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Volumn 183, Issue 4, 1996, Pages 1533-1544

Mitochondrial control of nuclear apoptosis

Author keywords

[No Author keywords available]

Indexed keywords

ATRACTYLOSIDE; BONGKREKIC ACID; BUTYL HYDROPEROXIDE; CALCIUM CHLORIDE; CALPASTATIN; CARBONYL CYANIDE CHLOROPHENYLHYDRAZONE; CYCLOSPORIN A; DEXAMETHASONE; DIAMIDE; DNA FRAGMENT; ETOPOSIDE; GUANOSINE 5' O (3 THIOTRIPHOSPHATE); INTERLEUKIN 1BETA CONVERTING ENZYME INHIBITOR; IONOMYCIN; MITOCHONDRIAL DNA; RUTHENIUM RED;

EID: 0029862706     PISSN: 00221007     EISSN: None     Source Type: Journal    
DOI: 10.1084/jem.183.4.1533     Document Type: Article
Times cited : (1281)

References (74)
  • 1
    • 0028268215 scopus 로고
    • Programmed cell death and Bcl-2 protection in the absence of a nucleus
    • Jacobson, M.D., J.F. Burne, and M.C. Raff. 1994. Programmed cell death and Bcl-2 protection in the absence of a nucleus. EMBO (Eur. Mol. Biol. Organ.) J. 13:1899-1910.
    • (1994) EMBO (Eur. Mol. Biol. Organ.) J. , vol.13 , pp. 1899-1910
    • Jacobson, M.D.1    Burne, J.F.2    Raff, M.C.3
  • 2
  • 3
    • 0028938366 scopus 로고
    • The target cell nucleus is not required for cell-mediated granzymeor Fas-based cytotoxicity
    • Nakajima, H., P. Golstein, and P.A. Henkart. 1995. The target cell nucleus is not required for cell-mediated granzymeor Fas-based cytotoxicity. J. Exp. Med. 181:1905-1909.
    • (1995) J. Exp. Med. , vol.181 , pp. 1905-1909
    • Nakajima, H.1    Golstein, P.2    Henkart, P.A.3
  • 4
    • 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., D.M. Farschon, and J.C. Reed. 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
  • 7
    • 0029125701 scopus 로고
    • Protease activation during apoptosis: Death by a thousand cuts?
    • Martin, S.J., and D.R. Green. 1995. Protease activation during apoptosis: death by a thousand cuts? Cell. 82:349-352.
    • (1995) Cell , vol.82 , pp. 349-352
    • Martin, S.J.1    Green, D.R.2
  • 8
    • 0027485950 scopus 로고
    • Temporal analysis of events associated with programmed cell death (apoptosis) of sympathetic neurons deprived of nerve growth factor
    • Deckwerth, T.L., and E.M. Johnson. 1993. Temporal analysis of events associated with programmed cell death (apoptosis) of sympathetic neurons deprived of nerve growth factor. J. Cell Biol. 123:1207-1222.
    • (1993) J. Cell Biol. , vol.123 , pp. 1207-1222
    • Deckwerth, T.L.1    Johnson, E.M.2
  • 9
    • 0028046038 scopus 로고
    • Commitment to apoptosis is associated with changes in mitochondrial biogenesis and activity in cell lines conditionally immortalized with simian virus 40
    • Vayssière, J.-L., P X. Petit, Y. Risler, and B. Mignotte. 1994. Commitment to apoptosis is associated with changes in mitochondrial biogenesis and activity in cell lines conditionally immortalized with simian virus 40. Proc. Natl. Acad. Sci. USA. 91:11752-11756.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 11752-11756
    • Vayssière, J.-L.1    Petit, P.X.2    Risler, Y.3    Mignotte, B.4
  • 10
    • 0028903933 scopus 로고
    • Reduction in mitochondrial potential constitutes an early irreversible step of programmed lymphocyte death in vivo
    • Zamzami, N., P. Marchetti, M. Castedo, C. Zanin, J.-L. Vayssière, P.X. Petit, and G. Kroemer. 1995. Reduction in mitochondrial potential constitutes an early irreversible step of programmed lymphocyte death in vivo. J. Exp. Med. 181: 1661-1672.
    • (1995) J. Exp. Med. , vol.181 , pp. 1661-1672
    • Zamzami, N.1    Marchetti, P.2    Castedo, M.3    Zanin, C.4    Vayssière, J.-L.5    Petit, P.X.6    Kroemer, G.7
  • 11
    • 0029036412 scopus 로고
    • Alterations of mitochondrial structure and function are early events of dexamethasone-induced thymocyte apoptosis
    • Petit, P.X., H. LeCoeur, E. Zorn, C. Duguet, B. Mignotte, and M.L. Gougeon. 1995. Alterations of mitochondrial structure and function are early events of dexamethasone-induced thymocyte apoptosis. J. Cell Biol. 130:157-167.
    • (1995) J. Cell Biol. , vol.130 , pp. 157-167
    • Petit, P.X.1    LeCoeur, H.2    Zorn, E.3    Duguet, C.4    Mignotte, B.5    Gougeon, M.L.6
  • 16
    • 0028939139 scopus 로고
    • Programmed cell death and Bcl-2 protection in very low oxygen
    • Jacobson, M.D., and M.C. RafF. 1995. Programmed cell death and Bcl-2 protection in very low oxygen. Nature (Lond.). 374:814-816.
    • (1995) Nature (Lond.) , vol.374 , pp. 814-816
    • Jacobson, M.D.1    Raff, M.C.2
  • 19
    • 0028053663 scopus 로고
    • Recent progress on regulation of the mitochondrial permeability transition pore; a cyclosporin-sensitive pore in the inner mitochondrial membrane
    • Bernardi, P., K.M. Broekemeier, and D.R. Pfeiffer. 1994. Recent progress on regulation of the mitochondrial permeability transition pore; a cyclosporin-sensitive pore in the inner mitochondrial membrane. J. Bioenerg. Biomembr. 26:509-517.
    • (1994) J. Bioenerg. Biomembr. , vol.26 , pp. 509-517
    • Bernardi, P.1    Broekemeier, K.M.2    Pfeiffer, D.R.3
  • 20
    • 0028091583 scopus 로고
    • Electrophysiology of the inner mitochondrial membrane
    • Zoratti, M., and I. Szabó. 1994. Electrophysiology of the inner mitochondrial membrane. J. Bioenerg. Biomembr. 26:543-553.
    • (1994) J. Bioenerg. Biomembr. , vol.26 , pp. 543-553
    • Zoratti, M.1    Szabó, I.2
  • 21
    • 0029043697 scopus 로고
    • Influence of metabolic inhibitors on mitochondrial permeability transition and glutathione status
    • Reed D.J., and M.K. Savage. 1995. Influence of metabolic inhibitors on mitochondrial permeability transition and glutathione status. Biochim. Biophys. Acta. 1271:43-50.
    • (1995) Biochim. Biophys. Acta , vol.1271 , pp. 43-50
    • Reed, D.J.1    Savage, M.K.2
  • 23
    • 0026687312 scopus 로고
    • Modulation of the mitochondrial permeability transition pore. Effect of protons and divalent cations
    • Bernardi, P., S. Vassanelli, P. Veronese, R. Colonna, I. Szabó, and M. Zoratti. 1992. Modulation of the mitochondrial permeability transition pore. Effect of protons and divalent cations. J. Biol. Chem. 267:2934-2939.
    • (1992) J. Biol. Chem. , vol.267 , pp. 2934-2939
    • Bernardi, P.1    Vassanelli, S.2    Veronese, P.3    Colonna, R.4    Szabó, I.5    Zoratti, M.6
  • 24
    • 0026801183 scopus 로고
    • Modulation of the mitochondrial cyclosporin A-sensitive permeability transition pore by the proton electrochemical gradient
    • Bernardi, P. 1992. Modulation of the mitochondrial cyclosporin A-sensitive permeability transition pore by the proton electrochemical gradient. J. Biol. Chem. 267:8834-8839.
    • (1992) J. Biol. Chem. , vol.267 , pp. 8834-8839
    • Bernardi, P.1
  • 25
    • 0026703122 scopus 로고
    • Modulation of the mitochondrial megachannel by divalent cations and protons
    • Szabó, I., P. Bernardi, and M. Zoratti. 1992. Modulation of the mitochondrial megachannel by divalent cations and protons. J. Biol. Chem. 267:2940-2946.
    • (1992) J. Biol. Chem. , vol.267 , pp. 2940-2946
    • Szabó, I.1    Bernardi, P.2    Zoratti, M.3
  • 26
    • 0027433653 scopus 로고
    • Physiological effectors modify voltage-sensing by the cyclosporin A-sensitive mitochondrial permeability transition pore
    • Petronilli, V., C. Cola, S. Massan, R. Colonna, and P. Bernardi. 1993. Physiological effectors modify voltage-sensing by the cyclosporin A-sensitive mitochondrial permeability transition pore. J. Biol. Chem. 268:21939-21945.
    • (1993) J. Biol. Chem. , vol.268 , pp. 21939-21945
    • Petronilli, V.1    Cola, C.2    Massan, S.3    Colonna, R.4    Bernardi, P.5
  • 27
    • 0027509946 scopus 로고
    • 2+ binding sites with opposing effects on the pore open probability
    • 2+ binding sites with opposing effects on the pore open probability. J. Biol. Chem 268:1005-1010.
    • (1993) J. Biol. Chem , vol.268 , pp. 1005-1010
    • Bernardi, P.1    Veronese, P.2    Petronilli, V.3
  • 29
    • 0028074839 scopus 로고
    • Regulation of the permeability transition pore, a voltage-dependent mitochondrial channel inhibited by cyclosporin A
    • Petronilli, V., A Nicolh, P. Costantini, R. Colonna, and P. Bernardi. 1994. Regulation of the permeability transition pore, a voltage-dependent mitochondrial channel inhibited by cyclosporin A. Biochim. Biophys. Acta. 1187:255-259.
    • (1994) Biochim. Biophys. Acta , vol.1187 , pp. 255-259
    • Petronilli, V.1    Nicolh, A.2    Costantini, P.3    Colonna, R.4    Bernardi, P.5
  • 30
    • 0026591024 scopus 로고
    • Isolation of the mitochondrial benzodiazepine receptor: Association with the voltage-dependent anion channel and the adenine nucleotide carrier
    • McEnery, M.W., A.M. Snowman, R.R. Trifiletti, and S.H. Snyder. 1992. Isolation of the mitochondrial benzodiazepine receptor: association with the voltage-dependent anion channel and the adenine nucleotide carrier. Proc. Natl. Acad. Sci. USA. 89:3170-3174.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 3170-3174
    • McEnery, M.W.1    Snowman, A.M.2    Trifiletti, R.R.3    Snyder, S.H.4
  • 31
    • 0019155420 scopus 로고
    • The ADP-ATP translocation in mitochondria, a membrane potential controlled transport
    • Klingenberg, M. 1980. The ADP-ATP translocation in mitochondria, a membrane potential controlled transport J. Membr. Biol 56:97-105.
    • (1980) J. Membr. Biol , vol.56 , pp. 97-105
    • Klingenberg, M.1
  • 33
    • 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 ntrcleotide 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 ntrcleotide translocase. Biochem. J. 268:153-160.
    • (1990) Biochem. J. , vol.268 , pp. 153-160
    • Halestrup, A.P.1    Davidson, A.M.2
  • 34
    • 0026718833 scopus 로고
    • Topography of the membrane-bound ADP/ ATP carrier assessed by enzymatic proteolysis
    • Marry, I., G. Brandolin, J. Gagnon, R. Brasseur, and P.V. Vignais. 1992. Topography of the membrane-bound ADP/ ATP carrier assessed by enzymatic proteolysis. Biochemistry. 31:4058-4065.
    • (1992) Biochemistry , vol.31 , pp. 4058-4065
    • Marry, I.1    Brandolin, G.2    Gagnon, J.3    Brasseur, R.4    Vignais, P.V.5
  • 35
    • 0028064745 scopus 로고
    • Importance of loops of mitochondrial ADP/ATP carrier for its transport activity deduced from reactivities of its cysteine residues with the sulfhydril reagent eosin-5-nialeimide
    • Majima, E , Y. Shinohara, N. Yamaguchi, Y.M. Hong, and H. Terada. 1994. Importance of loops of mitochondrial ADP/ATP carrier for its transport activity deduced from reactivities of its cysteine residues with the sulfhydril reagent eosin-5-nialeimide. Biochemistry. 33:9530-9536.
    • (1994) Biochemistry , vol.33 , pp. 9530-9536
    • Majima, E.1    Shinohara, Y.2    Yamaguchi, N.3    Hong, Y.M.4    Terada, H.5
  • 36
    • 0027998359 scopus 로고
    • Murine hepatocyte apoptosis induced in vitro and in vivo by TNF-alpha requires transcriptional arrest
    • Leist, M., F. Gantner, I Bohlinger, P.G. Germann, C. Tiegs, and A. Wendel. 1994. Murine hepatocyte apoptosis induced in vitro and in vivo by TNF-alpha requires transcriptional arrest. J. Immunol. 153:1778-1788.
    • (1994) J. Immunol. , vol.153 , pp. 1778-1788
    • Leist, M.1    Gantner, F.2    Bohlinger, I.3    Germann, P.G.4    Tiegs, C.5    Wendel, A.6
  • 37
    • 0027465502 scopus 로고
    • Glucocorticoid-mediated control of the clonal deletion and activation of peripheral T cells in vivo
    • Gonzalo, J.A., A. González-García, C. Martinez-A., and G. Kroemer. 1993. Glucocorticoid-mediated control of the clonal deletion and activation of peripheral T cells in vivo. J. Exp. Med. 177:1239-1246.
    • (1993) J. Exp. Med. , vol.177 , pp. 1239-1246
    • Gonzalo, J.A.1    González-García, A.2    Martinez-A, C.3    Kroemer, G.4
  • 39
    • 0028929484 scopus 로고
    • Mercuric chloride-induced programmed cell death of a murine T cell hybridoma: I Effect of the proto-oncogene Bcl-2
    • Aten, J., P. Prigent, P. Poncet, C. Blanpied, N. Claessen, P. Druet, and F. Hirsch. 1995. Mercuric chloride-induced programmed cell death of a murine T cell hybridoma: I Effect of the proto-oncogene Bcl-2. Cell. Immunol. 161:98-106.
    • (1995) Cell. Immunol. , vol.161 , pp. 98-106
    • Aten, J.1    Prigent, P.2    Poncet, P.3    Blanpied, C.4    Claessen, N.5    Druet, P.6    Hirsch, F.7
  • 40
    • 49849107093 scopus 로고
    • Elucidation of the chemical structure of bongkrekic acid. I. Isolation, purification and properties of bongkrekic acid
    • Lumbach, G.W.M., H.C. Cox, and W. Berends. 1970. Elucidation of the chemical structure of bongkrekic acid. I. Isolation, purification and properties of bongkrekic acid. Tetrahedron. 26:5993-5999.
    • (1970) Tetrahedron. , vol.26 , pp. 5993-5999
    • Lumbach, G.W.M.1    Cox, H.C.2    Berends, W.3
  • 41
    • 0025666621 scopus 로고
    • Mitotic chromatin condensation iri vitro using somaric cell extracts and nuclei with variable levels of endogenous topoisomerase II
    • Wood, E.R., and W.C. Earnshaw. 1990. Mitotic chromatin condensation iri vitro using somaric cell extracts and nuclei with variable levels of endogenous topoisomerase II. J. Cell Biol. 111:2839-2850.
    • (1990) J. Cell Biol. , vol.111 , pp. 2839-2850
    • Wood, E.R.1    Earnshaw, W.C.2
  • 42
    • 0027437541 scopus 로고
    • Nuclear events of apoptosis in vitro in cell-free mitotic extracts: A model system for analysis of the active phase of apoptosis
    • Lazebnik, Y.A., S. Cole, C.A. Cooke, W.G. Nelson, and W.C. Earnshaw. 1993. Nuclear events of apoptosis in vitro in cell-free mitotic extracts: a model system for analysis of the active phase of apoptosis. J. Cell Biol. 123:7-22.
    • (1993) J. Cell Biol. , vol.123 , pp. 7-22
    • Lazebnik, Y.A.1    Cole, S.2    Cooke, C.A.3    Nelson, W.G.4    Earnshaw, W.C.5
  • 43
    • 0020182282 scopus 로고
    • Mitochondrial modifications associated with the cytoplasmic male sterility in faba beans
    • Boutry, M., and M. Briquet. 1982. Mitochondrial modifications associated with the cytoplasmic male sterility in faba beans. Eur. J. Biochem 127:129-135.
    • (1982) Eur. J. Biochem , vol.127 , pp. 129-135
    • Boutry, M.1    Briquet, M.2
  • 44
    • 0026068601 scopus 로고
    • + T cells in mice tolerant to Staphylococcus aurens enterotoxin B
    • + T cells in mice tolerant to Staphylococcus aurens enterotoxin B. Nature (Lond.). 349: 245-248.
    • (1991) Nature (Lond.) , vol.349 , pp. 245-248
    • Kawabe, Y.1    Ochi, A.2
  • 45
    • 0025690822 scopus 로고
    • Analysis of the membrane potential of rat- And mouseliver mitochondria by flow cytometry and possible applications
    • Petit, P.X., J.E. O'Connor. D. Grunwald, and S.C Brown. 1990. Analysis of the membrane potential of rat- and mouseliver mitochondria by flow cytometry and possible applications. Eur. J. Biochem. 389-397.
    • (1990) Eur. J. Biochem. , pp. 389-397
    • Petit, P.X.1    O'Connor, J.E.2    Grunwald, D.3    Brown, S.C.4
  • 46
    • 0025726216 scopus 로고
    • A rapid simple method for measuring thymocyte apoptosis by propidium iodide staining and flow cytometry
    • Nicoletti, I., G. Mighorati, M.C. Pagliacci, and C. Riccardi. 1991. A rapid simple method for measuring thymocyte apoptosis by propidium iodide staining and flow cytometry. J. Immunol. Meth. 139:271-280.
    • (1991) J. Immunol. Meth. , vol.139 , pp. 271-280
    • Nicoletti, I.1    Mighorati, G.2    Pagliacci, M.C.3    Riccardi, C.4
  • 47
    • 0027133425 scopus 로고
    • Chemical, immunological, enzymatic, and genetic approaches to studying the arrangement of the peptide chain of the ADP/ATP earner in the mitochondrial membrane
    • Brandolin, G., A. Le-Saux, V. Trezeguet, G.J. Lauquinn, and P.V. Vignais. 1993. Chemical, immunological, enzymatic, and genetic approaches to studying the arrangement of the peptide chain of the ADP/ATP earner in the mitochondrial membrane. J. Bioenerg. Biomembr. 25:493-501.
    • (1993) J. Bioenerg. Biomembr. , vol.25 , pp. 493-501
    • Brandolin, G.1    Le-Saux, A.2    Trezeguet, V.3    Lauquinn, G.J.4    Vignais, P.V.5
  • 49
    • 0028239794 scopus 로고
    • The voltage sensor of the mitochondrial permeability transition pore is tuned by the oxidation-reduction state of vicinal thiols. Increase of the gating potential by oxidants and its reversal by reducing agents
    • Petronilh, V., P. Costantini, L. Scorrano, R. Colonna, S. Passamonti, and P. Bernardi. 1994. The voltage sensor of the mitochondrial permeability transition pore is tuned by the oxidation-reduction state of vicinal thiols. Increase of the gating potential by oxidants and its reversal by reducing agents. J Biol. Chem. 269:16638-16642.
    • (1994) J Biol. Chem. , vol.269 , pp. 16638-16642
    • Petronilh, V.1    Costantini, P.2    Scorrano, L.3    Colonna, R.4    Passamonti, S.5    Bernardi, P.6
  • 50
    • 0028938858 scopus 로고
    • Selective inhibition of the mitochondrial permeability transition pore at the oxidation-reduction sensitive dithiol by monobromobimane
    • Costantini, P , B.V. Chernyak, V. Petrornili, and P. Bernardi. 1995. Selective inhibition of the mitochondrial permeability transition pore at the oxidation-reduction sensitive dithiol by monobromobimane. FEBS (Fed. Eur. Biochem. Soc.) Lett. 362:239-242.
    • (1995) FEBS (Fed. Eur. Biochem. Soc.) Lett. , vol.362 , pp. 239-242
    • Costantini, P.1    Chernyak, B.V.2    Petrornili, V.3    Bernardi, P.4
  • 53
    • 0028999453 scopus 로고
    • Tumor necrosis factor-induced hepatocyte apoptosis precedes liver failure in experimental murine shock models
    • Leist, M., F. Gantner, I. Bohlinger, G. Tiegs, P.G. Germann, and A. Wendel. 1995. Tumor necrosis factor-induced hepatocyte apoptosis precedes liver failure in experimental murine shock models. Am J. Pathol. 146:1220-1234.
    • (1995) Am J. Pathol. , vol.146 , pp. 1220-1234
    • Leist, M.1    Gantner, F.2    Bohlinger, I.3    Tiegs, G.4    Germann, P.G.5    Wendel, A.6
  • 54
    • 0028915454 scopus 로고
    • Regulation of lymphocyte survival by the Bcl-2 gene family
    • Cory, S. 1995. Regulation of lymphocyte survival by the Bcl-2 gene family. Ann. Rev. Immunol. 13:513-543.
    • (1995) Ann. Rev. Immunol. , vol.13 , pp. 513-543
    • Cory, S.1
  • 55
    • 0027225445 scopus 로고
    • Structure-function analysis of the Bcl-2 oncoprotein. Addition of a heterologous transmembrane domain to portions of the Bcl-2β protein restores function as a regulator of cell survival
    • Tanaka. S., K. Saito, and J.C. Reed. 1993. Structure-function analysis of the Bcl-2 oncoprotein. Addition of a heterologous transmembrane domain to portions of the Bcl-2β protein restores function as a regulator of cell survival. J. Biol. Chem. 268:10920-10926.
    • (1993) J. Biol. Chem. , vol.268 , pp. 10920-10926
    • Tanaka, S.1    Saito, K.2    Reed, J.C.3
  • 56
    • 0027362667 scopus 로고
    • Investigation of the subcellular distribution of the bcl-2 oncoprotein: Residence in the nuclear envelope, endoplasmic reticulum, and outer nitochondrial 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 oncoprotein: residence in the nuclear envelope, endoplasmic reticulum, and outer nitochondrial 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
  • 57
    • 0028289951 scopus 로고
    • Role of membrane anchor domain of Bcl-2 in suppression of apoptosis caused by E1B-defective adenovirus
    • Nguyen, M., P.E. Branton, P.A. Walton, Z.N. Oltvai, S.J. Korsmeyer, and G.G. Shore. 1994. Role of membrane anchor domain of Bcl-2 in suppression of apoptosis caused by E1B-defective adenovirus. J Biol Chem. 269:16521-16524.
    • (1994) J Biol Chem. , vol.269 , pp. 16521-16524
    • Nguyen, M.1    Branton, P.E.2    Walton, P.A.3    Oltvai, Z.N.4    Korsmeyer, S.J.5    Shore, G.G.6
  • 59
    • 0028362488 scopus 로고
    • Bcl-2 inhibits glucocorticoid-induced apoptosis but only partially blocks calcium ionophore or cycloheximide-regulated apoptosis in S49 cells
    • Caron-Leshe, L.A.M., R.B. Evans, and J.A. Cidlowski. 1994. Bcl-2 inhibits glucocorticoid-induced apoptosis but only partially blocks calcium ionophore or cycloheximide-regulated apoptosis in S49 cells. FASEB (Fed. Am. Soc. Exp. Biol.) J. 8: 639-645.
    • (1994) FASEB (Fed. Am. Soc. Exp. Biol.) J. , vol.8 , pp. 639-645
    • Caron-Leshe, L.A.M.1    Evans, R.B.2    Cidlowski, J.A.3
  • 63
    • 0028149786 scopus 로고
    • Checkpoints of dueling dimers foil death wishes
    • Oltvai, Z.N., and S.J. Korsmeyer. 1994. Checkpoints of dueling dimers foil death wishes. Cell 79:189-192.
    • (1994) Cell , vol.79 , pp. 189-192
    • Oltvai, Z.N.1    Korsmeyer, S.J.2
  • 64
    • 0028085750 scopus 로고
    • BCL-2 expression and mitochondrial activity in leuketnic cells with different sensitivity to glucocorticoid-induced apoptosis
    • Smets, L.A., J. Van den Berg, D. Acton, B. Top, H. van Rooij, and M. Verwijs-Janssen. 1994. BCL-2 expression and mitochondrial activity in leuketnic cells with different sensitivity to glucocorticoid-induced apoptosis. Blood. 5:1613-1619.
    • (1994) Blood , vol.5 , pp. 1613-1619
    • Smets, L.A.1    Van Den Berg, J.2    Acton, D.3    Top, B.4    Van Rooij, H.5    Verwijs-Janssen, M.6
  • 65
    • 0027473778 scopus 로고
    • Tumour necrosis factor-alpha induces superoxide anion production in mitochondria of L929 cells
    • Hennet, T., C. Richter, and E. Peterhans. 1993. Tumour necrosis factor-alpha induces superoxide anion production in mitochondria of L929 cells. Biochem. J. 289:587-592.
    • (1993) Biochem. J. , vol.289 , pp. 587-592
    • Hennet, T.1    Richter, C.2    Peterhans, E.3
  • 66
    • 0028152659 scopus 로고
    • Cloning and molecular characterization of mouse bcl-x in B and T lymphocytes
    • Fang, W., J.J. Rivard, D.L. Mueller, and T.W. Behrens. 1994. Cloning and molecular characterization of mouse bcl-x in B and T lymphocytes. J. Immunol. 153:4388-4398.
    • (1994) J. Immunol. , vol.153 , pp. 4388-4398
    • Fang, W.1    Rivard, J.J.2    Mueller, D.L.3    Behrens, T.W.4
  • 67
    • 0028288277 scopus 로고
    • C. elegans cell survival gene ced-9 encodes a functional homolog of the mammalian proto-oncogene bcl-2
    • Hengartner, M.O., and H.R. Horvitz. 1994. C. elegans cell survival gene ced-9 encodes a functional homolog of the mammalian proto-oncogene bcl-2. Cell. 76:665-676.
    • (1994) Cell , vol.76 , pp. 665-676
    • Hengartner, M.O.1    Horvitz, H.R.2
  • 69
    • 0023821864 scopus 로고
    • 21 -dependent pore in heart mitochondria activated by inorganic phosphate and oxidadve stress
    • 21 -dependent pore in heart mitochondria activated by inorganic phosphate and oxidadve stress. Biochem. J. 255:357-360.
    • (1988) Biochem. J. , vol.255 , pp. 357-360
    • Crompton, M.1    Ellinger, H.2    Costi, A.3
  • 72
    • 0028907350 scopus 로고
    • 2+ depletion prevents anoxic death of hepatocytes by inhibiting mitochondrial permeability transition
    • 2+ depletion prevents anoxic death of hepatocytes by inhibiting mitochondrial permeability transition. Am J. Physiol. 268:C676-685.
    • (1995) Am J. Physiol. , vol.268
    • Pastorino, J.G.1    Snyder, J.W.2    Hoek, J.B.3    Farber, J.L.4
  • 73
    • 0028905958 scopus 로고
    • The peptide mastoparan is a potent facilitator of the mitochondrial permeability transition
    • Pfeiffer, D.R., T.I. Gudz, S.A. Novgorodov, and W.L. Erdahl. 1995. The peptide mastoparan is a potent facilitator of the mitochondrial permeability transition. J. Biol. Chem. 270: 4923-4932.
    • (1995) J. Biol. Chem. , vol.270 , pp. 4923-4932
    • Pfeiffer, D.R.1    Gudz, T.I.2    Novgorodov, S.A.3    Erdahl, W.L.4
  • 74
    • 0027136160 scopus 로고
    • The mitochondrial transport protein superfamily
    • Walker, J.E., and M.J. Runswick. 1993. The mitochondrial transport protein superfamily. J. Bioenerg. Biomembr. 5:435-446.
    • (1993) J. Bioenerg. Biomembr. , vol.5 , pp. 435-446
    • Walker, J.E.1    Runswick, M.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.