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Volumn 4, Issue NOV, 2014, Pages

The mitochondrial permeability transition pore and cancer: Molecular mechanisms involved in cell death

Author keywords

Apoptosis; ATP synthase; Cancer; Necrosis; Permeability transition pore; PTP; ROS; Tumors

Indexed keywords

MITOCHONDRIAL PERMEABILITY TRANSITION PORE;

EID: 84915815164     PISSN: None     EISSN: 2234943X     Source Type: Journal    
DOI: 10.3389/fonc.2014.00302     Document Type: Review
Times cited : (166)

References (148)
  • 1
    • 0018332596 scopus 로고
    • The Ca2+-induced membrane transition in mitochondria. I. The protective mechanisms
    • Hunter DR, Haworth RA. The Ca2+-induced membrane transition in mitochondria. I. The protective mechanisms. Arch Biochem Biophys (1979) 195:453-9. doi: 10.1016/0003-9861(79)90371-0
    • (1979) Arch Biochem Biophys , vol.195 , pp. 453-459
    • Hunter, D.R.1    Haworth, R.A.2
  • 2
    • 0025195033 scopus 로고
    • A heart mitochondrial Ca2(+)-dependent pore of possible relevance to re-perfusion-induced injury. Evidence that ADP facilitates pore interconversion between the closed and open states.
    • Crompton M, Costi A. A heart mitochondrial Ca2(+)-dependent pore of possible relevance to re-perfusion-induced injury. Evidence that ADP facilitates pore interconversion between the closed and open states. Biochem J (1990) 266:33-9.
    • (1990) Biochem J , vol.266 , pp. 33-39
    • Crompton, M.1    Costi, A.2
  • 3
    • 0027489228 scopus 로고
    • Oxidative damage to mitochondria is mediated by the Ca(2+)-dependent inner-membrane permeability transition.
    • Takeyama N, Matsuo N, Tanaka T. Oxidative damage to mitochondria is mediated by the Ca(2+)-dependent inner-membrane permeability transition. Biochem J (1993) 294(Pt 3):719-25.
    • (1993) Biochem J , vol.294 , pp. 719-725
    • Takeyama, N.1    Matsuo, N.2    Tanaka, T.3
  • 4
    • 34250729007 scopus 로고    scopus 로고
    • Cellular physiology biochemistry and biochemistry mitochondrial permeability transition pore opening as an endpoint to initiate cell death and as a putative target for cardioprotection
    • Javadov S, Karmazyn M. Cellular physiology biochemistry and biochemistry mitochondrial permeability transition pore opening as an endpoint to initiate cell death and as a putative target for cardioprotection. Cell Physiol Biochem (2007) 1:1-22. doi:10.1159/000103747
    • (2007) Cell Physiol Biochem , vol.1 , pp. 1-22
    • Javadov, S.1    Karmazyn, M.2
  • 5
    • 84857098116 scopus 로고    scopus 로고
    • Cyclosporin A and cardioprotection: from investigative tool to therapeutic agent
    • Hausenloy DJ, Boston-Griffiths EA, Yellon DM. Cyclosporin A and cardioprotection: from investigative tool to therapeutic agent. Br J Pharmacol (2012) 165:1235-45. doi:10.1111/j.1476-5381.2011.01700.x
    • (2012) Br J Pharmacol , vol.165 , pp. 1235-1245
    • Hausenloy, D.J.1    Boston-Griffiths, E.A.2    Yellon, D.M.3
  • 6
    • 83355166870 scopus 로고    scopus 로고
    • Cyclosporine-A as a neuroprotective agent against stroke: its translation from laboratory research to clinical application
    • Osman MM, Lulic D, Glover L, Stahl CE, Lau T, van Loveren H, et al. Cyclosporine-A as a neuroprotective agent against stroke: its translation from laboratory research to clinical application. Neuropeptides (2011) 45:359-68. doi:10.1016/j.npep.2011.04.002
    • (2011) Neuropeptides , vol.45 , pp. 359-368
    • Osman, M.M.1    Lulic, D.2    Glover, L.3    Stahl, C.E.4    Lau, T.5    van Loveren, H.6
  • 7
    • 21244446551 scopus 로고    scopus 로고
    • Properties of the permeability transition pore in mitochondria devoid of cyclophilin D
    • Basso E, Fante L, Fowlkes J, Petronilli V, Forte MA, Bernardi P. Properties of the permeability transition pore in mitochondria devoid of cyclophilin D. J Biol Chem (2005) 280:18558-61. doi:10.1074/jbc. C500089200
    • (2005) J Biol Chem , vol.280 , pp. 18558-18561
    • Basso, E.1    Fante, L.2    Fowlkes, J.3    Petronilli, V.4    Forte, M.A.5    Bernardi, P.6
  • 8
    • 24744460273 scopus 로고    scopus 로고
    • Cyclophilin D is a component of mitochondrial permeability transition and mediates neuronal cell death after focal cerebral ischemia
    • Schinzel AC, Takeuchi O, Huang Z, Fisher JK, Zhou Z, Rubens J, et al. Cyclophilin D is a component of mitochondrial permeability transition and mediates neuronal cell death after focal cerebral ischemia. Proc Natl Acad Sci U S A (2005) 102:12005-10. doi:10.1073/pnas.0505294102
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 12005-12010
    • Schinzel, A.C.1    Takeuchi, O.2    Huang, Z.3    Fisher, J.K.4    Zhou, Z.5    Rubens, J.6
  • 9
    • 0031587781 scopus 로고    scopus 로고
    • Release of cytochrome c from liver mitochondria during permeability transition
    • Kantrow SP, Piantadosi CA. Release of cytochrome c from liver mitochondria during permeability transition. Biochem Biophys Res Commun (1997) 232:669-71. doi:10.1006/bbrc.1997.6353
    • (1997) Biochem Biophys Res Commun , vol.232 , pp. 669-671
    • Kantrow, S.P.1    Piantadosi, C.A.2
  • 10
    • 0033521741 scopus 로고    scopus 로고
    • Molecular characterization of mitochondrial apoptosis-inducing factor
    • Susin SA, Lorenzo HK, Zamzami N, Marzo I, Snow BE, Brothers GM, et al. Molecular characterization of mitochondrial apoptosis-inducing factor. Nature (1999) 397:441-6. doi:10.1038/17135
    • (1999) Nature , vol.397 , pp. 441-446
    • Susin, S.A.1    Lorenzo, H.K.2    Zamzami, N.3    Marzo, I.4    Snow, B.E.5    Brothers, G.M.6
  • 11
    • 18044380272 scopus 로고    scopus 로고
    • Smac/DIABLO and cytochrome c are released from mitochondria through a similar mechanism during UV-induced apoptosis
    • Zhou LL, Zhou LY, Luo KQ, Chang DC. Smac/DIABLO and cytochrome c are released from mitochondria through a similar mechanism during UV-induced apoptosis. Apoptosis (2005) 10:289-99. doi:10.1007/s10495-005-0803-9
    • (2005) Apoptosis , vol.10 , pp. 289-299
    • Zhou, L.L.1    Zhou, L.Y.2    Luo, K.Q.3    Chang, D.C.4
  • 12
    • 0037440692 scopus 로고    scopus 로고
    • A Ca2+-induced mitochondrial permeability transition causes complete release of rat liver endonuclease G activity from its exclusive location within the mitochondrial intermembrane space. Identification of a novel endo-exonuclease activity residing within.
    • Davies AM, Hershman S, Stabley GJ, Hoek JB, Peterson J, Cahill A. A Ca2+-induced mitochondrial permeability transition causes complete release of rat liver endonuclease G activity from its exclusive location within the mitochondrial intermembrane space. Identification of a novel endo-exonuclease activity residing within. Nucleic Acids Res (2003) 31:1364-73. doi:10.1093/nar/gkg205
    • (2003) Nucleic Acids Res , vol.31 , pp. 1364-1373
    • Davies, A.M.1    Hershman, S.2    Stabley, G.J.3    Hoek, J.B.4    Peterson, J.5    Cahill, A.6
  • 13
    • 18144453327 scopus 로고    scopus 로고
    • Establishment of a cell-free system of neuronal apoptosis: comparison of premitochondrial, mitochondrial, and postmitochondrial phases
    • Ellerby HM, Martin SJ, Ellerby LM, Naiem SS, Rabizadeh S, Salvesen GS, et al. Establishment of a cell-free system of neuronal apoptosis: comparison of premitochondrial, mitochondrial, and postmitochondrial phases. J Neurosci (1997) 17:6165-78.
    • (1997) J Neurosci , vol.17 , pp. 6165-6178
    • Ellerby, H.M.1    Martin, S.J.2    Ellerby, L.M.3    Naiem, S.S.4    Rabizadeh, S.5    Salvesen, G.S.6
  • 14
    • 9544246860 scopus 로고    scopus 로고
    • Mitochondrial permeability transition is a central coordinating event of apoptosis
    • Marchetti P, Castedo M, Susin SA, Zamzami N, Hirsch T, Macho A, et al. Mitochondrial permeability transition is a central coordinating event of apoptosis. J Exp Med (1996) 184:1155-60. doi:10.1084/jem.184.3.1155
    • (1996) J Exp Med , vol.184 , pp. 1155-1160
    • Marchetti, P.1    Castedo, M.2    Susin, S.A.3    Zamzami, N.4    Hirsch, T.5    Macho, A.6
  • 15
    • 0032422488 scopus 로고    scopus 로고
    • Bax interacts with the permeability transition pore to induce permeability transition and cytochrome c release in isolated mitochondria
    • Narita M, Shimizu S, Ito T, Chittenden T, Lutz RJ, Matsuda H, et al. Bax interacts with the permeability transition pore to induce permeability transition and cytochrome c release in isolated mitochondria. Proc Natl Acad Sci (1998) 95:14681-6. doi:10.1073/pnas.95.25.14681
    • (1998) Proc Natl Acad Sci , vol.95 , pp. 14681-14686
    • Narita, M.1    Shimizu, S.2    Ito, T.3    Chittenden, T.4    Lutz, R.J.5    Matsuda, H.6
  • 16
    • 0032566649 scopus 로고    scopus 로고
    • Bax and adenine nucleotide translocator cooperate in the mitochondrial control of apoptosis
    • Marzo I, Brenner C, Zamzami N, Jürgensmeier JM, Susin SA, Vieira HL, et al. Bax and adenine nucleotide translocator cooperate in the mitochondrial control of apoptosis. Science (1998) 281:2027-31. doi:10.1126/science.281.5385.2027
    • (1998) Science , vol.281 , pp. 2027-2031
    • Marzo, I.1    Brenner, C.2    Zamzami, N.3    Jürgensmeier, J.M.4    Susin, S.A.5    Vieira, H.L.6
  • 18
    • 0032563604 scopus 로고    scopus 로고
    • Transient mitochondrial depolarizations reflect focal sarcoplasmic reticular calcium release in single rat cardiomyocytes
    • Duchen MR, Leyssens A, Crompton M. Transient mitochondrial depolarizations reflect focal sarcoplasmic reticular calcium release in single rat cardiomyocytes. J Cell Biol (1998) 142:975-88. doi:10.1083/jcb.142.4.975
    • (1998) J Cell Biol , vol.142 , pp. 975-988
    • Duchen, M.R.1    Leyssens, A.2    Crompton, M.3
  • 19
    • 24944518486 scopus 로고    scopus 로고
    • Biphasic cytochrome c release after transient global ischemia and its inhibition by hypothermia
    • Zhao H, Yenari MA, Cheng D, Sapolsky RM, Steinberg GK. Biphasic cytochrome c release after transient global ischemia and its inhibition by hypothermia. J Cereb Blood Flow Metab (2005) 25:1119-29. doi:10.1038/sj.jcbfm.9600111
    • (2005) J Cereb Blood Flow Metab , vol.25 , pp. 1119-1129
    • Zhao, H.1    Yenari, M.A.2    Cheng, D.3    Sapolsky, R.M.4    Steinberg, G.K.5
  • 21
    • 34948834748 scopus 로고    scopus 로고
    • Ca(2+)-dependent glycolysis activation mediates apoptotic ATP elevation in HeLa cells
    • Zamaraeva MV, Sabirov RZ, Manabe K, Okada Y. Ca(2+)-dependent glycolysis activation mediates apoptotic ATP elevation in HeLa cells. Biochem Biophys Res Commun (2007) 363:687-93. doi:10.1016/j.bbrc.2007.09.019
    • (2007) Biochem Biophys Res Commun , vol.363 , pp. 687-693
    • Zamaraeva, M.V.1    Sabirov, R.Z.2    Manabe, K.3    Okada, Y.4
  • 22
    • 15844375853 scopus 로고    scopus 로고
    • Loss of cyclophilin D reveals a critical role for mitochondrial permeability transition in cell death
    • Baines CP, Kaiser RA, Purcell NH, Blair NS, Osinska H, Hambleton MA, et al. Loss of cyclophilin D reveals a critical role for mitochondrial permeability transition in cell death. Nature (2005) 434:658-62. doi:10.1038/nature03434
    • (2005) Nature , vol.434 , pp. 658-662
    • Baines, C.P.1    Kaiser, R.A.2    Purcell, N.H.3    Blair, N.S.4    Osinska, H.5    Hambleton, M.A.6
  • 23
    • 79551576278 scopus 로고    scopus 로고
    • Ghrelin protects H9c2 cells from hydrogen peroxide-induced apoptosis through NF-κB and mitochondria-mediated signaling
    • Zhang Q, Huang W-D, Lv X-Y, Yang Y-M. Ghrelin protects H9c2 cells from hydrogen peroxide-induced apoptosis through NF-κB and mitochondria-mediated signaling. Eur J Pharmacol (2011) 654:142-9. doi:10.1016/j.ejphar.2010.12.011
    • (2011) Eur J Pharmacol , vol.654 , pp. 142-149
    • Zhang, Q.1    Huang, W-D.2    Lv, X-Y.3    Yang, Y-M.4
  • 24
    • 12144279912 scopus 로고    scopus 로고
    • Hydrogen peroxide as a signal controlling plant programmed cell death
    • Gechev TS, Hille J. Hydrogen peroxide as a signal controlling plant programmed cell death. J Cell Biol (2005) 168:17-20. doi:10.1083/jcb.200409170
    • (2005) J Cell Biol , vol.168 , pp. 17-20
    • Gechev, T.S.1    Hille, J.2
  • 25
    • 84907562802 scopus 로고    scopus 로고
    • Grape seed proanthocyanidins inhibit H2O2-induced osteoblastic MC3T3-E1 cell apoptosis via ameliorating H2O2-induced mitochondrial dysfunction
    • Zhang Z, Zheng L, Zhao Z, Shi J, Wang X, Huang J. Grape seed proanthocyanidins inhibit H2O2-induced osteoblastic MC3T3-E1 cell apoptosis via ameliorating H2O2-induced mitochondrial dysfunction. J Toxicol Sci (2014) 39:803-13. doi:10.2131/jts.39.803
    • (2014) J Toxicol Sci , vol.39 , pp. 803-813
    • Zhang, Z.1    Zheng, L.2    Zhao, Z.3    Shi, J.4    Wang, X.5    Huang, J.6
  • 26
    • 84866515571 scopus 로고    scopus 로고
    • MicroRNA-145 protects cardiomyocytes against hydrogen peroxide (H2O2)-induced apoptosis through targeting the mitochondria apoptotic pathway
    • Li R, Yan G, Li Q, Sun H, Hu Y, Sun J, et al. MicroRNA-145 protects cardiomyocytes against hydrogen peroxide (H2O2)-induced apoptosis through targeting the mitochondria apoptotic pathway. PLoS One (2012) 7:e44907. doi:10.1371/journal.pone.0044907
    • (2012) PLoS One , vol.7
    • Li, R.1    Yan, G.2    Li, Q.3    Sun, H.4    Hu, Y.5    Sun, J.6
  • 27
    • 84896732956 scopus 로고    scopus 로고
    • The endoplasmic reticulum-mitochondria connection: one touch, multiple functions
    • Marchi S, Patergnani S, Pinton P. The endoplasmic reticulum-mitochondria connection: one touch, multiple functions. Biochim Biophys Acta (2014) 1837:461-9. doi:10.1016/j.bbabio.2013.10.015
    • (2014) Biochim Biophys Acta , vol.1837 , pp. 461-469
    • Marchi, S.1    Patergnani, S.2    Pinton, P.3
  • 29
    • 42049101823 scopus 로고    scopus 로고
    • Ca2+ signaling, mitochondria and cell death
    • Giorgi C, Romagnoli A, Pinton P, Rizzuto R. Ca2+ signaling, mitochondria and cell death. Curr Mol Med (2008) 8:119-30. doi:10.2174/156652408783769571
    • (2008) Curr Mol Med , vol.8 , pp. 119-130
    • Giorgi, C.1    Romagnoli, A.2    Pinton, P.3    Rizzuto, R.4
  • 31
    • 84872117185 scopus 로고    scopus 로고
    • Downregulation of the mitochondrial calcium uniporter by cancer-related miR-25
    • Marchi S, Lupini L, Patergnani S, Rimessi A, Missiroli S, Bonora M, et al. Downregulation of the mitochondrial calcium uniporter by cancer-related miR-25. Curr Biol (2013) 23:58-63. doi:10.1016/j.cub.2012.11.026
    • (2013) Curr Biol , vol.23 , pp. 58-63
    • Marchi, S.1    Lupini, L.2    Patergnani, S.3    Rimessi, A.4    Missiroli, S.5    Bonora, M.6
  • 32
    • 84875233751 scopus 로고    scopus 로고
    • VDAC1: from structure to cancer therapy
    • Shoshan-Barmatz V, Mizrachi D. VDAC1: from structure to cancer therapy. Front Oncol (2012) 2:164. doi:10.3389/fonc.2012.00164
    • (2012) Front Oncol , vol.2 , pp. 164
    • Shoshan-Barmatz, V.1    Mizrachi, D.2
  • 33
    • 33845977959 scopus 로고    scopus 로고
    • Mitochondrial membrane permeabilization in cell death
    • Kroemer G, Galluzzi L, Brenner C. Mitochondrial membrane permeabilization in cell death. Physiol Rev (2007) 87:99-163. doi:10.1152/physrev.00013.2006
    • (2007) Physiol Rev , vol.87 , pp. 99-163
    • Kroemer, G.1    Galluzzi, L.2    Brenner, C.3
  • 34
    • 84883411678 scopus 로고    scopus 로고
    • Bax and Bak function as the outer membrane component of the mitochondrial permeability pore in regulating necrotic cell death in mice
    • Karch J, Kwong JQ, Burr AR, Sargent MA, Elrod JW, Peixoto PM, et al. Bax and Bak function as the outer membrane component of the mitochondrial permeability pore in regulating necrotic cell death in mice. Elife (2013) 2:e00772. doi:10.7554/eLife.00772
    • (2013) Elife , vol.2
    • Karch, J.1    Kwong, J.Q.2    Burr, A.R.3    Sargent, M.A.4    Elrod, J.W.5    Peixoto, P.M.6
  • 35
    • 0037418843 scopus 로고    scopus 로고
    • BAX and BAK regulation of endoplasmic reticulum Ca2+: a control point for apoptosis
    • Scorrano L, Oakes SA, Opferman JT, Cheng EH, Sorcinelli MD, Pozzan T, et al. BAX and BAK regulation of endoplasmic reticulum Ca2+: a control point for apoptosis. Science (2003) 300:135-9. doi:10.1126/science.1081208
    • (2003) Science , vol.300 , pp. 135-139
    • Scorrano, L.1    Oakes, S.A.2    Opferman, J.T.3    Cheng, E.H.4    Sorcinelli, M.D.5    Pozzan, T.6
  • 36
    • 1842333844 scopus 로고    scopus 로고
    • The reversible antiport-uniport conversion of the phosphate carrier from yeast mitochondria depends on the presence of a single cysteine
    • Schroers A, Krämer R, Wohlrab H. The reversible antiport-uniport conversion of the phosphate carrier from yeast mitochondria depends on the presence of a single cysteine. J Biol Chem (1997) 272:10558-64. doi:10.1074/jbc.272.16.10558
    • (1997) J Biol Chem , vol.272 , pp. 10558-10564
    • Schroers, A.1    Krämer, R.2    Wohlrab, H.3
  • 37
    • 55549091082 scopus 로고    scopus 로고
    • The mitochondrial phosphate carrier interacts with cyclophilin D and may play a key role in the permeability transition
    • Leung AWC, Varanyuwatana P, Halestrap AP. The mitochondrial phosphate carrier interacts with cyclophilin D and may play a key role in the permeability transition. J Biol Chem (2008) 283:26312-23. doi:10.1074/jbc. M805235200
    • (2008) J Biol Chem , vol.283 , pp. 26312-26323
    • Leung, A.W.C.1    Varanyuwatana, P.2    Halestrap, A.P.3
  • 38
    • 37849006735 scopus 로고    scopus 로고
    • A high-throughput screening for mammalian cell death effectors identifies the mitochondrial phosphate carrier as a regulator of cytochrome c release
    • Alcalá S, Klee M, Fernández J, Fleischer A, Pimentel-Muiños FX. A high-throughput screening for mammalian cell death effectors identifies the mitochondrial phosphate carrier as a regulator of cytochrome c release. Oncogene (2008) 27:44-54. doi:10.1038/sj.onc.1210600
    • (2008) Oncogene , vol.27 , pp. 44-54
    • Alcalá, S.1    Klee, M.2    Fernández, J.3    Fleischer, A.4    Pimentel-Muiños, F.X.5
  • 39
    • 84856526180 scopus 로고    scopus 로고
    • The roles of phosphate and the phosphate carrier in the mitochondrial permeability transition pore
    • Varanyuwatana P, Halestrap AP. The roles of phosphate and the phosphate carrier in the mitochondrial permeability transition pore. Mitochondrion (2012) 12:120-5. doi:10.1016/j.mito.2011.04.006
    • (2012) Mitochondrion , vol.12 , pp. 120-125
    • Varanyuwatana, P.1    Halestrap, A.P.2
  • 41
    • 84905042938 scopus 로고    scopus 로고
    • Genetic deletion of the mitochondrial phosphate carrier desensitizes the mitochondrial permeability transition pore and causes cardiomyopathy
    • Kwong JQ, Davis J, Baines CP, Sargent MA, Karch J, Wang X, et al. Genetic deletion of the mitochondrial phosphate carrier desensitizes the mitochondrial permeability transition pore and causes cardiomyopathy. Cell Death Differ (2014) 21:1209-17. doi:10.1038/cdd.2014.36
    • (2014) Cell Death Differ , vol.21 , pp. 1209-1217
    • Kwong, J.Q.1    Davis, J.2    Baines, C.P.3    Sargent, M.A.4    Karch, J.5    Wang, X.6
  • 42
    • 84862247742 scopus 로고    scopus 로고
    • Inhibition of complex I regulates the mitochondrial permeability transition through a phosphate-sensitive inhibitory site masked by cyclophilin D
    • Li B, Chauvin C, De Paulis D, De Oliveira F, Gharib A, Vial G, et al. Inhibition of complex I regulates the mitochondrial permeability transition through a phosphate-sensitive inhibitory site masked by cyclophilin D. Biochim Biophys Acta (2012) 1817:1628-34. doi:10.1016/j.bbabio.2012.05.011
    • (2012) Biochim Biophys Acta , vol.1817 , pp. 1628-1634
    • Li, B.1    Chauvin, C.2    De Paulis, D.3    De Oliveira, F.4    Gharib, A.5    Vial, G.6
  • 43
    • 0032524667 scopus 로고    scopus 로고
    • Regulation of the permeability transition pore in skeletal muscle mitochondria. Modulation by electron flow through the respiratory chain complex i.
    • Fontaine E, Eriksson O, Ichas F, Bernardi P. Regulation of the permeability transition pore in skeletal muscle mitochondria. Modulation by electron flow through the respiratory chain complex i. J Biol Chem (1998) 273:12662-8. doi:10.1074/jbc.273.20.12662
    • (1998) J Biol Chem , vol.273 , pp. 12662-12668
    • Fontaine, E.1    Eriksson, O.2    Ichas, F.3    Bernardi, P.4
  • 44
    • 2342431848 scopus 로고    scopus 로고
    • Opening of the mitochondrial permeability transition pore induces reactive oxygen species production at the level of the respiratory chain complex I
    • Batandier C, Leverve X, Fontaine E. Opening of the mitochondrial permeability transition pore induces reactive oxygen species production at the level of the respiratory chain complex I. J Biol Chem (2004) 279:17197-204. doi:10.1074/jbc. M310329200
    • (2004) J Biol Chem , vol.279 , pp. 17197-17204
    • Batandier, C.1    Leverve, X.2    Fontaine, E.3
  • 45
    • 79952837890 scopus 로고    scopus 로고
    • Modulation of F0F1-ATP synthase activity by cyclophilin D regulates matrix adenine nucleotide levels
    • Chinopoulos C, Konràd C, Kiss G, Metelkin E, Töröcsik B, Zhang SF, et al. Modulation of F0F1-ATP synthase activity by cyclophilin D regulates matrix adenine nucleotide levels. FEBS J (2011) 278:1112-25. doi:10.1111/j.1742-4658.2011.08026.x
    • (2011) FEBS J , vol.278 , pp. 1112-1125
    • Chinopoulos, C.1    Konràd, C.2    Kiss, G.3    Metelkin, E.4    Töröcsik, B.5    Zhang, S.F.6
  • 46
    • 84897967621 scopus 로고    scopus 로고
    • Molecular mechanisms of cell death: central implication of ATP synthase in mitochondrial permeability transition.
    • Bonora M, Wieckowski MR, Chinopoulos C, Kepp O, Kroemer G, Galluzzi L, et al. Molecular mechanisms of cell death: central implication of ATP synthase in mitochondrial permeability transition. Oncogene (2014). doi:10.1038/onc.2014.96
    • (2014) Oncogene
    • Bonora, M.1    Wieckowski, M.R.2    Chinopoulos, C.3    Kepp, O.4    Kroemer, G.5    Galluzzi, L.6
  • 47
    • 84916618668 scopus 로고    scopus 로고
    • Molecular identity of the mitochondrial permeability transition pore and its role in ischemia-reperfusion injury.
    • Morciano G, Giorgi C, Bonora M, Punzetti S, Pavasini R, Wieckowski MR, et al. Molecular identity of the mitochondrial permeability transition pore and its role in ischemia-reperfusion injury. J Mol Cell Cardiol (2014). doi:10.1016/j.yjmcc.2014.08.015
    • (2014) J Mol Cell Cardiol
    • Morciano, G.1    Giorgi, C.2    Bonora, M.3    Punzetti, S.4    Pavasini, R.5    Wieckowski, M.R.6
  • 49
    • 71749098386 scopus 로고    scopus 로고
    • Cyclophilin D modulates mitochondrial F0F1-ATP synthase by interacting with the lateral stalk of the complex
    • Giorgio V, Bisetto E, Soriano ME, Dabbeni-Sala F, Basso E, Petronilli V, et al. Cyclophilin D modulates mitochondrial F0F1-ATP synthase by interacting with the lateral stalk of the complex. J Biol Chem (2009) 284:33982-8. doi:10.1074/jbc. M109.020115
    • (2009) J Biol Chem , vol.284 , pp. 33982-33988
    • Giorgio, V.1    Bisetto, E.2    Soriano, M.E.3    Dabbeni-Sala, F.4    Basso, E.5    Petronilli, V.6
  • 50
    • 84874640414 scopus 로고    scopus 로고
    • Role of the c subunit of the FO ATP synthase in mitochondrial permeability transition
    • Bonora M, Bononi A, De Marchi E, Giorgi C, Lebiedzinska M, Marchi S, et al. Role of the c subunit of the FO ATP synthase in mitochondrial permeability transition. Cell Cycle (2013) 12:674-83. doi:10.4161/cc.23599
    • (2013) Cell Cycle , vol.12 , pp. 674-683
    • Bonora, M.1    Bononi, A.2    De Marchi, E.3    Giorgi, C.4    Lebiedzinska, M.5    Marchi, S.6
  • 51
    • 84901978868 scopus 로고    scopus 로고
    • The mitochondrial permeability transition pore is a dispensable element for mitochondrial calcium efflux
    • De Marchi E, Bonora M, Giorgi C, Pinton P. The mitochondrial permeability transition pore is a dispensable element for mitochondrial calcium efflux. Cell Calcium (2014) 56:1-13. doi:10.1016/j.ceca.2014.03.004
    • (2014) Cell Calcium , vol.56 , pp. 1-13
    • De Marchi, E.1    Bonora, M.2    Giorgi, C.3    Pinton, P.4
  • 52
    • 84893940629 scopus 로고    scopus 로고
    • Potential role of subunit c of F0F1-ATPase and subunit c of storage body in the mitochondrial permeability transition. Effect of the phosphorylation status of subunit c on pore opening.
    • Azarashvili T, Odinokova I, Bakunts A, Ternovsky V, Krestinina O, Tyynelä J, et al. Potential role of subunit c of F0F1-ATPase and subunit c of storage body in the mitochondrial permeability transition. Effect of the phosphorylation status of subunit c on pore opening. Cell Calcium (2014) 55:69-77. doi:10.1016/j.ceca.2013.12.002
    • (2014) Cell Calcium , vol.55 , pp. 69-77
    • Azarashvili, T.1    Odinokova, I.2    Bakunts, A.3    Ternovsky, V.4    Krestinina, O.5    Tyynelä, J.6
  • 53
    • 84904646147 scopus 로고    scopus 로고
    • An uncoupling channel within the c-subunit ring of the F1FO ATP synthase is the mitochondrial permeability transition pore.
    • Alavian KN, Beutner G, Lazrove E, Sacchetti S, Park H-A, Licznerski P, et al. An uncoupling channel within the c-subunit ring of the F1FO ATP synthase is the mitochondrial permeability transition pore. Proc Natl Acad Sci U S A (2014) 111(29):10580-5. doi:10.1073/pnas.1401591111
    • (2014) Proc Natl Acad Sci U S A , vol.111 , Issue.29 , pp. 10580-10585
    • Alavian, K.N.1    Beutner, G.2    Lazrove, E.3    Sacchetti, S.4    Park, H-A.5    Licznerski, P.6
  • 54
    • 79952284127 scopus 로고    scopus 로고
    • Hallmarks of cancer: the next generation
    • Hanahan D, Weinberg RA. Hallmarks of cancer: the next generation. Cell (2011) 144:646-74. doi:10.1016/j.cell.2011.02.013
    • (2011) Cell , vol.144 , pp. 646-674
    • Hanahan, D.1    Weinberg, R.A.2
  • 55
    • 41249101827 scopus 로고    scopus 로고
    • The mitochondrial permeability transition regulates cytochrome c release for apoptosis during endoplasmic reticulum stress by remodeling the cristae junction
    • Zhang D, Lu C, Whiteman M, Chance B, Armstrong JS. The mitochondrial permeability transition regulates cytochrome c release for apoptosis during endoplasmic reticulum stress by remodeling the cristae junction. J Biol Chem (2008) 283:3476-86. doi:10.1074/jbc. M707528200
    • (2008) J Biol Chem , vol.283 , pp. 3476-3486
    • Zhang, D.1    Lu, C.2    Whiteman, M.3    Chance, B.4    Armstrong, J.S.5
  • 56
    • 33745808321 scopus 로고    scopus 로고
    • Resveratrol-induced apoptosis is enhanced in acute lymphoblastic leukemia cells by modulation of the mitochondrial permeability transition pore
    • Zunino SJ, Storms DH. Resveratrol-induced apoptosis is enhanced in acute lymphoblastic leukemia cells by modulation of the mitochondrial permeability transition pore. Cancer Lett (2006) 240:123-34. doi:10.1016/j.canlet.2005.09.001
    • (2006) Cancer Lett , vol.240 , pp. 123-134
    • Zunino, S.J.1    Storms, D.H.2
  • 57
    • 0035355341 scopus 로고    scopus 로고
    • The Ca2+ concentration of the endoplasmic reticulum is a key determinant of ceramide-induced apoptosis: significance for the molecular mechanism of Bcl-2 action
    • Pinton P, Ferrari D, Rapizzi E, Di Virgilio F, Pozzan T, Rizzuto R. The Ca2+ concentration of the endoplasmic reticulum is a key determinant of ceramide-induced apoptosis: significance for the molecular mechanism of Bcl-2 action. EMBO J (2001) 20:2690-701. doi:10.1093/emboj/20.11.2690
    • (2001) EMBO J , vol.20 , pp. 2690-2701
    • Pinton, P.1    Ferrari, D.2    Rapizzi, E.3    Di Virgilio, F.4    Pozzan, T.5    Rizzuto, R.6
  • 58
    • 68949137001 scopus 로고    scopus 로고
    • Calcium elevation in mitochondria is the main Ca2+ requirement for mitochondrial permeability transition pore (mPTP) opening
    • Baumgartner HK, Gerasimenko JV, Thorne C, Ferdek P, Pozzan T, Tepikin AV, et al. Calcium elevation in mitochondria is the main Ca2+ requirement for mitochondrial permeability transition pore (mPTP) opening. J Biol Chem (2009) 284:20796-803. doi:10.1074/jbc. M109.025353
    • (2009) J Biol Chem , vol.284 , pp. 20796-20803
    • Baumgartner, H.K.1    Gerasimenko, J.V.2    Thorne, C.3    Ferdek, P.4    Pozzan, T.5    Tepikin, A.V.6
  • 59
    • 69049098806 scopus 로고    scopus 로고
    • Structural and functional link between the mitochondrial network and the endoplasmic reticulum
    • Giorgi C, De Stefani D, Bononi A, Rizzuto R, Pinton P. Structural and functional link between the mitochondrial network and the endoplasmic reticulum. Int J Biochem Cell Biol (2009) 41:1817-27. doi:10.1016/j.biocel.2009.04.010
    • (2009) Int J Biochem Cell Biol , vol.41 , pp. 1817-1827
    • Giorgi, C.1    De Stefani, D.2    Bononi, A.3    Rizzuto, R.4    Pinton, P.5
  • 60
    • 84898032907 scopus 로고    scopus 로고
    • A dialog on the first 20 years of PML research and the next 20 ahead
    • Bernardi R, PandolfiPP. A dialog on the first 20 years of PML research and the next 20 ahead. Front Oncol (2014) 4:23. doi:10.3389/fonc.2014.00023
    • (2014) Front Oncol , vol.4 , pp. 23
    • Bernardi, R.1    Pandolfi, P.P.2
  • 62
    • 84896718004 scopus 로고    scopus 로고
    • The mitochondrial calcium uniporter complex: molecular components, structure and physiopathological implications
    • Marchi S, Pinton P. The mitochondrial calcium uniporter complex: molecular components, structure and physiopathological implications. J Physiol (2014) 592:829-39. doi:10.1113/jphysiol.2013.268235
    • (2014) J Physiol , vol.592 , pp. 829-839
    • Marchi, S.1    Pinton, P.2
  • 63
    • 78649425814 scopus 로고    scopus 로고
    • PML regulates apoptosis at endoplasmic reticulum by modulating calcium release
    • Giorgi C, Ito K, Lin H, Santangelo C, Wieckowski MR, Lebiedzinska M, et al. PML regulates apoptosis at endoplasmic reticulum by modulating calcium release. Science (2010) 330:1247-51. doi:10.1126/science.1189157
    • (2010) Science , vol.330 , pp. 1247-1251
    • Giorgi, C.1    Ito, K.2    Lin, H.3    Santangelo, C.4    Wieckowski, M.R.5    Lebiedzinska, M.6
  • 64
    • 84887589243 scopus 로고    scopus 로고
    • Identification of PTEN at the ER and MAMs and its regulation of Ca(2+) signaling and apoptosis in a protein phosphatase-dependent manner
    • Bononi A, Bonora M, Marchi S, Missiroli S, Poletti F, Giorgi C, et al. Identification of PTEN at the ER and MAMs and its regulation of Ca(2+) signaling and apoptosis in a protein phosphatase-dependent manner. Cell Death Differ (2013) 20:1631-43. doi:10.1038/cdd.2013.77
    • (2013) Cell Death Differ , vol.20 , pp. 1631-1643
    • Bononi, A.1    Bonora, M.2    Marchi, S.3    Missiroli, S.4    Poletti, F.5    Giorgi, C.6
  • 65
    • 0034610995 scopus 로고    scopus 로고
    • Reduced loading of intracellular Ca(2+) stores and downregulation of capacitative Ca(2+) influx in Bcl-2-overexpressing cells
    • Pinton P, Ferrari D, Magalhães P, Schulze-OsthoffK, Di Virgilio F, Pozzan T, et al. Reduced loading of intracellular Ca(2+) stores and downregulation of capacitative Ca(2+) influx in Bcl-2-overexpressing cells. J Cell Biol (2000) 148:857-62. doi:10.1083/jcb.148.5.857
    • (2000) J Cell Biol , vol.148 , pp. 857-862
    • Pinton, P.1    Ferrari, D.2    Magalhães, P.3    Schulze-Osthoff, K.4    Di Virgilio, F.5    Pozzan, T.6
  • 66
    • 84878889924 scopus 로고    scopus 로고
    • Crosstalk between Bcl-2 family and Ras family small GTPases: potential cell fate regulation?
    • Kang J, Pervaiz S. Crosstalk between Bcl-2 family and Ras family small GTPases: potential cell fate regulation? Front Oncol (2012) 2:206. doi:10.3389/fonc.2012.00206
    • (2012) Front Oncol , vol.2 , pp. 206
    • Kang, J.1    Pervaiz, S.2
  • 67
    • 84899965504 scopus 로고    scopus 로고
    • H-Ras-driven tumoral maintenance is sustained through caveolin-1-dependent alterations in calcium signaling.
    • Rimessi A, Marchi S, Patergnani S, Pinton P. H-Ras-driven tumoral maintenance is sustained through caveolin-1-dependent alterations in calcium signaling. Oncogene (2014) 33(18):2329-40. doi:10.1038/onc.2013.192
    • (2014) Oncogene , vol.33 , Issue.18 , pp. 2329-2340
    • Rimessi, A.1    Marchi, S.2    Patergnani, S.3    Pinton, P.4
  • 68
    • 84859864623 scopus 로고    scopus 로고
    • Upsides and downsides of reactive oxygen species for cancer: the roles of reactive oxygen species in tumorigenesis, prevention, and therapy
    • Gupta SC, Hevia D, Patchva S, Park B, Koh W, Aggarwal BB. Upsides and downsides of reactive oxygen species for cancer: the roles of reactive oxygen species in tumorigenesis, prevention, and therapy. Antioxid Redox Signal (2012) 16:1295-322. doi:10.1089/ars.2011.4414
    • (2012) Antioxid Redox Signal , vol.16 , pp. 1295-1322
    • Gupta, S.C.1    Hevia, D.2    Patchva, S.3    Park, B.4    Koh, W.5    Aggarwal, B.B.6
  • 69
    • 84883415498 scopus 로고    scopus 로고
    • Reactive oxygen species in cancer biology and anticancer therapy
    • Yang Y, Karakhanova S, Werner J, Bazhin AV. Reactive oxygen species in cancer biology and anticancer therapy. Curr Med Chem (2013) 20:3677-92. doi:10.2174/0929867311320999165
    • (2013) Curr Med Chem , vol.20 , pp. 3677-3692
    • Yang, Y.1    Karakhanova, S.2    Werner, J.3    Bazhin, A.V.4
  • 70
    • 0036052593 scopus 로고    scopus 로고
    • Molecular and cellular characterization of imexon-resistant RPMI8226/I myeloma cells.
    • Available from:
    • Dvorakova K, Payne CM, Tome ME, Briehl MM, Vasquez MA, Waltmire CN, et al. Molecular and cellular characterization of imexon-resistant RPMI8226/I myeloma cells. Mol Cancer Ther (2002) 1:185-95. Available from: http://mct.aacrjournals.org/content/1/3/185.long
    • (2002) Mol Cancer Ther , vol.1 , pp. 185-195
    • Dvorakova, K.1    Payne, C.M.2    Tome, M.E.3    Briehl, M.M.4    Vasquez, M.A.5    Waltmire, C.N.6
  • 71
    • 24644441050 scopus 로고    scopus 로고
    • The thioredoxin reductase/thioredoxin system: novel redox targets for cancer therapy
    • Biaglow JE, Miller RA. The thioredoxin reductase/thioredoxin system: novel redox targets for cancer therapy. Cancer Biol Ther (2005) 4:6-13. doi:10.4161/cbt.4.1.1434
    • (2005) Cancer Biol Ther , vol.4 , pp. 6-13
    • Biaglow, J.E.1    Miller, R.A.2
  • 72
    • 2342455198 scopus 로고    scopus 로고
    • Mitochondrial superoxide dismutase: a promising target for new anticancer therapies
    • Pani G, Colavitti R, Bedogni B, Fusco S, Ferraro D, Borrello S, et al. Mitochondrial superoxide dismutase: a promising target for new anticancer therapies. Curr Med Chem (2004) 11:1299-308. doi:10.2174/0929867043365297
    • (2004) Curr Med Chem , vol.11 , pp. 1299-1308
    • Pani, G.1    Colavitti, R.2    Bedogni, B.3    Fusco, S.4    Ferraro, D.5    Borrello, S.6
  • 73
    • 33746912767 scopus 로고    scopus 로고
    • The permeability transition pore complex in cancer cell death
    • Brenner C, Grimm S. The permeability transition pore complex in cancer cell death. Oncogene (2006) 25:4744-56. doi:10.1038/sj.onc.1209609
    • (2006) Oncogene , vol.25 , pp. 4744-4756
    • Brenner, C.1    Grimm, S.2
  • 74
    • 77953131908 scopus 로고    scopus 로고
    • Targeting mitochondria for cancer therapy
    • Fulda S, Galluzzi L, Kroemer G. Targeting mitochondria for cancer therapy. Nat Rev Drug Discov (2010) 9:447-64. doi:10.1038/nrd3137
    • (2010) Nat Rev Drug Discov , vol.9 , pp. 447-464
    • Fulda, S.1    Galluzzi, L.2    Kroemer, G.3
  • 75
    • 0033798036 scopus 로고    scopus 로고
    • Characterization of porin isoforms expressed in tumor cells
    • Shinohara Y, Ishida T, Hino M, Yamazaki N, Baba Y, Terada H. Characterization of porin isoforms expressed in tumor cells. Eur J Biochem (2000) 267:6067-73. doi:10.1046/j.1432-1327.2000.01687.x
    • (2000) Eur J Biochem , vol.267 , pp. 6067-6073
    • Shinohara, Y.1    Ishida, T.2    Hino, M.3    Yamazaki, N.4    Baba, Y.5    Terada, H.6
  • 76
    • 0034257080 scopus 로고    scopus 로고
    • Relation of cell proliferation to expression of peripheral benzodiazepine receptors in human breast cancer cell lines
    • Beinlich A, Strohmeier R, Kaufmann M, Kuhl H. Relation of cell proliferation to expression of peripheral benzodiazepine receptors in human breast cancer cell lines. Biochem Pharmacol (2000) 60:397-402. doi:10.1016/S0006-2952(00)00325-7
    • (2000) Biochem Pharmacol , vol.60 , pp. 397-402
    • Beinlich, A.1    Strohmeier, R.2    Kaufmann, M.3    Kuhl, H.4
  • 77
    • 0035977186 scopus 로고    scopus 로고
    • Specific ligands of the peripheral benzodiazepine receptor induce apoptosis and cell cycle arrest in human colorectal cancer cells
    • Maaser K, Höpfner M, Jansen A, Weisinger G, Gavish M, Kozikowski AP, et al. Specific ligands of the peripheral benzodiazepine receptor induce apoptosis and cell cycle arrest in human colorectal cancer cells. Br J Cancer (2001) 85:1771-80. doi:10.1054/bjoc.2001.2181
    • (2001) Br J Cancer , vol.85 , pp. 1771-1780
    • Maaser, K.1    Höpfner, M.2    Jansen, A.3    Weisinger, G.4    Gavish, M.5    Kozikowski, A.P.6
  • 78
    • 0029781664 scopus 로고    scopus 로고
    • Expression of oxidative phosphorylation genes in renal tumors and tumoral cell lines
    • Faure Vigny H, Heddi A, Giraud S, Chautard D, Stepien G. Expression of oxidative phosphorylation genes in renal tumors and tumoral cell lines. Mol Carcinog (1996) 16:165-72. doi:10.1002/(SICI)1098-2744(199607)16:3165::AID-MC73.0.CO;2-G
    • (1996) Mol Carcinog , vol.16 , pp. 165-172
    • Faure Vigny, H.1    Heddi, A.2    Giraud, S.3    Chautard, D.4    Stepien, G.5
  • 79
    • 46649106720 scopus 로고    scopus 로고
    • Hexokinase II detachment from mitochondria triggers apoptosis through the permeability transition pore independent of voltage-dependent anion channels
    • Chiara F, Castellaro D, Marin O, Petronilli V, Brusilow WS, Juhaszova M, et al. Hexokinase II detachment from mitochondria triggers apoptosis through the permeability transition pore independent of voltage-dependent anion channels. PLoS One (2008) 3:e1852. doi:10.1371/journal.pone.0001852
    • (2008) PLoS One , vol.3
    • Chiara, F.1    Castellaro, D.2    Marin, O.3    Petronilli, V.4    Brusilow, W.S.5    Juhaszova, M.6
  • 80
    • 0030569305 scopus 로고    scopus 로고
    • Complexes between kinases, mitochondrial porin and adenylate translocator in rat brain resemble the permeability transition pore
    • Beutner G, Rück A, Riede B, Welte W, Brdiczka D. Complexes between kinases, mitochondrial porin and adenylate translocator in rat brain resemble the permeability transition pore. FEBS Lett (1996) 396:189-95. doi:10.1016/0014-5793(96)01092-7
    • (1996) FEBS Lett , vol.396 , pp. 189-195
    • Beutner, G.1    Rück, A.2    Riede, B.3    Welte, W.4    Brdiczka, D.5
  • 81
    • 0025942559 scopus 로고
    • Uncoupling protein is expressed in liver mitochondria of cold-exposed and newborn rats
    • Shinohara Y, Shima A, Kamida M, Terada H. Uncoupling protein is expressed in liver mitochondria of cold-exposed and newborn rats. FEBS Lett (1991) 293:173-4. doi:10.1016/0014-5793(91)81179-C
    • (1991) FEBS Lett , vol.293 , pp. 173-174
    • Shinohara, Y.1    Shima, A.2    Kamida, M.3    Terada, H.4
  • 82
    • 0029891049 scopus 로고    scopus 로고
    • Glucose catabolism in cancer cells: amplification of the gene encoding type II hexokinase
    • Rempel A, Mathupala SP, Griffin CA, Hawkins AL, Pedersen PL. Glucose catabolism in cancer cells: amplification of the gene encoding type II hexokinase. Cancer Res (1996) 56:2468-71.
    • (1996) Cancer Res , vol.56 , pp. 2468-2471
    • Rempel, A.1    Mathupala, S.P.2    Griffin, C.A.3    Hawkins, A.L.4    Pedersen, P.L.5
  • 83
    • 0942290437 scopus 로고    scopus 로고
    • In self-defence: hexokinase promotes voltage-dependent anion channel closure and prevents mitochondria-mediated apoptotic cell death
    • Azoulay-Zohar H, Israelson A, Abu-Hamad S, Shoshan-Barmatz V. In self-defence: hexokinase promotes voltage-dependent anion channel closure and prevents mitochondria-mediated apoptotic cell death. Biochem J (2004) 377:347-55. doi:10.1042/BJ20031465
    • (2004) Biochem J , vol.377 , pp. 347-355
    • Azoulay-Zohar, H.1    Israelson, A.2    Abu-Hamad, S.3    Shoshan-Barmatz, V.4
  • 84
    • 0021225510 scopus 로고
    • Isoenzyme pattern and subcellular localization of hexokinases in human breast cancer and nonpathological breast tissue
    • Gudnason V, Ingvarsson S, Jonasdottir A, Andresdottir V, Egilsson V. Isoenzyme pattern and subcellular localization of hexokinases in human breast cancer and nonpathological breast tissue. Int J Cancer (1984) 34:63-6. doi:10.1002/ijc.2910340111
    • (1984) Int J Cancer , vol.34 , pp. 63-66
    • Gudnason, V.1    Ingvarsson, S.2    Jonasdottir, A.3    Andresdottir, V.4    Egilsson, V.5
  • 85
    • 54949132875 scopus 로고    scopus 로고
    • Bcl-2 family proteins and cancer
    • Yip KW, Reed JC. Bcl-2 family proteins and cancer. Oncogene (2008) 27:6398-406. doi:10.1038/onc.2008.307
    • (2008) Oncogene , vol.27 , pp. 6398-6406
    • Yip, K.W.1    Reed, J.C.2
  • 88
    • 84863316405 scopus 로고    scopus 로고
    • Mediation of the antiapoptotic activity of Bcl-xL protein upon interaction with VDAC1 protein
    • Arbel N, Ben-Hail D, Shoshan-Barmatz V. Mediation of the antiapoptotic activity of Bcl-xL protein upon interaction with VDAC1 protein. J Biol Chem (2012) 287:23152-61. doi:10.1074/jbc. M112.345918
    • (2012) J Biol Chem , vol.287 , pp. 23152-23161
    • Arbel, N.1    Ben-Hail, D.2    Shoshan-Barmatz, V.3
  • 89
    • 80053560844 scopus 로고    scopus 로고
    • Bcl-xL regulates metabolic efficiency of neurons through interaction with the mitochondrial F1FO ATP synthase
    • Alavian KN, Li H, Collis L, Bonanni L, Zeng L, Sacchetti S, et al. Bcl-xL regulates metabolic efficiency of neurons through interaction with the mitochondrial F1FO ATP synthase. Nat Cell Biol (2011) 13:1224-33. doi:10.1038/ncb2330
    • (2011) Nat Cell Biol , vol.13 , pp. 1224-1233
    • Alavian, K.N.1    Li, H.2    Collis, L.3    Bonanni, L.4    Zeng, L.5    Sacchetti, S.6
  • 90
    • 84879138938 scopus 로고    scopus 로고
    • Gustafsson ÅB. Loss of MCL-1 leads to impaired autophagy and rapid development of heart failure.
    • Thomas RL, Roberts DJ, Kubli DA, Lee Y, Quinsay MN, Owens JB, et al. Gustafsson ÅB. Loss of MCL-1 leads to impaired autophagy and rapid development of heart failure. Genes Dev (2013) 27:1365-77. doi:10.1101/gad.215871.113
    • (2013) Genes Dev , vol.27 , pp. 1365-1377
    • Thomas, R.L.1    Roberts, D.J.2    Kubli, D.A.3    Lee, Y.4    Quinsay, M.N.5    Owens, J.B.6
  • 91
    • 0034688175 scopus 로고    scopus 로고
    • Bcl-2 and Bax regulate the channel activity of the mitochondrial adenine nucleotide translocator
    • Brenner C, Cadiou H, Vieira HL, Zamzami N, Marzo I, Xie Z, et al. Bcl-2 and Bax regulate the channel activity of the mitochondrial adenine nucleotide translocator. Oncogene (2000) 19:329-36. doi:10.1038/sj.onc.1203298
    • (2000) Oncogene , vol.19 , pp. 329-336
    • Brenner, C.1    Cadiou, H.2    Vieira, H.L.3    Zamzami, N.4    Marzo, I.5    Xie, Z.6
  • 92
    • 0031018674 scopus 로고    scopus 로고
    • Somatic Frameshift mutations in the BAX gene in colon cancers of the microsatellite mutator phenotype
    • Rampino N. Somatic Frameshift mutations in the BAX gene in colon cancers of the microsatellite mutator phenotype. Science (1997) 275:967-9. doi:10.1126/science.275.5302.967
    • (1997) Science , vol.275 , pp. 967-969
    • Rampino, N.1
  • 93
    • 0034718591 scopus 로고    scopus 로고
    • Mutational inactivation of the proapoptotic gene BAX confers selective advantage during tumor clonal evolution
    • Ionov Y, Yamamoto H, Krajewski S, Reed JC, Perucho M. Mutational inactivation of the proapoptotic gene BAX confers selective advantage during tumor clonal evolution. Proc Natl Acad Sci U S A (2000) 97:10872-7. doi:10.1073/pnas.190210897
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 10872-10877
    • Ionov, Y.1    Yamamoto, H.2    Krajewski, S.3    Reed, J.C.4    Perucho, M.5
  • 94
    • 0034635952 scopus 로고    scopus 로고
    • Bax degradation by the ubiquitin/proteasome-dependent pathway: involvement in tumor survival and progression
    • Li B, Dou QP. Bax degradation by the ubiquitin/proteasome-dependent pathway: involvement in tumor survival and progression. Proc Natl Acad Sci U S A (2000) 97:3850-5. doi:10.1073/pnas.070047997
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 3850-3855
    • Li, B.1    Dou, Q.P.2
  • 95
    • 0034662604 scopus 로고    scopus 로고
    • Mutations of the bak gene in human gastric and colorectal cancers.
    • Available from:
    • Kondo S, Shinomura Y, Miyazaki Y, Kiyohara T, Tsutsui S, Kitamura S, et al. Mutations of the bak gene in human gastric and colorectal cancers. Cancer Res (2000) 60:4328-30. Available from: http://cancerres.aacrjournals.org/content/60/16/4328.long
    • (2000) Cancer Res , vol.60 , pp. 4328-4330
    • Kondo, S.1    Shinomura, Y.2    Miyazaki, Y.3    Kiyohara, T.4    Tsutsui, S.5    Kitamura, S.6
  • 96
    • 0032600214 scopus 로고    scopus 로고
    • Bak expression and cell death occur in peritumorous tissue but not in pancreatic cancer cells
    • Graber HU, Friess H, Zimmermann A, Korc M, Adler G, Schmid R, et al. Bak expression and cell death occur in peritumorous tissue but not in pancreatic cancer cells. J Gastrointest Surg (1999) 3:74-80. doi:10.1016/S1091-255X(99)80012-2
    • (1999) J Gastrointest Surg , vol.3 , pp. 74-80
    • Graber, H.U.1    Friess, H.2    Zimmermann, A.3    Korc, M.4    Adler, G.5    Schmid, R.6
  • 97
    • 35348887850 scopus 로고    scopus 로고
    • Regulation of tumor cell mitochondrial homeostasis by an organelle-specific Hsp90 chaperone network
    • Kang BH, Plescia J, Dohi T, Rosa J, Doxsey SJ, Altieri DC. Regulation of tumor cell mitochondrial homeostasis by an organelle-specific Hsp90 chaperone network. Cell (2007) 131:257-70. doi:10.1016/j.cell.2007.08.028
    • (2007) Cell , vol.131 , pp. 257-270
    • Kang, B.H.1    Plescia, J.2    Dohi, T.3    Rosa, J.4    Doxsey, S.J.5    Altieri, D.C.6
  • 98
    • 78549293327 scopus 로고    scopus 로고
    • Heat shock protein 60 regulation of the mitochondrial permeability transition pore in tumor cells
    • Ghosh JC, Siegelin MD, Dohi T, Altieri DC. Heat shock protein 60 regulation of the mitochondrial permeability transition pore in tumor cells. Cancer Res (2010) 70:8988-93. doi:10.1158/0008-5472.CAN-10-2225
    • (2010) Cancer Res , vol.70 , pp. 8988-8993
    • Ghosh, J.C.1    Siegelin, M.D.2    Dohi, T.3    Altieri, D.C.4
  • 99
    • 41949125351 scopus 로고    scopus 로고
    • Hsp60 regulation of tumor cell apoptosis
    • Ghosh JC, Dohi T, Kang BH, Altieri DC. Hsp60 regulation of tumor cell apoptosis. J Biol Chem (2008) 283:5188-94. doi:10.1074/jbc. M705904200
    • (2008) J Biol Chem , vol.283 , pp. 5188-5194
    • Ghosh, J.C.1    Dohi, T.2    Kang, B.H.3    Altieri, D.C.4
  • 100
    • 84897461296 scopus 로고    scopus 로고
    • Chaperoning mitochondrial permeability transition: regulation of transition pore complex by a J-protein, DnaJC15
    • Sinha D, D'Silva P. Chaperoning mitochondrial permeability transition: regulation of transition pore complex by a J-protein, DnaJC15. Cell Death Dis (2014) 5:e1101. doi:10.1038/cddis.2014.72
    • (2014) Cell Death Dis , vol.5
    • Sinha, D.1    D'Silva, P.2
  • 101
    • 84872538586 scopus 로고    scopus 로고
    • HSP-molecular chaperones in cancer biogenesis and tumor therapy: an overview.
    • Available from:
    • Rappa F, Farina F, Zummo G, David S, Campanella C, Carini F, et al. HSP-molecular chaperones in cancer biogenesis and tumor therapy: an overview. Anticancer Res (2012) 32:5139-50. Available from: http://ar.iiarjournals.org/content/32/12/5139.long
    • (2012) Anticancer Res , vol.32 , pp. 5139-5150
    • Rappa, F.1    Farina, F.2    Zummo, G.3    David, S.4    Campanella, C.5    Carini, F.6
  • 102
    • 70350568650 scopus 로고    scopus 로고
    • Compartmentalized cancer drug discovery targeting mitochondrial Hsp90 chaperones
    • Kang BH, Altieri DC. Compartmentalized cancer drug discovery targeting mitochondrial Hsp90 chaperones. Oncogene (2009) 28:3681-8. doi:10.1038/onc.2009.227
    • (2009) Oncogene , vol.28 , pp. 3681-3688
    • Kang, B.H.1    Altieri, D.C.2
  • 103
    • 51649083933 scopus 로고    scopus 로고
    • Akt kinase reducing endoplasmic reticulum Ca2+ release protects cells from Ca2+-dependent apoptotic stimuli
    • Marchi S, Rimessi A, Giorgi C, Baldini C, Ferroni L, Rizzuto R, et al. Akt kinase reducing endoplasmic reticulum Ca2+ release protects cells from Ca2+-dependent apoptotic stimuli. Biochem Biophys Res Commun (2008) 375:501-5. doi:10.1016/j.bbrc.2008.07.153
    • (2008) Biochem Biophys Res Commun , vol.375 , pp. 501-505
    • Marchi, S.1    Rimessi, A.2    Giorgi, C.3    Baldini, C.4    Ferroni, L.5    Rizzuto, R.6
  • 104
    • 84868528894 scopus 로고    scopus 로고
    • The PI3K/AKT/mTOR pathway as a therapeutic target in endometrial cancer
    • Slomovitz BM, Coleman RL. The PI3K/AKT/mTOR pathway as a therapeutic target in endometrial cancer. Clin Cancer Res (2012) 18:5856-64. doi:10.1158/1078-0432.CCR-12-0662
    • (2012) Clin Cancer Res , vol.18 , pp. 5856-5864
    • Slomovitz, B.M.1    Coleman, R.L.2
  • 106
    • 84878437544 scopus 로고    scopus 로고
    • PI3K/Akt/mTOR pathway inhibitors in the therapy of pancreatic neuroendocrine tumors
    • Wolin EM. PI3K/Akt/mTOR pathway inhibitors in the therapy of pancreatic neuroendocrine tumors. Cancer Lett (2013) 335:1-8. doi:10.1016/j.canlet.2013.02.016
    • (2013) Cancer Lett , vol.335 , pp. 1-8
    • Wolin, E.M.1
  • 107
    • 85047692700 scopus 로고    scopus 로고
    • Glycogen synthase kinase-3beta mediates convergence of protection signaling to inhibit the mitochondrial permeability transition pore
    • Juhaszova M, Zorov DB, Kim S-H, Pepe S, Fu Q, Fishbein KW, et al. Glycogen synthase kinase-3beta mediates convergence of protection signaling to inhibit the mitochondrial permeability transition pore. J Clin Invest (2004) 113:1535-49. doi:10.1172/JCI200419906
    • (2004) J Clin Invest , vol.113 , pp. 1535-1549
    • Juhaszova, M.1    Zorov, D.B.2    Kim, S-H.3    Pepe, S.4    Fu, Q.5    Fishbein, K.W.6
  • 108
    • 57349143530 scopus 로고    scopus 로고
    • Glycogen synthase kinase 3beta (GSK3beta) in tumorigenesis and cancer chemotherapy
    • Luo J. Glycogen synthase kinase 3beta (GSK3beta) in tumorigenesis and cancer chemotherapy. Cancer Lett (2009) 273:194-200. doi:10.1016/j.canlet.2008.05.045
    • (2009) Cancer Lett , vol.273 , pp. 194-200
    • Luo, J.1
  • 109
    • 76249084726 scopus 로고    scopus 로고
    • Activation of mitochondrial ERK protects cancer cells from death through inhibition of the permeability transition
    • Rasola A, Sciacovelli M, Chiara F, Pantic B, Brusilow WS, Bernardi P. Activation of mitochondrial ERK protects cancer cells from death through inhibition of the permeability transition. Proc Natl Acad Sci U S A (2010) 107:726-31. doi:10.1073/pnas.0912742107
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 726-731
    • Rasola, A.1    Sciacovelli, M.2    Chiara, F.3    Pantic, B.4    Brusilow, W.S.5    Bernardi, P.6
  • 110
    • 0037968275 scopus 로고    scopus 로고
    • Protein kinase cepsilon interacts with and inhibits the permeability transition pore in cardiac mitochondria
    • Baines CP, Song C-X, Zheng Y-T, Wang G-W, Zhang J, Wang O-L, et al. Protein kinase cepsilon interacts with and inhibits the permeability transition pore in cardiac mitochondria. Circ Res (2003) 92:873-80. doi:10.1161/01.RES.0000069215.36389.8D
    • (2003) Circ Res , vol.92 , pp. 873-880
    • Baines, C.P.1    Song, C-X.2    Zheng, Y-T.3    Wang, G-W.4    Zhang, J.5    Wang, O-L.6
  • 111
    • 28144458325 scopus 로고    scopus 로고
    • Protein kinase C and preconditioning: role of the sarcoplasmic reticulum
    • Yamamura K, Steenbergen C, Murphy E. Protein kinase C and preconditioning: role of the sarcoplasmic reticulum. Am J Physiol Heart Circ Physiol (2005) 289:H2484-90. doi:10.1152/ajpheart.00590.2005
    • (2005) Am J Physiol Heart Circ Physiol , vol.289 , pp. H2484-H2490
    • Yamamura, K.1    Steenbergen, C.2    Murphy, E.3
  • 112
    • 84899484080 scopus 로고    scopus 로고
    • mTOR-targeted therapy: differential perturbation to mitochondrial membrane potential and permeability transition pore plays a role in therapeutic response
    • Kim JE, He Q, Chen Y, Shi C, Yu K. mTOR-targeted therapy: differential perturbation to mitochondrial membrane potential and permeability transition pore plays a role in therapeutic response. Biochem Biophys Res Commun (2014) 447:184-91. doi:10.1016/j.bbrc.2014.03.124
    • (2014) Biochem Biophys Res Commun , vol.447 , pp. 184-191
    • Kim, J.E.1    He, Q.2    Chen, Y.3    Shi, C.4    Yu, K.5
  • 113
    • 84884571942 scopus 로고    scopus 로고
    • GSK-3 and mitochondria in cancer cells
    • Chiara F, Rasola A. GSK-3 and mitochondria in cancer cells. Front Oncol (2013) 3:16. doi:10.3389/fonc.2013.00016
    • (2013) Front Oncol , vol.3 , pp. 16
    • Chiara, F.1    Rasola, A.2
  • 114
    • 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 (1999) 341(Pt 2):233-49. doi:10.1042/0264-6021:3410233
    • (1999) Biochem J , vol.341 , pp. 233-249
    • Crompton, M.1
  • 115
    • 0030826778 scopus 로고    scopus 로고
    • Cyclosporin A binding to mitochondrial cyclophilin inhibits the permeability transition pore and protects hearts from ischaemia/reperfusion injury
    • Halestrap AP, Connern CP, Griffiths EJ, Kerr PM. Cyclosporin A binding to mitochondrial cyclophilin inhibits the permeability transition pore and protects hearts from ischaemia/reperfusion injury. Mol Cell Biochem (1997) 174:167-72. doi:10.1023/A:1006879618176
    • (1997) Mol Cell Biochem , vol.174 , pp. 167-172
    • Halestrap, A.P.1    Connern, C.P.2    Griffiths, E.J.3    Kerr, P.M.4
  • 116
    • 84867022857 scopus 로고    scopus 로고
    • Reperfusion promotes mitochondrial dysfunction following focal cerebral ischemia in rats
    • Li J, Ma X, Yu W, Lou Z, Mu D, Wang Y, et al. Reperfusion promotes mitochondrial dysfunction following focal cerebral ischemia in rats. PLoS One (2012) 7:e46498. doi:10.1371/journal.pone.0046498
    • (2012) PLoS One , vol.7
    • Li, J.1    Ma, X.2    Yu, W.3    Lou, Z.4    Mu, D.5    Wang, Y.6
  • 117
    • 44349151470 scopus 로고    scopus 로고
    • Intermittent hypoxia is a key regulator of cancer cell and endothelial cell interplay in tumours
    • Toffoli S, Michiels C. Intermittent hypoxia is a key regulator of cancer cell and endothelial cell interplay in tumours. FEBS J (2008) 275:2991-3002. doi:10.1111/j.1742-4658.2008.06454.x
    • (2008) FEBS J , vol.275 , pp. 2991-3002
    • Toffoli, S.1    Michiels, C.2
  • 118
    • 85006768050 scopus 로고
    • The metabolism of tumors in the body
    • Warburg O, Wind F, Negelein E. The metabolism of tumors in the body. J Gen Physiol (1927) 8:519-30. doi:10.1085/jgp.8.6.519
    • (1927) J Gen Physiol , vol.8 , pp. 519-530
    • Warburg, O.1    Wind, F.2    Negelein, E.3
  • 119
  • 121
    • 78249286217 scopus 로고    scopus 로고
    • Cancer metabolism?: the Warburg effect today
    • Ferreira LMR. Cancer metabolism?: the Warburg effect today. Exp Mol Pathol (2010) 89:372-80. doi:10.1016/j.yexmp.2010.08.006
    • (2010) Exp Mol Pathol , vol.89 , pp. 372-380
    • Ferreira, L.M.R.1
  • 122
    • 41149105722 scopus 로고    scopus 로고
    • Mitochondria in cancer cells: what is so special about them?
    • Gogvadze V, Orrenius S, Zhivotovsky B. Mitochondria in cancer cells: what is so special about them? Trends Cell Biol (2008) 18:165-73. doi:10.1016/j.tcb.2008.01.006
    • (2008) Trends Cell Biol , vol.18 , pp. 165-173
    • Gogvadze, V.1    Orrenius, S.2    Zhivotovsky, B.3
  • 123
    • 13844250595 scopus 로고    scopus 로고
    • Hypoxia stimulates proliferation of human hepatoma cells through the induction of hexokinase II expression
    • Gwak G-Y, Yoon J-H, Kim KM, Lee H-S, Chung JW, Gores GJ. Hypoxia stimulates proliferation of human hepatoma cells through the induction of hexokinase II expression. J Hepatol (2005) 42:358-64. doi:10.1016/j.jhep.2004.11.020
    • (2005) J Hepatol , vol.42 , pp. 358-364
    • Gwak, G-Y.1    Yoon, J-H.2    Kim, K.M.3    Lee, H-S.4    Chung, J.W.5    Gores, G.J.6
  • 124
    • 0344653616 scopus 로고    scopus 로고
    • Complexes between porin, hexokinase, mitochondrial creatine kinase and adenylate translocator display properties of the permeability transition pore. Implication for regulation of permeability transition by the kinases.
    • Beutner G, Rück A, Riede B, Brdiczka D. Complexes between porin, hexokinase, mitochondrial creatine kinase and adenylate translocator display properties of the permeability transition pore. Implication for regulation of permeability transition by the kinases. Biochim Biophys Acta (1998) 1368:7-18. doi:10.1016/S0005-2736(97)00175-2
    • (1998) Biochim Biophys Acta , vol.1368 , pp. 7-18
    • Beutner, G.1    Rück, A.2    Riede, B.3    Brdiczka, D.4
  • 125
    • 84894384742 scopus 로고    scopus 로고
    • Respiratory complex I is essential to induce a Warburg profile in mitochondria-defective tumor cells
    • Calabrese C, Iommarini L, Kurelac I, Calvaruso MA, Capristo M, Lollini P-L, et al. Respiratory complex I is essential to induce a Warburg profile in mitochondria-defective tumor cells. Cancer Metab (2013) 1:11. doi:10.1186/2049-3002-1-11
    • (2013) Cancer Metab , vol.1 , pp. 11
    • Calabrese, C.1    Iommarini, L.2    Kurelac, I.3    Calvaruso, M.A.4    Capristo, M.5    Lollini, P-L.6
  • 126
    • 84874635096 scopus 로고    scopus 로고
    • Mitochondrial complex I activity and NAD+/NADH balance regulate breast cancer progression
    • Santidrian AF, Matsuno-Yagi A, Ritland M, Seo BB, LeBoeuf SE, Gay LJ, et al. Mitochondrial complex I activity and NAD+/NADH balance regulate breast cancer progression. J Clin Invest (2013) 123:1068-81. doi:10.1172/JCI64264
    • (2013) J Clin Invest , vol.123 , pp. 1068-1081
    • Santidrian, A.F.1    Matsuno-Yagi, A.2    Ritland, M.3    Seo, B.B.4    LeBoeuf, S.E.5    Gay, L.J.6
  • 128
    • 64549098628 scopus 로고    scopus 로고
    • A heteroplasmic, not homoplasmic, mitochondrial DNA mutation promotes tumorigenesis via alteration in reactive oxygen species generation and apoptosis
    • Park JS, Sharma LK, Li H, Xiang R, Holstein D, Wu J, et al. A heteroplasmic, not homoplasmic, mitochondrial DNA mutation promotes tumorigenesis via alteration in reactive oxygen species generation and apoptosis. Hum Mol Genet (2009) 18:1578-89. doi:10.1093/hmg/ddp069
    • (2009) Hum Mol Genet , vol.18 , pp. 1578-1589
    • Park, J.S.1    Sharma, L.K.2    Li, H.3    Xiang, R.4    Holstein, D.5    Wu, J.6
  • 129
    • 33746891176 scopus 로고    scopus 로고
    • Mitochondrial DNA mutations in human cancer
    • Chatterjee A, Mambo E, Sidransky D. Mitochondrial DNA mutations in human cancer. Oncogene (2006) 25:4663-74. doi:10.1038/sj.onc.1209604
    • (2006) Oncogene , vol.25 , pp. 4663-4674
    • Chatterjee, A.1    Mambo, E.2    Sidransky, D.3
  • 130
    • 77956937212 scopus 로고    scopus 로고
    • Generation of trans-mitochondrial mito-mice by the introduction of a pathogenic G13997A mtDNA from highly metastatic lung carcinoma cells
    • Yokota M, Shitara H, Hashizume O, Ishikawa K, Nakada K, Ishii R, et al. Generation of trans-mitochondrial mito-mice by the introduction of a pathogenic G13997A mtDNA from highly metastatic lung carcinoma cells. FEBS Lett (2010) 584:3943-8. doi:10.1016/j.febslet.2010.07.048
    • (2010) FEBS Lett , vol.584 , pp. 3943-3948
    • Yokota, M.1    Shitara, H.2    Hashizume, O.3    Ishikawa, K.4    Nakada, K.5    Ishii, R.6
  • 131
    • 43249112094 scopus 로고    scopus 로고
    • ROS-generating mitochondrial DNA mutations can regulate tumor cell metastasis
    • Ishikawa K, Takenaga K, Akimoto M, Koshikawa N, Yamaguchi A, Imanishi H, et al. ROS-generating mitochondrial DNA mutations can regulate tumor cell metastasis. Science (2008) 320:661-4. doi:10.1126/science.1156906
    • (2008) Science , vol.320 , pp. 661-664
    • Ishikawa, K.1    Takenaga, K.2    Akimoto, M.3    Koshikawa, N.4    Yamaguchi, A.5    Imanishi, H.6
  • 132
    • 84887478810 scopus 로고    scopus 로고
    • Perturbed mitochondrial Ca2+ signals as causes or consequences of mitophagy induction
    • Rimessi A, Bonora M, Marchi S, Patergnani S, Marobbio CMT, Lasorsa FM, et al. Perturbed mitochondrial Ca2+ signals as causes or consequences of mitophagy induction. Autophagy (2013) 9:1677-86. doi:10.4161/auto.24795
    • (2013) Autophagy , vol.9 , pp. 1677-1686
    • Rimessi, A.1    Bonora, M.2    Marchi, S.3    Patergnani, S.4    Marobbio, C.M.T.5    Lasorsa, F.M.6
  • 133
    • 77955861146 scopus 로고    scopus 로고
    • Autophagy in health and disease. 5. Mitophagy as a way of life.
    • Gottlieb RA, Carreira RS. Autophagy in health and disease. 5. Mitophagy as a way of life. Am J Physiol Cell Physiol (2010) 299:C203-10. doi:10.1152/ajpcell.00097.2010
    • (2010) Am J Physiol Cell Physiol , vol.299 , pp. C203-C210
    • Gottlieb, R.A.1    Carreira, R.S.2
  • 134
    • 0000097444 scopus 로고    scopus 로고
    • Detection of mitochondrial depolarization during autophagy by confocal fluorescence resonance energy transfer (CFRET)
    • Elmore SP, Qian T, Trost LC, Nishimura Y, Herman B, Lemasters JJ. Detection of mitochondrial depolarization during autophagy by confocal fluorescence resonance energy transfer (CFRET). Cell Vis J Anal Morphol (1997) 4:170-1.
    • (1997) Cell Vis J Anal Morphol , vol.4 , pp. 170-171
    • Elmore, S.P.1    Qian, T.2    Trost, L.C.3    Nishimura, Y.4    Herman, B.5    Lemasters, J.J.6
  • 135
    • 64549101639 scopus 로고    scopus 로고
    • Frameshift mutations of autophagy-related genes ATG2B, ATG5, ATG9B and ATG12 in gastric and colorectal cancers with microsatellite instability
    • Kang MR, Kim MS, Oh JE, Kim YR, Song SY, Kim SS, et al. Frameshift mutations of autophagy-related genes ATG2B, ATG5, ATG9B and ATG12 in gastric and colorectal cancers with microsatellite instability. J Pathol (2009) 217:702-6. doi:10.1002/path.2509
    • (2009) J Pathol , vol.217 , pp. 702-706
    • Kang, M.R.1    Kim, M.S.2    Oh, J.E.3    Kim, Y.R.4    Song, S.Y.5    Kim, S.S.6
  • 136
    • 0344142468 scopus 로고    scopus 로고
    • Cloning and genomic organization of beclin 1, a candidate tumor suppressor gene on chromosome 17q21
    • Aita VM, Liang XH, Murty VV, Pincus DL, Yu W, Cayanis E, et al. Cloning and genomic organization of beclin 1, a candidate tumor suppressor gene on chromosome 17q21. Genomics (1999) 59:59-65. doi:10.1006/geno.1999.5851
    • (1999) Genomics , vol.59 , pp. 59-65
    • Aita, V.M.1    Liang, X.H.2    Murty, V.V.3    Pincus, D.L.4    Yu, W.5    Cayanis, E.6
  • 137
    • 45049083880 scopus 로고    scopus 로고
    • Frameshift mutation of UVRAG, an autophagy-related gene, in gastric carcinomas with microsatellite instability
    • Kim MS, Jeong EG, Ahn CH, Kim SS, Lee SH, Yoo NJ. Frameshift mutation of UVRAG, an autophagy-related gene, in gastric carcinomas with microsatellite instability. Hum Pathol (2008) 39:1059-63. doi:10.1016/j.humpath.2007.11.013
    • (2008) Hum Pathol , vol.39 , pp. 1059-1063
    • Kim, M.S.1    Jeong, E.G.2    Ahn, C.H.3    Kim, S.S.4    Lee, S.H.5    Yoo, N.J.6
  • 138
    • 77951432631 scopus 로고    scopus 로고
    • The causes of cancer revisited: "mitochondrial malignancy" and ROS-induced oncogenic transformation - why mitochondria are targets for cancer therapy
    • Ralph SJ, Rodríguez-Enríquez S, Neuzil J, Saavedra E, Moreno-Sánchez R. The causes of cancer revisited: "mitochondrial malignancy" and ROS-induced oncogenic transformation - why mitochondria are targets for cancer therapy. Mol Aspects Med (2010) 31:145-70. doi:10.1016/j.mam.2010.02.008
    • (2010) Mol Aspects Med , vol.31 , pp. 145-170
    • Ralph, S.J.1    Rodríguez-Enríquez, S.2    Neuzil, J.3    Saavedra, E.4    Moreno-Sánchez, R.5
  • 142
    • 33846100356 scopus 로고    scopus 로고
    • A human colon cancer cell capable of initiating tumour growth in immunodeficient mice
    • O'Brien CA, Pollett A, Gallinger S, Dick JE. A human colon cancer cell capable of initiating tumour growth in immunodeficient mice. Nature (2007) 445:106-10. doi:10.1038/nature05372
    • (2007) Nature , vol.445 , pp. 106-110
    • O'Brien, C.A.1    Pollett, A.2    Gallinger, S.3    Dick, J.E.4
  • 144
    • 33750313208 scopus 로고    scopus 로고
    • Cancer stem cells - perspectives on current status and future directions: AACR workshop on cancer stem cells
    • Clarke MF, Dick JE, Dirks PB, Eaves CJ, Jamieson CHM, Jones DL, et al. Cancer stem cells - perspectives on current status and future directions: AACR workshop on cancer stem cells. Cancer Res (2006) 66:9339-44. doi:10.1158/0008-5472.CAN-06-3126
    • (2006) Cancer Res , vol.66 , pp. 9339-9344
    • Clarke, M.F.1    Dick, J.E.2    Dirks, P.B.3    Eaves, C.J.4    Jamieson, C.H.M.5    Jones, D.L.6
  • 146
    • 84900361541 scopus 로고    scopus 로고
    • Mitochondrial metabolism directs stemness and differentiation in P19 embryonal carcinoma stem cells.
    • Vega-Naredo I, Loureiro R, Mesquita KA, Barbosa IA, Tavares LC, Branco AF, et al. Mitochondrial metabolism directs stemness and differentiation in P19 embryonal carcinoma stem cells. Cell Death Differ (2014) 21(10):1560-74. doi:10.1038/cdd.2014.66
    • (2014) Cell Death Differ , vol.21 , Issue.10 , pp. 1560-1574
    • Vega-Naredo, I.1    Loureiro, R.2    Mesquita, K.A.3    Barbosa, I.A.4    Tavares, L.C.5    Branco, A.F.6
  • 147
    • 84855231244 scopus 로고    scopus 로고
    • Targeting mitochondria in fighting cancer
    • Gogvadze V. Targeting mitochondria in fighting cancer. Curr Pharm Des (2011) 17:4034-46. doi:10.2174/138161211798764933
    • (2011) Curr Pharm Des , vol.17 , pp. 4034-4046
    • Gogvadze, V.1
  • 148
    • 84890632015 scopus 로고    scopus 로고
    • Mitochondrial permeability transition pore as a selective target for anti-cancer therapy
    • Suh DH, Kim M-K, Kim HS, Chung HH, Song YS. Mitochondrial permeability transition pore as a selective target for anti-cancer therapy. Front Oncol (2013) 3:41. doi:10.3389/fonc.2013.00041
    • (2013) Front Oncol , vol.3 , pp. 41
    • Suh, D.H.1    Kim, M-K.2    Kim, H.S.3    Chung, H.H.4    Song, Y.S.5


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