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Volumn 5, Issue 5, 2000, Pages 225-230

Does the plant mitochondrion integrate cellular stress and regulate programmed cell death?

Author keywords

[No Author keywords available]

Indexed keywords

ANIMALIA; EUKARYOTA;

EID: 0034192503     PISSN: 13601385     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1360-1385(00)01605-8     Document Type: Note
Times cited : (270)

References (64)
  • 1
    • 0033539141 scopus 로고    scopus 로고
    • Interdigital cell death can occur through a necrotic and caspase-independent pathway
    • Chautan M.et al. Interdigital cell death can occur through a necrotic and caspase-independent pathway. Curr. Biol. 9:1999;967-970.
    • (1999) Curr. Biol. , vol.9 , pp. 967-970
    • Chautan, M.1
  • 2
    • 0032494143 scopus 로고    scopus 로고
    • Dual signaling of the Fas receptor: Initiation of both apoptotic and necrotic cell death pathways
    • Vercammen D.et al. Dual signaling of the Fas receptor: initiation of both apoptotic and necrotic cell death pathways. J. Exp Med. 188:1998;919-930.
    • (1998) J. Exp Med. , vol.188 , pp. 919-930
    • Vercammen, D.1
  • 3
    • 0031033274 scopus 로고    scopus 로고
    • Inhibition of Ced3/ICE-related proteases does not prevent cell death induced by oncogenes, DNA damage, or Bcl-2 homologue Bak
    • McCarthy N.J.et al. Inhibition of Ced3/ICE-related proteases does not prevent cell death induced by oncogenes, DNA damage, or Bcl-2 homologue Bak. J. Cell Biol. 136:1997;215-217.
    • (1997) J. Cell Biol. , vol.136 , pp. 215-217
    • McCarthy, N.J.1
  • 4
    • 0032544564 scopus 로고    scopus 로고
    • Apaf1 is required for mitochondrial pathways of apoptosis and brain development
    • Yoshida H.et al. Apaf1 is required for mitochondrial pathways of apoptosis and brain development. Cell. 94:1998;739-750.
    • (1998) Cell , vol.94 , pp. 739-750
    • Yoshida, H.1
  • 5
    • 15644364847 scopus 로고    scopus 로고
    • Essential contribution of caspase 3/CPP32 to apoptosis and its associated nuclear changes
    • Woo M.et al. Essential contribution of caspase 3/CPP32 to apoptosis and its associated nuclear changes. Genes Dev. 12:1998;806-819.
    • (1998) Genes Dev. , vol.12 , pp. 806-819
    • Woo, M.1
  • 6
    • 0032583164 scopus 로고    scopus 로고
    • Caspase-independent cell killing by Fas-associated protein with death domain
    • Kawahara A.et al. Caspase-independent cell killing by Fas-associated protein with death domain. J. Cell Biol. 143:1998;1353-1360.
    • (1998) J. Cell Biol. , vol.143 , pp. 1353-1360
    • Kawahara, A.1
  • 7
    • 0032765190 scopus 로고    scopus 로고
    • The nomenclature of cell death: Recommendations of an ad hoc committee of the society of toxicologic pathologists
    • Levin S.et al. The nomenclature of cell death: recommendations of an ad hoc committee of the society of toxicologic pathologists. Toxicol. Pathol. 27:1999;484-490.
    • (1999) Toxicol. Pathol. , vol.27 , pp. 484-490
    • Levin, S.1
  • 8
    • 0032404536 scopus 로고    scopus 로고
    • The central executioners of apoptosis: Caspases or mitochondria?
    • Green D., Kroemer G. The central executioners of apoptosis: caspases or mitochondria? Trends Cell Biol. 8:1998;267-271.
    • (1998) Trends Cell Biol. , vol.8 , pp. 267-271
    • Green, D.1    Kroemer, G.2
  • 9
    • 0030933841 scopus 로고    scopus 로고
    • Programmed cell death of plant tracheary elements differentiating in vitro
    • Groover A.T.et al. Programmed cell death of plant tracheary elements differentiating in vitro. Protoplasma. 196:1997;197-211.
    • (1997) Protoplasma , vol.196 , pp. 197-211
    • Groover, A.T.1
  • 10
    • 0027388946 scopus 로고
    • Do all programmed cell deaths occur via apoptosis?
    • Schwartz L.M.et al. Do all programmed cell deaths occur via apoptosis? Proc. Natl. Acad. Sci. U. S. A. 90:1993;980-984.
    • (1993) Proc. Natl. Acad. Sci. U. S. A. , vol.90 , pp. 980-984
    • Schwartz, L.M.1
  • 11
    • 0000660367 scopus 로고    scopus 로고
    • Logjam at the Styx: Programmed cell death in plants
    • Jones A.M., Dangl J.D. Logjam at the Styx: programmed cell death in plants. Trends Plant Sci. 1:1996;114-119.
    • (1996) Trends Plant Sci. , vol.1 , pp. 114-119
    • Jones, A.M.1    Dangl, J.D.2
  • 12
    • 0025283961 scopus 로고
    • Developmental cell death: Morphological diversity and multiple mechanisms
    • Clarke P.G.H. Developmental cell death: morphological diversity and multiple mechanisms. Anat. Embryol. 181:1990;195-213.
    • (1990) Anat. Embryol. , vol.181 , pp. 195-213
    • Clarke, P.G.H.1
  • 13
    • 0015928382 scopus 로고
    • Degeneration in the tail notochord of Rana temporaria larvae at metamorphic climax: Examination by electron microscopy
    • Fox H. Degeneration in the tail notochord of Rana temporaria larvae at metamorphic climax: examination by electron microscopy. Z. Zellforsch. Mikrosk. Anat. 138:1973;371-386.
    • (1973) Z. Zellforsch. Mikrosk. Anat. , vol.138 , pp. 371-386
    • Fox, H.1
  • 14
    • 0021133597 scopus 로고
    • Identical populations of phagocytes and dying neurons revealed by intravascularly injected horseradish peroxidase, and by endogenous glutaraldehyde-resistant acid phosphatase, in the brains of chick embryos
    • Clarke P.G.H. Identical populations of phagocytes and dying neurons revealed by intravascularly injected horseradish peroxidase, and by endogenous glutaraldehyde-resistant acid phosphatase, in the brains of chick embryos. Histochem. J. 16:1984;9555-9569.
    • (1984) Histochem. J. , vol.16 , pp. 9555-9569
    • Clarke, P.G.H.1
  • 15
    • 0002773832 scopus 로고
    • `Plastolysomes' plastids involved in the autolysis of the embryo suspensor in Phaseolus
    • Nagl W. `Plastolysomes' plastids involved in the autolysis of the embryo suspensor in Phaseolus. Z. Pflanzenphysiol. 85:1977;45-51.
    • (1977) Z. Pflanzenphysiol. , vol.85 , pp. 45-51
    • Nagl, W.1
  • 16
    • 0030933841 scopus 로고    scopus 로고
    • Programmed cell death of plant tracheary elements differentiating in vitro
    • Groover A.T.et al. Programmed cell death of plant tracheary elements differentiating in vitro. Protoplasma. 196:1997;197-211.
    • (1997) Protoplasma , vol.196 , pp. 197-211
    • Groover, A.T.1
  • 17
    • 0000474741 scopus 로고
    • Electron microscopy of gas space (aerenchyma) formation in adventitious roots of Zea mays L. subjected to oxygen shortage
    • Campbell R., Drew M.C. Electron microscopy of gas space (aerenchyma) formation in adventitious roots of Zea mays L. subjected to oxygen shortage. Planta. 157:1983;350-357.
    • (1983) Planta , vol.157 , pp. 350-357
    • Campbell, R.1    Drew, M.C.2
  • 18
    • 0031080649 scopus 로고    scopus 로고
    • Localization of hydrogen peroxide accumulation during the hypersensitive reaction of lettuce cells to Pseudomonas syringae pv. phaseolicola
    • Bestwick C.S.et al. Localization of hydrogen peroxide accumulation during the hypersensitive reaction of lettuce cells to Pseudomonas syringae pv. phaseolicola. Plant Cell. 9:1997;209-221.
    • (1997) Plant Cell , vol.9 , pp. 209-221
    • Bestwick, C.S.1
  • 19
    • 0000468105 scopus 로고
    • Early events in living epidermal cells and broad bean during infection with basidiospores of the cowpea rust fungus
    • Xu H., Mendgen K. Early events in living epidermal cells and broad bean during infection with basidiospores of the cowpea rust fungus. Can. J. Bot. 69:1991;2279-2285.
    • (1991) Can. J. Bot. , vol.69 , pp. 2279-2285
    • Xu, H.1    Mendgen, K.2
  • 20
    • 0031918742 scopus 로고    scopus 로고
    • The mitochondrial death/life regulator in apoptosis and necrosis
    • Kroemer G.et al. The mitochondrial death/life regulator in apoptosis and necrosis. Annu. Rev. Physiol. 60:1998;619-642.
    • (1998) Annu. Rev. Physiol. , vol.60 , pp. 619-642
    • Kroemer, G.1
  • 22
    • 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.et al. Cell-free apoptosis in Xenopus egg extracts: inhibition by Bcl-2 and requirement for an organelle fraction enriched in mitochondria. Cell. 79:1994;353-364.
    • (1994) Cell , vol.79 , pp. 353-364
    • Newmeyer, D.D.1
  • 23
    • 0031817144 scopus 로고    scopus 로고
    • Apoptosis: Unmasking the executioner
    • Wilson M.R. Apoptosis: unmasking the executioner. Cell Death Differ. 5:1998;646-652.
    • (1998) Cell Death Differ. , vol.5 , pp. 646-652
    • Wilson, M.R.1
  • 24
    • 0033596980 scopus 로고    scopus 로고
    • An APAF-1·cytochrome c multimeric complex is a functional apoptosome that activates procaspase-9
    • Zou H.et al. An APAF-1·cytochrome c multimeric complex is a functional apoptosome that activates procaspase-9. J. Biol. Chem. 274:1999;11549-11556.
    • (1999) J. Biol. Chem. , vol.274 , pp. 11549-11556
    • Zou, H.1
  • 25
    • 0032575752 scopus 로고    scopus 로고
    • Mitochondria and apoptosis
    • Green D.R., Reed J.C. Mitochondria and apoptosis. Science. 281:1998;1309-1312.
    • (1998) Science , vol.281 , pp. 1309-1312
    • Green, D.R.1    Reed, J.C.2
  • 26
    • 0033519705 scopus 로고    scopus 로고
    • Bcl-2 family proteins regulate the release of apoptogenic cytochrome c by the mitochondrial channel VDAC
    • Shimizu S.et al. Bcl-2 family proteins regulate the release of apoptogenic cytochrome c by the mitochondrial channel VDAC. Nature. 399:1999;483-487.
    • (1999) Nature , vol.399 , pp. 483-487
    • Shimizu, S.1
  • 27
    • 0032831667 scopus 로고    scopus 로고
    • Calcium induced release of mitochondrial cytochrome c by different mechanisms selective for brain versus liver
    • Andreyev A., Fiskum G. Calcium induced release of mitochondrial cytochrome c by different mechanisms selective for brain versus liver. Cell Death Differ. 6:1999;825-832.
    • (1999) Cell Death Differ. , vol.6 , pp. 825-832
    • Andreyev, A.1    Fiskum, G.2
  • 28
    • 0033565557 scopus 로고    scopus 로고
    • The mitochondrial permeability transition pore and its role in cell death
    • Crompton M. The mitochondrial permeability transition pore and its role in cell death. Biochem. J. 341:1999;233-249.
    • (1999) Biochem. J. , vol.341 , pp. 233-249
    • Crompton, M.1
  • 29
    • 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
    • Petronilli V.et al. 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. 269:1994;16638-16642.
    • (1994) J. Biol. Chem. , vol.269 , pp. 16638-16642
    • Petronilli, V.1
  • 30
    • 0032498185 scopus 로고    scopus 로고
    • Activation of the cardiac calcium release channel (ryanodine receptor) by poly-S-nitrosylation
    • Xu L.et al. Activation of the cardiac calcium release channel (ryanodine receptor) by poly-S-nitrosylation. Science. 279:1998;234-237.
    • (1998) Science , vol.279 , pp. 234-237
    • Xu, L.1
  • 31
    • 0030995428 scopus 로고    scopus 로고
    • On the voltage dependence of the mitochondrial permeability transition pore. A critical appraisal
    • Scorrano L.et al. On the voltage dependence of the mitochondrial permeability transition pore. A critical appraisal. J. Biol. Chem. 272:1997;12295-12299.
    • (1997) J. Biol. Chem. , vol.272 , pp. 12295-12299
    • Scorrano, L.1
  • 32
    • 0030041369 scopus 로고    scopus 로고
    • 2+ ions. A proposed model for phosphate-stimulated lipid peroxidation
    • 2+ ions. A proposed model for phosphate-stimulated lipid peroxidation. J. Biol. Chem. 271:1996;2929-2934.
    • (1996) J. Biol. Chem. , vol.271 , pp. 2929-2934
    • Kowaltowski, A.J.1
  • 33
    • 0033004242 scopus 로고    scopus 로고
    • Mechanisms of nitric oxide-dependent apoptosis: Involvement of mitochondrial mediators
    • Bosca L., Hortelano S. Mechanisms of nitric oxide-dependent apoptosis: involvement of mitochondrial mediators. Cell. Signal. 11:1999;239-244.
    • (1999) Cell. Signal. , vol.11 , pp. 239-244
    • Bosca, L.1    Hortelano, S.2
  • 34
    • 0032947296 scopus 로고    scopus 로고
    • Nitric oxide and mitochondrial respiration
    • Brown G.C. Nitric oxide and mitochondrial respiration. Biochim. Biophys. Acta. 1411:1999;351-369.
    • (1999) Biochim. Biophys. Acta , vol.1411 , pp. 351-369
    • Brown, G.C.1
  • 35
    • 0033198592 scopus 로고    scopus 로고
    • Mannose induces an endonuclease responsible for DNA laddering in plant cells
    • Stein J.C., Hansen G. Mannose induces an endonuclease responsible for DNA laddering in plant cells. Plant Physiol. 121:1999;71-79.
    • (1999) Plant Physiol. , vol.121 , pp. 71-79
    • Stein, J.C.1    Hansen, G.2
  • 36
    • 0003143078 scopus 로고    scopus 로고
    • The carbohydrate nutrition of tomato roots. VIII.: The mechanism of the inhibition by D-mannose of the respiration of excised roots
    • Goldsworthy A., Street H.E. The carbohydrate nutrition of tomato roots. VIII.: the mechanism of the inhibition by D-mannose of the respiration of excised roots. Ann. Bot. 29:1996;45-58.
    • (1996) Ann. Bot. , vol.29 , pp. 45-58
    • Goldsworthy, A.1    Street, H.E.2
  • 37
    • 0033408491 scopus 로고    scopus 로고
    • Translocation of cytochrome c from the mitochondria to the cytosol occurs during heat-induced programmed cell death in cucumber plants
    • Balk J.et al. Translocation of cytochrome c from the mitochondria to the cytosol occurs during heat-induced programmed cell death in cucumber plants. FEBS Lett. 463:1999;151-154.
    • (1999) FEBS Lett. , vol.463 , pp. 151-154
    • Balk, J.1
  • 38
    • 0032699832 scopus 로고    scopus 로고
    • Cytochrome c release and caspase activation during menadione-induced apoptosis in plants
    • Sun Y-L.et al. Cytochrome c release and caspase activation during menadione-induced apoptosis in plants. FEBS Lett. 462:1999;317-321.
    • (1999) FEBS Lett. , vol.462 , pp. 317-321
    • Sun, Y-L.1
  • 39
    • 0033030270 scopus 로고    scopus 로고
    • Apoptosis of mouse liver nuclei induced in the cytosol of carrot cells
    • Zhao Y.et al. Apoptosis of mouse liver nuclei induced in the cytosol of carrot cells. FEBS Lett. 448:1999;197-200.
    • (1999) FEBS Lett. , vol.448 , pp. 197-200
    • Zhao, Y.1
  • 40
    • 0033045528 scopus 로고    scopus 로고
    • The evolution of a mechanism of cell suicide
    • Blackstone N.W., Green D.R. The evolution of a mechanism of cell suicide. BioEssays. 21:1999;84-88.
    • (1999) BioEssays , vol.21 , pp. 84-88
    • Blackstone, N.W.1    Green, D.R.2
  • 41
    • 0030113929 scopus 로고    scopus 로고
    • Calcium-mediated apoptosis in a plant hypersensitive disease resistance response
    • Levine A.et al. Calcium-mediated apoptosis in a plant hypersensitive disease resistance response. Curr. Biol. 6:1996;427-437.
    • (1996) Curr. Biol. , vol.6 , pp. 427-437
    • Levine, A.1
  • 42
    • 0030443390 scopus 로고    scopus 로고
    • Transduction of an ethylene signal is required for cell death and lysis in the root cortex of maize during aerenchyma formation induced by hypoxia
    • He C-J.et al. Transduction of an ethylene signal is required for cell death and lysis in the root cortex of maize during aerenchyma formation induced by hypoxia. Plant Physiol. 112:1996;463-472.
    • (1996) Plant Physiol. , vol.112 , pp. 463-472
    • He, C-J.1
  • 43
    • 0033078011 scopus 로고    scopus 로고
    • Victorin induction of an apoptotic/senescence-like response in oats
    • Navarre D., Wolpert T.J. Victorin induction of an apoptotic/senescence-like response in oats. Plant Cell. 11:1999;237-250.
    • (1999) Plant Cell , vol.11 , pp. 237-250
    • Navarre, D.1    Wolpert, T.J.2
  • 44
    • 0032867712 scopus 로고    scopus 로고
    • Programmed cell death in transdifferentiating tracheary elements is triggered by a secreted protease
    • Groover A., Jones A.M. Programmed cell death in transdifferentiating tracheary elements is triggered by a secreted protease. Plant Physiol. 119:1999;375-384.
    • (1999) Plant Physiol. , vol.119 , pp. 375-384
    • Groover, A.1    Jones, A.M.2
  • 45
    • 0031742853 scopus 로고    scopus 로고
    • Role of calcium in signal transduction during the hypersensitive response caused by basidiospore-derived infection of the cowpea rust fungus
    • Xu H., Heath M.C. Role of calcium in signal transduction during the hypersensitive response caused by basidiospore-derived infection of the cowpea rust fungus. Plant Cell. 10:1998;585-597.
    • (1998) Plant Cell , vol.10 , pp. 585-597
    • Xu, H.1    Heath, M.C.2
  • 46
    • 0032103378 scopus 로고    scopus 로고
    • Cell-death mechanisms in maize
    • Buckner B.et al. Cell-death mechanisms in maize. Trends Plant Sci. 3:1998;218-223.
    • (1998) Trends Plant Sci. , vol.3 , pp. 218-223
    • Buckner, B.1
  • 47
    • 0343668457 scopus 로고    scopus 로고
    • Involvement of reactive oxygen species, glutathione metabolism, and lipid peroxidation in the Cf-dependent defense response of tomato cotyledons induced by race-specific elicitors of Cladosporium fulvum
    • May M.J.et al. Involvement of reactive oxygen species, glutathione metabolism, and lipid peroxidation in the Cf-dependent defense response of tomato cotyledons induced by race-specific elicitors of Cladosporium fulvum. Plant Physiol. 110:1996;1367-1379.
    • (1996) Plant Physiol. , vol.110 , pp. 1367-1379
    • May, M.J.1
  • 48
    • 0031430355 scopus 로고    scopus 로고
    • Two distinct sources of elicited reactive oxygen species in tobacco epidermal cells
    • Allan A.C., Fluhr R. Two distinct sources of elicited reactive oxygen species in tobacco epidermal cells. Plant Cell. 9:1997;1559-1572.
    • (1997) Plant Cell , vol.9 , pp. 1559-1572
    • Allan, A.C.1    Fluhr, R.2
  • 49
    • 0027951017 scopus 로고
    • Active oxygen species in plant defense against pathogens
    • Mehdy M.C. Active oxygen species in plant defense against pathogens. Plant Physiol. 105:1994;467-472.
    • (1994) Plant Physiol. , vol.105 , pp. 467-472
    • Mehdy, M.C.1
  • 50
    • 0031947649 scopus 로고    scopus 로고
    • Glutathione homeostasis in plants: Implications for environmental sensing and plant development
    • May M.J.et al. Glutathione homeostasis in plants: implications for environmental sensing and plant development. J. Exp. Biol. 49:1998;649-667.
    • (1998) J. Exp. Biol. , vol.49 , pp. 649-667
    • May, M.J.1
  • 51
    • 0030970357 scopus 로고    scopus 로고
    • Reactive oxidants and antioxidants: Relationship in green cells
    • Alscher R.G.et al. Reactive oxidants and antioxidants: relationship in green cells. Physiol. Plant. 100:1997;224-233.
    • (1997) Physiol. Plant. , vol.100 , pp. 224-233
    • Alscher, R.G.1
  • 52
    • 0029746193 scopus 로고    scopus 로고
    • Initiation of runaway cell death in an Arabidopsis mutant by extracellular superoxide
    • Jabs T.et al. Initiation of runaway cell death in an Arabidopsis mutant by extracellular superoxide. Science. 273:1996;1853-1856.
    • (1996) Science , vol.273 , pp. 1853-1856
    • Jabs, T.1
  • 53
    • 0028171293 scopus 로고
    • 2 from the oxidative burst orchestrates the plant hypersensitive disease resistance response
    • 2 from the oxidative burst orchestrates the plant hypersensitive disease resistance response. Cell. 79:1994;583-593.
    • (1994) Cell , vol.79 , pp. 583-593
    • Levine, A.1
  • 55
    • 0033180574 scopus 로고    scopus 로고
    • Role of active oxygen species and NO in plant defence responses
    • Bolwell G.P. Role of active oxygen species and NO in plant defence responses. Curr. Opin. Plant Biol. 2:1999;287-294.
    • (1999) Curr. Opin. Plant Biol. , vol.2 , pp. 287-294
    • Bolwell, G.P.1
  • 56
    • 0030592172 scopus 로고    scopus 로고
    • The permeability transition pore. Control points of a cyclosporin A-sensitive mitochondrial channel involved in cell death
    • Bernardi P. The permeability transition pore. Control points of a cyclosporin A-sensitive mitochondrial channel involved in cell death. Biochim. Biophys. Acta. 1275:1996;5-9.
    • (1996) Biochim. Biophys. Acta , vol.1275 , pp. 5-9
    • Bernardi, P.1
  • 57
    • 0032124749 scopus 로고    scopus 로고
    • A porphyrin pathway impairment is responsible for the phenotype of a dominant disease lesion mimic mutant of maize
    • Hu G.et al. A porphyrin pathway impairment is responsible for the phenotype of a dominant disease lesion mimic mutant of maize. Plant Cell. 10:1998;1095-1105.
    • (1998) Plant Cell , vol.10 , pp. 1095-1105
    • Hu, G.1
  • 58
    • 0030471143 scopus 로고    scopus 로고
    • Mitochondrial permeability transition triggers lymphocyte apoptosis
    • Marchetti P.et al. Mitochondrial permeability transition triggers lymphocyte apoptosis. J. Immunol. 157:1996;4830-4836.
    • (1996) J. Immunol. , vol.157 , pp. 4830-4836
    • Marchetti, P.1
  • 59
    • 0031037897 scopus 로고    scopus 로고
    • The release of cytochrome c from mitochondria: A primary site for Bcl-2 regulation of apoptosis
    • Kluck R.M.et al. The release of cytochrome c from mitochondria: a primary site for Bcl-2 regulation of apoptosis. Science. 275:1997;1132-1136.
    • (1997) Science , vol.275 , pp. 1132-1136
    • Kluck, R.M.1
  • 60
    • 0031036872 scopus 로고    scopus 로고
    • Prevention of apoptosis by Bcl-2: Release of cytochrome c from mitochondria blocked
    • Yang J.et al. Prevention of apoptosis by Bcl-2: release of cytochrome c from mitochondria blocked. Science. 27:1997;1129-1132.
    • (1997) Science , vol.27 , pp. 1129-1132
    • Yang, J.1
  • 61
    • 0010425129 scopus 로고    scopus 로고
    • Injected cytochrome c induces apoptosis
    • Zhivotovsky B.et al. Injected cytochrome c induces apoptosis. Nature. 391:1998;449-450.
    • (1998) Nature , vol.391 , pp. 449-450
    • Zhivotovsky, B.1
  • 62
    • 0032576692 scopus 로고    scopus 로고
    • Bcl-2 prolongs cell survival after Bax-induced release of cytochrome c
    • Rosse T.et al. Bcl-2 prolongs cell survival after Bax-induced release of cytochrome c. Nature. 391:1998;496-499.
    • (1998) Nature , vol.391 , pp. 496-499
    • Rosse, T.1
  • 63
    • 0033529332 scopus 로고    scopus 로고
    • Bax-induced cell death in tobacco is similar to the hypersensitive response
    • Lacomme C., Santa Cruz S. Bax-induced cell death in tobacco is similar to the hypersensitive response. Proc. Natl. Acad. Sci. U. S. A. 96:1999;7956-7961.
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 7956-7961
    • Lacomme, C.1    Santa Cruz, S.2
  • 64
    • 0033565453 scopus 로고    scopus 로고
    • XL and Ced-9 inhibit cell death in plants
    • XL and Ced-9 inhibit cell death in plants. Curr. Biol. 9:1999;775-778.
    • (1999) Curr. Biol. , vol.9 , pp. 775-778
    • Mitsuhara, I.1


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