메뉴 건너뛰기




Volumn 29, Issue 3, 2004, Pages 521-530

Mitochondrial Function in Apoptotic Neuronal Cell Death

Author keywords

Apoptosis; Cytochrome c; Mitochondria; Neurodegeneration

Indexed keywords

CYTOCHROME C;

EID: 1542318100     PISSN: 03643190     EISSN: None     Source Type: Journal    
DOI: 10.1023/B:NERE.0000014823.74782.b7     Document Type: Review
Times cited : (65)

References (115)
  • 1
    • 0015383455 scopus 로고
    • Apoptosis: A basic biological phenomenon with wide-ranging implications in tissue kinetics
    • Kerr, J. F., Wyllie, A. H., and Currie, A. R. 1972. Apoptosis: A basic biological phenomenon with wide-ranging implications in tissue kinetics. Br. J. Cancer 26:239-247.
    • (1972) Br. J. Cancer , vol.26 , pp. 239-247
    • Kerr, J.F.1    Wyllie, A.H.2    Currie, A.R.3
  • 3
    • 0032055973 scopus 로고    scopus 로고
    • Neuronal cell death
    • Pettmann, B. and Henderson, C. E. 1998. Neuronal cell death. Neuron 20:633-647.
    • (1998) Neuron , vol.20 , pp. 633-647
    • Pettmann, B.1    Henderson, C.E.2
  • 4
    • 0032999788 scopus 로고    scopus 로고
    • Poly (ADP-ribose) polymerase, nitric oxide and cell death
    • Peiper, A. A., Verma, A., Zhang, J., and Snyder, S. H. 1999. Poly (ADP-ribose) polymerase, nitric oxide and cell death. TiPS 20:171-181.
    • (1999) TiPS , vol.20 , pp. 171-181
    • Peiper, A.A.1    Verma, A.2    Zhang, J.3    Snyder, S.H.4
  • 5
    • 0033956278 scopus 로고    scopus 로고
    • Calpain and caspase: Can you tell the difference?
    • Wang, K. K. W. 2000. Calpain and caspase: Can you tell the difference? TiNS 23:20-26.
    • (2000) TiNS , vol.23 , pp. 20-26
    • Wang, K.K.W.1
  • 6
    • 0035575679 scopus 로고    scopus 로고
    • Programmed cell death: Alive and well in the new millennium
    • Kaufmann, S. H. and Hengartner, M. O. 2001 Programmed cell death: Alive and well in the new millennium. Trends Cell Biol. 11:526-534.
    • (2001) Trends Cell Biol. , vol.11 , pp. 526-534
    • Kaufmann, S.H.1    Hengartner, M.O.2
  • 7
    • 0032505127 scopus 로고    scopus 로고
    • Essential requirement for caspase-8/FLICE in the initiation of the Fas-induced apoptotic cascade
    • Juo, P., Kuo, C. J., Yuan, J., and Blenis, J. 1998. Essential requirement for caspase-8/FLICE in the initiation of the Fas-induced apoptotic cascade. Curr. Biol. 8:1001-1008.
    • (1998) Curr. Biol. , vol.8 , pp. 1001-1008
    • Juo, P.1    Kuo, C.J.2    Yuan, J.3    Blenis, J.4
  • 8
    • 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
  • 10
    • 0033782031 scopus 로고    scopus 로고
    • Cytochrome c release from mitochondria: All or nothing
    • Martinou, J. C., Desagher, S., and Antonsson, B. 2000. Cytochrome c release from mitochondria: All or nothing. Nat. Cell Biol. 2: E41-E43.
    • (2000) Nat. Cell Biol. , vol.2
    • Martinou, J.C.1    Desagher, S.2    Antonsson, B.3
  • 12
    • 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
  • 13
    • 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
  • 14
    • 0033083559 scopus 로고    scopus 로고
    • Neuronal cell death: A demise with different shapes
    • Nicotera, P., Leist, M., and Manzo, L. 1999. Neuronal cell death: A demise with different shapes. TiPS 20:46-51.
    • (1999) TiPS , vol.20 , pp. 46-51
    • Nicotera, P.1    Leist, M.2    Manzo, L.3
  • 15
    • 0030738366 scopus 로고    scopus 로고
    • Multiple sclerosis: Oligodendrocytes display cell death-related molecules in situ but do not undergo apoptosis
    • Bonetti, B. and Raine, C. S. 1997. Multiple sclerosis: Oligodendrocytes display cell death-related molecules in situ but do not undergo apoptosis. Ann. Neurol. 42:74-84.
    • (1997) Ann. Neurol. , vol.42 , pp. 74-84
    • Bonetti, B.1    Raine, C.S.2
  • 16
    • 0345647098 scopus 로고    scopus 로고
    • Glutamate neurotoxicity in mouse cortical neurons: Atypical necrosis with DNA ladders and chromatin condensation
    • Sohn, S., Kim, E. Y., and Gwag, B. J. 1998. Glutamate neurotoxicity in mouse cortical neurons: Atypical necrosis with DNA ladders and chromatin condensation. Neurosci. Lett. 240:147-150.
    • (1998) Neurosci. Lett. , vol.240 , pp. 147-150
    • Sohn, S.1    Kim, E.Y.2    Gwag, B.J.3
  • 17
    • 0031816414 scopus 로고    scopus 로고
    • Apoptosis, excitotoxicity, and neuropathology
    • Leist, M. and Nicotera, P. 1998. Apoptosis, excitotoxicity, and neuropathology. Exp. Cell Res. 239:183-201.
    • (1998) Exp. Cell Res. , vol.239 , pp. 183-201
    • Leist, M.1    Nicotera, P.2
  • 18
    • 0021926813 scopus 로고
    • Macrophage recognition of cells undergoing programmed cell death (apoptosis)
    • Duvall, E., Wyllie, A. H., and Morris, R. G. 1985. Macrophage recognition of cells undergoing programmed cell death (apoptosis). Immunology 56:351-358.
    • (1985) Immunology , vol.56 , pp. 351-358
    • Duvall, E.1    Wyllie, A.H.2    Morris, R.G.3
  • 19
    • 0034074468 scopus 로고    scopus 로고
    • Energy requirement for caspase activation and neuronal cell death
    • Nicotera, P., Leist, M., Fava, E., Berliocchi, L., and Volbracht, C. 2000. Energy requirement for caspase activation and neuronal cell death. Brain Pathol. 10:276-282.
    • (2000) Brain Pathol. , vol.10 , pp. 276-282
    • Nicotera, P.1    Leist, M.2    Fava, E.3    Berliocchi, L.4    Volbracht, C.5
  • 20
    • 0025265926 scopus 로고
    • The role of glutamate neurotoxicity in hypoxic-ischemic neuronal death
    • Choi, D. W. and Rothman, S. M. 1990. The role of glutamate neurotoxicity in hypoxic-ischemic neuronal death. Ann. Rev. Neurosci. 13:171-182.
    • (1990) Ann. Rev. Neurosci. , vol.13 , pp. 171-182
    • Choi, D.W.1    Rothman, S.M.2
  • 21
    • 0028924890 scopus 로고
    • Delayed neuronal death in the CA1 pyramidal cell layer of the gerbil hippocampus following transient ischemia is apoptosis
    • Nitatori, T., Sato, N., Waguri, S., Karasawa, Y., Araki, H., Shibanai, K., Kominami, E., and Uchiyama, Y. 1995. Delayed neuronal death in the CA1 pyramidal cell layer of the gerbil hippocampus following transient ischemia is apoptosis. J. Neurosci. 15:1001-1011.
    • (1995) J. Neurosci. , vol.15 , pp. 1001-1011
    • Nitatori, T.1    Sato, N.2    Waguri, S.3    Karasawa, Y.4    Araki, H.5    Shibanai, K.6    Kominami, E.7    Uchiyama, Y.8
  • 22
    • 0030273118 scopus 로고    scopus 로고
    • Neurobiology of disease
    • Choi, D. W. 1996. Neurobiology of disease. Curr. Opin. Neurobiol. 6:667-672.
    • (1996) Curr. Opin. Neurobiol. , vol.6 , pp. 667-672
    • Choi, D.W.1
  • 23
    • 0029153913 scopus 로고
    • Apoptosis and necrosis: Two distinct events induced, respectively, by mild and intense insults with N-methyl-D-aspartate or nitric oxide/superoxide in cortical cell cultures
    • Bonfoco, E., Krainc, D., Ankarcrona, M., Nicotera, P., and Lipton, S. A. 1995. Apoptosis and necrosis: Two distinct events induced, respectively, by mild and intense insults with N-methyl-D-aspartate or nitric oxide/superoxide in cortical cell cultures. Proc. Natl. Acad. Sci. USA 92:7162-7166.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 7162-7166
    • Bonfoco, E.1    Krainc, D.2    Ankarcrona, M.3    Nicotera, P.4    Lipton, S.A.5
  • 25
    • 0023767261 scopus 로고    scopus 로고
    • Non-competitive antagonists of N-methyl-D-aspartate receptors protect cortical and hippocampal cell cultures against glutamate neurotoxicity
    • Rondouin, G., Drian, M. J., Chicheportiche, R., Kamenka, J. M., and Privat, A. 1998. Non-competitive antagonists of N-methyl-D-aspartate receptors protect cortical and hippocampal cell cultures against glutamate neurotoxicity. Neurosci. Lett. 91:199-203.
    • (1998) Neurosci. Lett. , vol.91 , pp. 199-203
    • Rondouin, G.1    Drian, M.J.2    Chicheportiche, R.3    Kamenka, J.M.4    Privat, A.5
  • 26
  • 27
    • 0029827804 scopus 로고    scopus 로고
    • Mitochondria, calcium regulation, and acute glutamate excitotoxicity in cultured cerebellar granule cells
    • Budd, S. L. and Nicholls, D. G. 1996. Mitochondria, calcium regulation, and acute glutamate excitotoxicity in cultured cerebellar granule cells. J. Neurochem. 67:2282-2291.
    • (1996) J. Neurochem. , vol.67 , pp. 2282-2291
    • Budd, S.L.1    Nicholls, D.G.2
  • 28
    • 0033763403 scopus 로고    scopus 로고
    • Detection of high molecular weight DNA fragments characteristic of early stage apoptosis in cerebellar granule cells exposed to glutamate
    • Slagsvold, H. H., Marvik, O. J., Eidem, G., Kristoffersen, N., and Paulsen, R. E. 2000. Detection of high molecular weight DNA fragments characteristic of early stage apoptosis in cerebellar granule cells exposed to glutamate. Exp. Brain Res. 135:173-178.
    • (2000) Exp. Brain Res. , vol.135 , pp. 173-178
    • Slagsvold, H.H.1    Marvik, O.J.2    Eidem, G.3    Kristoffersen, N.4    Paulsen, R.E.5
  • 29
    • 0031041530 scopus 로고    scopus 로고
    • Slowly triggered excitotoxicity occurs by necrosis in cortical cultures
    • Gwag, B. J., Koh, J. Y., DeMaro, J. A., Ying, H. S., Jacquin, M., and Choi, D. W. 1997. Slowly triggered excitotoxicity occurs by necrosis in cortical cultures. Neuroscience 77:393-401.
    • (1997) Neuroscience , vol.77 , pp. 393-401
    • Gwag, B.J.1    Koh, J.Y.2    DeMaro, J.A.3    Ying, H.S.4    Jacquin, M.5    Choi, D.W.6
  • 30
    • 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
  • 31
    • 0036524672 scopus 로고    scopus 로고
    • Characterization of the cell death modes and the associated changes in cellular energy supply in response to AIPcS4-PDT
    • Plaetzer, K., Kiesslich, T., Krammer, B., and Hammerl, P. 2002. Characterization of the cell death modes and the associated changes in cellular energy supply in response to AIPcS4-PDT. Photochem. Photobiol. Sci. 1:172-177.
    • (2002) Photochem. Photobiol. Sci. , vol.1 , pp. 172-177
    • Plaetzer, K.1    Kiesslich, T.2    Krammer, B.3    Hammerl, P.4
  • 32
    • 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., Kuhnle, 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    Kuhnle, S.4    Nicotera, P.5
  • 34
    • 0032704329 scopus 로고    scopus 로고
    • Tributyltin-induced apoptosis requires glycolytic adenosine trisphosphate production
    • Stridh, H., Fava, E., Single, B., Nicotera, P., Orrenius, S., and Leist, M. 1999. Tributyltin-induced apoptosis requires glycolytic adenosine trisphosphate production. Chem. Res. Toxicol. 12:874-882.
    • (1999) Chem. Res. Toxicol. , vol.12 , pp. 874-882
    • Stridh, H.1    Fava, E.2    Single, B.3    Nicotera, P.4    Orrenius, S.5    Leist, M.6
  • 35
    • 0037308233 scopus 로고    scopus 로고
    • Mitochondrial permeability transition in the switch from necrotic to apoptotic cell death in ischemic rat hepatocytes
    • Kim, J. S., Qian, T., and Lemasters, J. J. 2003. Mitochondrial permeability transition in the switch from necrotic to apoptotic cell death in ischemic rat hepatocytes. Gastroenterology 124:494-503.
    • (2003) Gastroenterology , vol.124 , pp. 494-503
    • Kim, J.S.1    Qian, T.2    Lemasters, J.J.3
  • 36
    • 0033822094 scopus 로고    scopus 로고
    • D-Glucose prevents glutathione oxidation and mitochondrial damage after glutamate receptor stimulation in rat cortical primary neurons
    • Delgado-Esteban, M., Almeida, A., and Bolanos, J. P. 2000. D-Glucose prevents glutathione oxidation and mitochondrial damage after glutamate receptor stimulation in rat cortical primary neurons. J. Neurochem. 75:1618-1624.
    • (2000) J. Neurochem. , vol.75 , pp. 1618-1624
    • Delgado-Esteban, M.1    Almeida, A.2    Bolanos, J.P.3
  • 37
    • 0034705057 scopus 로고    scopus 로고
    • Mitochondrial and extramitochondrial apoptotic signaling pathways in cerebrocortical neurons
    • Budd, S. L., Tenneti, L., Lishnak, T., and Lipton, S. A. 2000. Mitochondrial and extramitochondrial apoptotic signaling pathways in cerebrocortical neurons. Proc. Natl. Acad. Sci. USA 97:6161-6166.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 6161-6166
    • Budd, S.L.1    Tenneti, L.2    Lishnak, T.3    Lipton, S.A.4
  • 38
    • 0034864018 scopus 로고    scopus 로고
    • Mitochondrial involvement in brain function and dysfunction: Relevance to aging, neurodegenerative disorders and longevity
    • Calabrese, V., Scapagnini, G., Giuffrida Stella, A. M., Bates, T. E., and Clark, J. B. 2001. Mitochondrial involvement in brain function and dysfunction: Relevance to aging, neurodegenerative disorders and longevity. Neurochem. Res. 26:739-764.
    • (2001) Neurochem. Res. , vol.26 , pp. 739-764
    • Calabrese, V.1    Scapagnini, G.2    Giuffrida Stella, A.M.3    Bates, T.E.4    Clark, J.B.5
  • 39
    • 0023851503 scopus 로고
    • Inhibitors of protein synthesis and RNA synthesis prevent neuronal death caused by nerve growth factor deprivation
    • Martin, D. P., Schmidt, R. E., DiStefano, P. S., Lowry, O. H., Carter, J. G., and Johnson, E. M. Jr. 1988. Inhibitors of protein synthesis and RNA synthesis prevent neuronal death caused by nerve growth factor deprivation. J. Cell Biol. 106:829-844.
    • (1988) J. Cell Biol. , vol.106 , pp. 829-844
    • Martin, D.P.1    Schmidt, R.E.2    DiStefano, P.S.3    Lowry, O.H.4    Carter, J.G.5    Johnson Jr., E.M.6
  • 40
    • 0031972678 scopus 로고    scopus 로고
    • Phosphorylation of c-Jun is necessary for apoptosis induced by survival signal withdrawal in cerebellar granule neurons
    • Watson, A., Eilers, A., Lallemand, D., Kyriakis, J., Rubin, L. L., and Ham, J. 1998. Phosphorylation of c-Jun is necessary for apoptosis induced by survival signal withdrawal in cerebellar granule neurons. J. Neurosci. 18:751-762.
    • (1998) J. Neurosci. , vol.18 , pp. 751-762
    • Watson, A.1    Eilers, A.2    Lallemand, D.3    Kyriakis, J.4    Rubin, L.L.5    Ham, J.6
  • 41
    • 0027483920 scopus 로고
    • Induction of apoptosis in cerebellar granule neurons by low potassium: Inhibition of death by insulin-like growth factor I and cAMP
    • D'Mello, S. R., Galli, C., Ciotti, T., and Calissano, P. 1993. Induction of apoptosis in cerebellar granule neurons by low potassium: Inhibition of death by insulin-like growth factor I and cAMP. Proc. Natl. Acad. Sci. USA 90:10989-10993.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 10989-10993
    • D'Mello, S.R.1    Galli, C.2    Ciotti, T.3    Calissano, P.4
  • 42
    • 0037032594 scopus 로고    scopus 로고
    • Differential activation of caspase-3 at two maturational stages during okadaic acid-induced rat neuronal death
    • Hong, H. N., Yoon, S. Y., Suh, J., Lee, J. H., and Kim, D. 2002. Differential activation of caspase-3 at two maturational stages during okadaic acid-induced rat neuronal death. Neurosci. Lett. 334:63-67.
    • (2002) Neurosci. Lett. , vol.334 , pp. 63-67
    • Hong, H.N.1    Yoon, S.Y.2    Suh, J.3    Lee, J.H.4    Kim, D.5
  • 43
    • 0036724767 scopus 로고    scopus 로고
    • Calpain activates caspase-3 during UV-induced neuronal death but only calpain is necessary for death
    • McCollum, A. T., Nasr, P., and Estus, S. 2002. Calpain activates caspase-3 during UV-induced neuronal death but only calpain is necessary for death. J. Neurochem. 82:1208-1220.
    • (2002) J. Neurochem. , vol.82 , pp. 1208-1220
    • McCollum, A.T.1    Nasr, P.2    Estus, S.3
  • 44
    • 0036859738 scopus 로고    scopus 로고
    • Defining characteristics of types I and II apoptotic cells in response to TRAIL
    • Özören, N. and El-Deiry, W. S. 2002. Defining characteristics of types I and II apoptotic cells in response to TRAIL. Neoplasia 4:551-557.
    • (2002) Neoplasia , vol.4 , pp. 551-557
    • Özören, N.1    El-Deiry, W.S.2
  • 45
    • 0344348821 scopus 로고    scopus 로고
    • Role of cytochrome c and dATP/ATP hydrolysis in Apaf-1-mediated caspase-9 activation and apoptosis
    • Hu, Y., Benedict, M. A., Ding, L., and Núñez, G. 1999. Role of cytochrome c and dATP/ATP hydrolysis in Apaf-1-mediated caspase-9 activation and apoptosis. EMBO J. 18:3586-3595.
    • (1999) EMBO J. , vol.18 , pp. 3586-3595
    • Hu, Y.1    Benedict, M.A.2    Ding, L.3    Núñez, G.4
  • 46
    • 0026582672 scopus 로고
    • Ribonucleotide reductase: Regulation, regulation, regulation
    • Elledge, S. J., Zhou, Z., and Allen, J. B. 1992. Ribonucleotide reductase: Regulation, regulation, regulation. Trends Biochem. Sci. 17:119-123.
    • (1992) Trends Biochem. Sci. , vol.17 , pp. 119-123
    • Elledge, S.J.1    Zhou, Z.2    Allen, J.B.3
  • 47
    • 0033547430 scopus 로고    scopus 로고
    • p53 accumulation in apoptotic macrophages is an energy demanding process that precedes cytochrome c release in response to nitric oxide
    • Brockhaus, F. and Brune, B. 1999. p53 accumulation in apoptotic macrophages is an energy demanding process that precedes cytochrome c release in response to nitric oxide. Oncogene 18:6403-6410.
    • (1999) Oncogene , vol.18 , pp. 6403-6410
    • Brockhaus, F.1    Brune, B.2
  • 48
    • 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
  • 52
    • 0035811496 scopus 로고    scopus 로고
    • Endonuclease G is an apoptotic DNase when released from mitochondria
    • Li, L. Y., Luo, X., and Wang, X. 2001. Endonuclease G is an apoptotic DNase when released from mitochondria. Nature 412:95-99.
    • (2001) Nature , vol.412 , pp. 95-99
    • Li, L.Y.1    Luo, X.2    Wang, X.3
  • 53
    • 0035811511 scopus 로고    scopus 로고
    • Mitochondrial endonuclease G is important for apoptosis in C. elegans
    • Parrish, J., Li, L., Klotz, K., Ledwich, D., Wang, X., and Xue, D. 2001. Mitochondrial endonuclease G is important for apoptosis in C. elegans. Nature 412:90-94.
    • (2001) Nature , vol.412 , pp. 90-94
    • Parrish, J.1    Li, L.2    Klotz, K.3    Ledwich, D.4    Wang, X.5    Xue, D.6
  • 59
    • 0030843575 scopus 로고    scopus 로고
    • Overexpression of Bcl-X(L) inhibits Ara-C-induced mitochondrial loss of cytochrome c and other perturbations that activate the molecular cascade of apoptosis
    • Kim, C. N., Wang, X., Huang, Y., Ibrado, A. M., Liu, L., Fang, G., and Bhalla, K. 1997. Overexpression of Bcl-X(L) inhibits Ara-C-induced mitochondrial loss of cytochrome c and other perturbations that activate the molecular cascade of apoptosis. Cancer Res. 57:3115-3120.
    • (1997) Cancer Res. , vol.57 , pp. 3115-3120
    • Kim, C.N.1    Wang, X.2    Huang, Y.3    Ibrado, A.M.4    Liu, L.5    Fang, G.6    Bhalla, K.7
  • 60
    • 0030741528 scopus 로고    scopus 로고
    • Cytochrome c activation of CPP32-like proteolysis plays a critical role in a Xenopus cell-free apoptosis system
    • Kluck, R. M., Martin, S. J., Hoffman, B. M., Zhou, J. S., Green, D. R., and Newmeyer, D. D. 1997. Cytochrome c activation of CPP32-like proteolysis plays a critical role in a Xenopus cell-free apoptosis system. EMBO J. 16:4639-4649.
    • (1997) EMBO J. , vol.16 , pp. 4639-4649
    • Kluck, R.M.1    Martin, S.J.2    Hoffman, B.M.3    Zhou, J.S.4    Green, D.R.5    Newmeyer, D.D.6
  • 61
    • 0037184910 scopus 로고    scopus 로고
    • Apocytochrome c blocks caspase-9 activation and Bax-induced apoptosis
    • Martin, A. G. and Fearnhead, H. O. 2002. Apocytochrome c blocks caspase-9 activation and Bax-induced apoptosis. J. Biol. Chem. 277:50834-50841.
    • (2002) J. Biol. Chem. , vol.277 , pp. 50834-50841
    • Martin, A.G.1    Fearnhead, H.O.2
  • 62
    • 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., 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.7    Jones, D.P.8    Wang, X.9
  • 63
    • 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
  • 64
    • 0034710942 scopus 로고    scopus 로고
    • Cytochrome c binding to Apaf-1: The effects of dATP and ionic strength
    • Purring-Koch, C. and McLendon, G. 2000 Cytochrome c binding to Apaf-1: The effects of dATP and ionic strength. Proc. Natl. Acad. Sci. USA 97:11928-11931.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 11928-11931
    • Purring-Koch, C.1    McLendon, G.2
  • 65
    • 0036723818 scopus 로고    scopus 로고
    • Cytochrome c release precedes mitochondrial membrane potential loss in cerebellar granule neuron apoptosis: Lack of mitochondrial swelling
    • Wigdal, S. S., Kirkland, R. A., Franklin, J. L., and Haak-Frendscho, M. 2002. Cytochrome c release precedes mitochondrial membrane potential loss in cerebellar granule neuron apoptosis: Lack of mitochondrial swelling. J. Neurochem. 82:1029-1038.
    • (2002) J. Neurochem. , vol.82 , pp. 1029-1038
    • Wigdal, S.S.1    Kirkland, R.A.2    Franklin, J.L.3    Haak-Frendscho, M.4
  • 66
    • 0034631832 scopus 로고    scopus 로고
    • Caspase inhibition extends the commitment to neuronal death beyond cytochrome c release to the point of mitochondrial depolarization
    • 150.1.131
    • Deshmukh, D., 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. 150.1.131.
    • (2000) J. Cell. Biol.
    • Deshmukh, D.1    Kuida, K.2    Johnson Jr., E.M.3
  • 67
    • 0037119178 scopus 로고    scopus 로고
    • N-Methyl-D-aspartate receptor and L-type voltage-gated Ca(2+) channel antagonists suppress the release of cytochrome c and the expression of procaspase-3 in rat hippocampus after global brain ischemia
    • Zhang, C., Shen, W., and Zhang, G. 2002. N-Methyl-D-aspartate receptor and L-type voltage-gated Ca(2+) channel antagonists suppress the release of cytochrome c and the expression of procaspase-3 in rat hippocampus after global brain ischemia. Neurosci. Lett. 328:265-268.
    • (2002) Neurosci. Lett. , vol.328 , pp. 265-268
    • Zhang, C.1    Shen, W.2    Zhang, G.3
  • 68
    • 0038587580 scopus 로고    scopus 로고
    • Bcl-2 overexpression protects against neuron loss within the ischemic margin following experimental stroke and inhibits cytochrome c translocation and caspase-3 activity
    • Zhao, H., Yenari, M. A., Cheng, D., Sapolsky, R. M., and Steinberg, G. K. 2003. Bcl-2 overexpression protects against neuron loss within the ischemic margin following experimental stroke and inhibits cytochrome c translocation and caspase-3 activity. J. Neurochem. 85:1026-1028.
    • (2003) J. Neurochem. , vol.85 , pp. 1026-1028
    • Zhao, H.1    Yenari, M.A.2    Cheng, D.3    Sapolsky, R.M.4    Steinberg, G.K.5
  • 73
    • 20244364788 scopus 로고    scopus 로고
    • Intranuclear localization of apoptosis-inducing factor (AIF) and large scale DNA fragmentation after traumatic brain injury in rats and in neuronal cultures exposed to peroxynitrite
    • Zhang, X., Chen, J., Graham, S. H., Du, L., Kochanek, P. M., Draviam, R., Guo, F., Nathaniel, P. D., Szabo, G., Watkins, S. C., and Clark, R. S. 2002. Intranuclear localization of apoptosis-inducing factor (AIF) and large scale DNA fragmentation after traumatic brain injury in rats and in neuronal cultures exposed to peroxynitrite. J. Neurochem. 82:181-191.
    • (2002) J. Neurochem. , vol.82 , pp. 181-191
    • Zhang, X.1    Chen, J.2    Graham, S.H.3    Du, L.4    Kochanek, P.M.5    Draviam, R.6    Guo, F.7    Nathaniel, P.D.8    Szabo, G.9    Watkins, S.C.10    Clark, R.S.11
  • 76
    • 0037191413 scopus 로고    scopus 로고
    • Subcellular localization of a promoter and an inhibitor of apoptosis (Smac/DIABLO and XIAP) during brain ischemia/reperfusion
    • Shibata, M., Hattori, H., Sasaki, T., Gotoh, J., Hamada, J., and Fukuuchi, Y. 2002. Subcellular localization of a promoter and an inhibitor of apoptosis (Smac/DIABLO and XIAP) during brain ischemia/reperfusion. Neuroreport 13:1985-1988.
    • (2002) Neuroreport , vol.13 , pp. 1985-1988
    • Shibata, M.1    Hattori, H.2    Sasaki, T.3    Gotoh, J.4    Hamada, J.5    Fukuuchi, Y.6
  • 77
    • 0037072873 scopus 로고    scopus 로고
    • Mechanisms of p75-mediated death of hippocampal neurons: Role of caspases
    • Troy, C. M., Friedman, J. E., and Friedman, W. J. 2002. Mechanisms of p75-mediated death of hippocampal neurons: Role of caspases. J. Biol. Chem. 277:34295-342302.
    • (2002) J. Biol. Chem. , vol.277 , pp. 34295-342302
    • Troy, C.M.1    Friedman, J.E.2    Friedman, W.J.3
  • 78
    • 0034785591 scopus 로고    scopus 로고
    • A serine protease, HtrA2, is released from the mitochondria and interacts with XIAP, inducing cell death
    • Suzuki, Y., Imai, Y., Nakayama, H., Takahashi, K., Takio, K., and Takahashi, R. 2001. A serine protease, HtrA2, is released from the mitochondria and interacts with XIAP, inducing cell death. Mol. Cells 8:613-621.
    • (2001) Mol. Cells , vol.8 , pp. 613-621
    • Suzuki, Y.1    Imai, Y.2    Nakayama, H.3    Takahashi, K.4    Takio, K.5    Takahashi, R.6
  • 79
    • 0037159784 scopus 로고    scopus 로고
    • Mechanisms of AIF-mediated apoptotic DNA degradation in Caenorhabditis elegans
    • Wang, X., Yang, C., Chai, J., Shi, Y., and Xue, D. 2002. Mechanisms of AIF-mediated apoptotic DNA degradation in Caenorhabditis elegans. Science 298:1587-1592.
    • (2002) Science , vol.298 , pp. 1587-1592
    • Wang, X.1    Yang, C.2    Chai, J.3    Shi, Y.4    Xue, D.5
  • 80
    • 0032192529 scopus 로고    scopus 로고
    • Evidence of a novel event during neuronal death: Development of competence-to-die in response to cytoplasmic cytochrome c
    • Deshmuckh, M. and Johnson E. M. Jr. 1998. Evidence of a novel event during neuronal death: Development of competence-to-die in response to cytoplasmic cytochrome c. Neuron 21:6?
    • (1998) Neuron , vol.21 , pp. 6
    • Deshmuckh, M.1    Johnson Jr., E.M.2
  • 81
    • 0037107134 scopus 로고    scopus 로고
    • Exogenous Smac induces competence and permits caspase activation in sympathetic neurons
    • Deshmukh, M., Du, C., Wang, X., and Johnson, E. M. Jr. 2002. Exogenous Smac induces competence and permits caspase activation in sympathetic neurons. J. Neurosci. 22:8018-8027.
    • (2002) J. Neurosci. , vol.22 , pp. 8018-8027
    • Deshmukh, M.1    Du, C.2    Wang, X.3    Johnson Jr., E.M.4
  • 84
    • 0030916417 scopus 로고    scopus 로고
    • DFF: A heterodimeric protein that functions downstream of caspase-3 to trigger DNA fragmentation during apoptosis
    • Liu, X., Zou, H., Slaughter, C., and Wang, X. 1997. DFF: A heterodimeric protein that functions downstream of caspase-3 to trigger DNA fragmentation during apoptosis. Cell 89:175-184.
    • (1997) Cell , vol.89 , pp. 175-184
    • Liu, X.1    Zou, H.2    Slaughter, C.3    Wang, X.4
  • 86
    • 0035894881 scopus 로고    scopus 로고
    • Caspase-9 activation results in downstream caspase-8 activation and bid cleavage in 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine-induced Parkinson's disease
    • Viswanath, V., Wu, Y., Boonplueang, R., Chen, S., Stevenson, F. F., Yantiri, F., Yang, L., Beal, M. F., and Andersen, J. K. 2001. Caspase-9 activation results in downstream caspase-8 activation and bid cleavage in 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine-induced Parkinson's disease. J. Neurosci. 21:9519-9528.
    • (2001) J. Neurosci. , vol.21 , pp. 9519-9528
    • Viswanath, V.1    Wu, Y.2    Boonplueang, R.3    Chen, S.4    Stevenson, F.F.5    Yantiri, F.6    Yang, L.7    Beal, M.F.8    Andersen, J.K.9
  • 87
    • 0033010059 scopus 로고    scopus 로고
    • Endogenous bax translocation in SH-SY5Y human neuroblastoma cells and cerebellar granule neurons undergoing apoptosis
    • McGinnis, K. M., Gnegy, M. E., and Wang, K. K. 1999. Endogenous bax translocation in SH-SY5Y human neuroblastoma cells and cerebellar granule neurons undergoing apoptosis. J. Neurochem. 72:1899-1906.
    • (1999) J. Neurochem. , vol.72 , pp. 1899-1906
    • McGinnis, K.M.1    Gnegy, M.E.2    Wang, K.K.3
  • 88
    • 0037193473 scopus 로고    scopus 로고
    • Intrinsic and extrinsic pathway signaling during neuronal apoptosis: Lessons from the analysis of mutant mice
    • Putcha, G. V., Harris, C. A., Moulder, K. L., Easton, R. M., Thompson, C. B., and Johnson, E. M. Jr. 2002. Intrinsic and extrinsic pathway signaling during neuronal apoptosis: Lessons from the analysis of mutant mice. J. Cell. Biol. 157:441-453.
    • (2002) J. Cell. Biol. , vol.157 , pp. 441-453
    • Putcha, G.V.1    Harris, C.A.2    Moulder, K.L.3    Easton, R.M.4    Thompson, C.B.5    Johnson Jr., E.M.6
  • 89
    • 0036847178 scopus 로고    scopus 로고
    • Membrane perturbations induced by the apoptotic Bax protein
    • Epand, R. F., Martinou, J. C., Montessuit, S., and Epand, R. M. 2002. Membrane perturbations induced by the apoptotic Bax protein. Biochem. J. 367:849-855.
    • (2002) Biochem. J. , vol.367 , pp. 849-855
    • Epand, R.F.1    Martinou, J.C.2    Montessuit, S.3    Epand, R.M.4
  • 92
    • 0029116916 scopus 로고
    • The mitochondrial permeability transition
    • Zoratti, M. and Szabo, I. 1995. The mitochondrial permeability transition. Biochim. Biophys. Acta 1241:139-176.
    • (1995) Biochim. Biophys. Acta , vol.1241 , pp. 139-176
    • Zoratti, M.1    Szabo, I.2
  • 93
    • 0017089948 scopus 로고
    • Relationship between configuration, function, and permeability in calcium-treated mitochondria
    • Hunter, D. R., Haworth, R. A., and Southard, J. H. 1976. Relationship between configuration, function, and permeability in calcium-treated mitochondria. J. Biol. Chem. 251:5069-5077.
    • (1976) J. Biol. Chem. , vol.251 , pp. 5069-5077
    • Hunter, D.R.1    Haworth, R.A.2    Southard, J.H.3
  • 94
    • 0032831667 scopus 로고    scopus 로고
    • Calcium induced release of mitochondrial cytochrome c by different mechanisms selective for brain versus liver
    • Andreyev, A. and Fiskum, G. 1999. Calcium induced release of mitochondrial cytochrome c by different mechanisms selective for brain versus liver. Cell. Death Differ. 6:825-832.
    • (1999) Cell. Death Differ. , vol.6 , pp. 825-832
    • Andreyev, A.1    Fiskum, G.2
  • 95
    • 0035292649 scopus 로고    scopus 로고
    • 2+ thresholds determine cytochrome c release of permeability transition pore opening in brain mitochondria
    • 2+ thresholds determine cytochrome c release of permeability transition pore opening in brain mitochondria. FASEB J. 80:565-567.
    • (2001) FASEB J. , vol.80 , pp. 565-567
    • Schild, L.1    Keilhoff, G.2    Augustin, W.3    Reiser, G.4    Striggow, F.5
  • 99
    • 0031772126 scopus 로고    scopus 로고
    • The mitochondrial permeability transition is required for tumor necrosis factor alpha-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 alpha-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
  • 100
    • 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
  • 101
    • 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
  • 102
    • 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
  • 103
    • 0031795088 scopus 로고    scopus 로고
    • Apoptosis, in human monocytic THP.1 cells, results in the release of cytochrome c from mitochondria prior to their ultracondensation, formation of outer membrane discontinuities and reduction in inner membrane potential
    • Zhuang, J., Dinsdale, D., and Cohen, G. M. 1998. Apoptosis, in human monocytic THP.1 cells, results in the release of cytochrome c from mitochondria prior to their ultracondensation, formation of outer membrane discontinuities and reduction in inner membrane potential. Cell. Death Differ. 5:953-962.
    • (1998) Cell. Death Differ. , vol.5 , pp. 953-962
    • Zhuang, J.1    Dinsdale, D.2    Cohen, G.M.3
  • 104
    • 0033178444 scopus 로고    scopus 로고
    • Caspase-dependent and -independent death of camptothecin-treated embryonic cortical neurons
    • Stefanis, L., Park, D. S., Friedman, W. J., and Greene, L. A. Caspase-dependent and -independent death of camptothecin-treated embryonic cortical neurons. J. Neurosci. 19:6235-6247.
    • J. Neurosci. , vol.19 , pp. 6235-6247
    • Stefanis, L.1    Park, D.S.2    Friedman, W.J.3    Greene, L.A.4
  • 105
    • 0033198273 scopus 로고    scopus 로고
    • Mitochondrial depolarization is not required for neuronal apoptosis
    • Krohn, A. J., Wahlbrink, T., and Prehn, J. H. Mitochondrial depolarization is not required for neuronal apoptosis. J. Neurosci. 19:7394-7404.
    • J. Neurosci. , vol.19 , pp. 7394-7404
    • Krohn, A.J.1    Wahlbrink, T.2    Prehn, J.H.3
  • 106
    • 0036313059 scopus 로고    scopus 로고
    • Calcium-induced cytochrome c release from CNS mitochondria is associated with the permeability transition and rupture of the outer membrane
    • Brustovetsky, N., Brustovetsky, T., Jemmerson, R., and Dubinsky, J. M. 2002. Calcium-induced cytochrome c release from CNS mitochondria is associated with the permeability transition and rupture of the outer membrane. J. Neurochem. 80:207-218.
    • (2002) J. Neurochem. , vol.80 , pp. 207-218
    • Brustovetsky, N.1    Brustovetsky, T.2    Jemmerson, R.3    Dubinsky, J.M.4
  • 108
    • 0037164865 scopus 로고    scopus 로고
    • Mitochondrial release of apoptosis-inducing factor occurs downstream of cytochrome c release in response to several proapoptotic stimuli
    • Arnoult, D., Parone, P., Martinou, J. C., Antonsson, B., Estaquier, J., and Ameisen, J. C. 2002. Mitochondrial release of apoptosis-inducing factor occurs downstream of cytochrome c release in response to several proapoptotic stimuli. J. Cell Biol. 159:923-929.
    • (2002) J. Cell Biol. , vol.159 , pp. 923-929
    • Arnoult, D.1    Parone, P.2    Martinou, J.C.3    Antonsson, B.4    Estaquier, J.5    Ameisen, J.C.6
  • 109
    • 0142049202 scopus 로고    scopus 로고
    • Mitochondrial membrane permeabilization and superoxide production during apoptosis: A single-cell analysis
    • Dussmann, H., Kogel, D., Rehm, M., and Prehn, J. H. 2003. Mitochondrial membrane permeabilization and superoxide production during apoptosis: A single-cell analysis. J. Biol. Chem. 278:12645-12649.
    • (2003) J. Biol. Chem. , vol.278 , pp. 12645-12649
    • Dussmann, H.1    Kogel, D.2    Rehm, M.3    Prehn, J.H.4
  • 110
    • 0037416139 scopus 로고    scopus 로고
    • The apoptosome pathway to caspase activation in primary human neutrophils exhibits dramatically reduced requirements for cytochrome C
    • Murphy, B. M., O'Neill, A. J., Adrain, C., Watson, R. W., and Martin, S. J. 2003. The apoptosome pathway to caspase activation in primary human neutrophils exhibits dramatically reduced requirements for cytochrome C. J. Exp. Med. 197:625-632.
    • (2003) J. Exp. Med. , vol.197 , pp. 625-632
    • Murphy, B.M.1    O'Neill, A.J.2    Adrain, C.3    Watson, R.W.4    Martin, S.J.5
  • 111
    • 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
  • 112
    • 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
  • 113
    • 0034658288 scopus 로고    scopus 로고
    • Caspase-mediated degradation of AMPA receptor subunits: A mechanism for preventing excitotoxic necrosis and ensuring apoptosis
    • Glazner, G. W., Chan, S. L., Lu, C., and Mattson, M. P. 2000. Caspase-mediated degradation of AMPA receptor subunits: A mechanism for preventing excitotoxic necrosis and ensuring apoptosis. J. Neurosci. 20:3641-3649.
    • (2000) J. Neurosci. , vol.20 , pp. 3641-3649
    • Glazner, G.W.1    Chan, S.L.2    Lu, C.3    Mattson, M.P.4
  • 114
    • 0032557511 scopus 로고    scopus 로고
    • Energy thresholds in brain mitochondria: Potential involvement in neurodegeneration
    • Davey, G. P., Peuchen, S., and Clark, J. B. 1998. Energy thresholds in brain mitochondria: Potential involvement in neurodegeneration. J. Biol. Chem. 80:12753-12757.
    • (1998) J. Biol. Chem. , vol.80 , pp. 12753-12757
    • Davey, G.P.1    Peuchen, S.2    Clark, J.B.3
  • 115


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.