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Volumn 116, Issue 3, 2003, Pages 525-536

Outer mitochondrial membrane permeabilization during apoptosis triggers caspase-independent mitochondrial and caspase-dependent plasma membrane potential depolarization: A single-cell analysis

Author keywords

Apoptosis; Confocal imaging; Mitochondrial membrane potential; Mitochondrial respiration; Plasma membrane potential

Indexed keywords

ADENOSINE TRIPHOSPHATASE (POTASSIUM SODIUM); CARBONYL CYANIDE 4 (TRIFLUOROMETHOXY)PHENYLHYDRAZONE; CASPASE; CASPASE INHIBITOR; CYTOCHROME C; GREEN FLUORESCENT PROTEIN; HYBRID PROTEIN; OLIGOMYCIN; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE;

EID: 0037326590     PISSN: 00219533     EISSN: None     Source Type: Journal    
DOI: 10.1242/jcs.00236     Document Type: Review
Times cited : (99)

References (55)
  • 1
    • 0032908855 scopus 로고    scopus 로고
    • Role of the intracellular domain of the β subunit in Na,K pump function
    • Abriel, H., Hasler, U., Geering, K. and Horisberger, J.-D. (1999). Role of the intracellular domain of the β subunit in Na,K pump function. Biochim. Biophys. Acta 1418, 85-96.
    • (1999) Biochim. Biophys. Acta , vol.1418 , pp. 85-96
    • Abriel, H.1    Hasler, U.2    Geering, K.3    Horisberger, J.-D.4
  • 2
    • 0030803271 scopus 로고    scopus 로고
    • Bcl-2 and the outer mitochondrial membrane in the inactivation of cytochrome c during Fas-mediated apoptosis
    • Adachi, S., Cross, A., Babior, B. and Gottlieb, R. (1997). Bcl-2 and the outer mitochondrial membrane in the inactivation of cytochrome c during Fas-mediated apoptosis. J. Biol. Chem. 272, 21878-21882.
    • (1997) J. Biol. Chem. , vol.272 , pp. 21878-21882
    • Adachi, S.1    Cross, A.2    Babior, B.3    Gottlieb, R.4
  • 3
    • 0033618445 scopus 로고    scopus 로고
    • Caspase independent/dependent regulation of K(+), cell shrinkage, and mitochondrial membrane potential during lymphocyte apoptosis
    • Bortner, C. and Cidlowski, J. (1999). Caspase independent/dependent regulation of K(+), cell shrinkage, and mitochondrial membrane potential during lymphocyte apoptosis. J. Biol. Chem. 274, 21953-21962.
    • (1999) J. Biol. Chem. , vol.274 , pp. 21953-21962
    • Bortner, C.1    Cidlowski, J.2
  • 4
    • 0035830843 scopus 로고    scopus 로고
    • Plasma membrane depolarization without repolarization is an early molecular event in anti-Fas-induced apoptosis
    • Bortner, C. D., Gómez-Angelats, M. and Cidlowski, J. A. (2001). Plasma membrane depolarization without repolarization is an early molecular event in anti-Fas-induced apoptosis. J. Biol. Chem. 276, 4304-4314.
    • (2001) J. Biol. Chem. , vol.276 , pp. 4304-4314
    • Bortner, C.D.1    Gómez-Angelats, M.2    Cidlowski, J.A.3
  • 5
    • 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. and Green, D. R. (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
  • 6
    • 0032496143 scopus 로고    scopus 로고
    • Superoxide in apoptosis. Mitochondrial generation triggered by cytochrome c loss
    • Cai, J. and Jones, D. P. (1998). Superoxide in apoptosis. Mitochondrial generation triggered by cytochrome c loss. J. Biol. Chem. 273, 11401-11404.
    • (1998) J. Biol. Chem. , vol.273 , pp. 11401-11404
    • Cai, J.1    Jones, D.P.2
  • 7
    • 0037182587 scopus 로고    scopus 로고
    • Cyclosporin A inhibits caspase-independent death of NGF-deprived sympathetic neurons: A potential role for mitochondrial permeability transition
    • Chang, L. and Johnson, E. J. (2002). Cyclosporin A inhibits caspase-independent death of NGF-deprived sympathetic neurons: a potential role for mitochondrial permeability transition. J. Cell Biol. 157, 771-781.
    • (2002) J. Cell Biol. , vol.157 , pp. 771-781
    • Chang, L.1    Johnson, E.J.2
  • 8
    • 0031569361 scopus 로고    scopus 로고
    • Membrane potential changes visualized in complete growth media through confocal laser scanning microscopy of bis-oxonol-loaded cells
    • Dall'Asta, V., Gatti, R., Orlandini, G., Rossi, P. A., Rotoli, B. M., Sala, R., Bussolati, O. and Gazzola, G. C. (1997). Membrane potential changes visualized in complete growth media through confocal laser scanning microscopy of bis-oxonol-loaded cells. Exp. Cell Res. 231, 260-268.
    • (1997) Exp. Cell Res. , vol.231 , pp. 260-268
    • Dall'Asta, V.1    Gatti, R.2    Orlandini, G.3    Rossi, P.A.4    Rotoli, B.M.5    Sala, R.6    Bussolati, O.7    Gazzola, G.C.8
  • 9
    • 0034631832 scopus 로고    scopus 로고
    • Caspase inhibition extends the commitment to neuronal death beyond cytochrome c release to the point of mitochondrial depolarization
    • Deshmukh, M., Kuida, K. and Johnson, E. M., Jr (2000). Caspase inhibition extends the commitment to neuronal death beyond cytochrome c release to the point of mitochondrial depolarization. J. Cell Biol. 150, 131-143.
    • (2000) J. Cell Biol. , vol.150 , pp. 131-143
    • Deshmukh, M.1    Kuida, K.2    Johnson E.M., Jr.3
  • 11
    • 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. and Wang, X. (2000). Smac, a mitochondrial protein that promotes cytochrome c-dependent caspase activation by eliminating IAP inhibition. Cell 102, 33-42.
    • (2000) Cell , vol.102 , pp. 33-42
    • Du, C.1    Fang, M.2    Li, Y.3    Li, L.4    Wang, X.5
  • 13
    • 0030915587 scopus 로고    scopus 로고
    • Intracellular ATP levels determine cell death fate by apoptosis or necrosis
    • Eguchi, Y., Shimizu, S. and Tsujimoto, Y. (1997). Intracellular ATP levels determine cell death fate by apoptosis or necrosis. Cancer Res. 57, 1835-1840.
    • (1997) Cancer Res. , vol.57 , pp. 1835-1840
    • Eguchi, Y.1    Shimizu, S.2    Tsujimoto, Y.3
  • 14
    • 0023928504 scopus 로고
    • Membrane potential can be determined in individual cells from the nernstian distribution of cationic dyes
    • Ehrenberg, B., Montana, V., Wei, M., Wuskell, J. and Loew, L. (1988). Membrane potential can be determined in individual cells from the nernstian distribution of cationic dyes. Biophys. J. 53, 785-794.
    • (1988) Biophys. J. , vol.53 , pp. 785-794
    • Ehrenberg, B.1    Montana, V.2    Wei, M.3    Wuskell, J.4    Loew, L.5
  • 15
    • 0034811051 scopus 로고    scopus 로고
    • Bcl-2 decreases voltage-gated K+ channel activity and enhances survival in vascular smooth muscle cells
    • Ekhterae, D., Platoshyn, O., Krick, S., Yu, Y., McDaniel, S. S. and Yuan, J. X. (2001). Bcl-2 decreases voltage-gated K+ channel activity and enhances survival in vascular smooth muscle cells. Am. J. Physiol. Cell Physiol. 281, C157-C165.
    • (2001) Am. J. Physiol. Cell Physiol. , vol.281
    • Ekhterae, D.1    Platoshyn, O.2    Krick, S.3    Yu, Y.4    McDaniel, S.S.5    Yuan, J.X.6
  • 16
    • 0034723201 scopus 로고    scopus 로고
    • Characterization of a novel human serine protease that has extensive homology to bacterial heat shock endoprotease HtrA and is regulated by kidney ischemia
    • Faccio, L., Fusco, C., Chen, A., Martinotti, S., Bonventre, J. and Zervos, A. (2000). Characterization of a novel human serine protease that has extensive homology to bacterial heat shock endoprotease HtrA and is regulated by kidney ischemia. J. Biol. Chem. 275, 2581-2588.
    • (2000) J. Biol. Chem. , vol.275 , pp. 2581-2588
    • Faccio, L.1    Fusco, C.2    Chen, A.3    Martinotti, S.4    Bonventre, J.5    Zervos, A.6
  • 17
    • 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. and Green, D. R. (2000). The coordinate release of cytochrome c during apoptosis is rapid, complete and kinetically invariant. Nat. Cell Biol. 2, 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
  • 18
    • 0033598713 scopus 로고    scopus 로고
    • Poly(ADP-ribose) polymerase is a mediator of necrotic cell death by ATP depletion
    • Ha, H. and Snyder, S. (1999). Poly(ADP-ribose) polymerase is a mediator of necrotic cell death by ATP depletion. Proc. Natl. Acad. Sci. USA 96, 13978-13982.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 13978-13982
    • Ha, H.1    Snyder, S.2
  • 19
    • 0034525374 scopus 로고    scopus 로고
    • The role of the Bcl-2 family in the regulation of outer mitochondrial membrane permeability
    • Harris, M. and Thompson, C. (2000). The role of the Bcl-2 family in the regulation of outer mitochondrial membrane permeability. Cell Death Differ. 7, 1182-1191.
    • (2000) Cell Death Differ. , vol.7 , pp. 1182-1191
    • Harris, M.1    Thompson, C.2
  • 21
    • 0033605376 scopus 로고    scopus 로고
    • Mitochondrial, depolarization accompanies cytochrome c release during apoptosis in PC6 cells
    • Heiskanen, K. M., Bhat, M. B., Wang, H. W., Ma, J. and Nieminen, A. L. (1999). Mitochondrial, depolarization accompanies cytochrome c release during apoptosis in PC6 cells. J. Biol. Chem. 274, 5654-5658.
    • (1999) J. Biol. Chem. , vol.274 , pp. 5654-5658
    • Heiskanen, K.M.1    Bhat, M.B.2    Wang, H.W.3    Ma, J.4    Nieminen, A.L.5
  • 22
    • 0027476151 scopus 로고
    • Bcl-2 blocks apoptosis in cells lacking mitochondrial DNA
    • Jacobson, M., Burne, J., King, M., Miyashita, T., Reed, J. and Raff, M. (1993). Bcl-2 blocks apoptosis in cells lacking mitochondrial DNA. Nature 361, 365-369.
    • (1993) Nature , vol.361 , pp. 365-369
    • Jacobson, M.1    Burne, J.2    King, M.3    Miyashita, T.4    Reed, J.5    Raff, M.6
  • 23
    • 0033198273 scopus 로고    scopus 로고
    • Mitochondrial depolarization is not required for neuronal apoptosis
    • Krohn, A. J., Wahlbrink, T. and Prehn, J. H. M. (1999). Mitochondrial depolarization is not required for neuronal apoptosis. J. Neurosci. 19, 7394-7404.
    • (1999) J. Neurosci. , vol.19 , pp. 7394-7404
    • Krohn, A.J.1    Wahlbrink, T.2    Prehn, J.H.M.3
  • 24
    • 0030900980 scopus 로고    scopus 로고
    • Intracellular adenosine triphosphate (ATP) concentration: A switch in the decision between apoptosis and necrosis
    • Leist, M., Single, B., Castoldi, A. F., Kühnle, S. and Nicotera, P. (1997). Intracellular adenosine triphosphate (ATP) concentration: A switch in the decision between apoptosis and necrosis. J. Exp. Med. 185, 1481-1486.
    • (1997) J. Exp. Med. , vol.185 , pp. 1481-1486
    • Leist, M.1    Single, B.2    Castoldi, A.F.3    Kühnle, S.4    Nicotera, P.5
  • 26
    • 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. and Wang, X. (1997). Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade. Cell 91, 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
  • 27
    • 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. and Wang, X. (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.N.2    Yang, J.3    Jemmerson, R.4    Wang, X.5
  • 28
    • 0034254932 scopus 로고    scopus 로고
    • Delayed mitochondrial dysfunction in excitotoxic neuron death: Cytochrome c release and a secondary increase in superoxide production
    • Luetjens, C. M., Bui, N. T., Sengpiel, B., Munstermann, G., Poppe, M., Krohn, A. J., Bauerbach, E., Krieglstein, J. and Prehn, J. H. M. (2000). Delayed mitochondrial dysfunction in excitotoxic neuron death: Cytochrome c release and a secondary increase in superoxide production. J. Neurosci. 20, 5715-5723.
    • (2000) J. Neurosci. , vol.20 , pp. 5715-5723
    • Luetjens, C.M.1    Bui, N.T.2    Sengpiel, B.3    Munstermann, G.4    Poppe, M.5    Krohn, A.J.6    Bauerbach, E.7    Krieglstein, J.8    Prehn, J.H.M.9
  • 30
    • 0037085380 scopus 로고    scopus 로고
    • Rapid kinetics of tBid-induced cytochrome c and Smac/DIABLO release and mitochondrial depolarization
    • Madesh, M., Antonsson, B., Srinivasula, M. S., Alnemri, E. S. and Hajnóczky, G. (2002). Rapid kinetics of tBid-induced cytochrome c and Smac/DIABLO release and mitochondrial depolarization. J. Biol. Chem. 277, 5651-5659.
    • (2002) J. Biol. Chem. , vol.277 , pp. 5651-5659
    • Madesh, M.1    Antonsson, B.2    Srinivasula, M.S.3    Alnemri, E.S.4    Hajnóczky, G.5
  • 31
    • 0034662989 scopus 로고    scopus 로고
    • Normotonic cell shrinkage because of disordered volume regulation is an early prerequisite to apoptosis
    • Maeno, E., Ishizaki, Y., Kanaseki, T., Hazama, A. and Okada, Y. (2000). Normotonic cell shrinkage because of disordered volume regulation is an early prerequisite to apoptosis. Proc. Natl. Acad. Sci. USA 97, 9487-9492.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 9487-9492
    • Maeno, E.1    Ishizaki, Y.2    Kanaseki, T.3    Hazama, A.4    Okada, Y.5
  • 33
    • 0033776271 scopus 로고    scopus 로고
    • Changes in intramitochondrial and cytosolic pH: Early events that modulate caspase activation during apoptosis
    • Matsuyama, S., Llopis, J., Deveraux, Q. L., Tsien, R. Y. and Reed, J. C. (2000). Changes in intramitochondrial and cytosolic pH: Early events that modulate caspase activation during apoptosis. Nat. Cell Biol. 2, 318-325.
    • (2000) Nat. Cell Biol. , vol.2 , pp. 318-325
    • Matsuyama, S.1    Llopis, J.2    Deveraux, Q.L.3    Tsien, R.Y.4    Reed, J.C.5
  • 34
    • 0035865134 scopus 로고    scopus 로고
    • A reversible component of mitochondrial respiratory dysfunction in apoptosis can be rescued by exogenous cytochrome c
    • Mootha, V. K., Wei, M. C., Buttle, K. F., Scorrano, L., Panoutsakopoulou, V., Mannella, C. A. and Korsmeyer, S. J. (2001). A reversible component of mitochondrial respiratory dysfunction in apoptosis can be rescued by exogenous cytochrome c. EMBO J. 20, 661-671.
    • (2001) EMBO J. , vol.20 , pp. 661-671
    • Mootha, V.K.1    Wei, M.C.2    Buttle, K.F.3    Scorrano, L.4    Panoutsakopoulou, V.5    Mannella, C.A.6    Korsmeyer, S.J.7
  • 35
    • 0034176843 scopus 로고    scopus 로고
    • Mitochondrial membrane potential and neuronal glutamate excitotoxicity: Mortality and millivolts
    • Nicholls, D. and Ward, M. (2000). Mitochondrial membrane potential and neuronal glutamate excitotoxicity: mortality and millivolts. Trends Neurosci. 23, 166-174.
    • (2000) Trends Neurosci. , vol.23 , pp. 166-174
    • Nicholls, D.1    Ward, M.2
  • 37
    • 0035851110 scopus 로고    scopus 로고
    • BH3 death domain peptide induces cell type-selective mitochondrial outer membrane permeability
    • Polster, B. M., Kinnally, K. W. and Fiskum, G. (2001). BH3 death domain peptide induces cell type-selective mitochondrial outer membrane permeability. J. Biol. Chem. 276, 37887-37894.
    • (2001) J. Biol. Chem. , vol.276 , pp. 37887-37894
    • Polster, B.M.1    Kinnally, K.W.2    Fiskum, G.3
  • 38
    • 0035400121 scopus 로고    scopus 로고
    • Dissipation of potassium and proton gradients inhibits mitochondrial hyperpolarization and cytochrome c release during neural apoptosis
    • Poppe, M., Reimertz, C., Dussmann, H., Krohn, A. J., Luetjens, C. M., Bockelmann, D., Nieminen, A. L., Kogel, D. and Prehn, J. H. M. (2001). Dissipation of potassium and proton gradients inhibits mitochondrial hyperpolarization and cytochrome c release during neural apoptosis. J. Neurosci. 21, 4551-4563.
    • (2001) J. Neurosci. , vol.21 , pp. 4551-4563
    • Poppe, M.1    Reimertz, C.2    Dussmann, H.3    Krohn, A.J.4    Luetjens, C.M.5    Bockelmann, D.6    Nieminen, A.L.7    Kogel, D.8    Prehn, J.H.M.9
  • 39
    • 0034781572 scopus 로고    scopus 로고
    • The mechanism of mitochondrial membrane potential retention following release of cytochrome c in apoptotic GT1-7 neural cells
    • Rego, A. C., Vesce, S. and Nicholls, D. G. (2001). The mechanism of mitochondrial membrane potential retention following release of cytochrome c in apoptotic GT1-7 neural cells. Cell Death Differ. 8, 995-1003.
    • (2001) Cell Death Differ. , vol.8 , pp. 995-1003
    • Rego, A.C.1    Vesce, S.2    Nicholls, D.G.3
  • 40
    • 0037025346 scopus 로고    scopus 로고
    • Single-cell fluorescence resonance energy transfer analysis demonstrates that caspase activation during apoptosis is a rapid process: Role of caspase-3
    • Rehm, M., Dussmann, H., Janicke, R. U., Tavaré, J. M., Kogel, D. and Prehn, J. H. M. (2002). Single-cell fluorescence resonance energy transfer analysis demonstrates that caspase activation during apoptosis is a rapid process: Role of caspase-3. J. Biol. Chem. 277, 24506-24514.
    • (2002) J. Biol. Chem. , vol.277 , pp. 24506-24514
    • Rehm, M.1    Dussmann, H.2    Janicke, R.U.3    Tavaré, J.M.4    Kogel, D.5    Prehn, J.H.M.6
  • 41
    • 0035469830 scopus 로고    scopus 로고
    • Rapid extracellular release of cytochrome c is specific for apoptosis and marks cell death in vivo
    • Renz, A., Berdel, W., Kreuter, M., Belka, C., Schulze-Osthoff, K. and Los, M. (2001). Rapid extracellular release of cytochrome c is specific for apoptosis and marks cell death in vivo. Blood 98, 1542-1548.
    • (2001) Blood , vol.98 , pp. 1542-1548
    • Renz, A.1    Berdel, W.2    Kreuter, M.3    Belka, C.4    Schulze-Osthoff, K.5    Los, M.6
  • 42
    • 0032538051 scopus 로고    scopus 로고
    • Quantitative assay by flow cytometry of the mitochondrial membrane potential in intact cells
    • Rottenberg, H. and Wu, S. (1998). Quantitative assay by flow cytometry of the mitochondrial membrane potential in intact cells. Biochim. Biophys. Acta 1404, 393-404.
    • (1998) Biochim. Biophys. Acta , vol.1404 , pp. 393-404
    • Rottenberg, H.1    Wu, S.2
  • 43
    • 0345120940 scopus 로고    scopus 로고
    • Measurement of mitochondrial membrane potential using fluorescent rhodamine derivatives
    • Scaduto, A., Russell, C. J., Grotyohann, A. and Lee, W. (1999). Measurement of mitochondrial membrane potential using fluorescent rhodamine derivatives. Biophys. J. 76, 469-477.
    • (1999) Biophys. J. , vol.76 , pp. 469-477
    • Scaduto, A.1    Russell, C.J.2    Grotyohann, A.3    Lee, W.4
  • 44
  • 47
    • 0034800367 scopus 로고    scopus 로고
    • Increased lactate production follows loss of mitochondrial membrane potential during apoptosis of human leukaemia cells
    • Tiefenthaler, M., Amberger, A., Bacher, N., Hartmann, B. L., Margreiter, R., Kofler, R. and Konwalinka, G. (2001). Increased lactate production follows loss of mitochondrial membrane potential during apoptosis of human leukaemia cells. Br. J. Haematol. 114, 574-580.
    • (2001) Br. J. Haematol. , vol.114 , pp. 574-580
    • Tiefenthaler, M.1    Amberger, A.2    Bacher, N.3    Hartmann, B.L.4    Margreiter, R.5    Kofler, R.6    Konwalinka, G.7
  • 48
    • 0034280126 scopus 로고    scopus 로고
    • Rapid caspase-3 activation during apoptosis revealed using fluorescence-resonance energy transfer
    • Tyas, L., Brophy, V. A., Pope, A., Rivett, A. J. and Tavaré, J. M. (2000). Rapid caspase-3 activation during apoptosis revealed using fluorescence-resonance energy transfer. EMBO Rep. 1, 266-270.
    • (2000) EMBO Rep. , vol.1 , pp. 266-270
    • Tyas, L.1    Brophy, V.A.2    Pope, A.3    Rivett, A.J.4    Tavaré, J.M.5
  • 49
    • 0034616942 scopus 로고    scopus 로고
    • Identification of DIABLO, a mammalian protein that promotes apoptosis by binding to and antagonizing IAP proteins
    • Verhagen, A. M., Ekert, P. G., Pakusch, M., Silke, J., Connolly, L. M., Reid, G. E., Moritz, R. L., Simpson, R. J. and Vaux, D. L. (2000). Identification of DIABLO, a mammalian protein that promotes apoptosis by binding to and antagonizing IAP proteins. Cell 102, 43-53.
    • (2000) Cell , vol.102 , pp. 43-53
    • Verhagen, A.M.1    Ekert, P.G.2    Pakusch, M.3    Silke, J.4    Connolly, L.M.5    Reid, G.E.6    Moritz, R.L.7    Simpson, R.J.8    Vaux, D.L.9
  • 50
    • 0034307759 scopus 로고    scopus 로고
    • Mitochondrial membrane potential and glutamate excitotoxicity in cultured cerebellar granule cells
    • Ward, M. W., Rego, A. C., Frenguelli, B. G. and Nicholls, D. G. (2000). Mitochondrial membrane potential and glutamate excitotoxicity in cultured cerebellar granule cells. J. Neurosci. 20, 7208-7219.
    • (2000) J. Neurosci. , vol.20 , pp. 7208-7219
    • Ward, M.W.1    Rego, A.C.2    Frenguelli, B.G.3    Nicholls, D.G.4
  • 51
    • 0035897408 scopus 로고    scopus 로고
    • Cytochrome c maintains mitochondrial transmembrane potential and ATP generation after outer mitochondrial membrane permeabilization during the apoptotic process
    • Waterhouse, N. J., Goldstein, J. C., von Ahsen, O., Schuler, M., Newmeyer, D. D. and Green, D. R. (2001). Cytochrome c maintains mitochondrial transmembrane potential and ATP generation after outer mitochondrial membrane permeabilization during the apoptotic process. J. Cell Biol. 153, 319-328.
    • (2001) J. Cell Biol. , vol.153 , pp. 319-328
    • Waterhouse, N.J.1    Goldstein, J.C.2    von Ahsen, O.3    Schuler, M.4    Newmeyer, D.D.5    Green, D.R.6
  • 52
    • 0035814933 scopus 로고    scopus 로고
    • Mitochondria are selectively eliminated from eukaryotic cells after blockade of caspases during apoptosis
    • Xue, L., Fletcher, G. and Tolkovsky, A. (2001). Mitochondria are selectively eliminated from eukaryotic cells after blockade of caspases during apoptosis. Curr. Biol. 11, 361-365.
    • (2001) Curr. Biol. , vol.11 , pp. 361-365
    • Xue, L.1    Fletcher, G.2    Tolkovsky, A.3
  • 54
    • 0035229427 scopus 로고    scopus 로고
    • The mitochondrion in apoptosis: How Pandora's box opens
    • Zamzami, N. and Kroemer, G. (2001). The mitochondrion in apoptosis: how Pandora's box opens. Nat. Rev. Mol. Cell Biol. 2, 67-71.
    • (2001) Nat. Rev. Mol. Cell Biol. , vol.2 , pp. 67-71
    • Zamzami, N.1    Kroemer, G.2
  • 55
    • 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. and Wang, X. (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.