosis
    • Green, D. R. & Reed, J. C. Mitochondria and apoptosis. Science 281, 1309-1311 (1998).
    • (1998) Science , vol.281 , pp. 1309-1311
    • Green, D.R.1    Reed, J.C.2
  • 10
    • 0033179760 scopus 로고    scopus 로고
    • Bcl-2 family members and the mitochondria in apoptosis
    • Gross, A., McDonnell, J. M. & Korsmeyer, S. J. Bcl-2 family members and the mitochondria in apoptosis. Genes Dev. 13, 1899-1911 (1999).
    • (1999) Genes Dev. , vol.13 , pp. 1899-1911
    • Gross, A.1    McDonnell, J.M.2    Korsmeyer, S.J.3
  • 11
    • 0033258120 scopus 로고    scopus 로고
    • Bcl-2 proteins: Regulators of apoptosis or of mitochondrial homeostasis?
    • Vander Heiden, M. G. & Thompson, C. B. Bcl-2 proteins: regulators of apoptosis or of mitochondrial homeostasis? Nat. Cell Biol. 1, E209-E216 (1999).
    • (1999) Nat. Cell Biol. , vol.1
    • Vander Heiden, M.G.1    Thompson, C.B.2
  • 13
    • 0035146929 scopus 로고    scopus 로고
    • Life-or-death decisions by the Bcl-2 protein family
    • Adams, J. M. & Cory, S. Life-or-death decisions by the Bcl-2 protein family. Trends Biochem. Sci. 26, 61-66 (2001).
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 61-66
    • Adams, J.M.1    Cory, S.2
  • 14
    • 0035890085 scopus 로고    scopus 로고
    • The expanding role of mitochondria in apoptosis
    • Wang, X. The expanding role of mitochondria in apoptosis. Genes Dev. 15, 2922-2933 (2001).
    • (2001) Genes Dev. , vol.15 , pp. 2922-2933
    • Wang, X.1
  • 16
    • 0033119367 scopus 로고    scopus 로고
    • Genetic control of programmed cell death in the nematode Caenorhabditis elegans
    • Horvitz, H. R. Genetic control of programmed cell death in the nematode Caenorhabditis elegans. Cancer Res. 59, S1701-S1706 (1999).
    • (1999) Cancer Res. , vol.59
    • Horvitz, H.R.1
  • 17
    • 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, 1955-1957 (1992). This demonstration that human BCL2 could replace the worm survival gene revealed the marked evolutionary conservation of the apoptotic machinery.
    • (1992) Science , vol.258 , pp. 1955-1957
    • Vaux, D.L.1    Weissman, I.L.2    Kim, S.K.3
  • 18
    • 0027525104 scopus 로고
    • The C. elegans cell death gene cell-3 encodes a protein similar to mammalian interleukin-1β-converting enzyme
    • Yuan, J., Shaham, S., Ledoux, S., Ellis, H. M. & Horvitz, H. R. The C. elegans cell death gene cell-3 encodes a protein similar to mammalian interleukin-1β-converting enzyme. Cell 75, 641-652 (1993). An illuminating moment, when developmental genetics and mammalian biochemistry converged to reveal that cell death is launched by the activation of a class of cysteine proteases, later called caspases.
    • (1993) Cell , vol.75 , pp. 641-652
    • Yuan, J.1    Shaham, S.2    Ledoux, S.3    Ellis, H.M.4    Horvitz, H.R.5
  • 19
    • 0036205587 scopus 로고    scopus 로고
    • Mechanisms of caspase activation and inhibition during apoptosis
    • Shi, Y. Mechanisms of caspase activation and inhibition during apoptosis. Mol. Cell 9, 459-470 (2002).
    • (2002) Mol. Cell , vol.9 , pp. 459-470
    • Shi, Y.1
  • 20
    • 0030715323 scopus 로고    scopus 로고
    • Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade
    • Li, P. et al. Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade. Cell 91, 479-489 (1997). Surprising revelation that activation of an apoptosis machine in mammalian cells depends on cytochrome c, which is released from the mitochondria of cells subjected to intracellular stress.
    • (1997) Cell , vol.91 , pp. 479-489
    • Li, P.1
  • 21
    • 0036598992 scopus 로고    scopus 로고
    • Targeting death and decoy receptors of the tumour-necrosis factor superfamily
    • Ashkenazi, A. Targeting death and decoy receptors of the tumour-necrosis factor superfamily. Nature Rev. Cancer 2, 420-430 (2002).
    • (2002) Nature Rev. Cancer , vol.2 , pp. 420-430
    • Ashkenazi, A.1
  • 22
    • 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, 609-619 (1993). First evidence that Bcl2 has pro-apoptotic relatives.
    • (1993) Cell , vol.74 , pp. 609-619
    • Oltvai, Z.N.1    Milliman, C.L.2    Korsmeyer, S.J.3
  • 23
    • 0028242493 scopus 로고
    • Assembly of Bcl-2 into microsomal and outer mitochondrial membranes
    • Janiak, F., Leber, B. & Andrews, D. W. Assembly of Bcl-2 into microsomal and outer mitochondrial membranes. J. Biol. Chem. 269, 9842-9849 (1994).
    • (1994) J. Biol. Chem. , vol.269 , pp. 9842-9849
    • Janiak, F.1    Leber, B.2    Andrews, D.W.3
  • 24
    • 5244224827 scopus 로고    scopus 로고
    • L, an inhibitor of programmed cell death
    • L, an inhibitor of programmed cell death. Nature 381, 335-341 (1996).
    • (1996) Nature , vol.381 , pp. 335-341
    • Muchmore, S.W.1
  • 25
    • 0035853130 scopus 로고    scopus 로고
    • Solution structure of the antiapoptotic protein Bcl-2
    • Petros, A. M. et al. Solution structure of the antiapoptotic protein Bcl-2. Proc. Natl. Acad. Sci. USA 98, 3012-3017 (2001).
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 3012-3017
    • Petros, A.M.1
  • 27
    • 0030614915 scopus 로고    scopus 로고
    • L-Bak peptide complex: Recognition between regulators of apoptosis
    • L-Bak peptide complex: recognition between regulators of apoptosis. Science 275, 983-986 (1997). Together with reference 24, this paper provided the first structural insight into how the pro- and anti-apoptotic Bcl2 family members interact.
    • (1997) Science , vol.275 , pp. 983-986
    • Sattler, M.1
  • 28
    • 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, 645-654 (2000). The structure of full-length Bax unexpectedly revealed that the carboxy-terminal tail needed for membrane association occludes its surface pocket.
    • (2000) Cell , vol.103 , pp. 645-654
    • Suzuki, M.1    Youle, R.J.2    Tjandra, N.3
  • 29
    • 0024521441 scopus 로고
    • Bcl-2-immunoglobulin transgenic mice demonstrate extended B cell survival and follicular lymphoproliferation
    • McDonnell, T. J. et al. Bcl-2-immunoglobulin transgenic mice demonstrate extended B cell survival and follicular lymphoproliferation. Cell 57, 79-88 (1989).
    • (1989) Cell , vol.57 , pp. 79-88
    • McDonnell, T.J.1
  • 30
    • 0025786164 scopus 로고
    • Bcl-2 transgene inhibits T cell death and perturbs thymic self-censorship
    • Strasser, A., Harris, A. W. & Cory, S. Bcl-2 transgene inhibits T cell death and perturbs thymic self-censorship. Cell 67, 889-899 (1991).
    • (1991) Cell , vol.67 , pp. 889-899
    • Strasser, A.1    Harris, A.W.2    Cory, S.3
  • 31
    • 0025939204 scopus 로고
    • Enforced BCL2 expression in B-lymphoid cells prolongs antibody responses and elicits autoimmune disease
    • Strasser, A. et al. Enforced BCL2 expression in B-lymphoid cells prolongs antibody responses and elicits autoimmune disease. Proc. Natl Acad. Sci. USA 88, 8661-8665 (1991).
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 8661-8665
    • Strasser, A.1
  • 32
    • 0025751550 scopus 로고
    • Bcl-2 inhibits multiple forms of apoptosis but not negative selection in thymocytes
    • Sentman, C. L., Shutter, J. R., Hockenbery, D., Kanagawa, O. & Korsmeyer, S. J. Bcl-2 inhibits multiple forms of apoptosis but not negative selection in thymocytes. Cell 67, 879-888 (1991).
    • (1991) Cell , vol.67 , pp. 879-888
    • Sentman, C.L.1    Shutter, J.R.2    Hockenbery, D.3    Kanagawa, O.4    Korsmeyer, S.J.5
  • 33
    • 0033593038 scopus 로고    scopus 로고
    • Constitutive Bcl-2 expression throughout the hematopoietic compartment affects multiple lineages and enhances progenitor cell survival
    • Ogilvy, S. et al. Constitutive Bcl-2 expression throughout the hematopoietic compartment affects multiple lineages and enhances progenitor cell survival. Proc. Natl Acad. Sci. USA 96, 14943-14948 (1999).
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 14943-14948
    • Ogilvy, S.1
  • 34
    • 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, 229-240 (1993).
    • (1993) Cell , vol.75 , pp. 229-240
    • Veis, D.J.1    Sorenson, C.M.2    Shutter, J.R.3    Korsmeyer, S.J.4
  • 35
    • 0028922885 scopus 로고
    • Massive cell death of immature hematopoietic cells and neurons in Bcl-x deficient mice
    • Motoyama, N. et al. Massive cell death of immature hematopoietic cells and neurons in Bcl-x deficient mice. Science 267, 1506-1510 (1995).
    • (1995) Science , vol.267 , pp. 1506-1510
    • Motoyama, N.1
  • 36
    • 13144267780 scopus 로고    scopus 로고
    • Apoptosis regulator Bcl-w is essential for spermatogenesis but appears otherwise redundant
    • Print, C. G. et al. Apoptosis regulator Bcl-w is essential for spermatogenesis but appears otherwise redundant. Proc. Natl Acad. Sci. USA 95, 12424-12431 (1998).
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 12424-12431
    • Print, C.G.1
  • 37
    • 0031906439 scopus 로고    scopus 로고
    • Testicular degeneration in Bcl-w-deficient mice
    • Ross, A. J. et al. Testicular degeneration in Bcl-w-deficient mice. Nature Genet. 18, 251-256 (1998).
    • (1998) Nature Genet. , vol.18 , pp. 251-256
    • Ross, A.J.1
  • 38
    • 0031743756 scopus 로고    scopus 로고
    • Accelerated neutrophil apoptosis in mice lacking A1-a, a subtype of the Bcl-2-related A1 gene
    • Hamasaki, A. et al. Accelerated neutrophil apoptosis in mice lacking A1-a, a subtype of the Bcl-2-related A1 gene. J. Exp. Med 188, 1985-1992 (1998).
    • (1998) J. Exp. Med. , vol.188 , pp. 1985-1992
    • Hamasaki, A.1
  • 40
    • 0033635733 scopus 로고    scopus 로고
    • BH3-only proteins - Essential initiators of apoptotic cell death
    • Huang, D. C. S. & Strasser, A. BH3-only proteins - essential initiators of apoptotic cell death. Cell 103, 839-842 (2000).
    • (2000) Cell , vol.103 , pp. 839-842
    • Huang, D.C.S.1    Strasser, A.2
  • 41
    • 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, 519-529 (1998). Discovery that the nematode genome also encodes a BH3-only protein that interacts with the Bcl2 homologue CED-9 and is essential for developmental cell death.
    • (1998) Cell , vol.93 , pp. 519-529
    • Conradt, B.1    Horvitz, H.R.2
  • 42
    • 0035876483 scopus 로고    scopus 로고
    • BH3-only proteins that bind pro-survival Bcl-2 family members fail to induce apoptosis in the absence of Bax and Bak
    • Zong, W. X., Lindsten, T. Ross, A. J., MacGregor, G. R. & Thompson, C. B. BH3-only proteins that bind pro-survival Bcl-2 family members fail to induce apoptosis in the absence of Bax and Bak. Genes Dev. 15, 1481-1486 (2001). Demonstration that apoptosis induced by diverse cytotoxic signals requires either Bax or Bak and that they act downstream of the BH3-only proteins.
    • (2001) Genes Dev. , vol.15 , pp. 1481-1486
    • Zong, W.X.1    Lindsten, T.2    Ross, A.J.3    MacGregor, G.R.4    Thompson, C.B.5
  • 43
    • 0034786019 scopus 로고    scopus 로고
    • L sequester BH3 domain-only molecules preventing BAX- and BAK-mediated mitochondrial apoptosis
    • L sequester BH3 domain- only molecules preventing BAX- and BAK-mediated mitochondrial apoptosis. Mol. Cell 8, 705-711 (2001).
    • (2001) Mol. Cell , vol.8 , pp. 705-711
    • Cheng, E.H.1
  • 44
    • 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. S., 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, 287-296 (1999). Discovery that the BH3-only protein Bim is tethered to the microtubules in healthy cells and translocates to Bcl2 pro-survival proteins during apoptosis.
    • (1999) Mol. Cell , vol.3 , pp. 287-296
    • Puthalakath, H.1    Huang, D.C.S.2    O'Reilly, L.A.3    King, S.M.4    Strasser, A.5
  • 45
    • 0035823238 scopus 로고    scopus 로고
    • Bmf: A pro-apoptotic BH3-only protein regulated by interaction with the myosin V actin motor complex, activated by anoikis
    • Puthalakath, H. et al. Bmf: a pro-apoptotic BH3-only protein regulated by interaction with the myosin V actin motor complex, activated by anoikis. Science 293, 1829-1832 (2001).
    • (2001) Science , vol.293 , pp. 1829-1832
    • Puthalakath, H.1
  • 47
    • 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, 491-501 (1998).
    • (1998) Cell , vol.94 , pp. 491-501
    • Li, H.1    Zhu, H.2    Xu, C.-J.3    Yuan, J.4
  • 48
    • 0032555716 scopus 로고    scopus 로고
    • Bid, a Bcl-2 interacting protein, mediates cytochrome c release from mitochondria in response to activation of cell surface death receptors
    • Luo, X., Budlhardjo, I., Zou, H., Slaughter, C. & Wang, X. Bid, a Bcl-2 interacting protein, mediates cytochrome c release from mitochondria in response to activation of cell surface death receptors. Cell 94, 481-90 (1998).
    • (1998) Cell , vol.94 , pp. 481-490
    • Luo, X.1    Budlhardjo, I.2    Zou, H.3    Slaughter, C.4    Wang, X.5
  • 49
    • 0034640281 scopus 로고    scopus 로고
    • Noxa, a BH3-only member of the Bcl-2 family and candidate mediator of p53-induced apoptosis
    • Oda, E. et al. Noxa, a BH3-only member of the Bcl-2 family and candidate mediator of p53-induced apoptosis. Science 288, 1053-1058 (2000).
    • (2000) Science , vol.288 , pp. 1053-1058
    • Oda, E.1
  • 50
    • 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, 673-682 (2001).
    • (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
  • 51
    • 0035265686 scopus 로고    scopus 로고
    • PUMA, a novel proapoptotic gene, is induced by p53
    • Nakano, K. & Vousden, K. H. PUMA, a novel proapoptotic gene, is induced by p53. Mol. Cell 7, 683-694 (2001).
    • (2001) Mol. Cell , vol.7 , pp. 683-694
    • Nakano, K.1    Vousden, K.H.2
  • 52
    • 0030854775 scopus 로고    scopus 로고
    • Molecular cloning of a novel polypeptide, DP5, induced during programmed neuronal death
    • Imaizumi, K. et al. Molecular cloning of a novel polypeptide, DP5, induced during programmed neuronal death. J. Biol. Chem. 272, 18842-18848 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 18842-18848
    • Imaizumi, K.1
  • 53
    • 0033607006 scopus 로고    scopus 로고
    • Bid-deficient mice are resistant to Fas-induced hepatocellular apoptosis
    • Yin, X.-M. et al. Bid-deficient mice are resistant to Fas-induced hepatocellular apoptosis. Nature 400, 886-891 (1999).
    • (1999) Nature , vol.400 , pp. 886-891
    • Yin, X.-M.1
  • 54
    • 0033607506 scopus 로고    scopus 로고
    • Proapoptotic Bcl-2 relative Bim required for certain apoptotic responses, leukocyte homeostasis, and to preclude autoimmunity
    • Bouillet, P. et al. Proapoptotic Bcl-2 relative Bim required for certain apoptotic responses, leukocyte homeostasis, and to preclude autoimmunity. Science 286, 1735-1738 (1999). Gene-knockout study reveals that the BH3-only protein Bim is a critical regulator of leukocyte homeostasis.
    • (1999) Science , vol.286 , pp. 1735-1738
    • Bouillet, P.1
  • 55
    • 0037148840 scopus 로고    scopus 로고
    • BH3-only Bcl-2 family member Bim is required for apoptosis of autoreactive thymocytes
    • Bouillet, P. et al. BH3-only Bcl-2 family member Bim is required for apoptosis of autoreactive thymocytes. Nature 415, 922-926 (2002).
    • (2002) Nature , vol.415 , pp. 922-926
    • Bouillet, P.1
  • 56
    • 0035053624 scopus 로고    scopus 로고
    • Induction of Bim, a proapoptotic BH3- only Bcl-2 family member, is critical for neuronal apoptosis
    • Putcha, G. V. et al. Induction of Bim, a proapoptotic BH3- only Bcl-2 family member, is critical for neuronal apoptosis. Neuron 29, 615-628 (2001).
    • (2001) Neuron , vol.29 , pp. 615-628
    • Putcha, G.V.1
  • 57
    • 0035514046 scopus 로고    scopus 로고
    • Degenerative disorders caused by Bcl-2 deficiency are prevented by loss of its BH3-only antagonist Bim
    • Bouillet, P., Cory, S., Zhang, L.-C., Strasser, A. & Adams, J. M. Degenerative disorders caused by Bcl-2 deficiency are prevented by loss of its BH3-only antagonist Bim. Dev. Cell 1, 645-653 (2001). The relative levels of BH3-only proteins and their pro-survival relatives is shown to be crucial in establishing the threshold for commitment of a cell to apoptosis and, therefore, for the control of tissue homeostasis.
    • (2001) Dev. Cell , vol.1 , pp. 645-653
    • Bouillet, P.1    Cory, S.2    Zhang, L.-C.3    Strasser, A.4    Adams, J.M.5
  • 59
    • 0033525591 scopus 로고    scopus 로고
    • Solution structure of BID, an intracellular amplifier of apoptotic signaling
    • Chou, J. J., Li, H., Salvesen, G. S., Yuan, J. & Wagner, G. Solution structure of BID, an intracellular amplifier of apoptotic signaling. Cell 96, 615-624 (1999).
    • (1999) Cell , vol.96 , pp. 615-624
    • Chou, J.J.1    Li, H.2    Salvesen, G.S.3    Yuan, J.4    Wagner, G.5
  • 60
    • 0033525749 scopus 로고    scopus 로고
    • Solution structure of the proapoptotic molecule BID: A structural basis for apoptotic agonists and antagonists
    • McDonnell, J. M., Fushman, D., Milliman, C. L., Korsmeyer, S. J. & Cowburn, D. Solution structure of the proapoptotic molecule BID: a structural basis for apoptotic agonists and antagonists. Cell 96, 625-634 (1999).
    • (1999) Cell , vol.96 , pp. 625-634
    • McDonnell, J.M.1    Fushman, D.2    Milliman, C.L.3    Korsmeyer, S.J.4    Cowburn, D.5
  • 61
    • 0034534795 scopus 로고    scopus 로고
    • Posttranslational N-myristoylation of BID as a molecular switch for targeting mitochondria and apoptosis
    • Zha, J., Weiler, S., Oh, K. J., Wei, M. C. & Korsmeyer, S. J. Posttranslational N-myristoylation of BID as a molecular switch for targeting mitochondria and apoptosis. Science 290, 1761-1765 (2000).
    • (2000) Science , vol.290 , pp. 1761-1765
    • Zha, J.1    Weiler, S.2    Oh, K.J.3    Wei, M.C.4    Korsmeyer, S.J.5
  • 62
    • 0034306169 scopus 로고    scopus 로고
    • Cardiolipin provides specificity for targeting of tBid to mitochondria
    • Lutter, M. et al. Cardiolipin provides specificity for targeting of tBid to mitochondria. Nature Cell Biol. 2, 754-761 (2000).
    • (2000) Nature Cell Biol. , vol.2 , pp. 754-761
    • Lutter, M.1
  • 63
    • 0034663829 scopus 로고    scopus 로고
    • tBID, a membrane-targeted death ligand, oligomerizes BAK to release cytochrome c
    • Wei, M. C. et al. tBID, a membrane-targeted death ligand, oligomerizes BAK to release cytochrome c. Genes Dev. 14, 2060-2071 (2000).
    • (2000) Genes Dev. , vol.14 , pp. 2060-2071
    • Wei, M.C.1
  • 64
    • 0037085380 scopus 로고    scopus 로고
    • Rapid kinetics of tBid-induced cytochrome c and Smac/DIABLO release and mitochondrial depolarization
    • Madesh, M., Antonsson, B., Srinivasula, S. M., Alnemi, E. S. & Hajnóczky, G. Rapid kinetics of tBid-induced cytochrome c and Smac/ DIABLO release and mitochondrial depolarization. J. Biol. Chem. 277, 5651-5659 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 5651-5659
    • Madesh, M.1    Antonsson, B.2    Srinivasula, S.M.3    Alnemi, E.S.4    Hajnóczky, G.5
  • 65
    • 0037023739 scopus 로고    scopus 로고
    • tBID Homooligomerizes in the mitochondrial membrane to induce apoptosis
    • Grinberg, M. et al. tBID Homooligomerizes in the mitochondrial membrane to induce apoptosis. J. Biol. Chem. 277, 12237-12245 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 12237-12245
    • Grinberg, M.1
  • 66
    • 0034508217 scopus 로고    scopus 로고
    • The combined functions of proapoptotic Bcl-2 family members Bak and Bax are essential for normal development of multiple tissues
    • Lindsten, T. et al. The combined functions of proapoptotic Bcl-2 family members Bak and Bax are essential for normal development of multiple tissues. Mol. Cell 6, 1389-1399 (2000). Multiple developmental defects in mice lacking both Bax and Bak reveal that at least one of these proteins is required for stress-induced cell death.
    • (2000) Mol. Cell , vol.6 , pp. 1389-1399
    • Lindsten, T.1
  • 67
    • 0035957653 scopus 로고    scopus 로고
    • Proapoptotic BAX and BAK: A requisite gateway to mitochondrial dysfunction and death
    • Wei, M. C. et al. Proapoptotic BAX and BAK: a requisite gateway to mitochondrial dysfunction and death. Science 292, 727-730 (2001).
    • (2001) Science , vol.292 , pp. 727-730
    • Wei, M.C.1
  • 68
    • 0032562796 scopus 로고    scopus 로고
    • Bax in murine thymus is a soluble monomeric protein that displays differential detergent-induced conformations
    • Hsu, Y.-T. & Youle, R. J. Bax in murine thymus is a soluble monomeric protein that displays differential detergent-induced conformations. J. Biol. Chem. 273, 10777-10783 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 10777-10783
    • Hsu, Y.-T.1    Youle, R.J.2
  • 69
    • 0035844867 scopus 로고    scopus 로고
    • Bax and Bak coalesce into novel mitochondria-associated clusters during apoptosis
    • Nechushtan, A., Smith, C. L., Lamensdorf, I., Yoon, S. H. & Youle, R. J. Bax and Bak coalesce into novel mitochondria-associated clusters during apoptosis. J. Cell Biol. 153, 1265-1276 (2001).
    • (2001) J. Cell Biol. , vol.153 , pp. 1265-1276
    • Nechushtan, A.1    Smith, C.L.2    Lamensdorf, I.3    Yoon, S.H.4    Youle, R.J.5
  • 70
    • 0035853811 scopus 로고    scopus 로고
    • Bax is present as a high molecular weight oligomer/complex in the mitochondrial membrane of apoptotic cells
    • Antonsson, B., Montessuit, S., Sanchez, B. & Martinou, J. C. Bax is present as a high molecular weight oligomer/complex in the mitochondrial membrane of apoptotic cells. J. Biol. Chem. 276, 11615-11623 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 11615-11623
    • Antonsson, B.1    Montessuit, S.2    Sanchez, B.3    Martinou, J.C.4
  • 71
    • 0035947596 scopus 로고    scopus 로고
    • Bcl-2 prevents Bax oligomerization in the mitochondrial outer membrane
    • Mikhailov, V. et al. Bcl-2 prevents Bax oligomerization in the mitochondrial outer membrane. J. Biol. Chem. 276, 18361-18374 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 18361-18374
    • Mikhailov, V.1
  • 72
    • 0033522391 scopus 로고    scopus 로고
    • Conformation of the Bax C-terminus regulates subcellular location and cell death
    • Nechushtan, A., Smith, C. L., Hsu, Y. T. & Youle, R. J. Conformation of the Bax C-terminus regulates subcellular location and cell death. EMBO J. 18, 2330-2341 (1999).
    • (1999) EMBO J. , vol.18 , pp. 2330-2341
    • Nechushtan, A.1    Smith, C.L.2    Hsu, Y.T.3    Youle, R.J.4
  • 73
    • 0033535347 scopus 로고    scopus 로고
    • Cell damage-induced conformational changes of the pro-apoptotic protein Bak in vivo precede the onset of apoptosis
    • Griffiths, G. J. et al. Cell damage-induced conformational changes of the pro-apoptotic protein Bak in vivo precede the onset of apoptosis. J. Cell Biol. 144, 903-914 (1999).
    • (1999) J. Cell Biol. , vol.144 , pp. 903-914
    • Griffiths, G.J.1
  • 74
    • 0034525413 scopus 로고    scopus 로고
    • VDAC regulation by the Bcl-2 family of proteins
    • Tsujimoto, Y. & Shimizu, S. VDAC regulation by the Bcl-2 family of proteins. Cell Death Differ. 7, 1174-1181 (2000).
    • (2000) Cell Death Differ. , vol.7 , pp. 1174-1181
    • Tsujimoto, Y.1    Shimizu, S.2
  • 75
    • 0035229427 scopus 로고    scopus 로고
    • The mitochondrion in apoptosis: How Pandora's box opens
    • Zamzami, N. & Kroemer, G. The mitochondrion in apoptosis: how Pandora's box opens. Nature Rev. Mol. Cell Biol. 2, 67-71 (2001).
    • (2001) Nature Rev. Mol. Cell Biol. , vol.2 , pp. 67-71
    • Zamzami, N.1    Kroemer, G.2
  • 76
    • 9844257587 scopus 로고    scopus 로고
    • Inhibition of Bax channel-forming activity by Bcl-2
    • Antonsson, B. et al. Inhibition of Bax channel-forming activity by Bcl-2. Science 277, 370-372 (1997).
    • (1997) Science , vol.277 , pp. 370-372
    • Antonsson, B.1
  • 77
    • 0034650523 scopus 로고    scopus 로고
    • Bax oligomerization is required for channel-forming activity in liposomes and to trigger cytochrome c release from mytochondria
    • Antonsson, B., Montessuit, S., Lauper, S., Eskes, R. & Martinou, J. C. Bax oligomerization is required for channel-forming activity in liposomes and to trigger cytochrome c release from mytochondria. Biochem. J. 345, 271-278 (2000).
    • (2000) Biochem. J. , vol.345 , pp. 271-278
    • Antonsson, B.1    Montessuit, S.2    Lauper, S.3    Eskes, R.4    Martinou, J.C.5
  • 78
    • 0034253592 scopus 로고    scopus 로고
    • BAX-dependent transport of cytochrome c reconstituted in pure liposomes
    • Saito, M., Korsmeyer, S. J. & Schlesinger, P. H. BAX-dependent transport of cytochrome c reconstituted in pure liposomes. Nature Cell Biol. 2, 553-555 (2000).
    • (2000) Nature Cell Biol. , vol.2 , pp. 553-555
    • Saito, M.1    Korsmeyer, S.J.2    Schlesinger, P.H.3
  • 79
    • 0035956426 scopus 로고    scopus 로고
    • A novel, high conductance channel of mitochondria linked to apoptosis in mammalian cells and Bax expression in yeast
    • Pavlov, E. V. et al. A novel, high conductance channel of mitochondria linked to apoptosis in mammalian cells and Bax expression in yeast. J. Cell Biol. 155, 725-732 (2001).
    • (2001) J. Cell Biol. , vol.155 , pp. 725-732
    • Pavlov, E.V.1
  • 80
    • 0032518787 scopus 로고    scopus 로고
    • Bim: A novel member of the Bcl-2 family that promotes apoptosis
    • O'Connor, L. et al. Bim: a novel member of the Bcl-2 family that promotes apoptosis. EMBO J. 17, 384-395 (1998).
    • (1998) EMBO J. , vol.17 , pp. 384-395
    • O'Connor, L.1
  • 81
    • 0034712042 scopus 로고    scopus 로고
    • Translocation of C. elegans CED-4 to nuclear membranes during programmed cell death
    • Chen, F. et al. Translocation of C. elegans CED-4 to nuclear membranes during programmed cell death. Science 287, 1485-1489 (2000).
    • (2000) Science , vol.287 , pp. 1485-1489
    • Chen, F.1
  • 82
    • 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 C. elegans
    • del Peso, L., González, V. M., Inohara, N., Ellis, R. E. & Núñez, G. Disruption of the CED-9/CED-4 complex by EGL-1 is a critical step for programmed cell death in C. elegans. J. Biol. Chem. 275, 27205-27211 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 27205-27211
    • Del Peso, L.1    González, V.M.2    Inohara, N.3    Ellis, R.E.4    Núñez, G.5
  • 83
    • 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. USA 97, 11916-11921 (2000).
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 11916-11921
    • Parrish, J.1    Metters, H.2    Chen, L.3    Xue, D.4
  • 84
    • 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, 665-676 (1994).
    • (1994) Cell , vol.76 , pp. 665-676
    • Hengartner, M.O.1    Horvitz, H.R.2
  • 85
    • 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, 405-413 (1997).
    • (1997) Cell , vol.90 , pp. 405-413
    • Zou, H.1    Henzel, W.J.2    Liu, X.3    Lutschg, A.4    Wang, X.5
  • 87
    • 0033578303 scopus 로고    scopus 로고
    • Bcl-2 family members do not inhibit apoptosis by binding the caspase-activator Apaf-1
    • Moriishi, K., Huang, D. C. S., Cory, S. & Adams, J. M. Bcl-2 family members do not inhibit apoptosis by binding the caspase-activator Apaf-1. Proc. Natl Acad. Sci. USA 96, 9683-9688 (1999).
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 9683-9688
    • Moriishi, K.1    Huang, D.C.S.2    Cory, S.3    Adams, J.M.4
  • 88
    • 0032509354 scopus 로고    scopus 로고
    • WD-40 repeat region regulates Apaf-1 self-association and procaspase-9 activation
    • Hu, Y., Ding, L., Spencer, D. M. & Núñez, G. WD-40 repeat region regulates Apaf-1 self-association and procaspase-9 activation. J. Biol. Chem. 273, 33489-33494 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 33489-33494
    • Hu, Y.1    Ding, L.2    Spencer, D.M.3    Núñez, G.4
  • 89
    • 0031037897 scopus 로고    scopus 로고
    • The release of cytochrome c from mitochondria: A primary site for Bcl-2 regulation of apoptosis
    • Kluck, R. M., Bossy-Wetzel, E., Green, D. R. & Newmeyer, D. D. The release of cytochrome c from mitochondria: a primary site for Bcl-2 regulation of apoptosis. Science 275, 1132-1136 (1997).
    • (1997) Science , vol.275 , pp. 1132-1136
    • Kluck, R.M.1    Bossy-Wetzel, E.2    Green, D.R.3    Newmeyer, D.D.4
  • 90
    • 0031036872 scopus 로고    scopus 로고
    • Prevention of apoptosis by Bcl-2: Release of cytochrome c from mitochondria blocked
    • Yang, J. et al. Prevention of apoptosis by Bcl-2: release of cytochrome c from mitochondria blocked. [Au: ok?] Science 275, 1129-1132 (1997).
    • (1997) Science , vol.275 , pp. 1129-1132
    • Yang, J.1
  • 91
    • 0032799633 scopus 로고    scopus 로고
    • Caspases: Their intracellular localization and translocation during apoptosis
    • Zhivotovsky, B., Samali, A., Gahm, A. & Orrenius, S. Caspases: their intracellular localization and translocation during apoptosis. Cell Death Differ. 6, 644-651 (1999).
    • (1999) Cell Death Differ. , vol.6 , pp. 644-651
    • Zhivotovsky, B.1    Samali, A.2    Gahm, A.3    Orrenius, S.4
  • 92
    • 0037128924 scopus 로고    scopus 로고
    • The role of cytochrome c in caspase activation in Drosophila melanogaster cells
    • Dorstyn, L. et al. The role of cytochrome c in caspase activation in Drosophila melanogaster cells. J. Cell Biol. 156, 1089-1098 (2002).
    • (2002) J. Cell Biol. , vol.156 , pp. 1089-1098
    • Dorstyn, L.1
  • 93
    • 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, 1077-1087 (2002).
    • (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
  • 94
    • 0032544449 scopus 로고    scopus 로고
    • Apaf-1 (CED-4 homologue) regulates programmed cell death in mammalian development
    • Cecconi, F., Alvarez-Bolado, G., Meyer, B. I., Roth, K. A. & Gruss, P. Apaf-1 (CED-4 homologue) regulates programmed cell death in mammalian development. Cell 94, 727-737 (1998).
    • (1998) Cell , vol.94 , pp. 727-737
    • Cecconi, F.1    Alvarez-Bolado, G.2    Meyer, B.I.3    Roth, K.A.4    Gruss, P.5
  • 95
    • 0032544564 scopus 로고    scopus 로고
    • Apaf1 is required for mitochondrial pathways of apoptosis and brain development
    • Yoshida, H. et al. Apaf1 is required for mitochondrial pathways of apoptosis and brain development. Cell 94, 739-750 (1998).
    • (1998) Cell , vol.94 , pp. 739-750
    • Yoshida, H.1
  • 96
    • 0032493910 scopus 로고    scopus 로고
    • Reduced apoptosis and cytochrome c-mediated caspase activation in mice lacking caspase 9
    • Kuida, K. et al. Reduced apoptosis and cytochrome c-mediated caspase activation in mice lacking caspase 9. Cell 94, 325-337 (1998).
    • (1998) Cell , vol.94 , pp. 325-337
    • Kuida, K.1
  • 97
    • 0032493870 scopus 로고    scopus 로고
    • Differential requirement for caspase 9 in apoptotic pathways in vivo
    • Hakem, R. et al. Differential requirement for caspase 9 in apoptotic pathways in vivo. Cell 94, 339-352 (1998).
    • (1998) Cell , vol.94 , pp. 339-352
    • Hakem, R.1
  • 98
    • 0035817727 scopus 로고    scopus 로고
    • Embryonic neuronal death due to neurotrophin and neurotransmitter deprivation occurs independent of Apaf-1
    • Honarpour, N. et al. Embryonic neuronal death due to neurotrophin and neurotransmitter deprivation occurs independent of Apaf-1. Neuroscience 106, 263-274 (2001).
    • (2001) Neuroscience , vol.106 , pp. 263-274
    • Honarpour, N.1
  • 99
    • 0034652010 scopus 로고    scopus 로고
    • Adult Apaf-1-deficient mice exhibit male infertility
    • Honarpour, N. et al. Adult Apaf-1-deficient mice exhibit male infertility. Dev. Biol. 218, 248-258 (2000).
    • (2000) Dev. Biol. , vol.218 , pp. 248-258
    • Honarpour, N.1
  • 100
    • 0036499206 scopus 로고    scopus 로고
    • The apoptotic protease-activating factor 1-mediated pathway of apoptosis is dispensable for negative selection of thymocytes
    • Hara, H. et al. The apoptotic protease-activating factor 1-mediated pathway of apoptosis is dispensable for negative selection of thymocytes. J. Immunol. 168, 2288-2295 (2002).
    • (2002) J. Immunol. , vol.168 , pp. 2288-2295
    • Hara, H.1
  • 101
    • 0034658350 scopus 로고    scopus 로고
    • Apoptotic protease activating factor 1 (Apaf-1)-independent cell death suppression by Bcl-2
    • Haraguchi, M. et al. Apoptotic protease activating factor 1 (Apaf-1)-independent cell death suppression by Bcl-2. J. Exp. Med. 191, 1709-1720 (2000).
    • (2000) J. Exp. Med. , vol.191 , pp. 1709-1720
    • Haraguchi, M.1
  • 102
    • 0034640102 scopus 로고    scopus 로고
    • Cytochrome c deficiency causes embryonic lethality and attenuates stress-induced apoptosis
    • Li, K. et al. Cytochrome c deficiency causes embryonic lethality and attenuates stress-induced apoptosis. Cell 101, 389-399 (2000).
    • (2000) Cell , vol.101 , pp. 389-399
    • Li, K.1
  • 103
    • 0032472329 scopus 로고    scopus 로고
    • Mitochondrial cytochrome c release in apoptosis occurs upstream of DEVD-specific caspase activation and independently of mitochondrial transmembrane depolarization
    • Bossy-Wetzel, E., Newmeyer, D. D. & Green, D. R. Mitochondrial cytochrome c release in apoptosis occurs upstream of DEVD-specific caspase activation and independently of mitochondrial transmembrane depolarization. EMBO J. 17, 37-49 (1998).
    • (1998) EMBO J. , vol.17 , pp. 37-49
    • Bossy-Wetzel, E.1    Newmeyer, D.D.2    Green, D.R.3
  • 104
    • 0035870123 scopus 로고    scopus 로고
    • Caspase-dependent cytosolic release of cytochrome c and membrane translocation of Bax in p53-induced apoptosis
    • Gao, C. F. et al. Caspase-dependent cytosolic release of cytochrome c and membrane translocation of Bax in p53-induced apoptosis. Exp. Cell Res. 265, 145-151 (2001).
    • (2001) Exp. Cell Res. , vol.265 , pp. 145-151
    • Gao, C.F.1
  • 105
    • 0034648698 scopus 로고    scopus 로고
    • Matrix detachment induces caspase-dependent cytochrome c release from mitochondria: Inhibition by PKB/Akt but not Raf signalling
    • Rytömaa, M., Lehmann, K. & Downward, J. Matrix detachment induces caspase-dependent cytochrome c release from mitochondria: inhibition by PKB/Akt but not Raf signalling. Oncogene 19, 4461-4468 (2000).
    • (2000) Oncogene , vol.19 , pp. 4461-4468
    • Rytömaa, M.1    Lehmann, K.2    Downward, J.3
  • 106
    • 0033531926 scopus 로고    scopus 로고
    • L function and induce apoptosis through cytochrome c-independent activation of caspases
    • L function and induce apoptosis through cytochrome c-independent activation of caspases. J. Biol. Chem. 214, 13298-13304 (1999).
    • (1999) J. Biol. Chem. , vol.214 , pp. 13298-13304
    • Holinger, E.P.1    Chittenden, T.2    Lutz, R.J.3
  • 107
    • 0033229866 scopus 로고    scopus 로고
    • p53 regulates mitochondrial membrane potential through reactive oxygen species and induces cytochrome c-independent apoptosis blocked by Bcl-2
    • Li, P.-F., Dietz, R. & von Harsdorf, R. p53 regulates mitochondrial membrane potential through reactive oxygen species and induces cytochrome c-independent apoptosis blocked by Bcl-2. EMBO J. 18, 6027-6036 (1999).
    • (1999) EMBO J. , vol.18 , pp. 6027-6036
    • Li, P.-F.1    Dietz, R.2    Von Harsdorf, R.3
  • 109
    • 0142144272 scopus 로고    scopus 로고
    • Caspase-2 is required for stress-induced apoptosis and acts prior to mitochondrial permeabilization
    • in the press
    • Lassus, P., Opitz-Araya, X. & Lazebnik, Y. Caspase-2 is required for stress-induced apoptosis and acts prior to mitochondrial permeabilization. Science (in the press). In certain cell lines, stress stimuli are shown to activate caspase-2 upstream of mitochondrial disruption. Together with other recent findings by Marsden et al. (see text), this work argues strongly that Bcl2 function extends beyond guarding mitochondrial integrity and is likely to involve direct regulation of the activation of several initiator caspases.
    • Science
    • Lassus, P.1    Opitz-Araya, X.2    Lazebnik, Y.3
  • 110
    • 0033542461 scopus 로고    scopus 로고
    • Bcl-2 targeted to the endoplasmic reticulum can inhibit apoptosis induced by Myc but not etoposide in Rat-1 fibroblasts
    • Lee, S. T. et al. Bcl-2 targeted to the endoplasmic reticulum can inhibit apoptosis induced by Myc but not etoposide in Rat-1 fibroblasts. Oncogene 181, 3520-3528 (1999).
    • (1999) Oncogene , vol.181 , pp. 3520-3528
    • Lee, S.T.1
  • 111
    • 0034604033 scopus 로고    scopus 로고
    • Apoptotic crosstalk between the endoplasmic reticulum and mitochondria controlled by Bcl-2
    • Häcki, J. et al. Apoptotic crosstalk between the endoplasmic reticulum and mitochondria controlled by Bcl-2. Oncogene 19, 2286-2295 (2000).
    • (2000) Oncogene , vol.19 , pp. 2286-2295
    • Häcki, J.1
  • 112
    • 0035211935 scopus 로고    scopus 로고
    • Wild-type, mitochondrial and ER-restricted Bcl-2 inhibit DNA damage-induced apoptosis but do not affect death receptor-induced apoptosis
    • Rudner, J. et al. Wild-type, mitochondrial and ER-restricted Bcl-2 inhibit DNA damage-induced apoptosis but do not affect death receptor-induced apoptosis. J. Cell Sci. 114, 4161-4172 (2001).
    • (2001) J. Cell Sci. , vol.114 , pp. 4161-4172
    • Rudner, J.1
  • 113
    • 0012053647 scopus 로고    scopus 로고
    • Coupling endoplasmic reticulum stress to the cell death program: An Apaf-1-independent intrinsic pathway
    • Rao, R. V. et al. Coupling endoplasmic reticulum stress to the cell death program: an Apaf-1-independent intrinsic pathway. J. Biol. Chem. 27, 27 (2002).
    • (2002) J. Biol. Chem. , vol.27 , pp. 27
    • Rao, R.V.1
  • 114
    • 0034610743 scopus 로고    scopus 로고
    • Caspase-12 mediates endoplasmic-reticulum-specific apoptosis and cytotoxicity by amyloid-β
    • Nakagawa, T. et al. Caspase-12 mediates endoplasmic-reticulum-specific apoptosis and cytotoxicity by amyloid-β. Nature 403, 98-103 (2000).
    • (2000) Nature , vol.403 , pp. 98-103
    • Nakagawa, T.1
  • 115
    • 0036168620 scopus 로고    scopus 로고
    • Formation of noncanonical high molecular weight caspase-3 and -6 complexes and activation of caspase-12 during serum starvation induced apoptosis in AKR-2B mouse fibroblasts
    • Klic, M., Schafer, R., Hoppe, J. & Kagerhuber, U. Formation of noncanonical high molecular weight caspase-3 and -6 complexes and activation of caspase-12 during serum starvation induced apoptosis in AKR-2B mouse fibroblasts. Cell Death Differ. 9, 125-137 (2002).
    • (2002) Cell Death Differ. , vol.9 , pp. 125-137
    • Klic, M.1    Schafer, R.2    Hoppe, J.3    Kagerhuber, U.4
  • 116
    • 0037062951 scopus 로고    scopus 로고
    • RNA interference
    • Hannon, G. J. RNA interference, Nature 418, 244-251 (2002).
    • (2002) Nature , vol.418 , pp. 244-251
    • Hannon, G.J.1
  • 117
    • 0033153086 scopus 로고    scopus 로고
    • The role of caspases in development, immunity, and apoptotic signal transduction: Lessons from knockout mice
    • Los, M., Wesselborg, S. & Schulze-Osthoff, K. The role of caspases in development, immunity, and apoptotic signal transduction: lessons from knockout mice. Immunity 10, 629-639 (1999).
    • (1999) Immunity , vol.10 , pp. 629-639
    • Los, M.1    Wesselborg, S.2    Schulze-Osthoff, K.3
  • 118
    • 2142759177 scopus 로고    scopus 로고
    • Apoptosomes: Engines for caspase activation
    • in the press
    • Adams, J. M. & Cory, S. Apoptosomes: engines for caspase activation. Curr. Opin. Cell Biol. (in the press).
    • Curr. Opin. Cell Biol.
    • Adams, J.M.1    Cory, S.2
  • 119
  • 120
    • 0034698878 scopus 로고    scopus 로고
    • Cross-talk between two cysteine protease families. Activation of caspase-12 by calpain in apoptosis
    • Nakagawa, T. & Yuan, J. Cross-talk between two cysteine protease families. Activation of caspase-12 by calpain in apoptosis. J. Cell Biol. 150, 887-894 (2000).
    • (2000) J. Cell Biol. , vol.150 , pp. 887-894
    • Nakagawa, T.1    Yuan, J.2
  • 121
    • 0027461627 scopus 로고
    • Eμ-bcl-2 transgene facilitates spontaneous transformation of early pre-B and immunoglobulin-secreting cells but not T cells
    • Strasser, A., Harris, A. W. & Cory, S. Eμ-bcl-2 transgene facilitates spontaneous transformation of early pre-B and immunoglobulin-secreting cells but not T cells. Oncogene 8, 1-9 (1993).
    • (1993) Oncogene , vol.8 , pp. 1-9
    • Strasser, A.1    Harris, A.W.2    Cory, S.3
  • 122
    • 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, 331-333 (1990). First in vivo evidence that Bcl2 is tumorigenic and can collaborate with Myc in tumour development.
    • (1990) Nature , vol.348 , pp. 331-333
    • Strasser, A.1    Harris, A.W.2    Bath, M.L.3    Cory, S.4
  • 123
    • 0030669560 scopus 로고    scopus 로고
    • Overexpression of Bcl-2 inhibits alveolar cell apoptosis during involution and accelerates c-Myc-induced tumorigenesis of the mammary gland in transgenic mice
    • Jager, R., Herzer, U., Schenkel, J. & Weiher, H. Overexpression of Bcl-2 inhibits alveolar cell apoptosis during involution and accelerates c-Myc-induced tumorigenesis of the mammary gland in transgenic mice. Oncogene 15, 1787-1795 (1997).
    • (1997) Oncogene , vol.15 , pp. 1787-1795
    • Jager, R.1    Herzer, U.2    Schenkel, J.3    Weiher, H.4
  • 124
    • 0029833679 scopus 로고    scopus 로고
    • The rise and fall of apoptosis during multistage tumorigenesis: Down-modulation contributes to tumor progression from angiogenic progenitors
    • Naik, P., Karrim, J. & Hanahan, D. The rise and fall of apoptosis during multistage tumorigenesis: down-modulation contributes to tumor progression from angiogenic progenitors. Genes Dev. 10, 2105-2116 (1996).
    • (1996) Genes Dev. , vol.10 , pp. 2105-2116
    • Naik, P.1    Karrim, J.2    Hanahan, D.3
  • 125
    • 0037013147 scopus 로고    scopus 로고
    • Suppression of Myc-induced apoptosis in β cells exposes multiple oncogenic properties of Myc and triggers carcinogenic progression
    • Pelengaris, S., Khan, M. & I. E. G. Suppression of Myc-induced apoptosis in β cells exposes multiple oncogenic properties of Myc and triggers carcinogenic progression. Cell 109, 321-334 (2002).
    • (2002) Cell , vol.109 , pp. 321-334
    • Pelengaris, S.1    Khan, M.2
  • 126
    • 0035910748 scopus 로고    scopus 로고
    • BCL-2 cooperates with promyelocytic leukemia retinoic acid receptor α chimeric protein (PMLRARα) to block neutrophil differentiation and initiate acute leukemia
    • Kogan, S. C. et al. BCL-2 cooperates with promyelocytic leukemia retinoic acid receptor α chimeric protein (PMLRARα) to block neutrophil differentiation and initiate acute leukemia. J. Exp. Med. 193, 531-543 (2001).
    • (2001) J. Exp. Med. , vol.193 , pp. 531-543
    • Kogan, S.C.1
  • 127
    • 0032529166 scopus 로고    scopus 로고
    • L by a Jak kinase-dependent pathway is bypassed in murine hematopoietic malignancies
    • L by a Jak kinase-dependent pathway is bypassed in murine hematopoietic malignancies. Genes Dev, 12, 2475-2487 (1998).
    • (1998) Genes Dev. , vol.12 , pp. 2475-2487
    • Packham, G.1
  • 128
    • 0031018674 scopus 로고    scopus 로고
    • Somatic frameshift mutations in the Bax gene in colon cancers of the microsatellite mutator phenotype
    • Rampino, N. et al. Somatic frameshift mutations in the Bax gene in colon cancers of the microsatellite mutator phenotype. Science 275, 967-969 (1997).
    • (1997) Science , vol.275 , pp. 967-969
    • Rampino, N.1
  • 129
    • 0034662604 scopus 로고    scopus 로고
    • Mutations of the BAK gene in human gastric and colorectal cancers
    • Kondo, S. et al. Mutations of the BAK gene in human gastric and colorectal cancers. Cancer Res. 60, 4328-4330 (2000).
    • (2000) Cancer Res. , vol.60 , pp. 4328-4330
    • Kondo, S.1
  • 130
    • 0032522953 scopus 로고    scopus 로고
    • Hematopoetic malignancies demonstrate loss-of-function mutations of BAX
    • Meijerink, J. P. P. et al. Hematopoetic malignancies demonstrate loss-of-function mutations of BAX. Blood 91, 2991-2997 (1998).
    • (1998) Blood , vol.91 , pp. 2991-2997
    • Meijerink, J.P.P.1
  • 131
    • 0030938089 scopus 로고    scopus 로고
    • Bax-deficiency promotes drug resistance and oncogenic transformation by attenuating p53-dependent apoptosis
    • McCurrach, M. E., Connor, T. M. F., Knudson, C. M., Korsmeyer, S. J. & Lowe, S. W. Bax-deficiency promotes drug resistance and oncogenic transformation by attenuating p53-dependent apoptosis. Proc. Natl Acad. Sci. USA 94, 2345-2349 (1997).
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 2345-2349
    • McCurrach, M.E.1    Connor, T.M.F.2    Knudson, C.M.3    Korsmeyer, S.J.4    Lowe, S.W.5
  • 132
    • 0031038137 scopus 로고    scopus 로고
    • Bax suppresses tumorigenesis and stimulates apoptosis in vivo
    • Yin, C. Y., Knudson, C. M., Korsmeyer, S. J. & Van Dyke, T. Bax suppresses tumorigenesis and stimulates apoptosis in vivo. Nature 385, 637-640 (1997).
    • (1997) Nature , vol.385 , pp. 637-640
    • Yin, C.Y.1    Knudson, C.M.2    Korsmeyer, S.J.3    Van Dyke, T.4
  • 133
    • 0034718591 scopus 로고    scopus 로고
    • Mutational inactivation of the proapoptotic gene BAX confers selective advantage during tumor clonal evolution
    • Ionov, Y., Yamamoto, H., Krajewski, S., Reed, J. C. & Perucho, M. Mutational inactivation of the proapoptotic gene BAX confers selective advantage during tumor clonal evolution. Proc. Natl Acad. Sci. USA 97, 10872-10877 (2000).
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 10872-10877
    • Ionov, Y.1    Yamamoto, H.2    Krajewski, S.3    Reed, J.C.4    Perucho, M.5
  • 134
    • 0033557805 scopus 로고    scopus 로고
    • Rel-dependent induction of A1 transcription is required to protect B cells from antigen receptor ligation-induced apoptosis
    • Grumont, R. J., Rourke, I. J. & Gerondakis, S. Rel-dependent induction of A1 transcription is required to protect B cells from antigen receptor ligation-induced apoptosis. Genes Dev. 13, 400-411 (1999).
    • (1999) Genes Dev. , vol.13 , pp. 400-411
    • Grumont, R.J.1    Rourke, I.J.2    Gerondakis, S.3
  • 135
    • 0034719680 scopus 로고    scopus 로고
    • The transcription factor NF-κB: Control of oncogenesis and cancer therapy resistance
    • Mayo, M. W. & Baldwin, A. S. The transcription factor NF-κB: control of oncogenesis and cancer therapy resistance. Biochim. Biophys. Acta 1470, M55-M62 (2000).
    • (2000) Biochim. Biophys. Acta , vol.1470
    • Mayo, M.W.1    Baldwin, A.S.2
  • 136
    • 0035487104 scopus 로고    scopus 로고
    • The INK4a/ARF network in tumour suppression
    • Sherr, C. J. The INK4a/ARF network in tumour suppression. Nature Rev. Mol. Cell Biol. 2, 731-737 (2001).
    • (2001) Nature Rev. Mol. Cell Biol. , vol.2 , pp. 731-737
    • Sherr, C.J.1
  • 137
    • 0028072523 scopus 로고
    • DNA damage can induce apoptosis in proliferating lymphoid cells via p53-independent mechanisms inhibitable by Bcl-2
    • Strasser, A., Harris, A. W., Jacks, T. & Cory, S. DNA damage can induce apoptosis in proliferating lymphoid cells via p53-independent mechanisms inhibitable by Bcl-2. Cell 79, 329-339 (1994).
    • (1994) Cell , vol.79 , pp. 329-339
    • Strasser, A.1    Harris, A.W.2    Jacks, T.3    Cory, S.4
  • 138
    • 0033826530 scopus 로고    scopus 로고
    • Genetic analysis of chemoresistance in primary murine lymphomas
    • Schmitt, C. A., Rosenthal, C. T. & Lowe, S. W. Genetic analysis of chemoresistance in primary murine lymphomas. Nature Med. 6, 1029-1035 (2000).
    • (2000) Nature Med. , vol.6 , pp. 1029-1035
    • Schmitt, C.A.1    Rosenthal, C.T.2    Lowe, S.W.3
  • 139
    • 0037050735 scopus 로고    scopus 로고
    • Upregulation of Bcl-2 is involved in the mediation of chemotherapy resistance in human small cell lung cancer cell lines
    • Sartorius, U. A. & Krammer, P. H. Upregulation of Bcl-2 is involved in the mediation of chemotherapy resistance in human small cell lung cancer cell lines. Int. J. Cancer 97, 584-592 (2002).
    • (2002) Int. J. Cancer , vol.97 , pp. 584-592
    • Sartorius, U.A.1    Krammer, P.H.2
  • 140
    • 0034602188 scopus 로고    scopus 로고
    • Role of BAX in the apoptotic response to anticancer agents
    • Zhang, L., Yu, J., Park, B. H., Kinzler, K. W. & Vogelstein, B. Role of BAX in the apoptotic response to anticancer agents. Science 290, 989-992 (2000).
    • (2000) Science , vol.290 , pp. 989-992
    • Zhang, L.1    Yu, J.2    Park, B.H.3    Kinzler, K.W.4    Vogelstein, B.5
  • 141
    • 0034641932 scopus 로고    scopus 로고
    • From bench to clinic with apoptosis-based therapeutic agents
    • Nicholson, D. W. From bench to clinic with apoptosis-based therapeutic agents. Nature 407, 810-816 (2000).
    • (2000) Nature , vol.407 , pp. 810-816
    • Nicholson, D.W.1
  • 142
    • 0034691130 scopus 로고    scopus 로고
    • Structure-based discovery of an organic compound that binds Bcl-2 protein and induces apoptosis of tumor cells
    • Wang, J. L. et al. Structure-based discovery of an organic compound that binds Bcl-2 protein and induces apoptosis of tumor cells. Proc. Natl Acad. Sci. USA 97, 7124-7129 (2000).
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 7124-7129
    • Wang, J.L.1
  • 144
    • 0035147650 scopus 로고    scopus 로고
    • Antimycin A mimics a cell-death-inducing Bcl-2 homology domain 3
    • Tzung, S. P. et al. Antimycin A mimics a cell-death-inducing Bcl-2 homology domain 3. Nature Cell Biol. 3, 183-191 (2001).
    • (2001) Nature Cell Biol. , vol.3 , pp. 183-191
    • Tzung, S.P.1
  • 145
    • 0034722884 scopus 로고    scopus 로고
    • Bcl-2 family proteins as targets for anticancer drug design
    • Huang, Z. Bcl-2 family proteins as targets for anticancer drug design. Oncogene 19, 6627-6631 (2000).
    • (2000) Oncogene , vol.19 , pp. 6627-6631
    • Huang, Z.1
  • 146
    • 0036710477 scopus 로고    scopus 로고
    • Prospects for targeting the Bcl-2 family of proteins to develop novel cytotoxic drugs
    • in the press
    • Baell, J. B. & Huang, D. C. S. Prospects for targeting the Bcl-2 family of proteins to develop novel cytotoxic drugs. Biochem. Pharmacol. (in the press)
    • Biochem. Pharmacol.
    • Baell, J.B.1    Huang, D.C.S.2
  • 148
    • 0032575750 scopus 로고    scopus 로고
    • Caspases: Enemies within
    • Thornberry, N. A. & Lazebnik, Y. Caspases: enemies within. Science 281, 1312-1316 (1998).
    • (1998) Science , vol.281 , pp. 1312-1316
    • Thornberry, N.A.1    Lazebnik, Y.2
  • 149
    • 0033573020 scopus 로고    scopus 로고
    • Caspase-9 and APAF-1 form an active holoenzyme
    • Rodriguez, J. & Lazebnik, Y. Caspase-9 and APAF-1 form an active holoenzyme. Genes Dev. 13, 3179-3184 (1999).
    • (1999) Genes Dev. , vol.13 , pp. 3179-3184
    • Rodriguez, J.1    Lazebnik, Y.2
  • 150
    • 0036187036 scopus 로고    scopus 로고
    • Three-dimensional structure of the apoptosome: Implications for assembly, procaspase-9 binding, and activation
    • Acehan, D. et al. Three-dimensional structure of the apoptosome: implications for assembly, procaspase-9 binding, and activation. Mol. Cell 9, 423-432 (2002).
    • (2002) Mol. Cell , vol.9 , pp. 423-432
    • Acehan, D.1
  • 151
    • 0034694083 scopus 로고    scopus 로고
    • Granzyme B-mediated cytochrome c release is regulated by the Bcl-2 family members Bid and Bax
    • Heibein, J. A. et al. Granzyme B-mediated cytochrome c release is regulated by the Bcl-2 family members Bid and Bax. J. Exp. Med 192, 1391-1402 (2000).
    • (2000) J. Exp. Med. , vol.192 , pp. 1391-1402
    • Heibein, J.A.1
  • 152
    • 0037041392 scopus 로고    scopus 로고
    • p63 and p73 are required for p53-dependent apoptosis in response to DNA damage
    • Flores, E. R. et al. p63 and p73 are required for p53-dependent apoptosis in response to DNA damage. Nature 416, 560-564(2002).
    • (2002) Nature , vol.416 , pp. 560-564
    • Flores, E.R.1
  • 153
    • 0029609086 scopus 로고
    • Bcl-2 and Fas/APO-1 regulate distinct pathways to lymphocyte apoptosis
    • Strasser, A., Harris, A. W., Huang, D. C. S., Krammer, P. H. & Cory, S. Bcl-2 and Fas/APO-1 regulate distinct pathways to lymphocyte apoptosis. EMBO J. 14, 6136-6147 (1995). Bcl2 was found to be unable to block apoptosis triggered by the newly discovered 'death-receptor' pathway, establishing that there are at least two distinct pathways to apoptosis in mammalian cells.
    • (1995) EMBO J. , vol.14 , pp. 6136-6147
    • Strasser, A.1    Harris, A.W.2    Huang, D.C.S.3    Krammer, P.H.4    Cory, S.5
  • 154
    • 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, 254-256 (1991).
    • (1991) Nature , vol.349 , pp. 254-256
    • McDonnell, T.J.1    Korsmeyer, S.J.2


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