메뉴 건너뛰기




Volumn 20, Issue 9, 2000, Pages 3125-3136

Biochemical and genetic analysis of the mitochondrial response of yeast to BAX and BCL-X(L)

Author keywords

[No Author keywords available]

Indexed keywords

CYCLOPHILIN; CYTOCHROME C OXIDASE; PROTEIN BAX; PROTEIN BCL X; REACTIVE OXYGEN METABOLITE;

EID: 0033993820     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.20.9.3125-3136.2000     Document Type: Article
Times cited : (147)

References (86)
  • 1
    • 0032575688 scopus 로고    scopus 로고
    • The Bcl-2 protein family: Arbiters of cell survival
    • Adams, J. M., and S. Cory. 1998. The Bcl-2 protein family: arbiters of cell survival. Science 281:1322-1326.
    • (1998) Science , vol.281 , pp. 1322-1326
    • Adams, J.M.1    Cory, S.2
  • 3
    • 0030873947 scopus 로고    scopus 로고
    • Multicopy suppressors of phenotypes resulting from the absence of yeast VDAC encode a VDAC-like protein
    • Blachly-Dyson, E., J. Song, W. J. Wolfgang, M. Colombini, and M. Forte. 1997. Multicopy suppressors of phenotypes resulting from the absence of yeast VDAC encode a VDAC-like protein. Mol. Cell. Biol. 17:5727-5738.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 5727-5738
    • Blachly-Dyson, E.1    Song, J.2    Wolfgang, W.J.3    Colombini, M.4    Forte, M.5
  • 4
    • 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., D. D. Newmeyer, and D. R. Green. 1998. 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) EMBO J. , vol.17 , pp. 37-49
    • Bossy-Wetzel, E.1    Newmeyer, D.D.2    Green, D.R.3
  • 5
    • 0032422634 scopus 로고    scopus 로고
    • The molecular structure of mitochondrial contact sites. Their role in regulation of energy metabolism and permeability transition
    • Brdiczka, D., G. Beutner, A. Ruck, M. Dolder, and T. Wallimann. 1998. The molecular structure of mitochondrial contact sites. Their role in regulation of energy metabolism and permeability transition. Biofactors 8:235-242.
    • (1998) Biofactors , vol.8 , pp. 235-242
    • Brdiczka, D.1    Beutner, G.2    Ruck, A.3    Dolder, M.4    Wallimann, T.5
  • 6
    • 0032535730 scopus 로고    scopus 로고
    • Blood cells with reduced mitochondrial membrane potential and cytosolic cytochrome C can survive and maintain clonogenicity given appropriate signals to suppress apoptosis
    • Chen, Q., N. Takeyama, G. Brady, A. J. Watson, and C. Dive. 1998. Blood cells with reduced mitochondrial membrane potential and cytosolic cytochrome C can survive and maintain clonogenicity given appropriate signals to suppress apoptosis. Blood 92:4545-4553.
    • (1998) Blood , vol.92 , pp. 4545-4553
    • Chen, Q.1    Takeyama, N.2    Brady, G.3    Watson, A.J.4    Dive, C.5
  • 8
    • 0028157171 scopus 로고
    • Subcellular localization of the Bcl-2 protein in malignant and normal lymphoid cells
    • de Jong, D., F. A. Prins, D. Y. Mason, J. C. Reed, G. B. van Ommen, and P. M. Kluin. 1994. Subcellular localization of the Bcl-2 protein in malignant and normal lymphoid cells. Cancer Res. 54:256-260.
    • (1994) Cancer Res. , vol.54 , pp. 256-260
    • De Jong, D.1    Prins, F.A.2    Mason, D.Y.3    Reed, J.C.4    Van Ommen, G.B.5    Kluin, P.M.6
  • 10
    • 0025915949 scopus 로고
    • ADP/ATP translocator is essential only for anaerobic growth of yeast Saccharomyces cerevisiae
    • Drgon, T., L. Sabova, N. Nelson, and J. Kolarov. 1991. ADP/ATP translocator is essential only for anaerobic growth of yeast Saccharomyces cerevisiae. FEBS Lett. 289:159-162.
    • (1991) FEBS Lett. , vol.289 , pp. 159-162
    • Drgon, T.1    Sabova, L.2    Nelson, N.3    Kolarov, J.4
  • 12
    • 0032535140 scopus 로고    scopus 로고
    • A link between cell cycle and cell death: Bax and Bcl-2 modulate Cdk2 activation during thymocyte apoptosis
    • Gil-Gomez, G., A. Berns, and H. J. Brady. 1998. A link between cell cycle and cell death: Bax and Bcl-2 modulate Cdk2 activation during thymocyte apoptosis. EMBO J. 17:7209-7218.
    • (1998) EMBO J. , vol.17 , pp. 7209-7218
    • Gil-Gomez, G.1    Berns, A.2    Brady, H.J.3
  • 14
    • 0032404536 scopus 로고    scopus 로고
    • The central executioners of apoptosis: Caspases or mitochondria?
    • Green, D., and G. Kroemer. 1998. The central executioners of apoptosis: caspases or mitochondria? Trends Cell Biol. 8:267-271.
    • (1998) Trends Cell Biol. , vol.8 , pp. 267-271
    • Green, D.1    Kroemer, G.2
  • 15
    • 0032575752 scopus 로고    scopus 로고
    • Mitochondria and apoptosis
    • Green, D., and J. Reed. 1998. Mitochondria and apoptosis. Science 281: 1309-1312.
    • (1998) Science , vol.281 , pp. 1309-1312
    • Green, D.1    Reed, J.2
  • 16
    • 0030052107 scopus 로고    scopus 로고
    • Role of mitochondria and C-terminal membrane anchor of Bcl-2 in Bax induced growth arrest and mortality in Saccharomyces cerevisiae
    • Greenhalf, W., C. Stephan, and B. Chaudhuri. 1996. Role of mitochondria and C-terminal membrane anchor of Bcl-2 in Bax induced growth arrest and mortality in Saccharomyces cerevisiae. FEBS Lett. 380:169-175.
    • (1996) FEBS Lett. , vol.380 , pp. 169-175
    • Greenhalf, W.1    Stephan, C.2    Chaudhuri, B.3
  • 17
  • 18
    • 0032528118 scopus 로고    scopus 로고
    • Enforced dimerization of BAX results in its translocation, mitochondrial dysfunction and apoptosis
    • Gross, A., J. Jockel, M. C. Wei, and S. J. Korsmeyer. 1998. Enforced dimerization of BAX results in its translocation, mitochondrial dysfunction and apoptosis. EMBO J. 17:3878-3885.
    • (1998) EMBO J. , vol.17 , pp. 3878-3885
    • Gross, A.1    Jockel, J.2    Wei, M.C.3    Korsmeyer, S.J.4
  • 19
    • 0033179760 scopus 로고    scopus 로고
    • BCL-2 family members and the mitochondria in apoptosis
    • Gross, A., J. McDonnell, and S. Korsmeyer. 1999a. BCL-2 family members and the mitochondria in apoptosis. Genes Dev. 13:1899-1911.
    • (1999) Genes Dev. , vol.13 , pp. 1899-1911
    • Gross, A.1    McDonnell, J.2    Korsmeyer, S.3
  • 21
    • 0026741882 scopus 로고
    • Anti-Cdc25 antibodies inhibit guanyl nucleotide-dependent adenylyl cyclase of Saccharomyces cerevisiae and cross-react with a 150-kilodalton mammalian protein
    • Gross, E., I. Marbach, D. Engelberg, M. Segal, G. Simchen, and A. Levitzki. 1992. Anti-Cdc25 antibodies inhibit guanyl nucleotide-dependent adenylyl cyclase of Saccharomyces cerevisiae and cross-react with a 150-kilodalton mammalian protein. Mol. Cell. Biol. 12:2653-2661.
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 2653-2661
    • Gross, E.1    Marbach, I.2    Engelberg, D.3    Segal, M.4    Simchen, G.5    Levitzki, A.6
  • 22
    • 0025204548 scopus 로고
    • Bcl-2 is an inner mitochondrial membrane protein that blocks programmed cell death
    • Hockenbery, D., G. Nunez, C. Milliman, R. D. Schreiber, and S. J. Korsmeyer. 1990. Bcl-2 is an inner mitochondrial membrane protein that blocks programmed cell death. Nature 348:334-336.
    • (1990) Nature , vol.348 , pp. 334-336
    • Hockenbery, D.1    Nunez, G.2    Milliman, C.3    Schreiber, R.D.4    Korsmeyer, S.J.5
  • 24
    • 0030047365 scopus 로고    scopus 로고
    • Functional dissection of the human Bcl-2 protein: Sequence requirements for inhibition of apoptosis
    • Hunter, J. J., B. L. Bond, and T. G. Parslow. 1996. Functional dissection of the human Bcl-2 protein: sequence requirements for inhibition of apoptosis. Mol. Cell. Biol. 16:877-883.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 877-883
    • Hunter, J.J.1    Bond, B.L.2    Parslow, T.G.3
  • 25
    • 1842417077 scopus 로고    scopus 로고
    • Human Bak induces cell death in Schizosaccharomyces pombe with morphological changes similar to those with apoptosis in mammalian cells
    • Ink, B., M. Zornig, B. Baum, N. Hajibagheri, C. James, T. Chittenden, and G. Evan. 1997. Human Bak induces cell death in Schizosaccharomyces pombe with morphological changes similar to those with apoptosis in mammalian cells. Mol. Cell. Biol. 17:2458-2474.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 2458-2474
    • Ink, B.1    Zornig, M.2    Baum, B.3    Hajibagheri, N.4    James, C.5    Chittenden, T.6    Evan, G.7
  • 26
    • 0030947095 scopus 로고    scopus 로고
    • Programmed cell death in animal development
    • Jacobson, M. D., M. Weil, and M. C. Raff. 1997. Programmed cell death in animal development. Cell 88:347-354.
    • (1997) Cell , vol.88 , pp. 347-354
    • Jacobson, M.D.1    Weil, M.2    Raff, M.C.3
  • 27
    • 0030826637 scopus 로고    scopus 로고
    • Properties of a cyclosporin-insensitive permeability transition pore in yeast mitochondria
    • Jung, D. W., P. C. Bradshaw, and D. R. Pfeiffer. 1997. Properties of a cyclosporin-insensitive permeability transition pore in yeast mitochondria. J. Biol. Chem. 272:21104-21112.
    • (1997) J. Biol. Chem. , vol.272 , pp. 21104-21112
    • Jung, D.W.1    Bradshaw, P.C.2    Pfeiffer, D.R.3
  • 29
    • 0031037897 scopus 로고    scopus 로고
    • The release of cytochrome c from mitochondria: A primary site for Bcl-2 regulation of apoptosis
    • Kluck, R. M., E. Bossy-Wetzel, D. R. Green, and D. D. Newmeyer. 1997. The release of cytochrome c from mitochondria: a primary site for Bcl-2 regulation of apoptosis. Science 275:1132-1136.
    • (1997) Science , vol.275 , pp. 1132-1136
    • Kluck, R.M.1    Bossy-Wetzel, E.2    Green, D.R.3    Newmeyer, D.D.4
  • 30
    • 0030861571 scopus 로고    scopus 로고
    • Bcl-2 and Bax function independently to regulate cell death
    • Knudson, C. M., and S. J. Korsmeyer. 1997. Bcl-2 and Bax function independently to regulate cell death. Nat. Genet. 16:358-363.
    • (1997) Nat. Genet. , vol.16 , pp. 358-363
    • Knudson, C.M.1    Korsmeyer, S.J.2
  • 31
    • 0027362667 scopus 로고
    • Investigation of the subcellular distribution of the Bcl-2 onco-protein: Residence in the nuclear envelope, endoplasmic reticulum, and outer mitochondrial membranes
    • Krajewski, S., S. Tanaka, S. Takayama, M. J. Schibler, W. Fenton, and J. C. Reed. 1993. Investigation of the subcellular distribution of the Bcl-2 onco-protein: residence in the nuclear envelope, endoplasmic reticulum, and outer mitochondrial membranes. Cancer Res. 53:4701-4714.
    • (1993) Cancer Res. , vol.53 , pp. 4701-4714
    • Krajewski, S.1    Tanaka, S.2    Takayama, S.3    Schibler, M.J.4    Fenton, W.5    Reed, J.C.6
  • 32
    • 0024288852 scopus 로고    scopus 로고
    • Separate genes encode functionally equivalent ADP/ATP carrier proteins in Saccharomyces cerevisiae. Isolation and analysis of AAC2
    • Lawson, J. E., and M. G. Douglas. 1998. Separate genes encode functionally equivalent ADP/ATP carrier proteins in Saccharomyces cerevisiae. Isolation and analysis of AAC2. J. Biol. Chem. 263:14812-14818.
    • (1998) J. Biol. Chem. , vol.263 , pp. 14812-14818
    • Lawson, J.E.1    Douglas, M.G.2
  • 33
    • 0021165666 scopus 로고
    • Differential regulation of the duplicated isocytochrome c genes in yeast
    • Laz, T. M., D. F. Pietras, and F. Sherman. 1984. Differential regulation of the duplicated isocytochrome c genes in yeast. Proc. Natl. Acad. Sci. USA 81:4475-4479.
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 4475-4479
    • Laz, T.M.1    Pietras, D.F.2    Sherman, F.3
  • 35
    • 0030715323 scopus 로고    scopus 로고
    • Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade
    • Li, P., D. Nijhawan, I. Budihardjo, S. M. Srinivasula, M. Ahmad, E. S. Alnemri, and X. Wang. 1997. Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade. Cell 91:474-489.
    • (1997) Cell , vol.91 , pp. 474-489
    • Li, P.1    Nijhawan, D.2    Budihardjo, I.3    Srinivasula, S.M.4    Ahmad, M.5    Alnemri, E.S.6    Wang, X.7
  • 37
    • 0029843941 scopus 로고    scopus 로고
    • Cross talk between cell death and cell cycle progression: Bcl-2 regulates NFAT-mediated activation
    • Linette, G., Y. Li, K. Roth, and S. Korsmeyer. 1996. Cross talk between cell death and cell cycle progression: Bcl-2 regulates NFAT-mediated activation. Proc. Natl. Acad. Sci. USA 93:4545-9552.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 4545-9552
    • Linette, G.1    Li, Y.2    Roth, K.3    Korsmeyer, S.4
  • 38
    • 0030581151 scopus 로고    scopus 로고
    • Induction of apoptotic program in cell-free extracts: Requirement for dATP and cytochrome c
    • Liu, X., C. Kim, J. Yang, R. Jemmerson, and X. Wang. 1996. Induction of apoptotic program in cell-free extracts: requirement for dATP and cytochrome c. Cell 86:147-157.
    • (1996) Cell , vol.86 , pp. 147-157
    • Liu, X.1    Kim, C.2    Yang, J.3    Jemmerson, R.4    Wang, X.5
  • 39
    • 0029042961 scopus 로고
    • Gene disruption with PCR products in Saccharomyces cerevisiae
    • Lorenz, M. C., R. S. Muir, E. Lim, J. McElver, S. C. Weber, and J. Heitman. 1995. Gene disruption with PCR products in Saccharomyces cerevisiae. Gene 158:113-117.
    • (1995) Gene , vol.158 , pp. 113-117
    • Lorenz, M.C.1    Muir, R.S.2    Lim, E.3    McElver, J.4    Weber, S.C.5    Heitman, J.6
  • 40
    • 0032555716 scopus 로고    scopus 로고
    • Bcl-2 interacting protein, mediates cytochrome c release from mitochondria in response to activation of cell surface death receptors
    • Luo, X., I. Budihardjo, H. Zou, C. Slaughter, and X. Wang. 1998. Bcl-2 interacting protein, mediates cytochrome c release from mitochondria in response to activation of cell surface death receptors. Cell 94:481-490.
    • (1998) Cell , vol.94 , pp. 481-490
    • Luo, X.1    Budihardjo, I.2    Zou, H.3    Slaughter, C.4    Wang, X.5
  • 41
  • 44
    • 0033535345 scopus 로고    scopus 로고
    • The release of cytochrome c from mitochondria during apoptosis of NGF-deprived sympathetic neurons is a reversible event
    • Martinou, I., S. Desagher, R. Eskes, B. Antonsson, E. Andre, S. Fakan, and J. C. Martinou. 1999. The release of cytochrome c from mitochondria during apoptosis of NGF-deprived sympathetic neurons is a reversible event. J. Cell Biol. 144:883-889.
    • (1999) J. Cell Biol. , vol.144 , pp. 883-889
    • Martinou, I.1    Desagher, S.2    Eskes, R.3    Antonsson, B.4    Andre, E.5    Fakan, S.6    Martinou, J.C.7
  • 48
    • 0031993196 scopus 로고    scopus 로고
    • The mitochondrial FOF1-ATPase proton pump is required for function of the proapoptotic protein Bax in yeast and mammalian cells
    • Matsuyama, S., Q. Xu, J. Velours, and J. C. Reed. 1998. The mitochondrial FOF1-ATPase proton pump is required for function of the proapoptotic protein Bax in yeast and mammalian cells. Mol. Cell 1:327-336.
    • (1998) Mol. Cell , vol.1 , pp. 327-336
    • Matsuyama, S.1    Xu, Q.2    Velours, J.3    Reed, J.C.4
  • 49
    • 0031033274 scopus 로고    scopus 로고
    • Inhibition of Ced-3/ICE-related proteases does not prevent cell death induced by oncogenes, DNA damage, or the Bcl-2 homologue Bak
    • McCarthy, N. J., M. K. Whyte, C. S. Gilbert, and G. I. Evan. 1997. Inhibition of Ced-3/ICE-related proteases does not prevent cell death induced by oncogenes, DNA damage, or the Bcl-2 homologue Bak. J. Cell Biol. 136: 215-227.
    • (1997) J. Cell Biol. , vol.136 , pp. 215-227
    • McCarthy, N.J.1    Whyte, M.K.2    Gilbert, C.S.3    Evan, G.I.4
  • 54
    • 0032422488 scopus 로고    scopus 로고
    • Bax interacts with the permeability transition pore to induce permeability transition and cytochrome c release in isolated mitochondria
    • Narita, M., S. Shimizu, T. Ito, T. Chittenden, R. J. Lutz, H. Matsuda, and Y. Tsujimoto. 1998. Bax interacts with the permeability transition pore to induce permeability transition and cytochrome c release in isolated mitochondria. Proc. Natl. Acad. Sci. USA 95:14681-14686.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 14681-14686
    • Narita, M.1    Shimizu, S.2    Ito, T.3    Chittenden, T.4    Lutz, R.J.5    Matsuda, H.6    Tsujimoto, Y.7
  • 55
    • 0033522391 scopus 로고    scopus 로고
    • Conformation of the Bax C-terminus regulates subcellular location and cell death
    • Nechushtan, A., C. L. Smith, Y. T. Hsu, and R. J. Youle. 1999. Conformation of the Bax C-terminus regulates subcellular location and cell death. EMBO J. 18:2330-2341.
    • (1999) EMBO J. , vol.18 , pp. 2330-2341
    • Nechushtan, A.1    Smith, C.L.2    Hsu, Y.T.3    Youle, R.J.4
  • 57
    • 0032571294 scopus 로고    scopus 로고
    • The overexpression of Bax produces cell death upon induction of the mitochondrial permeability transition
    • Pastorino, J. G., S. T. Chen, M. Tafani, J. W. Snyder, and J. L. Farber. 1998. The overexpression of Bax produces cell death upon induction of the mitochondrial permeability transition. J. Biol. Chem. 273:7770-7775.
    • (1998) J. Biol. Chem. , vol.273 , pp. 7770-7775
    • Pastorino, J.G.1    Chen, S.T.2    Tafani, M.3    Snyder, J.W.4    Farber, J.L.5
  • 58
    • 0024829751 scopus 로고
    • Protein import into mitochondria: ATP-dependent protein translocation activity in a submitochondrial fraction enriched in membrane contact sites and specific proteins
    • Pon, L., T. Moll, D. Vestweber, B. Marshallsay, and G. Schatz. 1989. Protein import into mitochondria: ATP-dependent protein translocation activity in a submitochondrial fraction enriched in membrane contact sites and specific proteins. J. Cell Biol. 109:2603-2616.
    • (1989) J. Cell Biol. , vol.109 , pp. 2603-2616
    • Pon, L.1    Moll, T.2    Vestweber, D.3    Marshallsay, B.4    Schatz, G.5
  • 60
    • 0032815221 scopus 로고    scopus 로고
    • Comparison of the effects of bax-expression in yeast under fermentative and respiratory conditions: Investigation of the role of adenine nucleotides carrier and cytochrome c
    • Priault, M., N. Camougrand, B. Chaudhuri, J. Schaeffer, and S. Manon. 1999. Comparison of the effects of bax-expression in yeast under fermentative and respiratory conditions: investigation of the role of adenine nucleotides carrier and cytochrome c. FEBS Lett. 456:232-238.
    • (1999) FEBS Lett. , vol.456 , pp. 232-238
    • Priault, M.1    Camougrand, N.2    Chaudhuri, B.3    Schaeffer, J.4    Manon, S.5
  • 61
    • 0033559998 scopus 로고    scopus 로고
    • Investigation of bax-induced release of cytochrome c from yeast mitochondria permeability of mitochondrial membranes, role of VDAC and ATP requirement
    • Priault, M., B. Chaudhuri, A. Clow, N. Camougrand, and S. Manon. 1999. Investigation of bax-induced release of cytochrome c from yeast mitochondria permeability of mitochondrial membranes, role of VDAC and ATP requirement. Eur. J. Biochem. 260:684-691.
    • (1999) Eur. J. Biochem. , vol.260 , pp. 684-691
    • Priault, M.1    Chaudhuri, B.2    Clow, A.3    Camougrand, N.4    Manon, S.5
  • 63
    • 0025979877 scopus 로고
    • Targeting, disruption, replacement, and allele rescue: Integrative DNA transformation in yeast
    • Rothstein, R. 1991. Targeting, disruption, replacement, and allele rescue: integrative DNA transformation in yeast. Methods Enzymol. 194:281-301.
    • (1991) Methods Enzymol. , vol.194 , pp. 281-301
    • Rothstein, R.1
  • 67
    • 0033519705 scopus 로고    scopus 로고
    • Bcl-2 family proteins regulate the release of apoptogenic cytochrome c by the mitochondrial channel VDAC
    • Shimizu, S., M. Narita, and Y. Tsujimoto. 1999. Bcl-2 family proteins regulate the release of apoptogenic cytochrome c by the mitochondrial channel VDAC. Nature 399:483-487.
    • (1999) Nature , vol.399 , pp. 483-487
    • Shimizu, S.1    Narita, M.2    Tsujimoto, Y.3
  • 68
    • 0024669291 scopus 로고
    • A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae
    • Sikorski, R. S., and P. Hieter. 1989. A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae. Genetics 122:19-27.
    • (1989) Genetics , vol.122 , pp. 19-27
    • Sikorski, R.S.1    Hieter, A.P.2
  • 71
    • 0032504575 scopus 로고    scopus 로고
    • Mitochondria as regulators of apoptosis: Doubt no more
    • Susin, S. A., N. Zamzami, and G. Kroemer. 1998. Mitochondria as regulators of apoptosis: doubt no more. Biochim. Biophys. Acta 1366:151-165.
    • (1998) Biochim. Biophys. Acta , vol.1366 , pp. 151-165
    • Susin, S.A.1    Zamzami, N.2    Kroemer, G.3
  • 73
    • 0030915927 scopus 로고    scopus 로고
    • Modulation of cell death in yeast by the Bcl-2 family of proteins
    • Tao, W., C. Kurschner, and J. I. Morgan. 1997. Modulation of cell death in yeast by the Bcl-2 family of proteins. J. Biol. Chem. 272:15547-15552.
    • (1997) J. Biol. Chem. , vol.272 , pp. 15547-15552
    • Tao, W.1    Kurschner, C.2    Morgan, J.I.3
  • 74
    • 0028943734 scopus 로고
    • Apoptosis in the pathogenesis and treatment of disease
    • Thompson, C. B. 1995. Apoptosis in the pathogenesis and treatment of disease. Science 267:1456-1462.
    • (1995) Science , vol.267 , pp. 1456-1462
    • Thompson, C.B.1
  • 76
    • 0031660082 scopus 로고    scopus 로고
    • Mutagenesis of the BH3 domain of BAX identifies residues critical for dimerization and killing
    • Wang, K., A. Gross, G. Waksman, and S. J. Korsmeyer. 1998. Mutagenesis of the BH3 domain of BAX identifies residues critical for dimerization and killing. Mol. Cell. Biol. 18:6083-6089.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 6083-6089
    • Wang, K.1    Gross, A.2    Waksman, G.3    Korsmeyer, S.J.4
  • 80
    • 0029906828 scopus 로고    scopus 로고
    • BAX-induced cell death may not require interleukin 1 beta-converting enzyme-like proteases
    • Xiang, J., D. T. Chao, and S. J. Korsmeyer. 1996. BAX-induced cell death may not require interleukin 1 beta-converting enzyme-like proteases. Proc. Natl. Acad. Sci. USA 93:14559-14563.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 14559-14563
    • Xiang, J.1    Chao, D.T.2    Korsmeyer, S.J.3
  • 81
  • 82
    • 0029848765 scopus 로고    scopus 로고
    • Structure-function comparisons of the proapoptotic protein Bax in yeast and mammalian cells
    • Zha, H., H. A. Fisk, M. P. Yaffe, N. Mahajan, B. Herman, and J. C. Reed. 1996a. Structure-function comparisons of the proapoptotic protein Bax in yeast and mammalian cells. Mol. Cell. Biol. 16:6494-6508.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 6494-6508
    • Zha, H.1    Fisk, H.A.2    Yaffe, M.P.3    Mahajan, N.4    Herman, B.5    Reed, J.C.6
  • 83
    • 0031436251 scopus 로고    scopus 로고
    • Heterodimerization-independent functions of cell death regulatory proteins Bax and Bcl-2 in yeast and mammalian cells
    • Zha, H., and J. Reed. 1997. Heterodimerization-independent functions of cell death regulatory proteins Bax and Bcl-2 in yeast and mammalian cells. J. Biol. Chem. 272:31482-31488.
    • (1997) J. Biol. Chem. , vol.272 , pp. 31482-31488
    • Zha, H.1    Reed, A.J.2
  • 85
    • 0029116916 scopus 로고
    • The mitochondrial permeability transition
    • Zoratti, M., and I. Szabo. 1995. The mitochondrial permeability transition. Biochim. Biophys. Acta 1241:139-176.
    • (1995) Biochim. Biophys. Acta , vol.1241 , pp. 139-176
    • Zoratti, M.1    Szabo, I.2
  • 86
    • 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., W. J. Henzel, X. Liu, A. Lutschg, and X. Wang. 1997. 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) 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.