메뉴 건너뛰기




Volumn 51, Issue 5, 2010, Pages 406-416

Mitochondria as decision-makers in cell death

Author keywords

Apoptosis; Cytochrome c; Mitochondrial membrane; Necrosis; Permeability transition

Indexed keywords

1,2,3,6 TETRAHYDRO 1 METHYL 4 PHENYLPYRIDINE; APOPTOSIS REGULATORY PROTEIN; APOPTOSOME; CARDIOLIPIN; CASPASE; CYANIDE; CYCLOSPORIN A; CYTOCHROME; CYTOCHROME C; DACTINOMYCIN; LIPID; MENADIONE; PROTEIN BAK; PROTEIN BAX; PROTEIN BCL 2; PROTEIN BCL XL; PROTEIN MCL 1; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; SANGLIFEHRIN A; SERINE PROTEINASE OMI; STAUROSPORINE; VOLTAGE DEPENDENT ANION CHANNEL;

EID: 77953488144     PISSN: 08936692     EISSN: 10982280     Source Type: Journal    
DOI: 10.1002/em.20564     Document Type: Review
Times cited : (106)

References (103)
  • 1
    • 4143093663 scopus 로고    scopus 로고
    • Bax interacts with the voltage dependent anion channel and mediates ethanol-induced apoptosis in rat hepatocytes
    • Adachi M, Higuchi H, Miura S, Azuma T, Inokuchi S, Saito H, Kato S, Ishii H, et al. 2004. Bax interacts with the voltage dependent anion channel and mediates ethanol-induced apoptosis in rat hepatocytes. Am J Physiol 287:G695-G705.
    • (2004) Am J Physiol , vol.287
    • Adachi, M.1    Higuchi, H.2    Miura, S.3    Azuma, T.4    Inokuchi, S.5    Saito, H.6    Kato, S.7    Ishii, H.8
  • 3
  • 4
    • 34948863896 scopus 로고    scopus 로고
    • Hydrogen peroxide inhibits caspase-dependent apoptosis by inactivating procaspase-9 in an iron-dependent manner
    • Barbouti A, Amorgianiotis C, Kolettas E, Kanavaros P, Galaris D. 2007. Hydrogen peroxide inhibits caspase-dependent apoptosis by inactivating procaspase-9 in an iron-dependent manner. Free Radic Biol Med 43:1377-1387.
    • (2007) Free Radic Biol Med , vol.43 , pp. 1377-1387
    • Barbouti, A.1    Amorgianiotis, C.2    Kolettas, E.3    Kanavaros, P.4    Galaris, D.5
  • 5
    • 0037147239 scopus 로고    scopus 로고
    • Bax-type apoptotic proteins porate pure lipid bilayers through a mechanism sensitive to intrinsic monolayer curvature
    • Basanez G, Sharpe JC, Brandt TB, Hardwick JM, Zimmerberg J. 2002. Bax-type apoptotic proteins porate pure lipid bilayers through a mechanism sensitive to intrinsic monolayer curvature. J Biol Chem 277:49360-49365.
    • (2002) J Biol Chem , vol.277 , pp. 49360-49365
    • Basanez, G.1    Sharpe, J.C.2    Brandt, T.B.3    Hardwick, J.M.4    Zimmerberg, J.5
  • 6
    • 55549126837 scopus 로고    scopus 로고
    • Phosphate is essential for inhibition of the mitochondrial permeability transition pore by cyclosporin a by cyclophilin D ablation
    • Basso E, Petronilli V, Forte MA, Bernardi P. 2008. Phosphate is essential for inhibition of the mitochondrial permeability transition pore by cyclosporin A, by cyclophilin D ablation. J Biol Chem 283:26307-26311.
    • (2008) J Biol Chem , vol.283 , pp. 26307-26311
    • Basso, E.1    Petronilli, V.2    Forte, Ma.3    Bernardi, P.4
  • 7
    • 36448951977 scopus 로고    scopus 로고
    • Hierarchical recruitment by AMPA but not by staurosporine of pro-apoptotic mitochondrial signaling in cultured cortical neurons: Evidence for caspase-dependent/independent cross-talk
    • Beart PM, Lim ML, Chen B, Diwakarla S, Mercer LD, Cheung NS, Nagley P. 2007. Hierarchical recruitment by AMPA but not by staurosporine of pro-apoptotic mitochondrial signaling in cultured cortical neurons: Evidence for caspase-dependent/independent cross-talk. J Neurochem 103:2408-2427.
    • (2007) J Neurochem , vol.103 , pp. 2408-2427
    • Beart, P.M.1    Lim, M.L.2    Chen, B.3    Diwakarla, S.4    Mercer, L.D.5    Cheung, N.S.6    Nagley, P.7
  • 9
    • 0029998621 scopus 로고    scopus 로고
    • The permeability transition pore as a mitochondrial calcium release channel: A critical appraisal
    • Bernardi P, 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
  • 10
    • 0035816440 scopus 로고    scopus 로고
    • Caspases are reversibly inactivated by hydrogen peroxide
    • Borutaite V, Brown GC. 2001. Caspases are reversibly inactivated by hydrogen peroxide. FEBS Lett 500:114-118.
    • (2001) FEBS Lett , vol.500 , pp. 114-118
    • Borutaite, V.1    Brown, G.C.2
  • 11
    • 0344012010 scopus 로고    scopus 로고
    • Nitric oxide induces apoptosis via hydrogen peroxide, but necrosis via energy and thiol depletion
    • Borutaite V, Brown GC. 2003. Nitric oxide induces apoptosis via hydrogen peroxide, but necrosis via energy and thiol depletion. Free Radic Biol Med 35:1457-1468.
    • (2003) Free Radic Biol Med , vol.35 , pp. 1457-1468
    • Borutaite, V.1    Brown, G.C.2
  • 12
    • 35748954935 scopus 로고    scopus 로고
    • Mitochondrial regulation of caspase activation by cytochrome oxidase and tetramethylphenylenediamine via cytosolic cytochrome c redox state
    • Borutaite V, Brown GC. 2007. Mitochondrial regulation of caspase activation by cytochrome oxidase and tetramethylphenylenediamine via cytosolic cytochrome c redox state. J Biol Chem 282:31124-31130.
    • (2007) J Biol Chem , vol.282 , pp. 31124-31130
    • Borutaite, V.1    Brown, G.C.2
  • 13
    • 0033980876 scopus 로고    scopus 로고
    • Nitric oxide donors, nitrosothiols and mitochondrial respiration inhibitors induce caspase activation by different mechanisms
    • Borutaite V, Morkuniene R, Brown GC. 2000. Nitric oxide donors, nitrosothiols and mitochondrial respiration inhibitors induce caspase activation by different mechanisms. FEBS Lett 467:155-159.
    • (2000) FEBS Lett , vol.467 , pp. 155-159
    • Borutaite, V.1    Morkuniene, R.2    Brown, G.C.3
  • 14
    • 0344951187 scopus 로고    scopus 로고
    • Inhibition of mitochondrial permeability transition prevents mitochondrial dysfunction cytochrome c release and apoptosis induced by heart ischemia
    • Borutaite V, Jekabsone A, Morkuniene R, Brown GC. 2003. Inhibition of mitochondrial permeability transition prevents mitochondrial dysfunction, cytochrome c release and apoptosis induced by heart ischemia. J Mol Cel Cardiol 35:357-366.
    • (2003) J Mol Cel Cardiol , vol.35 , pp. 357-366
    • Borutaite, V.1    Jekabsone, A.2    Morkuniene, R.3    Brown, G.C.4
  • 15
    • 16244367786 scopus 로고    scopus 로고
    • Nitric oxide from inducible nitric oxide synthase sensitizes the inflamed aorta to hypoxic damage via respiratory inhibition
    • Borutaite V, Moncada S, Brown GC. 2005. Nitric oxide from inducible nitric oxide synthase sensitizes the inflamed aorta to hypoxic damage via respiratory inhibition. Shock 23:319-323.
    • (2005) Shock , vol.23 , pp. 319-323
    • Borutaite, V.1    Moncada, S.2    Brown, G.C.3
  • 16
    • 7744224359 scopus 로고    scopus 로고
    • Regulation of mitochondrial membrane permeabilization by BCL-2 family proteins and caspases
    • Breckenridge DG, Xue D. 2004. Regulation of mitochondrial membrane permeabilization by BCL-2 family proteins and caspases. Curr Opin Cell Biol 16:647-652.
    • (2004) Curr Opin Cell Biol , vol.16 , pp. 647-652
    • Breckenridge, D.G.1    Xue, D.2
  • 17
    • 34249825521 scopus 로고    scopus 로고
    • Nitric oxide and mitochondria
    • Brown GC. 2007. Nitric oxide and mitochondria. Front Biosci 12:1024-1033.
    • (2007) Front Biosci , vol.12 , pp. 1024-1033
    • Brown, G.C.1
  • 18
    • 46349098382 scopus 로고    scopus 로고
    • Regulation of apoptosis by the redox state of cytochrome c
    • Brown GC, Borutaite V. 2008. Regulation of apoptosis by the redox state of cytochrome c. Biochim Biophys Acta 1777:877-881.
    • (2008) Biochim Biophys Acta , vol.1777 , pp. 877-881
    • Brown, G.C.1    Borutaite, V.2
  • 19
    • 0033796250 scopus 로고    scopus 로고
    • Mitochondrial free radical generation, oxidative stress and aging
    • Cadenas E, Davies KJ. 2000. Mitochondrial free radical generation, oxidative stress and aging. Free Radic Biol Med 29:222-230.
    • (2000) Free Radic Biol Med , vol.29 , pp. 222-230
    • Cadenas, E.1    Davies, K.J.2
  • 20
    • 33645556312 scopus 로고    scopus 로고
    • Bax translocates to mitochondria of heart cells during simulated ischemia: Involvement of AMP-activated and p38 mitogen-activated protein kinases
    • Capano M, Crompton M. 2006. Bax translocates to mitochondria of heart cells during simulated ischemia: Involvement of AMP-activated and p38 mitogen-activated protein kinases. Biochem J 395:57-64.
    • (2006) Biochem J , vol.395 , pp. 57-64
    • Capano, M.1    Crompton, M.2
  • 22
    • 33846272138 scopus 로고    scopus 로고
    • Role of cardiolipin alterations in mitochondrial dysfunction and disease
    • Chicco AJ, Sparagna GC. 2007. Role of cardiolipin alterations in mitochondrial dysfunction and disease. Am J Physiol Cell Physiol 292:C33-C44.
    • (2007) Am J Physiol Cell Physiol , vol.292
    • Chicco, A.J.1    Sparagna, G.C.2
  • 23
    • 0036716281 scopus 로고    scopus 로고
    • The Bcl2 family: Regulators of the cellular life-or-death switch
    • Cory S, Adams JM. 2002. The Bcl2 family: Regulators of the cellular life-or-death switch. Nat Rev Cancer 2:647-656.
    • (2002) Nat Rev Cancer , vol.2 , pp. 647-656
    • Cory, S.1    Adams, J.M.2
  • 24
    • 0033565557 scopus 로고    scopus 로고
    • The mitochondrial permeability transition pore and its role in cell death
    • Crompton M. 1999. The mitochondrial permeability transition pore and its role in cell death. Biochem J 341:233-249.
    • (1999) Biochem J , vol.341 , pp. 233-249
    • Crompton, M.1
  • 27
    • 16344374718 scopus 로고    scopus 로고
    • Mitochondrial function and myocardial aging. A critical analysis of the role of permeability transition
    • Di Lisa F, Bernardi P. 2005. Mitochondrial function and myocardial aging. A critical analysis of the role of permeability transition. Cardiovasc Res 66:222-232.
    • (2005) Cardiovasc Res , vol.66 , pp. 222-232
    • Di Lisa, F.1    Bernardi, P.2
  • 28
    • 2342564508 scopus 로고    scopus 로고
    • Bcl-2 and calcium: Controversy beneath the surface
    • Distelhorst CW, Shore GC. 2004. Bcl-2 and calcium: Controversy beneath the surface. Oncogene 23:2875-2880.
    • (2004) Oncogene , vol.23 , pp. 2875-2880
    • Distelhorst, C.W.1    Shore, G.C.2
  • 29
    • 58149505960 scopus 로고    scopus 로고
    • Differential insult-dependent recruitment of the intrinsic mitochondrial pathway during neuronal programmed cell death
    • Diwakarla S, Nagley P, Hughes ML, Chen B, Beart PM. 2009. Differential insult-dependent recruitment of the intrinsic mitochondrial pathway during neuronal programmed cell death. Cell Mol Life Sci 66:156-172.
    • (2009) Cell Mol Life Sci , vol.66 , pp. 156-172
    • Diwakarla, S.1    Nagley, P.2    Hughes, M.L.3    Chen, B.4    Beart, P.M.5
  • 30
    • 0036086130 scopus 로고    scopus 로고
    • Free radicals in the physiological control of cell function
    • Droge W. 2002. Free radicals in the physiological control of cell function. Physiol Rev 82:47-95. (Pubitemid 34654215)
    • (2002) Physiological Reviews , vol.82 , Issue.1 , pp. 47-95
    • Droge, W.1
  • 32
    • 0027381281 scopus 로고
    • On the involvement of a cyclosporin a sensitive mitochondrial pore in myocardial reperfusion injury
    • Duchen MR, McGuinness O, Brown LA, Crompton M. 1993. On the involvement of a cyclosporin A sensitive mitochondrial pore in myocardial reperfusion injury. Cardiovasc Res 27:1790-1794. (Pubitemid 23337871)
    • (1993) Cardiovascular Research , vol.27 , Issue.10 , pp. 1790-1794
    • Duchen, M.R.1    McGuinness, O.2    Brown, L.A.3    Crompton, M.4
  • 33
    • 0030915587 scopus 로고    scopus 로고
    • Intracellular ATP levels determine cell death fate by apoptosis or necrosis
    • Eguchi Y, Shimizu S, Tsujimoto Y. 1997. Intracellular ATP levels determine cell death fate by apoptosis or necrosis. Canc Res 57:1835-1840. (Pubitemid 27209706)
    • (1997) Cancer Research , vol.57 , Issue.10 , pp. 1835-1840
    • Eguchi, Y.1    Shimizu, S.2    Tsujimoto, Y.3
  • 34
    • 36348953730 scopus 로고    scopus 로고
    • Nitric oxide and mitochondrial signaling: From physiology to pathophysiology
    • Erusalimsky JD, Moncada S. 2007. Nitric oxide and mitochondrial signaling: From physiology to pathophysiology. Arterioscler Thromb Vasc Biol 27:2524-2531.
    • (2007) Arterioscler Thromb Vasc Biol , vol.27 , pp. 2524-2531
    • Erusalimsky, J.D.1    Moncada, S.2
  • 35
    • 34548809235 scopus 로고    scopus 로고
    • Prothymosin-alpha1 prevents necrosis and apoptosis following stroke
    • Fujita R, Ueda H. 2007. Prothymosin-alpha1 prevents necrosis and apoptosis following stroke. Cell Death Differ 14:1839-1842.
    • (2007) Cell Death Differ , vol.14 , pp. 1839-1842
    • Fujita, R.1    Ueda, H.2
  • 39
    • 0027761474 scopus 로고
    • Protection by cyclosporin a of ischemia/ reperfusion-induced damage in isolated rat hearts
    • Griffiths EJ, Halestrap AP. 1993. Protection by cyclosporin A of ischemia/ reperfusion-induced damage in isolated rat hearts. J Mol Cell Cardiol 25:1461-1469.
    • (1993) J Mol Cell Cardiol , vol.25 , pp. 1461-1469
    • Griffiths, E.J.1    Halestrap, A.P.2
  • 40
    • 0035891057 scopus 로고    scopus 로고
    • Cellular damage signals promote sequential changes at the N-terminus and BH-1 domain of the pro-apoptotic protein Bak
    • Griffiths GJ, Corfe BM, Savory P, Leech S, Esposti MD, Hickman JA, Dive C. 2001. Cellular damage signals promote sequential changes at the N-terminus and BH-1 domain of the pro-apoptotic protein Bak. Oncogene 20:7668-7676.
    • (2001) Oncogene , vol.20 , pp. 7668-7676
    • Griffiths, G.J.1    Corfe, B.M.2    Savory, P.3    Leech, S.4    Esposti, M.D.5    Hickman, J.A.6    Dive, C.7
  • 41
    • 1142273368 scopus 로고    scopus 로고
    • Mitochondrial permeability transition pore opening during myocardial reperfusion - A target for cardioprotection
    • Halestrap AP, Clarke SJ, Javadov SA. 2004. Mitochondrial permeability transition pore opening during myocardial reperfusion - A target for cardioprotection. Cardiovasc Res 61:372-385.
    • (2004) Cardiovasc Res , vol.61 , pp. 372-385
    • Halestrap, A.P.1    Clarke, S.J.2    Javadov, S.A.3
  • 42
    • 67349117275 scopus 로고    scopus 로고
    • What is the mitochondrial permeability transition pore?
    • Halestrap AP. 2009. What is the mitochondrial permeability transition pore? J Mol Cell Cardiol 46:821-831.
    • (2009) J Mol Cell Cardiol , vol.46 , pp. 821-831
    • Halestrap, A.P.1
  • 43
    • 0032504709 scopus 로고    scopus 로고
    • Elucidating the molecular mechanism of the permeability transition pore and its role in reperfusion injury of the heart
    • Halestrap AP, Kerr PM, Javadov S, Woodfield KY. 1998. Elucidating the molecular mechanism of the permeability transition pore and its role in reperfusion injury of the heart. Biochim Biophys Acta 1366:79-94.
    • (1998) Biochim Biophys Acta , vol.1366 , pp. 79-94
    • Halestrap, A.P.1    Kerr, P.M.2    Javadov, S.3    Woodfield, K.Y.4
  • 44
    • 0031973203 scopus 로고    scopus 로고
    • Importance of the redox state of cytochrome c during caspase activation in cytosolic extracts
    • Hampton MB, Zhivotovsky B, Slater AFG, Burgess DH, Orrenius S. 1998. Importance of the redox state of cytochrome c during caspase activation in cytosolic extracts. Biochem J 329:95-99. (Pubitemid 28022295)
    • (1998) Biochemical Journal , vol.329 , Issue.1 , pp. 95-99
    • Hampton, M.B.1    Zhivotovsky, B.2    Slater, A.F.G.3    Burgess, D.H.4    Orrenius, S.5
  • 45
    • 0037165630 scopus 로고    scopus 로고
    • Interaction with substrate sensitises caspase-3 to inactivation by hydrogen peroxide
    • Hampton MB, Stamenkovic I, Winterbourn CC. 2002. Interaction with substrate sensitises caspase-3 to inactivation by hydrogen peroxide. FEBS Lett 517:229-232.
    • (2002) FEBS Lett , vol.517 , pp. 229-232
    • Hampton, M.B.1    Stamenkovic, I.2    Winterbourn, C.C.3
  • 46
    • 0035451525 scopus 로고    scopus 로고
    • Does the redox status of cytochrome C act as a fail-safe mechanism in the regulation of programmed cell death?
    • Hancock JT, Desikan R, Neill SJ. 2001. Does the redox status of cytochrome C act as a fail-safe mechanism in the regulation of programmed cell death? Free Radic Biol Med 31:697-703.
    • (2001) Free Radic Biol Med , vol.31 , pp. 697-703
    • Hancock, J.T.1    Desikan, R.2    Neill, S.J.3
  • 47
    • 0345490687 scopus 로고    scopus 로고
    • Inhibiting mitochondrial permeability transition pore opening at reperfusion protects against ischaemia-reperfusion injury
    • Hausenloy DJ, Duchen MR, Yellon DM. 2003. Inhibiting mitochondrial permeability transition pore opening at reperfusion protects against ischaemia-reperfusion injury. Cardiovasc Res 60:617-625.
    • (2003) Cardiovasc Res , vol.60 , pp. 617-625
    • Hausenloy, D.J.1    Duchen, M.R.2    Yellon, D.M.3
  • 48
    • 0037070178 scopus 로고    scopus 로고
    • Regulated and unregulated mitochondrial permeability transition pores: A new paradigm of pore structure and function?
    • He L, Lemasters JJ. 2002. Regulated and unregulated mitochondrial permeability transition pores: A new paradigm of pore structure and function? FEBS Lett 512:1-7.
    • (2002) FEBS Lett , vol.512 , pp. 1-7
    • He, L.1    Lemasters, J.J.2
  • 50
    • 0027208289 scopus 로고
    • Phospholipid asymmetry of the outer membrane of rat liver mitochondria. Evidence for the presence of cardiolipin on the outside of the outer membrane
    • Hovius R, Thijssen J, van der Linden P, Nicolay K, de Kruijff B. 1993. Phospholipid asymmetry of the outer membrane of rat liver mitochondria. Evidence for the presence of cardiolipin on the outside of the outer membrane. FEBS Lett 330:71-76.
    • (1993) FEBS Lett , vol.330 , pp. 71-76
    • Hovius, R.1    Thijssen, J.2    Van Der Linden, P.3    Nicolay, K.4    De Kruijff, B.5
  • 51
    • 0032562796 scopus 로고    scopus 로고
    • Bax in murine thymus is a soluble monomeric protein that displays differential detergent-induced conformations
    • Hsu YT, Youle RJ. 1998. Bax in murine thymus is a soluble monomeric protein that displays differential detergent-induced conformations. J Biol Chem 273:10777-10783.
    • (1998) J Biol Chem , vol.273 , pp. 10777-10783
    • Hsu, Y.T.1    Youle, R.J.2
  • 52
    • 0034786749 scopus 로고    scopus 로고
    • Dependence of permeability transition pore opening and cytochrome c release from mitochondria on mitochondria energetic status
    • Huang X, Zhai D, Huang Y. 2001. Dependence of permeability transition pore opening and cytochrome c release from mitochondria on mitochondria energetic status. Mol Cell Biochem 224:1-7.
    • (2001) Mol Cell Biochem , vol.224 , pp. 1-7
    • Huang, X.1    Zhai, D.2    Huang, Y.3
  • 53
    • 0018332596 scopus 로고
    • The Ca21-induced membrane transition in mitochondria. I. The protective mechanisms
    • Hunter DR, Haworth RA. 1979a. The Ca21-induced membrane transition in mitochondria. I. The protective mechanisms. Arch Biochem Biophys 195:453-459.
    • (1979) Arch Biochem Biophys , vol.195 , pp. 453-459
    • Hunter, D.R.1    Haworth, R.A.2
  • 54
    • 0018332598 scopus 로고
    • The Ca2+-induced membrane transition in mitochondria. III. Transitional Ca2+ release
    • Hunter DR, Haworth RA. 1979b. The Ca2+-induced membrane transition in mitochondria. III. Transitional Ca2+ release. Arch Biochem Biophys 195:468-477.
    • (1979) Arch Biochem Biophys , vol.195 , pp. 468-477
    • Hunter, D.R.1    Haworth, R.A.2
  • 55
    • 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, Mazat JP. 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
  • 59
    • 20844451123 scopus 로고    scopus 로고
    • AMP-activated protein kionase: Ancient energy gauge provides clues to modern understanding of metabolism
    • Kahn BB, Alquier T, Carling D, Hardie DG. 2005. AMP-activated protein kionase: Ancient energy gauge provides clues to modern understanding of metabolism. Cell Metab 1:15-25.
    • (2005) Cell Metab , vol.1 , pp. 15-25
    • Kahn, B.B.1    Alquier, T.2    Carling, D.3    Hardie, D.G.4
  • 60
    • 46749136790 scopus 로고    scopus 로고
    • Induction of immunological tolerance by apoptotic cells requires caspase-dependent oxidation of high-mobility group box-1 protein
    • Kazama H, Ricci JE, Herndon JM, Hoppe G, Green DR, Ferguson TA. 2008. Induction of immunological tolerance by apoptotic cells requires caspase-dependent oxidation of high-mobility group box-1 protein. Immunity 29:21-32.
    • (2008) Immunity , vol.29 , pp. 21-32
    • Kazama, H.1    Ricci, J.E.2    Herndon, J.M.3    Hoppe, G.4    Green, D.R.5    Ferguson, T.A.6
  • 62
    • 0030741528 scopus 로고    scopus 로고
    • Cytochrome c activation of CPP32-like proteolysis plays a critical role in a Xenopus cell-free apoptosis system
    • Kluck RM, Martin SJ, Hoffman BM, Zhou JS, Green DR, Newmeyer DD. 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
  • 64
    • 33845977959 scopus 로고    scopus 로고
    • Mitochondrial membrane permeabilization in cell death
    • DOI 10.1152/physrev.00013.2006
    • Kroemer G, Galluzzi L, Brenner C. 2007. Mitochondrial membrane permeabilization in cell death. Physiol Rev 87:99-163. (Pubitemid 46209992)
    • (2007) Physiological Reviews , vol.87 , Issue.1 , pp. 99-163
    • Kroemer, G.1    Galluzzi, L.2    Brenner, C.3
  • 66
    • 0033563776 scopus 로고    scopus 로고
    • Inhibition of mitochondrial ATP generation by nitric oxide switches apoptosis to necrosis
    • Leist M, Single B, Naumann H, Fava E, Simon B, Kuhnle S, Nicotera P. 1999a. Inhibition of mitochondrial ATP generation by nitric oxide switches apoptosis to necrosis. Exp Cell Res 249:396-403.
    • (1999) Exp Cell Res , vol.249 , pp. 396-403
    • Leist, M.1    Single, B.2    Naumann, H.3    Fava, E.4    Simon, B.5    Kuhnle, S.6    Nicotera, P.7
  • 67
    • 0033614496 scopus 로고    scopus 로고
    • Nitric oxide inhibits execution of apoptosis at two distinct ATP-dependent steps upstream and downstream of mitochondrial cytochrome c release
    • Leist M, Single B, Naumann H, Fava E, Simon B, Kuhnle S, Nicotera P. 1999b. Nitric oxide inhibits execution of apoptosis at two distinct ATP-dependent steps upstream and downstream of mitochondrial cytochrome c release. Biochem Biophys Res Commun 258:215-221.
    • (1999) Biochem Biophys Res Commun , vol.258 , pp. 215-221
    • Leist, M.1    Single, B.2    Naumann, H.3    Fava, E.4    Simon, B.5    Kuhnle, S.6    Nicotera, P.7
  • 68
    • 0032608336 scopus 로고    scopus 로고
    • Necraptosis and the mitochondrial permeability transition: Shared pathways to necrosis and necraptosis
    • Lemasters JJ. 1999. Necraptosis and the mitochondrial permeability transition: Shared pathways to necrosis and necraptosis. Am J Physiol 276:G1-G6.
    • (1999) Am J Physiol , vol.276
    • Lemasters, J.J.1
  • 69
    • 50949108782 scopus 로고    scopus 로고
    • Cardiolipin as an oxidative target in cardiac mitochondria in the aged rat
    • Lesnefsky EJ, Hoppel CL. 2008. Cardiolipin as an oxidative target in cardiac mitochondria in the aged rat. Biochim Biophys Acta 1777:1020-1027.
    • (2008) Biochim Biophys Acta , vol.1777 , pp. 1020-1027
    • Lesnefsky, E.J.1    Hoppel, C.L.2
  • 70
    • 23944436951 scopus 로고    scopus 로고
    • Enhancement of cyanide-induced mitochondrial dysfunction and cortical cell necrosis by uncoupling protein-2
    • Li L, Prabhakaran K, Mills EM, Borowitz JL, Isom GE. 2005. Enhancement of cyanide-induced mitochondrial dysfunction and cortical cell necrosis by uncoupling protein-2. Toxicol Sci 86:116-124.
    • (2005) Toxicol Sci , vol.86 , pp. 116-124
    • Li, L.1    Prabhakaran, K.2    Mills, E.M.3    Borowitz, J.L.4    Isom, G.E.5
  • 71
    • 14644441669 scopus 로고    scopus 로고
    • Newcomers in the process of mitochondrial permeabilization
    • Lucken-Ardjomande S, Martinou JC. 2005. Newcomers in the process of mitochondrial permeabilization. J Cell Sci 118:473-483.
    • (2005) J Cell Sci , vol.118 , pp. 473-483
    • Lucken-Ardjomande, S.1    Martinou, J.C.2
  • 73
    • 0033495895 scopus 로고    scopus 로고
    • Blockade of the mitochondrial permeability transition pore diminishes infarct size in the rat after transient middle cerebral artery occlusion
    • Matsumoto S, Friberg H, Ferrand-Drake M, Wieloch T. 1999. Blockade of the mitochondrial permeability transition pore diminishes infarct size in the rat after transient middle cerebral artery occlusion. J Cereb Blood Flow Metab 19:736-741. (Pubitemid 30159798)
    • (1999) Journal of Cerebral Blood Flow and Metabolism , vol.19 , Issue.7 , pp. 736-741
    • Matsumoto, S.1    Friberg, H.2    Ferrand-Drake, M.3    Wieloch, T.4
  • 74
    • 57049143140 scopus 로고    scopus 로고
    • Mitochondria in neuroplasticity and neurological disorders
    • Mattson MP, Gleichmann M, Cheng A. 2008. Mitochondria in neuroplasticity and neurological disorders. Neuron 60:748-766.
    • (2008) Neuron , vol.60 , pp. 748-766
    • Mattson, M.P.1    Gleichmann, M.2    Cheng, A.3
  • 75
    • 14744274465 scopus 로고    scopus 로고
    • Regulation of Fas (CD95)-induced apoptotic and necrotic cell death by reactive oxygen species in macrophages
    • Medan D, Wang L, Toledo D, Lu B, Stehlik C, Jiang BH, Shi X, Rojanasakul Y. 2005. Regulation of Fas (CD95)-induced apoptotic and necrotic cell death by reactive oxygen species in macrophages. J Cell Physiol 203:78-84.
    • (2005) J Cell Physiol , vol.203 , pp. 78-84
    • Medan, D.1    Wang, L.2    Toledo, D.3    Lu, B.4    Stehlik, C.5    Jiang, B.H.6    Shi, X.7    Rojanasakul, Y.8
  • 76
    • 32444443812 scopus 로고    scopus 로고
    • Age-dependent cell death and the role of ATP in hydrogen peroxide-induced apoptosis and necrosis
    • Miyoshi N, Oubrahim H, Chock PB, Stadtman ER. 2006. Age-dependent cell death and the role of ATP in hydrogen peroxide-induced apoptosis and necrosis. Proc Natl Acad Sci USA 103:1727-1731.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 1727-1731
    • Miyoshi, N.1    Oubrahim, H.2    Chock, P.B.3    Stadtman, E.R.4
  • 77
    • 58249093939 scopus 로고    scopus 로고
    • How mitochondria produce reactive oxygen species?
    • Murphy MP. 2009. How mitochondria produce reactive oxygen species? Biochem J 417:105-111.
    • (2009) Biochem J , vol.417 , pp. 105-111
    • Murphy, M.P.1
  • 79
    • 0035844867 scopus 로고    scopus 로고
    • Bax and Bak coalesce into novel mitochondria-associated clusters during apoptosis
    • Nechushtan A, Smith CL, Lamensdorf I, Yoon SH, Youle RJ. 2001. Bax and Bak coalesce into novel mitochondria-associated clusters during apoptosis. J Cell Biol 153:1265-1276.
    • (2001) J Cell Biol , vol.153 , pp. 1265-1276
    • Nechushtan, A.1    Smith, C.L.2    Lamensdorf, I.3    Yoon, S.H.4    Youle, R.J.5
  • 80
    • 67650741483 scopus 로고    scopus 로고
    • Mitochondrial targeting tBid/Bax: A role for the TOM complex
    • Ott M, Norberg E, Zhivotovsky B, Orrenius S. 2009. Mitochondrial targeting tBid/Bax: A role for the TOM complex. Cell Death Differ 16:1075-1082.
    • (2009) Cell Death Differ , vol.16 , pp. 1075-1082
    • Ott, M.1    Norberg, E.2    Zhivotovsky, B.3    Orrenius, S.4
  • 82
    • 54949110895 scopus 로고    scopus 로고
    • Calcium and apoptosis: ER-mitochondrial Ca21 transfer in the control of apoptosis
    • Pinton P, Giorgi C, Siviero R, Zecchini E, Rizzuto R. 2009. Calcium and apoptosis: ER-mitochondrial Ca21 transfer in the control of apoptosis. Oncogene 27:6407-6418.
    • (2009) Oncogene , vol.27 , pp. 6407-6418
    • Pinton, P.1    Giorgi, C.2    Siviero, R.3    Zecchini, E.4    Rizzuto, R.5
  • 83
    • 14944381765 scopus 로고    scopus 로고
    • Cardiolipin and phosphatidylglycerol are not required for the in vivo action of Bcl-2 family proteins
    • Polcic P, Su X, Fowlkes J, Blachly-Dyson E, Dowhan W, Forte M. 2005. Cardiolipin and phosphatidylglycerol are not required for the in vivo action of Bcl-2 family proteins. Cell Death Differ 12:310-312.
    • (2005) Cell Death Differ , vol.12 , pp. 310-312
    • Polcic, P.1    Su, X.2    Fowlkes, J.3    Blachly-Dyson, E.4    Dowhan, W.5    Forte, M.6
  • 84
    • 0035851110 scopus 로고    scopus 로고
    • BH3 Death Domain Peptide Induces Cell Type-selective Mitochondrial Outer Membrane Permeability
    • Polster BM, Kinnally KW, Fiskum G. 2001. BH3 death domain peptide induces cell type-selective mitochondrial outer membrane permeability. J Biol Chem 276:37887-37894. (Pubitemid 37384036)
    • (2001) Journal of Biological Chemistry , vol.276 , Issue.41 , pp. 37887-37894
    • Polster, B.M.1    Kinnally, K.W.2    Fiskum, G.3
  • 85
    • 14844328621 scopus 로고    scopus 로고
    • Calpain I inducescleavage and release of apoptosis-inducing factor from isolated mitochondria
    • Polster BM, Basanez G, Etxebarria A, Hardwick JM, Nichols DG. 2005. Calpain I inducescleavage and release of apoptosis-inducing factor from isolated mitochondria. J Biol Chem 280:6447-6454.
    • (2005) J Biol Chem , vol.280 , pp. 6447-6454
    • Polster, B.M.1    Basanez, G.2    Etxebarria, A.3    Hardwick, J.M.4    Nichols, D.G.5
  • 86
    • 49249118742 scopus 로고    scopus 로고
    • Neurotoxic effect of oligomeric and fibrilar species of amyloid-beta peptide 1-42: Involvement of endoplasmic reticulum calcium release in oligomer-induced cell death
    • Resende R, Ferreiro E, Pereira C, Resende De Oliveira C. 2008. Neurotoxic effect of oligomeric and fibrilar species of amyloid-beta peptide 1-42: Involvement of endoplasmic reticulum calcium release in oligomer-induced cell death. Neuroscience 155:725-737.
    • (2008) Neuroscience , vol.155 , pp. 725-737
    • Resende, R.1    Ferreiro, E.2    Pereira, C.3    De Resende Oliveira, C.4
  • 89
    • 0037427412 scopus 로고    scopus 로고
    • Mechanisms of cytochrome c release by proapoptotic BCL-2 family members
    • Scorrano L, Korsmeyer SJ. 2003. Mechanisms of cytochrome c release by proapoptotic BCL-2 family members. Biochem Biophys Res Commun 304:437-444.
    • (2003) Biochem Biophys Res Commun , vol.304 , pp. 437-444
    • Scorrano, L.1    Korsmeyer, S.J.2
  • 90
    • 26444453262 scopus 로고    scopus 로고
    • Mitochondrial ceramide and the induction of apoptosis
    • Siskind LJ. 2005. Mitochondrial ceramide and the induction of apoptosis. J Bioenerg Biomembr 37:143-153.
    • (2005) J Bioenerg Biomembr , vol.37 , pp. 143-153
    • Siskind, L.J.1
  • 91
    • 33646389796 scopus 로고    scopus 로고
    • Bioenergetic aspects of apoptosis, necrosis and mitoptosis
    • Skulachev VP. 2006. Bioenergetic aspects of apoptosis, necrosis and mitoptosis. Apoptosis 11:473-485.
    • (2006) Apoptosis , vol.11 , pp. 473-485
    • Skulachev, V.P.1
  • 93
    • 29144432723 scopus 로고    scopus 로고
    • Suppression of the proapoptotic unction of cytochrome c by singlet oxygen via a heme redox state-independent mechanism
    • Suto D, Sato K, Ohba Y, Yoshimura T, Fuji J. 2005. Suppression of the proapoptotic unction of cytochrome c by singlet oxygen via a heme redox state-independent mechanism. Biochem J 392:399-406.
    • (2005) Biochem J , vol.392 , pp. 399-406
    • Suto, D.1    Sato, K.2    Ohba, Y.3    Yoshimura, T.4    Fuji, J.5
  • 94
    • 67849119416 scopus 로고    scopus 로고
    • Prothymosin a and cell death mode switch, a novel target for the prevention of cerebral ischemia-induced damage
    • Ueda H. 2009. Prothymosin a and cell death mode switch, a novel target for the prevention of cerebral ischemia-induced damage. Pharmacol Therapeut 123:323-333.
    • (2009) Pharmacol Therapeut , vol.123 , pp. 323-333
    • Ueda, H.1
  • 95
    • 14944355121 scopus 로고    scopus 로고
    • Cell death mode switch from necrosis to apoptosis in brain
    • Ueda H, Fujita R. 2004. Cell death mode switch from necrosis to apoptosis in brain. Biol Pharm Bull 27:950-955.
    • (2004) Biol Pharm Bull , vol.27 , pp. 950-955
    • Ueda, H.1    Fujita, R.2
  • 96
    • 44449175599 scopus 로고    scopus 로고
    • Analysis of endogenous Bax complexes during apoptosis using blue native PAGE: Implications for Bax activation and oligomerization
    • Valentijn AJ, Upton JP, Gilmore AP. 2008. Analysis of endogenous Bax complexes during apoptosis using blue native PAGE: Implications for Bax activation and oligomerization. Biochem J 412:347-357.
    • (2008) Biochem J , vol.412 , pp. 347-357
    • Valentijn, A.J.1    Upton, J.P.2    Gilmore, A.P.3
  • 98
    • 57049132739 scopus 로고    scopus 로고
    • Glucose metabolism inhibits apoptosis in neurons and cancer cells by redox inactivation of cytochrome c
    • Vaughn AE, Deshmukh M. 2008. Glucose metabolism inhibits apoptosis in neurons and cancer cells by redox inactivation of cytochrome c. Nat Cell Biol 10:1477-1483.
    • (2008) Nat Cell Biol , vol.10 , pp. 1477-1483
    • Vaughn, A.E.1    Deshmukh, M.2
  • 100
    • 22244464818 scopus 로고    scopus 로고
    • Proapoptotic Bak is sequestered by Mcl-1 and Bcl-xL, but not Bcl-2, until displaced by BH3-only proteins
    • Willis SN, Chen L, Dewson G, Wei A, Naik E, Fletcher JI, Adams JM, Huang DCS. 2005. Proapoptotic Bak is sequestered by Mcl-1 and Bcl-xL, but not Bcl-2, until displaced by BH3-only proteins. Genes Dev 19:1294-1305.
    • (2005) Genes Dev , vol.19 , pp. 1294-1305
    • Willis, S.N.1    Chen, L.2    Dewson, G.3    Wei, A.4    Naik, E.5    Fletcher, J.I.6    Adams, J.M.7    Huang, D.C.S.8
  • 102
    • 27644597606 scopus 로고    scopus 로고
    • Mitochondrial permeability transition in apoptosis and necrosis
    • Zamzami N, Larochette N, Kroemer G. 2005. Mitochondrial permeability transition in apoptosis and necrosis. Cell Death Differ 12:1478-1480.
    • (2005) Cell Death Differ , vol.12 , pp. 1478-1480
    • Zamzami, N.1    Larochette, N.2    Kroemer, G.3
  • 103
    • 0029116916 scopus 로고
    • The mitochondrial permeability transition
    • Zoratti M, 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.