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Volumn 18, Issue 22, 1999, Pages 6349-6361

Apoptosis driven by IP3-linked mitochondrial calcium signals

Author keywords

Apoptosis; Ca2+; IP3; Local signalling; Mitochondria

Indexed keywords

CALCIUM ION; CASPASE; CYTOCHROME C; INOSITOL TRISPHOSPHATE; RECEPTOR;

EID: 0033570890     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/18.22.6349     Document Type: Article
Times cited : (443)

References (72)
  • 1
    • 0028793257 scopus 로고
    • Glutamate-induced neuronal death: A succession of necrosis or apoptosis depending on mitochondrial function
    • Ankarcrona, M., Dypbukt, J.M., Bonfoco, E., Zhivotovsky, B., Orrenius, S., Lipton, S.A. and Nicotera, P. (1995) Glutamate-induced neuronal death: a succession of necrosis or apoptosis depending on mitochondrial function. Neuron, 15, 961-973.
    • (1995) Neuron , vol.15 , pp. 961-973
    • Ankarcrona, M.1    Dypbukt, J.M.2    Bonfoco, E.3    Zhivotovsky, B.4    Orrenius, S.5    Lipton, S.A.6    Nicotera, P.7
  • 2
    • 0030888185 scopus 로고    scopus 로고
    • The AM and FM of calcium signalling
    • Berridge, M.J. (1997) The AM and FM of calcium signalling. Nature, 386, 759-760.
    • (1997) Nature , vol.386 , pp. 759-760
    • Berridge, M.J.1
  • 3
    • 0032531818 scopus 로고    scopus 로고
    • Calcium - A life and death signal
    • Berridge, M.J., Bootman, M.D. and Lipp, P. (1998) Calcium - a life and death signal. Nature, 395, 645-648.
    • (1998) Nature , vol.395 , pp. 645-648
    • Berridge, M.J.1    Bootman, M.D.2    Lipp, P.3
  • 4
    • 0029998621 scopus 로고    scopus 로고
    • The permeability transition pore as a mitochondrial calcium release channel: A critical appraisal
    • Bernardi, P. and Petronilli, V. (1996) The permeability transition pore as a mitochondrial calcium release channel: a critical appraisal. J. Bioenerg. Biomembr., 28, 131-138.
    • (1996) J. Bioenerg. Biomembr. , vol.28 , pp. 131-138
    • Bernardi, P.1    Petronilli, V.2
  • 8
    • 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
  • 9
    • 0031772126 scopus 로고    scopus 로고
    • The mitochondrial permeability transition is required for tumor necrosis factor α-mediated apoptosis and cytochrome c release
    • Bradham, C.A., Qian, T., Streetz, K., Trautwein, C., Brenner, D.A. and Lemasters, J.J. (1998) The mitochondrial permeability transition is required for tumor necrosis factor α-mediated apoptosis and cytochrome c release. Mol. Cell. Biol., 18, 6353-6364.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 6353-6364
    • Bradham, C.A.1    Qian, T.2    Streetz, K.3    Trautwein, C.4    Brenner, D.A.5    Lemasters, J.J.6
  • 10
    • 0024360271 scopus 로고
    • Cyclosporin A is a potent inhibitor of the inner membrane permeability transition in liver mitochondria
    • Broekemeier, K.M., Dempsey, M.E. and Pfeiffer, D.R. (1989) Cyclosporin A is a potent inhibitor of the inner membrane permeability transition in liver mitochondria. J. Biol. Chem., 264, 7826-7830.
    • (1989) J. Biol. Chem. , vol.264 , pp. 7826-7830
    • Broekemeier, K.M.1    Dempsey, M.E.2    Pfeiffer, D.R.3
  • 12
    • 0028831997 scopus 로고
    • Calcium signaling
    • Clapham, D.E. (1995) Calcium signaling. Cell, 80, 259-268.
    • (1995) Cell , vol.80 , pp. 259-268
    • Clapham, D.E.1
  • 13
    • 0033521586 scopus 로고    scopus 로고
    • Quasi-synaptic calcium signal transmission between endoplasmic reticulum and mitochondria
    • Csordás,G., Thomas, A.P. and Hajnóczky, G. (1999) Quasi-synaptic calcium signal transmission between endoplasmic reticulum and mitochondria. EMBO J., 18, 96-108.
    • (1999) EMBO J. , vol.18 , pp. 96-108
    • Csordás, G.1    Thomas, A.P.2    Hajnóczky, G.3
  • 14
    • 0026475219 scopus 로고
    • Stable expression of the calbindin-D28K complementary DNA interferes with the apoptotic pathway in lymphocytes
    • Dowd, D.R., MacDonald, P.N., Komm, B.S., Haussler, M.R. and Miesfeld, R.L. (1992) Stable expression of the calbindin-D28K complementary DNA interferes with the apoptotic pathway in lymphocytes. Mol Endocrinol., 6, 1843-1848.
    • (1992) Mol Endocrinol. , vol.6 , pp. 1843-1848
    • Dowd, D.R.1    MacDonald, P.N.2    Komm, B.S.3    Haussler, M.R.4    Miesfeld, R.L.5
  • 15
    • 0033118649 scopus 로고    scopus 로고
    • Contributions of mitochondria to animal physiology: From homeostatic sensor to calcium signalling and cell death
    • Duchen, M.R. (1999) Contributions of mitochondria to animal physiology: from homeostatic sensor to calcium signalling and cell death. J. Physiol (Lond.), 516, 1-17.
    • (1999) J. Physiol (Lond.) , vol.516 , pp. 1-17
    • Duchen, M.R.1
  • 16
    • 0032524667 scopus 로고    scopus 로고
    • Regulation of the permeability transition pore in skeletal muscle mitochondria. Modulation by electron flow through the respiratory chain complex I
    • Fontaine, E., Eriksson, O., Ichas, F. and Bernardi, P. (1998) Regulation of the permeability transition pore in skeletal muscle mitochondria. Modulation by electron flow through the respiratory chain complex I. J. Biol. Chem., 273, 12662-12668
    • (1998) J. Biol. Chem. , vol.273 , pp. 12662-12668
    • Fontaine, E.1    Eriksson, O.2    Ichas, F.3    Bernardi, P.4
  • 17
    • 1842330849 scopus 로고    scopus 로고
    • Direct effect of ceramide on the mitochondrial electron transport chain leads to generation of reactive oxygen species. Role of mitochondrial glutathione
    • Garcia-Ruiz, C., Colell, A., Mari, M., Morales, A. and Fernandez-Checa, J.C. (1997) Direct effect of ceramide on the mitochondrial electron transport chain leads to generation of reactive oxygen species. Role of mitochondrial glutathione. J. Biol. Chem., 272, 11369-11377.
    • (1997) J. Biol. Chem. , vol.272 , pp. 11369-11377
    • Garcia-Ruiz, C.1    Colell, A.2    Mari, M.3    Morales, A.4    Fernandez-Checa, J.C.5
  • 18
    • 0032404536 scopus 로고    scopus 로고
    • The central executioners of apoptosis: Caspases or mitochondria?
    • Green, D. and Kroemer, G. (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
  • 19
    • 0032575752 scopus 로고    scopus 로고
    • Mitochondria and apoptosis
    • Green, D.R. and Reed, J.C. (1998) Mitochondria and apoptosis. Science, 281, 1309-1312.
    • (1998) Science , vol.281 , pp. 1309-1312
    • Green, D.R.1    Reed, J.C.2
  • 20
    • 0030856714 scopus 로고    scopus 로고
    • Direct inhibition of mitochondrial respiratory chain complex III by cell-permeable ceramide
    • Gudz, T.I., Tserng, K.Y. and Hoppel, C.L. (1997) Direct inhibition of mitochondrial respiratory chain complex III by cell-permeable ceramide. J. Biol. Chem., 272, 24154-24158.
    • (1997) J. Biol. Chem. , vol.272 , pp. 24154-24158
    • Gudz, T.I.1    Tserng, K.Y.2    Hoppel, C.L.3
  • 22
    • 0029143569 scopus 로고
    • Decoding of cytosolic calcium oscillations in the mitochondria
    • Hajnóczky, G., Robb-Gaspers, L.D., Seitz, M.B. and Thomas, A.P. (1995) Decoding of cytosolic calcium oscillations in the mitochondria. Cell, 82, 415-424.
    • (1995) Cell , vol.82 , pp. 415-424
    • Hajnóczky, G.1    Robb-Gaspers, L.D.2    Seitz, M.B.3    Thomas, A.P.4
  • 23
    • 0025193488 scopus 로고
    • 2+-induced large-amplitude swelling of liver and heart mitochondria by cyclosporin is probably caused by the inhibitor binding to mitochondrial-matrix peptidyl-prolyl cis-trans isomerase and preventing it interacting with the adenine nucleotide translocase
    • 2+-induced large-amplitude swelling of liver and heart mitochondria by cyclosporin is probably caused by the inhibitor binding to mitochondrial-matrix peptidyl-prolyl cis-trans isomerase and preventing it interacting with the adenine nucleotide translocase. Biochem. J., 268, 153-160.
    • (1990) Biochem. J. , vol.268 , pp. 153-160
    • Halestrap, A.P.1    Davidson, A.M.2
  • 24
    • 0031973203 scopus 로고    scopus 로고
    • Importance of the redox state of cytochrome c during caspase activation in cytosolic extracts
    • Hampton, M.B., Zhivotovsky, B., Slater, A.F., Burgess, D.H. and Orrenius, S. (1998) Importance of the redox state of cytochrome c during caspase activation in cytosolic extracts. Biochem. J., 329, 95-99.
    • (1998) Biochem. J. , vol.329 , pp. 95-99
    • Hampton, M.B.1    Zhivotovsky, B.2    Slater, A.F.3    Burgess, D.H.4    Orrenius, S.5
  • 25
    • 0030824575 scopus 로고    scopus 로고
    • Maintenance of calcium homeostasis in the endoplasmic reticulum by Bcl-2
    • He, H., Lam, M., McCormick, T.S. and Distelhorst, C.W. (1997) Maintenance of calcium homeostasis in the endoplasmic reticulum by Bcl-2. J. Cell Biol, 138, 1219-1228.
    • (1997) J. Cell Biol , vol.138 , pp. 1219-1228
    • He, H.1    Lam, M.2    McCormick, T.S.3    Distelhorst, C.W.4
  • 26
    • 0025204548 scopus 로고
    • Bcl-2 is an inner mitochondrial membrane protein thai blocks programmed cell death
    • Hockenbery, D., Nunez, G., Milliman, C., Schreiber, R.D. and Korsmeyer, S.J. (1990) Bcl-2 is an inner mitochondrial membrane protein thai 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
  • 27
    • 0038421272 scopus 로고    scopus 로고
    • Imaging the permeability pore transition in single mitochondria
    • Hüser, J., Rechenmacher, C.E. and Blatter, L.A. (1998) Imaging the permeability pore transition in single mitochondria. Biophys. J., 74, 2129-2137.
    • (1998) Biophys. J. , vol.74 , pp. 2129-2137
    • Hüser, J.1    Rechenmacher, C.E.2    Blatter, L.A.3
  • 28
    • 0032504717 scopus 로고    scopus 로고
    • From calcium signaling to cell death: Two conformations for the mitochondrial permeability transition pore. Switching from low- to high-conductance state
    • Ichas, F. and Mazat, J.P. (1998) From calcium signaling to cell death: two conformations for the mitochondrial permeability transition pore. Switching from low- to high-conductance state. Biochim. Biophys. Acta, 1366, 33-50.
    • (1998) Biochim. Biophys. Acta , vol.1366 , pp. 33-50
    • Ichas, F.1    Mazat, J.P.2
  • 29
    • 0031587822 scopus 로고    scopus 로고
    • Mitochondria are excitable organelles capable of generating and conveying electrical and calcium signals
    • Ichas, F., Jouaville, L.S. and Mazat, J.P. (1997) Mitochondria are excitable organelles capable of generating and conveying electrical and calcium signals. Cell, 89, 1145-1153.
    • (1997) Cell , vol.89 , pp. 1145-1153
    • Ichas, F.1    Jouaville, L.S.2    Mazat, J.P.3
  • 32
    • 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. and Newmeyer, D.D. (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
  • 34
    • 0032902145 scopus 로고    scopus 로고
    • Pivotal role of mitochondrial calcium uptake in neural cell apoptosis and necrosis
    • Kruman, I.I. and Mattson, M.P. (1999) Pivotal role of mitochondrial calcium uptake in neural cell apoptosis and necrosis. J. Neurochem., 72, 529-540.
    • (1999) J. Neurochem. , vol.72 , pp. 529-540
    • Kruman, I.I.1    Mattson, M.P.2
  • 35
    • 0032504568 scopus 로고    scopus 로고
    • The mitochondrial permeability transition in cell death: A common mechanism in necrosis, apoptosis and autophagy
    • Lemasters, JJ. et al. (1998) The mitochondrial permeability transition in cell death: a common mechanism in necrosis, apoptosis and autophagy. Biochim. Biophys. Acta, 1366, 177-196.
    • (1998) Biochim. Biophys. Acta , vol.1366 , pp. 177-196
    • Lemasters, J.J.1
  • 36
    • 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. and Yuan, J. (1998) Cleavage of BID by caspase 8 mediates the mitochondrial damage in the Fas pathway of apoptosis. Cell, 94, 491-501.
    • (1998) Cell , vol.94 , pp. 491-501
    • Li, H.1    Zhu, H.2    Xu, C.J.3    Yuan, J.4
  • 37
    • 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
  • 38
    • 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
  • 39
    • 0032555716 scopus 로고    scopus 로고
    • Bid, a Bcl2 interacting protein, mediates cytochrome c release from mitochondria in response to activation of cell surface death receptors
    • Luo, X., Budihardjo, I., Zou, H., Slaughter, C. and Wang, X. (1998) Bid, a Bcl2 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
  • 40
    • 0032566649 scopus 로고    scopus 로고
    • Bax and adenine nucleotide translocator co-operate in the mitochondrial control of apoptosis
    • Marzo, I. et al. (1998) Bax and adenine nucleotide translocator co-operate in the mitochondrial control of apoptosis. Science, 281, 2027-2031.
    • (1998) Science , vol.281 , pp. 2027-2031
    • Marzo, I.1
  • 41
    • 0030316478 scopus 로고    scopus 로고
    • The role of calcium in the regulation of apoptosis
    • McConkey, D.J. (1996) The role of calcium in the regulation of apoptosis. Scanning Microsc., 10, 777-793.
    • (1996) Scanning Microsc. , vol.10 , pp. 777-793
    • McConkey, D.J.1
  • 43
    • 0025319665 scopus 로고
    • Role of calcium ions in regulation of mammalian intramitochondrial metabolism
    • McCormack, J.G., Halestrap, A.P. and Denton, R.M. (1990) Role of calcium ions in regulation of mammalian intramitochondrial metabolism. Physiol. Rev., 70, 391-425.
    • (1990) Physiol. Rev. , vol.70 , pp. 391-425
    • McCormack, J.G.1    Halestrap, A.P.2    Denton, R.M.3
  • 44
    • 0028019746 scopus 로고
    • Cell-free apoptosis in Xenopus egg extracts: Inhibition by Bcl-2 and requirement for an organelle fraction enriched in mitochondria
    • Newmeyer, D.D., Farschon, D.M. and Reed, J.C. (1994) Cell-free apoptosis in Xenopus egg extracts: inhibition by Bcl-2 and requirement for an organelle fraction enriched in mitochondria. Cell, 79, 353-364
    • (1994) Cell , vol.79 , pp. 353-364
    • Newmeyer, D.D.1    Farschon, D.M.2    Reed, J.C.3
  • 45
    • 0032421139 scopus 로고    scopus 로고
    • Neuronal excitotoxicity: The role of mitochondria
    • Nicholls, D.G. and Budd, S.L. (1998) Neuronal excitotoxicity: the role of mitochondria. Biofactors, 8, 287-299.
    • (1998) Biofactors , vol.8 , pp. 287-299
    • Nicholls, D.G.1    Budd, S.L.2
  • 46
    • 0029068871 scopus 로고
    • Identification and inhibition of the ICE/CED-3 protease necessary for mammalian apoptosis
    • Nicholson, D.W. et al. (1995) Identification and inhibition of the ICE/CED-3 protease necessary for mammalian apoptosis. Nature, 376, 37-43.
    • (1995) Nature , vol.376 , pp. 37-43
    • Nicholson, D.W.1
  • 47
    • 0031977191 scopus 로고    scopus 로고
    • The role of calcium in apoptosis
    • Nicotera, P. and Orrenius, S. (1998) The role of calcium in apoptosis. Cell Calcium, 23, 173-180.
    • (1998) Cell Calcium , vol.23 , pp. 173-180
    • Nicotera, P.1    Orrenius, S.2
  • 49
    • 0027485461 scopus 로고
    • Bcl-2 functions in an antioxidant pathway to prevent apoptosis
    • Oltvai, Z.N., Yin, X.M., Milliman, C.L. and Korsmeyer, S.J. (1993) Bcl-2 functions in an antioxidant pathway to prevent apoptosis. Cell, 75, 241-251.
    • (1993) Cell , vol.75 , pp. 241-251
    • Oltvai, Z.N.1    Yin, X.M.2    Milliman, C.L.3    Korsmeyer, S.J.4
  • 50
    • 0032571294 scopus 로고    scopus 로고
    • The overexpression of Bax produces cell death upon induction of the mitochondrial permeability transition
    • Pastorino, J.G., Chen, S.T., Tafani, M., Snyder, J.W. and Farber, J.L. (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
  • 53
    • 0032498210 scopus 로고    scopus 로고
    • Calcium signaling: Up, down, up, down. What's the point?
    • Putney, J.W.,Jr (1998) Calcium signaling: up, down, up, down. What's the point? Science, 279, 191-192.
    • (1998) Science , vol.279 , pp. 191-192
    • Putney J.W., Jr.1
  • 54
    • 1842375100 scopus 로고    scopus 로고
    • Implication of mitochondrial hydrogen peroxide generation in ceramide-induced apoptosis
    • Quillet-Mary, A., Jaffrezou, J.P, Mansat, V., Bordier, C., Naval, J. and Laurent, G. (1997) Implication of mitochondrial hydrogen peroxide generation in ceramide-induced apoptosis. J. Biol. Chem., 272, 21388-21395.
    • (1997) J. Biol. Chem. , vol.272 , pp. 21388-21395
    • Quillet-Mary, A.1    Jaffrezou, J.P.2    Mansat, V.3    Bordier, C.4    Naval, J.5    Laurent, G.6
  • 55
    • 0030782177 scopus 로고    scopus 로고
    • Cytochrome c: Can't live with it-can't live without it
    • Reed, J.C. (1997) Cytochrome c: can't live with it-can't live without it. Cell, 91, 559-562.
    • (1997) Cell , vol.91 , pp. 559-562
    • Reed, J.C.1
  • 56
    • 0025830873 scopus 로고
    • J-aggregate formation of a carbocyanine as a quantitative fluorescent indicator of membrane potential
    • Reers, M., Smith, T.W. and Chen, L.B. (1991) J-aggregate formation of a carbocyanine as a quantitative fluorescent indicator of membrane potential. Biochemistry, 30, 4480-4486.
    • (1991) Biochemistry , vol.30 , pp. 4480-4486
    • Reers, M.1    Smith, T.W.2    Chen, L.B.3
  • 57
    • 0027340729 scopus 로고
    • 3-sensitive channels that are sensed by neighboring mitochondria
    • 3-sensitive channels that are sensed by neighboring mitochondria. Science, 262, 744-747.
    • (1993) Science , vol.262 , pp. 744-747
    • Rizzuto, R.1    Brini, M.2    Murgia, M.3    Pozzan, T.4
  • 61
    • 0027505303 scopus 로고
    • Induction of apoptotic cell death in chronic lymphocytic leukemia by 2-chloro-2′-deoxyadenosine and 9-β-D-arabinosyl-2-fluoroadenine
    • Robertson, L.E., Chubb, S., Meyn, R.E., Story, M., Ford, R., Hittelman, W.N. and Plunkett, W. (1993) Induction of apoptotic cell death in chronic lymphocytic leukemia by 2-chloro-2′-deoxyadenosine and 9-β-D-arabinosyl-2-fluoroadenine. Blood, 81, 143-50.
    • (1993) Blood , vol.81 , pp. 143-150
    • Robertson, L.E.1    Chubb, S.2    Meyn, R.E.3    Story, M.4    Ford, R.5    Hittelman, W.N.6    Plunkett, W.7
  • 62
    • 0030580287 scopus 로고    scopus 로고
    • Why are mitochondria involved in apoptosis? Permeability transition pores and apoptosis as selective mechanisms to eliminate superoxide-producing mitochondria and cell
    • Skulachev, V.P. (1996) Why are mitochondria involved in apoptosis? Permeability transition pores and apoptosis as selective mechanisms to eliminate superoxide-producing mitochondria and cell. FEBS Lett., 397, 7-10.
    • (1996) FEBS Lett. , vol.397 , pp. 7-10
    • Skulachev, V.P.1
  • 63
    • 0026565365 scopus 로고
    • A role for calcium in regulating apoptosis in rat thymocytes irradiated in vitro
    • Story, M.D., Stephens, L.C., Tomasovic, S.P. and Meyn, R.E. (1992) A role for calcium in regulating apoptosis in rat thymocytes irradiated in vitro. Int. J. Radiat. Biol., 61, 243-251.
    • (1992) Int. J. Radiat. Biol. , vol.61 , pp. 243-251
    • Story, M.D.1    Stephens, L.C.2    Tomasovic, S.P.3    Meyn, R.E.4
  • 65
    • 0033521741 scopus 로고    scopus 로고
    • Molecular characterization of mitochondrial apoptosis-inducing factor
    • Susin, S.A. et al (1999) Molecular characterization of mitochondrial apoptosis-inducing factor. Nature, 397, 441-446.
    • (1999) Nature , vol.397 , pp. 441-446
    • Susin, S.A.1
  • 67
    • 0026507126 scopus 로고
    • A novel heterodimeric cysteine protease is required for interleukin-1 β processing in monocytes
    • Thornberry, N.A. et al. (1992) A novel heterodimeric cysteine protease is required for interleukin-1 β processing in monocytes. Nature, 356, 768-774.
    • (1992) Nature , vol.356 , pp. 768-774
    • Thornberry, N.A.1
  • 68
    • 0033537768 scopus 로고    scopus 로고
    • 2+-induced apoptosis through calcineurin dephosphorylation of BAD
    • 2+-induced apoptosis through calcineurin dephosphorylation of BAD. Science, 284, 339-343.
    • (1999) Science , vol.284 , pp. 339-343
    • Wang, H.G.1
  • 69
    • 0031036872 scopus 로고    scopus 로고
    • Prevention of apoptosis by Bcl-2: Release of cytochrome c from mitochondria blocked
    • Yang, J., Liu, X., Bhalla, K., Kim, C.N., Ibrado, A.M., Cai, J., Peng, T.I., Jones, D.P. and Wang, X. (1997) Prevention of apoptosis by Bcl-2: release of cytochrome c from mitochondria blocked. Science, 275, 1129-1132.
    • (1997) Science , vol.275 , pp. 1129-1132
    • Yang, J.1    Liu, X.2    Bhalla, K.3    Kim, C.N.4    Ibrado, A.M.5    Cai, J.6    Peng, T.I.7    Jones, D.P.8    Wang, X.9
  • 70
    • 0027525104 scopus 로고
    • The C. elegans cell death gene ced-3 encodes a protein similar to mammalian interleukin-1β-converting enzyme
    • Yuan, J., Shaham, S., Ledoux, S., Ellis, H.M. and Horvitz, H.R. (1993) The C. elegans cell death gene ced-3 encodes a protein similar to mammalian interleukin-1β-converting enzyme. Cell, 75, 641-652.
    • (1993) Cell , vol.75 , pp. 641-652
    • Yuan, J.1    Shaham, S.2    Ledoux, S.3    Ellis, H.M.4    Horvitz, H.R.5
  • 71
    • 0029101644 scopus 로고
    • Sequential reduction of mitochondrial transmembrane potential and generation of reactive oxygen species in early programmed cell death
    • Zamzami, N. et al. (1995) Sequential reduction of mitochondrial transmembrane potential and generation of reactive oxygen species in early programmed cell death. J. Exp. Med., 182, 367-377.
    • (1995) J. Exp. Med. , vol.182 , pp. 367-377
    • Zamzami, N.1
  • 72
    • 0032500670 scopus 로고    scopus 로고
    • N-methyl-D-aspartate inhibits apoptosis through activation of phosphatidylinositol 3-kinase in cerebellar granule neurons. A role for insulin receptor substrate-1 in the neurotrophic action of n-methyl-D-aspartate and its inhibition by ethanol
    • Zhang, F.X., Rubin, R. and Rooney, T.A. (1998) N-Methyl-D-aspartate inhibits apoptosis through activation of phosphatidylinositol 3-kinase in cerebellar granule neurons. A role for insulin receptor substrate-1 in the neurotrophic action of n-methyl-D-aspartate and its inhibition by ethanol. J. Biol. Chem., 273, 26596-26602.
    • (1998) J. Biol. Chem. , vol.273 , pp. 26596-26602
    • Zhang, F.X.1    Rubin, R.2    Rooney, T.A.3


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