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Volumn 33, Issue 49, 2014, Pages 5569-5581

Mitochondrial ion channels as oncological targets

Author keywords

direct targeting; ion channels; mitochondria; pharmacology

Indexed keywords

CALCIUM; ION CHANNEL; MITOCHONDRIAL PROTEIN; MITOCHONDRIAL UNCOUPLING PROTEIN; PORIN; POTASSIUM CHANNEL; REACTIVE OXYGEN METABOLITE;

EID: 84925224409     PISSN: 09509232     EISSN: 14765594     Source Type: Journal    
DOI: 10.1038/onc.2013.578     Document Type: Review
Times cited : (86)

References (194)
  • 1
    • 84870206960 scopus 로고    scopus 로고
    • Mitochondria: Master regulators of danger signalling
    • Galluzzi L, Kepp O, Kroemer G. Mitochondria: Master regulators of danger signalling. Nat Rev Mol Cell Biol 2012; 13: 780-788.
    • (2012) Nat Rev Mol Cell Biol , vol.13 , pp. 780-788
    • Galluzzi, L.1    Kepp, O.2    Kroemer, G.3
  • 3
    • 84872006971 scopus 로고    scopus 로고
    • Where killers meet-permeabilization of the outer mitochondrial membrane during apoptosis
    • Bender T, Martinou JC. Where killers meet-permeabilization of the outer mitochondrial membrane during apoptosis. Cold Spring Harb Perspect Biol 2013; 5: A011106.
    • (2013) Cold Spring Harb Perspect Biol , vol.5 , pp. a011106
    • Bender, T.1    Martinou, J.C.2
  • 5
    • 57649233079 scopus 로고    scopus 로고
    • The role of mitochondria in reactive oxygen species metabolism and signaling
    • Starkov AA. The role of mitochondria in reactive oxygen species metabolism and signaling. Ann NY Acad Sci 2008; 1147: 37-52.
    • (2008) Ann NY Acad Sci , vol.1147 , pp. 37-52
    • Starkov, A.A.1
  • 6
    • 58249093939 scopus 로고    scopus 로고
    • How mitochondria produce reactive oxygen species
    • Murphy MP. How mitochondria produce reactive oxygen species. Biochem J 2009; 417: 1-13.
    • (2009) Biochem J , vol.417 , pp. 1-13
    • Murphy, M.P.1
  • 7
    • 0037726805 scopus 로고    scopus 로고
    • Intrinsic and extrinsic uncoupling of oxidative phosphorylation
    • Kadenbach B. Intrinsic and extrinsic uncoupling of oxidative phosphorylation. Biochim Biophys Acta 2003; 1604: 77-94.
    • (2003) Biochim Biophys Acta , vol.1604 , pp. 77-94
    • Kadenbach, B.1
  • 8
    • 77952673393 scopus 로고    scopus 로고
    • Mitochondrial potassium channels and reactive oxygen species
    • Malinska D, Mirandola SR, Kunz WS. Mitochondrial potassium channels and reactive oxygen species. FEBS Lett 2010; 584: 2043-2048.
    • (2010) FEBS Lett , vol.584 , pp. 2043-2048
    • Malinska, D.1    Mirandola, S.R.2    Kunz, W.S.3
  • 10
    • 0031594853 scopus 로고    scopus 로고
    • A model of O2.-generation in the complex III of the electron transport chain
    • Demin OV, Kholodenko BN, Skulachev VP. A model of O2.-generation in the complex III of the electron transport chain. Mol Cell Biochem 1998; 184: 21-33.
    • (1998) Mol Cell Biochem , vol.184 , pp. 21-33
    • Demin, O.V.1    Kholodenko, B.N.2    Skulachev, V.P.3
  • 11
    • 85006126409 scopus 로고    scopus 로고
    • Mitochondrial ion channels/transporters as sensors and regulators of cellular redox signaling
    • PMID: 24180309
    • O-Uchi J, Ryu SY, Jhun BS, Hurst S, Sheu SS. Mitochondrial ion channels/transporters as sensors and regulators of cellular redox signaling. Antioxid Redox Signal 2013; PMID: 24180309.
    • (2013) Antioxid Redox Signal
    • O-Uchi, J.1    Ryu, S.Y.2    Jhun, B.S.3    Hurst, S.4    Sheu, S.S.5
  • 12
    • 84871139444 scopus 로고    scopus 로고
    • A refined analysis of superoxide production by mitochondrial sn-glycerol 3-phosphate dehydrogenase
    • Orr AL, Quinlan CL, Perevoshchikova IV, Brand MD. A refined analysis of superoxide production by mitochondrial sn-glycerol 3-phosphate dehydrogenase. J Biol Chem 2012; 287: 42921-42935.
    • (2012) J Biol Chem , vol.287 , pp. 42921-42935
    • Orr, A.L.1    Quinlan, C.L.2    Perevoshchikova, I.V.3    Brand, M.D.4
  • 13
    • 84879430920 scopus 로고    scopus 로고
    • Sites of reactive oxygen species generation by mitochondria oxidizing different substrates
    • Quinlan CL, Perevoshchikova IV, Hey-Mogensen M, Orr AL, Brand MD. Sites of reactive oxygen species generation by mitochondria oxidizing different substrates. Redox Biol 2013; 1: 304-312.
    • (2013) Redox Biol , vol.1 , pp. 304-312
    • Quinlan, C.L.1    Perevoshchikova, I.V.2    Hey-Mogensen, M.3    Orr, A.L.4    Brand, M.D.5
  • 14
    • 84862292292 scopus 로고    scopus 로고
    • Oxidative stress, tumor microenvironment, and metabolic reprogramming: A diabolic liaison
    • Fiaschi T, Chiarugi P. Oxidative stress, tumor microenvironment, and metabolic reprogramming: A diabolic liaison. Int J Cell Biol 2012; 2012: 762825.
    • (2012) Int J Cell Biol , vol.2012 , pp. 762825
    • Fiaschi, T.1    Chiarugi, P.2
  • 15
  • 16
    • 82755166890 scopus 로고    scopus 로고
    • Inhibition of pyruvate kinase M2 by reactive oxygen species contributes to cellular antioxidant responses
    • Anastasiou D, Poulogiannis G, Asara JM, Boxer MB, Jiang JK, Shen M et al. Inhibition of pyruvate kinase M2 by reactive oxygen species contributes to cellular antioxidant responses. Science 2011; 334: 1278-1283.
    • (2011) Science , vol.334 , pp. 1278-1283
    • Anastasiou, D.1    Poulogiannis, G.2    Asara, J.M.3    Boxer, M.B.4    Jiang, J.K.5    Shen, M.6
  • 18
    • 76049083966 scopus 로고    scopus 로고
    • Reactive oxygen species, cellular redox systems, and apoptosis
    • Circu ML, Aw TY. Reactive oxygen species, cellular redox systems, and apoptosis. Free Radic Biol Med 2010; 48: 749-762.
    • (2010) Free Radic Biol Med , vol.48 , pp. 749-762
    • Circu, M.L.1    Aw, T.Y.2
  • 20
    • 33746359639 scopus 로고    scopus 로고
    • The death-associated protein kinases: Structure, function, and beyond
    • Bialik S, Kimchi A. The death-associated protein kinases: Structure, function, and beyond. Annu Rev Biochem 2006; 75: 189-210.
    • (2006) Annu Rev Biochem , vol.75 , pp. 189-210
    • Bialik, S.1    Kimchi, A.2
  • 21
  • 22
    • 78149359658 scopus 로고    scopus 로고
    • Multistep and multitask Bax activation
    • Ghibelli L, Diederich M. Multistep and multitask Bax activation. Mitochondrion 2010; 10: 604-613.
    • (2010) Mitochondrion , vol.10 , pp. 604-613
    • Ghibelli, L.1    Diederich, M.2
  • 23
    • 68949141833 scopus 로고    scopus 로고
    • Opening the doors to cytochrome c: Changes in mitochondrial shape and apoptosis
    • Scorrano L. Opening the doors to cytochrome c: Changes in mitochondrial shape and apoptosis. Int J Biochem Cell Biol 2009; 41: 1875-1883.
    • (2009) Int J Biochem Cell Biol , vol.41 , pp. 1875-1883
    • Scorrano, L.1
  • 24
    • 79952708659 scopus 로고    scopus 로고
    • Mitochondrial outer membrane permeabilization during apoptosis: The role of mitochondrial fission
    • Landes T, Martinou JC. Mitochondrial outer membrane permeabilization during apoptosis: The role of mitochondrial fission. Biochim Biophys Acta 2011; 1813: 540-545.
    • (2011) Biochim Biophys Acta , vol.1813 , pp. 540-545
    • Landes, T.1    Martinou, J.C.2
  • 25
    • 67650071137 scopus 로고    scopus 로고
    • Targeting cancer cells by ROS-mediated mechanisms: A radical therapeutic approach?
    • Trachootham D, Alexandre J, Huang P. Targeting cancer cells by ROS-mediated mechanisms: A radical therapeutic approach? Nat Rev Drug Discov 2009; 8: 579-591.
    • (2009) Nat Rev Drug Discov , vol.8 , pp. 579-591
    • Trachootham, D.1    Alexandre, J.2    Huang, P.3
  • 26
    • 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, Rodr?guez-Enr?quez 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: 145-170.
    • (2010) Mol Aspects Med , vol.31 , pp. 145-170
    • Ralph, S.J.1    Rodŕguez-Enŕquez, S.2    Neuzil, J.3    Saavedra, E.4    Moreno-Sánchez, R.5
  • 27
    • 84860389709 scopus 로고    scopus 로고
    • Inhibitors of succinate: Quinone reductase/Complex II regulate production of mitochondrial reactive oxygen species and protect normal cells from ischemic damage but induce specific cancer cell death
    • Ralph SJ, Moreno-Sánchez R, Neuzil J, Rodr?guez-Enr?quez S. Inhibitors of succinate: Quinone reductase/Complex II regulate production of mitochondrial reactive oxygen species and protect normal cells from ischemic damage but induce specific cancer cell death. Pharm Res 2011; 28: 2695-2730.
    • (2011) Pharm Res , vol.28 , pp. 2695-2730
    • Ralph, S.J.1    Moreno-Sánchez, R.2    Neuzil, J.3    Rodŕguez-Enŕquez, S.4
  • 28
    • 58149105356 scopus 로고    scopus 로고
    • Cancer cell killing via ROS: To increase or decrease, that is the question
    • Wang J, Yi J. Cancer cell killing via ROS: To increase or decrease, that is the question. Cancer Biol Ther 2008; 7: 1875-1884.
    • (2008) Cancer Biol Ther , vol.7 , pp. 1875-1884
    • Wang, J.1    Yi, J.2
  • 29
    • 1642540210 scopus 로고    scopus 로고
    • The mitochondrial calcium uniporter is a highly selective ion channel
    • Kirichok Y, Krapivinsky G, Clapham DE. The mitochondrial calcium uniporter is a highly selective ion channel. Nature 2004; 427: 360-364.
    • (2004) Nature , vol.427 , pp. 360-364
    • Kirichok, Y.1    Krapivinsky, G.2    De, C.3
  • 31
    • 80054953358 scopus 로고    scopus 로고
    • After half a century mitochondrial calcium in-and efflux machineries reveal themselves
    • Drago I, Pizzo P, Pozzan T. After half a century mitochondrial calcium in-and efflux machineries reveal themselves. EMBO J 2011; 30: 4119-4125.
    • (2011) EMBO J , vol.30 , pp. 4119-4125
    • Drago, I.1    Pizzo, P.2    Pozzan, T.3
  • 33
    • 80052627393 scopus 로고    scopus 로고
    • Mitochondrial permeability transition in Ca(2)-dependent apoptosis and necrosis
    • Rasola A, Bernardi P. Mitochondrial permeability transition in Ca(2)-dependent apoptosis and necrosis. Cell Calcium 2011; 50: 222-233.
    • (2011) Cell Calcium , vol.50 , pp. 222-233
    • Rasola, A.1    Bernardi, P.2
  • 34
    • 77955291571 scopus 로고    scopus 로고
    • Oxidative stress caused by mitochondrial calcium overload
    • Peng TI, Jou MJ. Oxidative stress caused by mitochondrial calcium overload. Ann NY Acad Sci 2010; 1201: 183-188.
    • (2010) Ann NY Acad Sci , vol.1201 , pp. 183-188
    • Peng, T.I.1    Jou, M.J.2
  • 35
    • 33746824336 scopus 로고    scopus 로고
    • Elevated cytosolic Na decreases mitochondrial Ca2 uptake during excitation-contraction coupling and impairs energetic adaptation in cardiac myocytes
    • Maack C, Cortassa S, Aon MA, Ganesan AN, Liu T, O'Rourke B. Elevated cytosolic Na decreases mitochondrial Ca2 uptake during excitation-contraction coupling and impairs energetic adaptation in cardiac myocytes. Circ Res 2006; 99: 172-182.
    • (2006) Circ Res , vol.99 , pp. 172-182
    • Maack, C.1    Cortassa, S.2    Aon, M.A.3    Ganesan, A.N.4    Liu, T.5    O'Rourke, B.6
  • 36
    • 18744432273 scopus 로고
    • Towards the molecular basis for the regulation of mitochondrial dehydrogenases by calcium ions
    • Nichols BJ, Denton RM. Towards the molecular basis for the regulation of mitochondrial dehydrogenases by calcium ions. Mol Cell Biochem 1995; 149-150: 203-212.
    • (1995) Mol Cell Biochem , vol.149-150 , pp. 203-212
    • Nichols, B.J.1    Denton, R.M.2
  • 37
    • 68649090226 scopus 로고    scopus 로고
    • Regulation of mitochondrial dehydrogenases by calcium ions
    • Denton RM. Regulation of mitochondrial dehydrogenases by calcium ions. Biochim Biophys Acta 2009; 1787: 1309-1316.
    • (2009) Biochim Biophys Acta , vol.1787 , pp. 1309-1316
    • Denton, R.M.1
  • 38
    • 34249945104 scopus 로고    scopus 로고
    • The cancer cell's ?power plants' as promising therapeutic targets: An overview
    • Pedersen PL. The cancer cell's ?power plants' as promising therapeutic targets: An overview. J Bioenerg Biomembr 2007; 39: 1-12.
    • (2007) J Bioenerg Biomembr , vol.39 , pp. 1-12
    • Pedersen, P.L.1
  • 39
    • 84866665390 scopus 로고    scopus 로고
    • Mitochondria and cancer
    • Wallace DC. Mitochondria and cancer. Nat Rev Cancer. 2012; 12: 685-698.
    • (2012) Nat Rev Cancer. , vol.12 , pp. 685-698
    • Wallace, D.C.1
  • 40
    • 0023194165 scopus 로고
    • The regulation of the oxidation of fatty acids and other substrates in rat heart mitochondria by changes in the matrix volume induced by osmotic strength, valinomycin and Ca2
    • Halestrap AP. The regulation of the oxidation of fatty acids and other substrates in rat heart mitochondria by changes in the matrix volume induced by osmotic strength, valinomycin and Ca2. Biochem J 1987; 244: 159-164.
    • (1987) Biochem J , vol.244 , pp. 159-164
    • Halestrap, A.P.1
  • 41
    • 72049130859 scopus 로고    scopus 로고
    • Energetic performance is improved by specific activation of K fluxes through K(Ca) channels in heart mitochondria
    • Aon MA, Cortassa S, Wei AC, Grunnet M, O'Rourke B. Energetic performance is improved by specific activation of K fluxes through K(Ca) channels in heart mitochondria. Biochim Biophys Acta 2010; 1797: 71-80.
    • (2010) Biochim Biophys Acta , vol.1797 , pp. 71-80
    • Aon, M.A.1    Cortassa, S.2    Wei, A.C.3    Grunnet, M.4    O'Rourke, B.5
  • 43
    • 84879508600 scopus 로고    scopus 로고
    • Putative structural and functional coupling of the mitochondrial BKCa channel to the respiratory chain
    • Bednarczyk P, Wieckowski MR, Broszkiewicz M, Skowronek K, Siemen D, Szewczyk A. Putative structural and functional coupling of the mitochondrial BKCa channel to the respiratory chain. PLoS One 2013; 8: E68125.
    • (2013) PLoS One , vol.8 , pp. e68125
    • Bednarczyk, P.1    Wieckowski, M.R.2    Broszkiewicz, M.3    Skowronek, K.4    Siemen, D.5    Szewczyk, A.6
  • 44
    • 84884909413 scopus 로고    scopus 로고
    • Mitochondrial cristae shape determines respiratory chain supercomplexes assembly and respiratory efficiency
    • Cogliati S, Frezza C, Soriano ME, Varanita T, Quintana-Cabrera R, Corrado M et al. Mitochondrial cristae shape determines respiratory chain supercomplexes assembly and respiratory efficiency. Cell 2013; 155: 160-171.
    • (2013) Cell , vol.155 , pp. 160-171
    • Cogliati, S.1    Frezza, C.2    Soriano, M.E.3    Varanita, T.4    Quintana-Cabrera, R.5    Corrado, M.6
  • 45
    • 77952951097 scopus 로고    scopus 로고
    • Hexokinase inhibits flux of fluorescently labeled ATP through mitochondrial outer membrane porin
    • Perevoshchikova IV, Zorov SD, Kotova EA, Zorov DB, Antonenko YN. Hexokinase inhibits flux of fluorescently labeled ATP through mitochondrial outer membrane porin. FEBS Lett 2010; 584: 2397-2402.
    • (2010) FEBS Lett , vol.584 , pp. 2397-2402
    • Perevoshchikova, I.V.1    Zorov, S.D.2    Kotova, E.A.3    Zorov, D.B.4    Antonenko, Y.N.5
  • 46
    • 29344468832 scopus 로고    scopus 로고
    • Voltage-dependent anion channel (VDAC) as mitochondrial governator-thinking outside the box
    • Lemasters JJ, Holmuhamedov E. Voltage-dependent anion channel (VDAC) as mitochondrial governator-thinking outside the box. Biochim Biophys Acta 2006; 1762: 181-190.
    • (2006) Biochim Biophys Acta , vol.1762 , pp. 181-190
    • Lemasters, J.J.1    Holmuhamedov, E.2
  • 47
    • 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: 347-355.
    • (2004) Biochem J , vol.377 , pp. 347-355
    • Azoulay-Zohar, H.1    Israelson, A.2    Abu-Hamad, S.3    Shoshan-Barmatz, V.4
  • 50
    • 84856695390 scopus 로고    scopus 로고
    • Physiology of potassium channels in the inner membrane of mitochondria
    • Szabò I, Leanza L, Gulbins E, Zoratti M. Physiology of potassium channels in the inner membrane of mitochondria. Pflugers Arch 2012; 463: 231-246.
    • (2012) Pflugers Arch , vol.463 , pp. 231-246
    • Szabò, I.1    Leanza, L.2    Gulbins, E.3    Zoratti, M.4
  • 52
    • 84859742112 scopus 로고    scopus 로고
    • VDAC blockage by phosphorothioate oligonucleotides and its implication in apoptosis
    • Tan W. VDAC blockage by phosphorothioate oligonucleotides and its implication in apoptosis. Biochim Biophys Acta 2012; 1818: 1555-1561.
    • (2012) Biochim Biophys Acta , vol.1818 , pp. 1555-1561
    • Tan, W.1
  • 53
    • 79551641146 scopus 로고    scopus 로고
    • Gene expression meta-analysis identifies VDAC1 as a predictor of poor outcome in early stage non-small cell lung cancer
    • Grills C, Jithesh PV, Blayney J, Zhang SD, Fennell DA. Gene expression meta-analysis identifies VDAC1 as a predictor of poor outcome in early stage non-small cell lung cancer. PLoS One 2011; 6: E14635.
    • (2011) PLoS One , vol.6 , pp. e14635
    • Grills, C.1    Jithesh, P.V.2    Blayney, J.3    Zhang, S.D.4    Fennell, D.A.5
  • 54
    • 84859777452 scopus 로고    scopus 로고
    • The role of VDAC in cell death: Friend or foe?
    • McCommis KS, Baines CP. The role of VDAC in cell death: Friend or foe? Biochim Biophys Acta, 2012; 1818: 1444-1450.
    • (2012) Biochim Biophys Acta , vol.1818 , pp. 1444-1450
    • McCommis, K.S.1    Baines, C.P.2
  • 55
    • 84857757702 scopus 로고    scopus 로고
    • Mitochondrial VDAC1 function in cell life and death and a target for cancer therapy
    • Shoshan-Barmatz V, Golan M. Mitochondrial VDAC1: Function in cell life and death and a target for cancer therapy. Curr Med Chem 2012; 19: 714-735.
    • (2012) Curr Med Chem , vol.19 , pp. 714-735
    • Shoshan-Barmatz, V.1    Golan, M.2
  • 56
    • 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.
    • (2012) Front Oncol , vol.2 , pp. 164
    • Shoshan-Barmatz, V.1    Mizrachi, D.2
  • 57
    • 79951699777 scopus 로고    scopus 로고
    • Hexokinase 2 is a key mediator of aerobic glycolysis and promotes tumor growth in human glioblastoma multiforme
    • Wolf A, Agnihotri S, Micallef J, Mukherjee J, Sabha N, Cairns R et al. Hexokinase 2 is a key mediator of aerobic glycolysis and promotes tumor growth in human glioblastoma multiforme. J Exp Med 2011; 208: 313-326.
    • (2011) J Exp Med , vol.208 , pp. 313-326
    • Wolf, A.1    Agnihotri, S.2    Micallef, J.3    Mukherjee, J.4    Sabha, N.5    Cairns, R.6
  • 58
    • 77954400635 scopus 로고    scopus 로고
    • Downregulation of voltage-dependent anion channel-1 expression by RNA interference prevents cancer cell growth in vivo
    • Koren I, Raviv Z, Shoshan-Barmatz V. Downregulation of voltage-dependent anion channel-1 expression by RNA interference prevents cancer cell growth in vivo. Cancer Biol Ther 2010; 9: 1046-1052.
    • (2010) Cancer Biol Ther , vol.9 , pp. 1046-1052
    • Koren, I.1    Raviv, Z.2    Shoshan-Barmatz, V.3
  • 60
    • 77954516857 scopus 로고    scopus 로고
    • Dominant-negative VDAC1 mutants reveal oligomeric VDAC1 to be the active unit in mitochondria-mediated apoptosis
    • Mader A, Abu-Hamad S, Arbel N, Gutié rrez-Aguilar M, Shoshan-Barmatz V. Dominant-negative VDAC1 mutants reveal oligomeric VDAC1 to be the active unit in mitochondria-mediated apoptosis. Biochem J 2010; 429: 147-155.
    • (2010) Biochem J , vol.429 , pp. 147-155
    • Mader, A.1    Abu-Hamad, S.2    Arbel, N.3    Gutiérrez-Aguilar, M.4    Shoshan-Barmatz, V.5
  • 61
    • 84858081016 scopus 로고    scopus 로고
    • Increased expression of VDAC1 sensitizes carcinoma cells to apoptosis induced by DNA cross-linking agents
    • Sharaf el dein O, Gallerne C, Brenner C, Lemaire C. Increased expression of VDAC1 sensitizes carcinoma cells to apoptosis induced by DNA cross-linking agents. Biochem Pharmacol 2012; 83: 1172-1182.
    • (2012) Biochem Pharmacol , vol.83 , pp. 1172-1182
    • Sharafeldein, O.1    Gallerne, C.2    Brenner, C.3    Lemaire, C.4
  • 62
    • 0036510541 scopus 로고    scopus 로고
    • Mitochondrial binding of hexokinase II inhibits Bax-induced cytochrome c release and apoptosis
    • Pastorino JG, Shulga N, Hoek JB. Mitochondrial binding of hexokinase II inhibits Bax-induced cytochrome c release and apoptosis. J Biol Chem 2002; 277: 7610-7618.
    • (2002) J Biol Chem , vol.277 , pp. 7610-7618
    • Pastorino, J.G.1    Shulga, N.2    Hoek, J.B.3
  • 63
    • 79956048183 scopus 로고    scopus 로고
    • Hexokinase regulates Bax-mediated mitochondrial membrane injury following ischemic stress
    • Gall JM, Wong V, Pimental DR, Havasi A, Wang Z, Pastorino JG et al. Hexokinase regulates Bax-mediated mitochondrial membrane injury following ischemic stress. Kidney Int 2011; 79: 1207-1216.
    • (2011) Kidney Int , vol.79 , pp. 1207-1216
    • Gall, J.M.1    Wong, V.2    Pimental, D.R.3    Havasi, A.4    Wang, Z.5    Pastorino, J.G.6
  • 64
    • 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.
    • (2008) PLoS One , vol.3 , pp. e1852
    • Chiara, F.1    Castellaro, D.2    Marin, O.3    Petronilli, V.4    Brusilow, W.S.5    Juhaszova, M.6
  • 65
    • 0036240569 scopus 로고    scopus 로고
    • Plant stress hormones suppress the proliferation and induce apoptosis in human cancer cells
    • Fingrut O, Flescher E. Plant stress hormones suppress the proliferation and induce apoptosis in human cancer cells. Leukemia 2002; 16: 608-616.
    • (2002) Leukemia , vol.16 , pp. 608-616
    • Fingrut, O.1    Flescher, E.2
  • 66
    • 84867447062 scopus 로고    scopus 로고
    • Methyljasmonate displays in vitro and in vivo activity against multiple myeloma cells
    • Klippel S, Jakubikova J, Delmore J, Ooi M, McMillin D, Kastritis E et al. Methyljasmonate displays in vitro and in vivo activity against multiple myeloma cells. Br J Haematol 2012; 159: 340-351.
    • (2012) Br J Haematol , vol.159 , pp. 340-351
    • Klippel, S.1    Jakubikova, J.2    Delmore, J.3    Ooi, M.4    McMillin, D.5    Kastritis, E.6
  • 67
    • 79957990169 scopus 로고    scopus 로고
    • A preliminary study of the local treatment of preneoplastic and malignant skin lesions using methyl jasmonate
    • Palmieri B, Iannitti T, Capone S, Flescher E. A preliminary study of the local treatment of preneoplastic and malignant skin lesions using methyl jasmonate. Eur Rev Med Pharmacol Sci 2011; 15: 333-336.
    • (2011) Eur Rev Med Pharmacol Sci , vol.15 , pp. 333-336
    • Palmieri, B.1    Iannitti, T.2    Capone, S.3    Flescher, E.4
  • 68
    • 16644392664 scopus 로고    scopus 로고
    • Methyl jasmonate induces apoptosis through induction of Bax/Bcl-XS and activation of caspase-3 via ROS production in A549 cells
    • Kim JH, Lee SY, Oh SY, Han SI, Park HG, Yoo MA et al. Methyl jasmonate induces apoptosis through induction of Bax/Bcl-XS and activation of caspase-3 via ROS production in A549 cells. Oncol Rep 2004; 12: 1233-1238.
    • (2004) Oncol Rep , vol.12 , pp. 1233-1238
    • Kim, J.H.1    Lee, S.Y.2    Oh, S.Y.3    Han, S.I.4    Park, H.G.5    Yoo, M.A.6
  • 69
    • 53749096199 scopus 로고    scopus 로고
    • Methyl jasmonate downregulates expression of proliferating cell nuclear antigen and induces apoptosis in human neuroblastoma cell lines
    • Tong QS, Jiang GS, Zheng LD, Tang ST, Cai JB, Liu Y et al. Methyl jasmonate downregulates expression of proliferating cell nuclear antigen and induces apoptosis in human neuroblastoma cell lines. Anticancer Drugs 2008; 19: 573-581.
    • (2008) Anticancer Drugs , vol.19 , pp. 573-581
    • Tong, Q.S.1    Jiang, G.S.2    Zheng, L.D.3    Tang, S.T.4    Cai, J.B.5    Liu, Y.6
  • 70
    • 66349108684 scopus 로고    scopus 로고
    • AKR1C isoforms represent a novel cellular target for jasmonates alongside their mitochondrial-mediated effects
    • Davies NJ, Hayden RE, Simpson PJ, Birtwistle J, Mayer K, Ride JP et al. AKR1C isoforms represent a novel cellular target for jasmonates alongside their mitochondrial-mediated effects. Cancer Res 2009; 69: 4769-4775.
    • (2009) Cancer Res , vol.69 , pp. 4769-4775
    • Davies, N.J.1    Hayden, R.E.2    Simpson, P.J.3    Birtwistle, J.4    Mayer, K.5    Ride, J.P.6
  • 71
    • 0037372349 scopus 로고    scopus 로고
    • Selective reduction of AKR1C2 in prostate cancer and its role in DHT metabolism
    • Ji Q, Chang L, VanDenBerg D, Stanczyk FZ, Stolz A. Selective reduction of AKR1C2 in prostate cancer and its role in DHT metabolism. Prostate 2003; 54: 275-289.
    • (2003) Prostate , vol.54 , pp. 275-289
    • Ji, Q.1    Chang, L.2    Vandenberg, D.3    Stanczyk, F.Z.4    Stolz, A.5
  • 73
    • 66949116366 scopus 로고    scopus 로고
    • Intermediate conductance Ca2-activated potassium channel (KCa3.1) in the inner mitochondrial membrane of human colon cancer cells
    • De Marchi U, Sassi N, Fioretti B, Catacuzzeno L, Cereghetti GM, Szabò I et al. Intermediate conductance Ca2-activated potassium channel (KCa3.1) in the inner mitochondrial membrane of human colon cancer cells. Cell Calcium 2009; 45: 509-516.
    • (2009) Cell Calcium , vol.45 , pp. 509-516
    • De Marchi, U.1    Sassi, N.2    Fioretti, B.3    Catacuzzeno, L.4    Cereghetti, G.M.5    Szabò, I.6
  • 74
    • 84862491784 scopus 로고    scopus 로고
    • General sensitization of melanoma cells for TRAIL-induced apoptosis by the potassium channel inhibitor TRAM-34 depends on release of SMAC
    • Quast SA, Berger A, Buttstädt N, Friebel K, Schö nherr R, Eberle J. General sensitization of melanoma cells for TRAIL-induced apoptosis by the potassium channel inhibitor TRAM-34 depends on release of SMAC. PLoS One 2012; 7: E39290.
    • (2012) PLoS One , vol.7 , pp. e39290
    • Quast, S.A.1    Berger, A.2    Buttstädt, N.3    Friebel, K.4    Schönherr, R.5    Eberle, J.6
  • 76
    • 9744221185 scopus 로고    scopus 로고
    • Hexokinasemitochondria interaction mediated by Akt is required to inhibit apoptosis in the presence or absence of Bax and Bak
    • Majewski N, Nogueira V, Bhaskar P, Coy PE, Skeen JE, Gottlob K et al. Hexokinasemitochondria interaction mediated by Akt is required to inhibit apoptosis in the presence or absence of Bax and Bak. Mol Cell 2004; 16: 819-830.
    • (2004) Mol Cell , vol.16 , pp. 819-830
    • Majewski, N.1    Nogueira, V.2    Bhaskar, P.3    Coy, P.E.4    Skeen, J.E.5    Gottlob, K.6
  • 77
    • 84857471980 scopus 로고    scopus 로고
    • 3-Bromopyruvate (3BP) a fast acting, promising, powerful, specific, and effective ?small molecule' anti-cancer agent taken from labside to bedside: Introduction to a special issue
    • Pedersen PL. 3-Bromopyruvate (3BP) a fast acting, promising, powerful, specific, and effective ?small molecule' anti-cancer agent taken from labside to bedside: Introduction to a special issue. J Bioenerg Biomembr 2012; 44: 1-6.
    • (2012) J Bioenerg Biomembr , vol.44 , pp. 1-6
    • Pedersen, P.L.1
  • 78
    • 84858704865 scopus 로고    scopus 로고
    • 3-Bromopyruvate: Targets and outcomes
    • Shoshan MC. 3-Bromopyruvate: Targets and outcomes. J Bioenerg Biomembr 2012; 44: 7-15.
    • (2012) J Bioenerg Biomembr , vol.44 , pp. 7-15
    • Shoshan, M.C.1
  • 79
    • 84862809596 scopus 로고    scopus 로고
    • A translational study case report on the small molecule energy blocker 3-bromopyruvate (3BP) as a potent anticancer agent: From bench side to bedside
    • Ko YH, Verhoeven HA, Lee MJ, Corbin DJ, Vogl TJ, Pedersen PL. A translational study case report on the small molecule energy blocker 3-bromopyruvate (3BP) as a potent anticancer agent: From bench side to bedside. J Bioenerg Biomembr 2012; 44: 163-170.
    • (2012) J Bioenerg Biomembr , vol.44 , pp. 163-170
    • Ko, Y.H.1    Verhoeven, H.A.2    Lee, M.J.3    Corbin, D.J.4    Vogl, T.J.5    Pedersen, P.L.6
  • 80
    • 84858698219 scopus 로고    scopus 로고
    • Targeting aerobic glycolysis: 3-bromopyruvate as a promising anticancer drug
    • Cardaci S, Desideri E, Ciriolo MR. Targeting aerobic glycolysis: 3-bromopyruvate as a promising anticancer drug. J Bioenerg Biomembr 2012; 44: 17-29.
    • (2012) J Bioenerg Biomembr , vol.44 , pp. 17-29
    • Cardaci, S.1    Desideri, E.2    Ciriolo, M.R.3
  • 82
    • 84862777922 scopus 로고    scopus 로고
    • Over-expression of GAPDH in human colorectal carcinoma as a preferred target of 3-bromopyruvate propyl ester
    • Tang Z, Yuan S, Hu Y, Zhang H, Wu W, Zeng Z et al. Over-expression of GAPDH in human colorectal carcinoma as a preferred target of 3-bromopyruvate propyl ester. J Bioenerg Biomembr 2012; 44: 117-125.
    • (2012) J Bioenerg Biomembr , vol.44 , pp. 117-125
    • Tang, Z.1    Yuan, S.2    Hu, Y.3    Zhang, H.4    Wu, W.5    Zeng, Z.6
  • 83
    • 84858708745 scopus 로고    scopus 로고
    • Effect of the antitumoral alkylating agent 3-bromopyruvate on mitochondrial respiration: Role of mitochondrially bound hexokinase
    • Rodrigues-Ferreira C, da Silva AP, Galina A. Effect of the antitumoral alkylating agent 3-bromopyruvate on mitochondrial respiration: Role of mitochondrially bound hexokinase. J Bioenerg Biomembr 2012; 44: 39-49.
    • (2012) J Bioenerg Biomembr , vol.44 , pp. 39-49
    • Rodrigues-Ferreira, C.1    Da Silva, A.P.2    Galina, A.3
  • 85
    • 84863012289 scopus 로고    scopus 로고
    • PKCE promotes oncogenic functions of ATF2 in the nucleus while blocking its apoptotic function at mitochondria
    • Lau E, Kluger H, Varsano T, Lee KY, Scheffler I, Rimm DL et al. PKCE promotes oncogenic functions of ATF2 in the nucleus while blocking its apoptotic function at mitochondria. Cell 2012; 148: 543-555.
    • (2012) Cell , vol.148 , pp. 543-555
    • Lau, E.1    Kluger, H.2    Varsano, T.3    Lee, K.Y.4    Scheffler, I.5    Rimm, D.L.6
  • 86
    • 34250372956 scopus 로고    scopus 로고
    • RAS-RAF-MEK-dependent oxidative cell death involving voltage-dependent anion channels
    • Yagoda N, von Rechenberg M, Zaganjor E, Bauer AJ, Yang WS, Fridman DJ et al. RAS-RAF-MEK-dependent oxidative cell death involving voltage-dependent anion channels. Nature 2007; 447: 864-868.
    • (2007) Nature , vol.447 , pp. 864-868
    • Yagoda, N.1    Von Rechenberg, M.2    Zaganjor, E.3    Bauer, A.J.4    Yang, W.S.5    Fridman, D.J.6
  • 87
    • 77049126374 scopus 로고    scopus 로고
    • Closure of VDAC causes oxidative stress and accelerates the Ca(2)-induced mitochondrial permeability transition in rat liver mitochondria
    • Tikunov A, Johnson CB, Pediaditakis P, Markevich N, Macdonald JM, Lemasters JJ et al. Closure of VDAC causes oxidative stress and accelerates the Ca(2)-induced mitochondrial permeability transition in rat liver mitochondria. Arch Biochem Biophys 2010; 495: 174-181.
    • (2010) Arch Biochem Biophys , vol.495 , pp. 174-181
    • Tikunov, A.1    Johnson, C.B.2    Pediaditakis, P.3    Markevich, N.4    Macdonald, J.M.5    Lemasters, J.J.6
  • 88
    • 52449132327 scopus 로고    scopus 로고
    • Mitochondrial voltage-dependent anion channels (VDACs) as novel pharmacological targets for anti-cancer agents
    • Simamura E, Shimada H, Hatta T, Hirai K. Mitochondrial voltage-dependent anion channels (VDACs) as novel pharmacological targets for anti-cancer agents. J Bioenerg Biomembr 2008; 40: 213-217.
    • (2008) J Bioenerg Biomembr , vol.40 , pp. 213-217
    • Simamura, E.1    Shimada, H.2    Hatta, T.3    Hirai, K.4
  • 89
    • 0034525413 scopus 로고    scopus 로고
    • VDAC regulation by the Bcl-2 family of proteins
    • Tsujimoto Y, Shimizu S. VDAC regulation by the Bcl-2 family of proteins. Cell Death Differ 2000; 7: 1174-1181.
    • (2000) Cell Death Differ , vol.7 , pp. 1174-1181
    • Tsujimoto, Y.1    Shimizu, S.2
  • 91
    • 46749123261 scopus 로고    scopus 로고
    • Hierarchical involvement of Bak, VDAC1 and Bax in cisplatin-induced cell death
    • Tajeddine N, Galluzzi L, Kepp O, Hangen E, Morselli E, Senovilla L et al. Hierarchical involvement of Bak, VDAC1 and Bax in cisplatin-induced cell death. Oncogene 2008; 27: 4221-4232.
    • (2008) Oncogene , vol.27 , pp. 4221-4232
    • Tajeddine, N.1    Galluzzi, L.2    Kepp, O.3    Hangen, E.4    Morselli, E.5    Senovilla, L.6
  • 92
    • 71749121777 scopus 로고    scopus 로고
    • Outer membrane VDAC1 controls permeability transition of the inner mitochondrial membrane in cellulo during stress-induced apoptosis
    • Tomasello F, Messina A, Lartigue L, Schembri L, Medina C, Reina S et al. Outer membrane VDAC1 controls permeability transition of the inner mitochondrial membrane in cellulo during stress-induced apoptosis. Cell Res 2009; 19: 1363-1376.
    • (2009) Cell Res , vol.19 , pp. 1363-1376
    • Tomasello, F.1    Messina, A.2    Lartigue, L.3    Schembri, L.4    Medina, C.5    Reina, S.6
  • 93
    • 34247895697 scopus 로고    scopus 로고
    • Voltage-dependent anion channels are dispensable for mitochondrial-dependent cell death
    • Baines CP, Kaiser RA, Sheik T, Craigen WJ, Molkentin JD. Voltage-dependent anion channels are dispensable for mitochondrial-dependent cell death. Nat Cell Biol 2007; 9: 550-555.
    • (2007) Nat Cell Biol , vol.9 , pp. 550-555
    • Baines, C.P.1    Kaiser, R.A.2    Sheik, T.3    Craigen, W.J.4    Molkentin, J.D.5
  • 94
    • 0034697365 scopus 로고    scopus 로고
    • Electrophysiological study of a novel large pore formed by Bax and the voltage-dependent anion channel that is permeable to cytochrome c
    • Shimizu S, Ide T, Yanagida T, Tsujimoto Y. Electrophysiological study of a novel large pore formed by Bax and the voltage-dependent anion channel that is permeable to cytochrome c. J Biol Chem 2000; 275: 12321-12325.
    • (2000) J Biol Chem , vol.275 , pp. 12321-12325
    • Shimizu, S.1    Ide, T.2    Yanagida, T.3    Tsujimoto, Y.4
  • 95
    • 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: 23152-23161.
    • (2012) J Biol Chem , vol.287 , pp. 23152-23161
    • Arbel, N.1    Ben-Hail, D.2    Shoshan-Barmatz, V.3
  • 96
    • 84884994343 scopus 로고    scopus 로고
    • VDAC1-based peptides: Novel pro-apoptotic agents and potential therapeutics for B-cell chronic lymphocytic leukemia
    • Prezma T, Shteinfer A, Admoni L, Raviv Z, Sela I, Levi I, Shoshan-Barmatz V. VDAC1-based peptides: Novel pro-apoptotic agents and potential therapeutics for B-cell chronic lymphocytic leukemia. Cell Death Dis 2013; 4: E809.
    • (2013) Cell Death Dis , vol.4 , pp. e809
    • Prezma, T.1    Shteinfer, A.2    Admoni, L.3    Raviv, Z.4    Sela, I.5    Levi, I.6    Shoshan-Barmatz, V.7
  • 97
    • 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: 4744-4756.
    • (2006) Oncogene , vol.25 , pp. 4744-4756
    • Brenner, C.1    Grimm, S.2
  • 98
    • 84883776628 scopus 로고    scopus 로고
    • The mitochondrial permeability transition pore: A mystery solved?
    • Bernardi P. The mitochondrial permeability transition pore: A mystery solved? Front Physiol 2013; 4: 95.
    • (2013) Front Physiol , vol.4 , pp. 95
    • Bernardi, P.1
  • 99
    • 0025905910 scopus 로고
    • The giant channel of the inner mitochondrial membrane is inhibited by cyclosporin A
    • Szabó I, Zoratti M. The giant channel of the inner mitochondrial membrane is inhibited by cyclosporin A. J Biol Chem 1991; 266: 3376-3379.
    • (1991) J Biol Chem , vol.266 , pp. 3376-3379
    • Szabó, I.1    Zoratti, M.2
  • 101
    • 77952671613 scopus 로고    scopus 로고
    • Signal transduction to the permeability transition pore
    • Rasola A, Sciacovelli M, Pantic B, Bernard P. Signal transduction to the permeability transition pore. FEBS Lett 2010; 584: 1989-1896.
    • (2010) FEBS Lett , vol.584 , pp. 1989-1896
    • Rasola, A.1    Sciacovelli, M.2    Pantic, B.3    Bernard, P.4
  • 102
    • 84858158689 scopus 로고    scopus 로고
    • SCaMC-1 promotes cancer cell survival by desensitizing mitochondrial permeability transition via ATP/ADP-mediated matrix Ca(2) buffering
    • Traba J, Del Arco A, Duchen MR, Szabadkai G, Satrú stegui J. SCaMC-1 promotes cancer cell survival by desensitizing mitochondrial permeability transition via ATP/ADP-mediated matrix Ca(2) buffering. Cell Death Differ 2012; 19: 650-660.
    • (2012) Cell Death Differ , vol.19 , pp. 650-660
    • Traba, J.1    Del Arco, A.2    Duchen, M.R.3    Szabadkai, G.4    Satrústegui, J.5
  • 104
    • 84871186542 scopus 로고    scopus 로고
    • Chemotherapeutic induction of mitochondrial oxidative stress activates GSK-3a/b and Bax, leading to permeability transition pore opening and tumor cell death
    • Chiara F, Gambalunga A, Sciacovelli M, Nicolli A, Ronconi L, Fregona D et al. Chemotherapeutic induction of mitochondrial oxidative stress activates GSK-3a/b and Bax, leading to permeability transition pore opening and tumor cell death. Cell Death Dis 2012; 3: E444.
    • (2012) Cell Death Dis , vol.3 , pp. e444
    • Chiara, F.1    Gambalunga, A.2    Sciacovelli, M.3    Nicolli, A.4    Ronconi, L.5    Fregona, D.6
  • 105
    • 84857782861 scopus 로고    scopus 로고
    • Pharmaceutical development of the novel arsenical based cancer therapeutic GSAO for Phase i clinical trial
    • Elliott MA, Ford SJ, Prasad E, Dick LJ, Farmer H, Hogg PJ et al. Pharmaceutical development of the novel arsenical based cancer therapeutic GSAO for Phase I clinical trial. Int J Pharm 2012; 426: 67-75.
    • (2012) Int J Pharm , vol.426 , pp. 67-75
    • Elliott, M.A.1    Ford, S.J.2    Prasad, E.3    Dick, L.J.4    Farmer, H.5    Hogg, P.J.6
  • 106
    • 84867722747 scopus 로고    scopus 로고
    • Physiological roles of the permeability transition pore
    • Brenner C, Moulin M. Physiological roles of the permeability transition pore. Circ Res 2012; 111: 1237-1247.
    • (2012) Circ Res , vol.111 , pp. 1237-1247
    • Brenner, C.1    Moulin, M.2
  • 107
    • 41949109107 scopus 로고    scopus 로고
    • Mitoparan and target-selective chimeric analogues: Membrane translocation and intracellular redistribution induces mitochondrial apoptosis
    • Jones S, Martel C, Belzacq-Casagrande AS, Brenner C, Howl J. Mitoparan and target-selective chimeric analogues: Membrane translocation and intracellular redistribution induces mitochondrial apoptosis. Biochim Biophys Acta 2008; 1783: 849-863.
    • (2008) Biochim Biophys Acta , vol.1783 , pp. 849-863
    • Jones, S.1    Martel, C.2    Belzacq-Casagrande, A.S.3    Brenner, C.4    Howl, J.5
  • 108
    • 0036177759 scopus 로고    scopus 로고
    • BMAP-28, an antibiotic peptide of innate immunity, induces cell death through opening of the mitochondrial permeability transition pore
    • Risso A, Braidot E, Sordano MC, Vianello A, Macr? F, Skerlavaj B et al. BMAP-28, an antibiotic peptide of innate immunity, induces cell death through opening of the mitochondrial permeability transition pore. Mol Cell Biol 2002; 22: 1926-1935.
    • (2002) Mol Cell Biol , vol.22 , pp. 1926-1935
    • Risso, A.1    Braidot, E.2    Sordano, M.C.3    Vianello, A.4    Macr, F.5    Skerlavaj, B.6
  • 109
    • 84856574356 scopus 로고    scopus 로고
    • Tuning the activity of mitochondria-penetrating peptides for delivery or disruption
    • Horton KL, Pereira MP, Stewart KM, Fonseca SB, Kelley SO. Tuning the activity of mitochondria-penetrating peptides for delivery or disruption. Chembiochem 2012; 13: 476-485.
    • (2012) Chembiochem , vol.13 , pp. 476-485
    • Horton, K.L.1    Pereira, M.P.2    Stewart, K.M.3    Fonseca, S.B.4    Kelley, S.O.5
  • 110
    • 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 USA 2010; 107: 726-731.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 726-731
    • Rasola, A.1    Sciacovelli, M.2    Chiara, F.3    Pantic, B.4    Brusilow, W.S.5    Bernardi, P.6
  • 111
    • 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.
    • (2013) Front Oncol , vol.3 , pp. 16
    • Chiara, F.1    Rasola, A.2
  • 112
    • 26244458767 scopus 로고    scopus 로고
    • Jasmonates-a new family of anti-cancer agents
    • Flescher E. Jasmonates-a new family of anti-cancer agents. Anticancer Drugs 2005; 16: 911-916.
    • (2005) Anticancer Drugs , vol.16 , pp. 911-916
    • Flescher, E.1
  • 113
    • 33845642967 scopus 로고    scopus 로고
    • Jasmonates in cancer therapy
    • Flescher E. Jasmonates in cancer therapy. Cancer Lett 2007; 245: 1-10.
    • (2007) Cancer Lett , vol.245 , pp. 1-10
    • Flescher, E.1
  • 115
    • 63649110495 scopus 로고    scopus 로고
    • Drugs targeting the mitochondrial pore act as cytotoxic and cytostatic agents in temozolomide-resistant glioma cells
    • Lena A, Rechichi M, Salvetti A, Bartoli B, Vecchio D, Scarcelli V et al. Drugs targeting the mitochondrial pore act as cytotoxic and cytostatic agents in temozolomide-resistant glioma cells. J Transl Med 2009; 7: 13.
    • (2009) J Transl Med , vol.7 , pp. 13
    • Lena, A.1    Rechichi, M.2    Salvetti, A.3    Bartoli, B.4    Vecchio, D.5    Scarcelli, V.6
  • 116
    • 79953803842 scopus 로고    scopus 로고
    • Targeting the mitochondrial permeability transition: Cardiac ischemia-reperfusion versus carcinogenesis
    • Javadov S, Hunter JC, Barreto-Torres G, Parodi-Rullan R. Targeting the mitochondrial permeability transition: Cardiac ischemia-reperfusion versus carcinogenesis. Cell Physiol Biochem 2011; 27: 179-190.
    • (2011) Cell Physiol Biochem , vol.27 , pp. 179-190
    • Javadov, S.1    Hunter, J.C.2    Barreto-Torres, G.3    Parodi-Rullan, R.4
  • 117
    • 35548974344 scopus 로고    scopus 로고
    • Mitochondrially targeted effects of berberine [Natural Yellow 18,5,6-dihydro-9,10-dimethoxybenzo(g)-1,3-benzodioxolo(5,6-a) quinolizinium] on K1735-M2 mouse melanoma cells: Comparison with direct effects on isolated mitochondrial fractions
    • Pereira GC, Branco AF, Matos JA, Pereira SL, Parke D, Perkins EL et al. Mitochondrially targeted effects of berberine [Natural Yellow 18, 5,6-dihydro-9,10-dimethoxybenzo(g)-1,3-benzodioxolo(5,6-a) quinolizinium] on K1735-M2 mouse melanoma cells: Comparison with direct effects on isolated mitochondrial fractions. J Pharmacol Exp Ther 2007; 323: 636-649.
    • (2007) J Pharmacol Exp Ther , vol.323 , pp. 636-649
    • Pereira, G.C.1    Branco, A.F.2    Matos, J.A.3    Pereira, S.L.4    Parke, D.5    Perkins, E.L.6
  • 118
    • 51849122083 scopus 로고    scopus 로고
    • Mechanisms of berberine (natural yellow 18)-induced mitochondrial dysfunction: Interaction with the adenine nucleotide translocator
    • Pereira CV, Machado NG, Oliveira PJ. Mechanisms of berberine (natural yellow 18)-induced mitochondrial dysfunction: Interaction with the adenine nucleotide translocator. Toxicol Sci 2008; 105: 408-417.
    • (2008) Toxicol Sci , vol.105 , pp. 408-417
    • Pereira, C.V.1    Machado, N.G.2    Oliveira, P.J.3
  • 119
    • 34250304602 scopus 로고    scopus 로고
    • Honokiol induces a necrotic cell death through the mitochondrial permeability transition pore
    • Li L, Han W, Gu Y, Qiu S, Lu Q, Jin J et al. Honokiol induces a necrotic cell death through the mitochondrial permeability transition pore. Cancer Res 2007; 67: 4894-4903.
    • (2007) Cancer Res , vol.67 , pp. 4894-4903
    • Li, L.1    Han, W.2    Gu, Y.3    Qiu, S.4    Lu, Q.5    Jin, J.6
  • 121
    • 68149156097 scopus 로고    scopus 로고
    • Involvement of mitochondrial permeability transition pore opening in alpha-bisabolol induced apoptosis
    • Cavalieri E, Bergamini C, Mariotto S, Leoni S, Perbellini L, Darra E et al. Involvement of mitochondrial permeability transition pore opening in alpha-bisabolol induced apoptosis. FEBS J 2009; 276: 3990-4000.
    • (2009) FEBS J , vol.276 , pp. 3990-4000
    • Cavalieri, E.1    Bergamini, C.2    Mariotto, S.3    Leoni, S.4    Perbellini, L.5    Darra, E.6
  • 122
    • 34250748014 scopus 로고    scopus 로고
    • Shikonin circumvents cancer drug resistance by induction of a necroptotic death
    • Han W, Li L, Qiu S, Lu Q, Pan Q, Gu Y et al. Shikonin circumvents cancer drug resistance by induction of a necroptotic death. Mol Cancer Ther 2007; 6: 1641-1649.
    • (2007) Mol Cancer Ther , vol.6 , pp. 1641-1649
    • Han, W.1    Li, L.2    Qiu, S.3    Lu, Q.4    Pan, Q.5    Gu, Y.6
  • 123
    • 0024360271 scopus 로고
    • Cyclosporin A is a potent inhibitor of the inner membrane permeability transition in liver mitochondria
    • Broekemeier KM, Dempsey ME, Pfeiffer DR. Cyclosporin A is a potent inhibitor of the inner membrane permeability transition in liver mitochondria. J Biol Chem 1989; 264: 7826-7830.
    • (1989) J Biol Chem , vol.264 , pp. 7826-7830
    • Broekemeier, K.M.1    Dempsey, M.E.2    Pfeiffer, D.R.3
  • 124
    • 0023821864 scopus 로고
    • Inhibition by cyclosporin A of a Ca2-dependent pore in heart mitochondria activated by inorganic phosphate and oxidative stress
    • Crompton M, Ellinger H, Costi A. Inhibition by cyclosporin A of a Ca2-dependent pore in heart mitochondria activated by inorganic phosphate and oxidative stress. Biochem. J 1988; 255: 357-360.
    • (1988) Biochem. J , vol.255 , pp. 357-360
    • Crompton, M.1    Ellinger, H.2    Costi, A.3
  • 125
    • 0023263612 scopus 로고
    • Action of cyclosporine on mitochondrial calcium fluxes
    • Fournier N, Ducet G, Crevat A. Action of cyclosporine on mitochondrial calcium fluxes. J Bioenerg Biomembr 1987; 19: 297-303.
    • (1987) J Bioenerg Biomembr , vol.19 , pp. 297-303
    • Fournier, N.1    Ducet, G.2    Crevat, A.3
  • 126
    • 76049119424 scopus 로고    scopus 로고
    • Cyclosporine A suppresses keratinocyte cell death through MMPTP inhibition in a model for skin cancer in organ transplant recipients
    • Norman KG, Canter JA, Shi M, Milne GL, Morrow JD, Sligh JE. Cyclosporine A suppresses keratinocyte cell death through MMPTP inhibition in a model for skin cancer in organ transplant recipients. Mitochondrion 2010; 10: 94-101.
    • (2010) Mitochondrion , vol.10 , pp. 94-101
    • Norman, K.G.1    Canter, J.A.2    Shi, M.3    Milne, G.L.4    Morrow, J.D.5    Sligh, J.E.6
  • 128
    • 77953758600 scopus 로고    scopus 로고
    • Role of Kv1.3 mitochondrial potassium channel in apoptotic signalling in lymphocytes
    • Gulbins E, Sassi N, Grassmè H, Zoratti M, Szabò I. Role of Kv1.3 mitochondrial potassium channel in apoptotic signalling in lymphocytes. Biochim Biophys Acta 2010; 1797: 1251-1259.
    • (2010) Biochim Biophys Acta , vol.1797 , pp. 1251-1259
    • Gulbins, E.1    Sassi, N.2    Grassmè, H.3    Zoratti, M.4    Szabò, I.5
  • 129
    • 51149089082 scopus 로고    scopus 로고
    • Mitochondrial potassium channel Kv1.3 mediates Bax-induced apoptosis in lymphocytes
    • Szabó I, Bock J, Grassmé H, Soddemann M, Wilker B, Lang F et al. Mitochondrial potassium channel Kv1.3 mediates Bax-induced apoptosis in lymphocytes. Proc Natl Acad Sci USA 2008; 105: 14861-14866.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 14861-14866
    • Szabó, I.1    Bock, J.2    Grassmé, H.3    Soddemann, M.4    Wilker, B.5    Lang, F.6
  • 130
    • 79951681014 scopus 로고    scopus 로고
    • Single-point mutations of a lysine residue change function of Bax and Bcl-xL expressed in Bax-and Bakless mouse embryonic fibroblasts: Novel insights into the molecular mechanisms of Bax-induced apoptosis
    • Szabò I, Soddemann M, Leanza L, Zoratti M, Gulbins E. Single-point mutations of a lysine residue change function of Bax and Bcl-xL expressed in Bax-and Bakless mouse embryonic fibroblasts: Novel insights into the molecular mechanisms of Bax-induced apoptosis. Cell Death Differ 2011; 18: 427-438.
    • (2011) Cell Death Differ , vol.18 , pp. 427-438
    • Szabò, I.1    Soddemann, M.2    Leanza, L.3    Zoratti, M.4    Gulbins, E.5
  • 131
    • 21844464054 scopus 로고    scopus 로고
    • Bax forms multispanning monomers that oligomerize to permeabilize membranes during apoptosis
    • Annis MG, Soucie EL, Dlugosz PJ, Cruz-Aguado JA, Penn LZ, Leber B et al. Bax forms multispanning monomers that oligomerize to permeabilize membranes during apoptosis. EMBO J 24: 2096-2103.
    • EMBO J , vol.24 , pp. 2096-2103
    • Annis, M.G.1    Soucie, E.L.2    Dlugosz, P.J.3    Cruz-Aguado, J.A.4    Penn, L.Z.5    Leber, B.6
  • 132
    • 84870410761 scopus 로고    scopus 로고
    • Induction of apoptosis in macrophages via Kv1.3 and Kv1.5 potassium channels
    • Leanza L, Zoratti M, Gulbins E, Szabò I. Induction of apoptosis in macrophages via Kv1.3 and Kv1.5 potassium channels. Curr Med Chem 2012; 19: 5394-5404.
    • (2012) Curr Med Chem , vol.19 , pp. 5394-5404
    • Leanza, L.1    Zoratti, M.2    Gulbins, E.3    Szabò, I.4
  • 133
    • 84863473765 scopus 로고    scopus 로고
    • Inhibitors of mitochondrial Kv1.3 channels induce Bax/Bak-independent death of cancer cells
    • Leanza L, Henry B, Sassi N, Zoratti M, Chandy KG, Gulbins E et al. Inhibitors of mitochondrial Kv1.3 channels induce Bax/Bak-independent death of cancer cells. EMBO Mol Med 2012; 4: 577-593.
    • (2012) EMBO Mol Med , vol.4 , pp. 577-593
    • Leanza, L.1    Henry, B.2    Sassi, N.3    Zoratti, M.4    Chandy, K.G.5    Gulbins, E.6
  • 134
    • 84881479922 scopus 로고    scopus 로고
    • Clofazimine, Psora-4 and PAP-1, inhibitors of the potassium channel Kv1.3, as a new and selective therapeutic strategy in chronic lymphocytic leukemia
    • Leanza L, Trentin L, Becker KA, Frezzato F, Zoratti M, Semenzato G et al. Clofazimine, Psora-4 and PAP-1, inhibitors of the potassium channel Kv1.3, as a new and selective therapeutic strategy in chronic lymphocytic leukemia. Leukemia 2013; 27: 1782-1785.
    • (2013) Leukemia , vol.27 , pp. 1782-1785
    • Leanza, L.1    Trentin, L.2    Becker, K.A.3    Frezzato, F.4    Zoratti, M.5    Semenzato, G.6
  • 135
    • 67650071137 scopus 로고    scopus 로고
    • Targeting cancer cells by ROS-mediated mechanisms: A radical therapeutic approach?
    • Trachootham D, Alexandre J, Huang P. Targeting cancer cells by ROS-mediated mechanisms: A radical therapeutic approach? Nat Rev Drug Discov 2009; 8: 579-591.
    • (2009) Nat Rev Drug Discov , vol.8 , pp. 579-591
    • Trachootham, D.1    Alexandre, J.2    Huang, P.3
  • 136
    • 0141509869 scopus 로고    scopus 로고
    • Inhibition of mitochondrial respiration: A novel strategy to enhance drug-induced apoptosis in human leukemia cells by a reactive oxygen species-mediated mechanism
    • Pelicano H, Feng L, Zhou Y, Carew JS, Hileman EO, Plunkett W et al. Inhibition of mitochondrial respiration: A novel strategy to enhance drug-induced apoptosis in human leukemia cells by a reactive oxygen species-mediated mechanism. J Biol Chem 2003; 278: 37832-37839.
    • (2003) J Biol Chem , vol.278 , pp. 37832-37839
    • Pelicano, H.1    Feng, L.2    Zhou, Y.3    Carew, J.S.4    Hileman, E.O.5    Plunkett, W.6
  • 137
    • 58049211941 scopus 로고    scopus 로고
    • Clofazimine inhibits human Kv1.3 potassium channel by perturbing calcium oscillation in T lymphocytes
    • Ren YR, Pan F, Parvez S, Fleig A, Chong CR, Xu J et al. Clofazimine inhibits human Kv1.3 potassium channel by perturbing calcium oscillation in T lymphocytes. PLoS One 2008; 3: E4009.
    • (2008) PLoS One , vol.3 , pp. e4009
    • Ren, Y.R.1    Pan, F.2    Parvez, S.3    Fleig, A.4    Chong, C.R.5    Xu, J.6
  • 138
    • 84857771935 scopus 로고    scopus 로고
    • Targeting the voltage-dependent K() channels Kv1.3 and Kv1.5 as tumor biomarkers for cancer detection and prevention
    • Felipe A, Bielanska J, Comes N, Vallejo A, Roig S, Ramón Y, Cajal S et al. Targeting the voltage-dependent K() channels Kv1.3 and Kv1.5 as tumor biomarkers for cancer detection and prevention. Curr Med Chem 2012; 19: 661-674.
    • (2012) Curr Med Chem , vol.19 , pp. 661-674
    • Felipe, A.1    Bielanska, J.2    Comes, N.3    Vallejo, A.4    Roig, S.5    Ramón, Y.6    Cajal, S.7
  • 139
    • 84892959692 scopus 로고    scopus 로고
    • Correlation between potassium channel expression and sensitivity to drug-induced cell death in tumor cell lines
    • PMID:23701546
    • Leanza L, O' Reilly P, Doyle A, Venturini E, Zoratti M, Szegezdi E et al. Correlation between potassium channel expression and sensitivity to drug-induced cell death in tumor cell lines. Curr Pharm Des 2013; PMID:23701546.
    • (2013) Curr Pharm des
    • Leanza, L.1    O'Reilly, P.2    Doyle, A.3    Venturini, E.4    Zoratti, M.5    Szegezdi, E.6
  • 140
    • 84884843703 scopus 로고    scopus 로고
    • A diterpenoid derivate compound targets selenocysteine of thioredoxin reductases and induces bax/bak-independent apoptosis
    • Liu J, Mu C, Yue W, Li J, Ma B, Zhao L et al. A diterpenoid derivate compound targets selenocysteine of Thioredoxin Reductases and induces Bax/Bak-independent apoptosis. Free Radic Biol Med 2013; 63: 485-494.
    • (2013) Free Radic Biol Med , vol.63 , pp. 485-494
    • Liu, J.1    Mu, C.2    Yue, W.3    Li, J.4    Ma, B.5    Zhao, L.6
  • 141
    • 84855425097 scopus 로고    scopus 로고
    • Phenylarsine oxide induces apoptosis in Bax-and Bak-deficient cells through upregulation of Bim
    • Ni B, Ma Q, Li B, Zhao L, Liu Y, Zhu Y, Chen Q. Phenylarsine oxide induces apoptosis in Bax-and Bak-deficient cells through upregulation of Bim. Clin Cancer Res 2012; 18: 140-145.
    • (2012) Clin Cancer Res , vol.18 , pp. 140-145
    • Ni, B.1    Ma, Q.2    Li, B.3    Zhao, L.4    Liu, Y.5    Zhu, Y.6    Chen, Q.7
  • 142
    • 33845603436 scopus 로고    scopus 로고
    • Gossypol induces Bax/Bakindependent activation of apoptosis and cytochrome c release via a conformational change in Bcl-2
    • Lei X, Chen Y, Du G, Yu W, Wang X, Qu H et al. Gossypol induces Bax/Bakindependent activation of apoptosis and cytochrome c release via a conformational change in Bcl-2. FASEB J 2006; 20: 2147-2149.
    • (2006) FASEB J , vol.20 , pp. 2147-2149
    • Lei, X.1    Chen, Y.2    Du, G.3    Yu, W.4    Wang, X.5    Qu, H.6
  • 143
    • 0036131142 scopus 로고    scopus 로고
    • Tumor-cell resistance to death receptor-induced apoptosis through mutational inactivation of the proapoptotic Bcl-2 homolog Bax
    • LeBlanc H, Lawrence D, Varfolomeev E, Totpal K, Morlan J, Schow P et al. Tumor-cell resistance to death receptor-induced apoptosis through mutational inactivation of the proapoptotic Bcl-2 homolog Bax. Nat Med 2002; 8: 274-281.
    • (2002) Nat Med , vol.8 , pp. 274-281
    • Leblanc, H.1    Lawrence, D.2    Varfolomeev, E.3    Totpal, K.4    Morlan, J.5    Schow, P.6
  • 144
    • 0030938089 scopus 로고    scopus 로고
    • Bax-deficiency promotes drug resistance and oncogenic transformation by attenuating p53-dependent apoptosis
    • McCurrach ME, Connor TM, Knudson CM, Korsmeyer SJ, Lowe SW. Bax-deficiency promotes drug resistance and oncogenic transformation by attenuating p53-dependent apoptosis. Proc Natl Acad Sci USA 1997; 94: 2345-2349.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 2345-2349
    • McCurrach, M.E.1    Connor, T.M.2    Knudson, C.M.3    Korsmeyer, S.J.4    Lowe, S.W.5
  • 146
    • 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 USA 2000; 97: 10872-10877.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 10872-10877
    • Ionov, Y.1    Yamamoto, H.2    Krajewski, S.3    Reed, J.C.4    Perucho, M.5
  • 147
    • 77953777012 scopus 로고    scopus 로고
    • An investigation of the occurrence and properties of the mitochondrial intermediate conductance Ca2-activated K channel mtKCa3.1
    • Sassi N, De Marchi U, Fioretti B, Biasutto L, Gulbins E, Francolini F et al. An investigation of the occurrence and properties of the mitochondrial intermediate conductance Ca2-activated K channel mtKCa3.1. Biochim Biophys Acta Bioenergetics 2010; 1797: 1260-1267.
    • (2010) Biochim Biophys Acta Bioenergetics , vol.1797 , pp. 1260-1267
    • Sassi, N.1    De Marchi, U.2    Fioretti, B.3    Biasutto, L.4    Gulbins, E.5    Francolini, F.6
  • 148
    • 84870201962 scopus 로고    scopus 로고
    • Protection against cardiac injury by small Ca(2)-sensitive K() channels identified in guinea pig cardiac inner mitochondrial membrane
    • 2013
    • Stowe DF, Gadicherla AK, Zhou Y, Aldakkak M, Cheng Q, Kwok WM et al. Protection against cardiac injury by small Ca(2)-sensitive K() channels identified in guinea pig cardiac inner mitochondrial membrane. Biochim Biophys Acta 2013; 1828: 427-442 2013.
    • (2013) Biochim Biophys Acta , vol.1828 , pp. 427-442
    • Stowe, D.F.1    Gadicherla, A.K.2    Zhou, Y.3    Aldakkak, M.4    Cheng, Q.5    Kwok, W.M.6
  • 149
    • 84876209070 scopus 로고    scopus 로고
    • Mitochondrial small conductance SK2 channels prevent glutamate-induced oxytosis and mitochondrial dysfunction
    • Dolga AM, Netter MF, Perocchi F, Doti N, Meissner L, Tobaben S et al. Mitochondrial small conductance SK2 channels prevent glutamate-induced oxytosis and mitochondrial dysfunction. J Biol Chem 2013; 288: 10792-10804.
    • (2013) J Biol Chem , vol.288 , pp. 10792-10804
    • Dolga, A.M.1    Netter, M.F.2    Perocchi, F.3    Doti, N.4    Meissner, L.5    Tobaben, S.6
  • 150
    • 84870373756 scopus 로고    scopus 로고
    • Intracellular BK(Ca) (iBK(Ca)) channels
    • Singh H, Stefani E, Toro L. Intracellular BK(Ca) (iBK(Ca)) channels. J Physiol 2012; 23: 5937-5947.
    • (2012) J Physiol , vol.23 , pp. 5937-5947
    • Singh, H.1    Stefani, E.2    Toro, L.3
  • 152
    • 84864468399 scopus 로고    scopus 로고
    • The potassium channel opener CGS7184 activates Ca2 release from the endoplasmic reticulum
    • Wrzosek A, Tomaskova Z, Ondrias K, Lukasiak A, Szewczyk A. The potassium channel opener CGS7184 activates Ca2 release from the endoplasmic reticulum. Eur J Pharmacol 2012; 690: 60-67.
    • (2012) Eur J Pharmacol , vol.690 , pp. 60-67
    • Wrzosek, A.1    Tomaskova, Z.2    Ondrias, K.3    Lukasiak, A.4    Szewczyk, A.5
  • 153
    • 41049085767 scopus 로고    scopus 로고
    • Mitochondrial expression of the two-pore domain TASK-3 channels in malignantly transformed and non-malignant human cells
    • Rusznák Z, Bakondi G, Kosztka L, Pocsai K, Dienes B, Fodor J et al. Mitochondrial expression of the two-pore domain TASK-3 channels in malignantly transformed and non-malignant human cells. Virchows Arch 2008; 452: 415-426.
    • (2008) Virchows Arch , vol.452 , pp. 415-426
    • Rusznák, Z.1    Bakondi, G.2    Kosztka, L.3    Pocsai, K.4    Dienes, B.5    Fodor, J.6
  • 154
    • 18744406306 scopus 로고    scopus 로고
    • TASK-3 immunoreactivity is present but shows differential distribution in the human gastrointestinal tract
    • Kovács I, Pocsai K, Czifra G, Sarkadi L, Szü cs G, Nemes Z et al. TASK-3 immunoreactivity is present but shows differential distribution in the human gastrointestinal tract. Virchows Arch 2005; 446: 402-410.
    • (2005) Virchows Arch , vol.446 , pp. 402-410
    • Kovács, I.1    Pocsai, K.2    Czifra, G.3    Sarkadi, L.4    Szücs, G.5    Nemes, Z.6
  • 155
    • 79960729426 scopus 로고    scopus 로고
    • Inhibition of TASK-3 (KCNK9) channel biosynthesis changes cell morphology and decreases both DNA content and mitochondrial function of melanoma cells maintained in cell culture
    • Kosztka L, Rusznák Z, Nagy D, Nagy Z, Fodor J, Szucs G et al. Inhibition of TASK-3 (KCNK9) channel biosynthesis changes cell morphology and decreases both DNA content and mitochondrial function of melanoma cells maintained in cell culture. Melanoma Res 2011; 21: 308-322.
    • (2011) Melanoma Res , vol.21 , pp. 308-322
    • Kosztka, L.1    Rusznák, Z.2    Nagy, D.3    Nagy, Z.4    Fodor, J.5    Szucs, G.6
  • 157
    • 84863163077 scopus 로고    scopus 로고
    • Reduction of breast cancer cell migration via up-regulation of TASK-3 two-pore domain K channel
    • Lee GW, Park HS, Kim EJ, Cho YW, Kim GT, Mun YJ et al. Reduction of breast cancer cell migration via up-regulation of TASK-3 two-pore domain K channel. Acta Physiol 2012; 204: 513-524.
    • (2012) Acta Physiol , vol.204 , pp. 513-524
    • Lee, G.W.1    Park, H.S.2    Kim, E.J.3    Cho, Y.W.4    Kim, G.T.5    Mun, Y.J.6
  • 158
    • 84876762744 scopus 로고    scopus 로고
    • Expression and prognostic significance of the oncogenic K2P potassium channel KCNK9 (TASK-3) in ovarian carcinoma
    • Innamaa A, Jackson L, Asher V, Van Shalkwyk G, Warren A, Hay D et al. Expression and prognostic significance of the oncogenic K2P potassium channel KCNK9 (TASK-3) in ovarian carcinoma. Anticancer Res 2013; 33: 1401-1408.
    • (2013) Anticancer Res , vol.33 , pp. 1401-1408
    • Innamaa, A.1    Jackson, L.2    Asher, V.3    Van Shalkwyk, G.4    Warren, A.5    Hay, D.6
  • 159
    • 84867564026 scopus 로고    scopus 로고
    • Mechanism of fatty-acid-dependent UCP1 uncoupling in brown fat mitochondria
    • Fedorenko A, Lishko PV, Kirichok Y. Mechanism of fatty-acid-dependent UCP1 uncoupling in brown fat mitochondria. Cell 2012; 151: 400-413.
    • (2012) Cell , vol.151 , pp. 400-413
    • Fedorenko, A.1    Lishko, P.V.2    Kirichok, Y.3
  • 160
    • 84861134135 scopus 로고    scopus 로고
    • Toward understanding the mechanism of ion transport activity of neuronal uncoupling proteins UCP2,UCP4, and UCP5
    • Hoang T, Smith MD, Jelokhani-Niaraki M. Toward understanding the mechanism of ion transport activity of neuronal uncoupling proteins UCP2, UCP4, and UCP5. Biochemistry 2012; 51: 4004-4014.
    • (2012) Biochemistry , vol.51 , pp. 4004-4014
    • Hoang, T.1    Smith, M.D.2    Jelokhani-Niaraki, M.3
  • 161
    • 0347989317 scopus 로고    scopus 로고
    • Brown adipose tissue: Function and physiological significance
    • Cannon B, Nedergaard J. Brown adipose tissue: Function and physiological significance. Physiol Rev 2004; 84: 277-359.
    • (2004) Physiol Rev , vol.84 , pp. 277-359
    • Cannon, B.1    Nedergaard, J.2
  • 162
    • 77949913600 scopus 로고    scopus 로고
    • Uncoupling protein-2 and cancer
    • Baffy G. Uncoupling protein-2 and cancer. Mitochondrion 2010; 10: 243-252.
    • (2010) Mitochondrion , vol.10 , pp. 243-252
    • Baffy, G.1
  • 163
    • 80051578926 scopus 로고    scopus 로고
    • Mitochondrial recoupling a novel therapeutic strategy for cancer?
    • Baffy G, Derdak Z, Robson SC. Mitochondrial recoupling: A novel therapeutic strategy for cancer? Br J Cancer 2011; 105: 469-474.
    • (2011) Br J Cancer , vol.105 , pp. 469-474
    • Baffy, G.1    Derdak, Z.2    Robson, S.C.3
  • 165
    • 0033667705 scopus 로고    scopus 로고
    • Disruption of the uncoupling protein-2 gene in mice reveals a role in immunity and reactive oxygen species production
    • Arsenijevic D, Onuma H, Pecqueur C, Raimbault S, Manning BS, Miroux B et al. Disruption of the uncoupling protein-2 gene in mice reveals a role in immunity and reactive oxygen species production. Nat Genet 2000; 26: 435-439.
    • (2000) Nat Genet , vol.26 , pp. 435-439
    • Arsenijevic, D.1    Onuma, H.2    Pecqueur, C.3    Raimbault, S.4    Manning, B.S.5    Miroux, B.6
  • 166
    • 42349088894 scopus 로고    scopus 로고
    • The mitochondrial uncoupling protein-2 promotes chemoresistance in cancer cells
    • Derdak Z, Mark NM, Beldi G, Robson SC, Wands JR, Baffy G. The mitochondrial uncoupling protein-2 promotes chemoresistance in cancer cells. Cancer Res 2008; 68: 2813-2819.
    • (2008) Cancer Res , vol.68 , pp. 2813-2819
    • Derdak, Z.1    Mark, N.M.2    Beldi, G.3    Robson, S.C.4    Wands, J.R.5    Baffy, G.6
  • 167
    • 48549088300 scopus 로고    scopus 로고
    • The Warburg effect in leukemia-stroma cocultures is mediated by mitochondrial uncoupling associated with uncoupling protein 2 activation
    • Samudio I, Fiegl M, McQueen T, Clise-Dwyer K, Andreeff M. The Warburg effect in leukemia-stroma cocultures is mediated by mitochondrial uncoupling associated with uncoupling protein 2 activation. Cancer Res 2008; 68: 5198-5205.
    • (2008) Cancer Res , vol.68 , pp. 5198-5205
    • Samudio, I.1    Fiegl, M.2    McQueen, T.3    Clise-Dwyer, K.4    Andreeff, M.5
  • 168
    • 80052848190 scopus 로고    scopus 로고
    • Cellular model of Warburg effect identifies tumor promoting function of UCP2 in breast cancer and its suppression by genipin
    • Ayyasamy V, Owens KM, Desouki MM, Liang P, Bakin A, Thangaraj K et al. Cellular model of Warburg effect identifies tumor promoting function of UCP2 in breast cancer and its suppression by genipin. PLoS One 2011; 6: E24792.
    • (2011) PLoS One , vol.6 , pp. e24792
    • Ayyasamy, V.1    Owens, K.M.2    Desouki, M.M.3    Liang, P.4    Bakin, A.5    Thangaraj, K.6
  • 169
    • 84872326962 scopus 로고    scopus 로고
    • Mitochondrial dysfunction in breast cancer cells prevents tumor growth: Understanding chemoprevention with metformin
    • Sanchez-Alvarez R, Martinez-Outschoorn UE, Lamb R, Hulit J, Howell A, Gandara R et al. Mitochondrial dysfunction in breast cancer cells prevents tumor growth: Understanding chemoprevention with metformin. Cell Cycle 2013; 12: 172-182.
    • (2013) Cell Cycle , vol.12 , pp. 172-182
    • Sanchez-Alvarez, R.1    Martinez-Outschoorn, U.E.2    Lamb, R.3    Hulit, J.4    Howell, A.5    Gandara, R.6
  • 170
    • 80051936634 scopus 로고    scopus 로고
    • A forty-kilodalton protein of the inner membrane is the mitochondrial calcium uniporter
    • De Stefani D, Raffaello A, Teardo E, Szabò I, Rizzuto R. A forty-kilodalton protein of the inner membrane is the mitochondrial calcium uniporter. Nature 2011; 476: 336-340.
    • (2011) Nature , vol.476 , pp. 336-340
    • De Stefani, D.1    Raffaello, A.2    Teardo, E.3    Szabò, I.4    Rizzuto, R.5
  • 171
    • 80051946060 scopus 로고    scopus 로고
    • Integrative genomics identifies MCU as an essential component of the mitochondrial calcium uniporter
    • Baughman JM, Perocchi F, Girgis HS, Plovanich M, Belcher-Timme CA, Sancak Y et al. Integrative genomics identifies MCU as an essential component of the mitochondrial calcium uniporter. Nature 2011; 476: 341-345.
    • (2011) Nature , vol.476 , pp. 341-345
    • Baughman, J.M.1    Perocchi, F.2    Girgis, H.S.3    Plovanich, M.4    Belcher-Timme, C.A.5    Sancak, Y.6
  • 172
    • 0035355341 scopus 로고    scopus 로고
    • The Ca2 concentration of the endoplasmic reticulum is a key determinant of ceramideinduced 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 ceramideinduced apoptosis: Significance for the molecular mechanism of Bcl-2 action. EMBO J 2001; 20: 2690-2701.
    • (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
  • 173
    • 84868027665 scopus 로고    scopus 로고
    • MICU1 is an essential gatekeeper for MCU-mediated mitochondrial Ca(2) uptake that regulates cell survival
    • Mallilankaraman K, Doonan P, Cárdenas C, Chandramoorthy HC, Mü ller M, Miller R et al. MICU1 is an essential gatekeeper for MCU-mediated mitochondrial Ca(2) uptake that regulates cell survival. Cell 2012; 151: 630-644.
    • (2012) Cell , vol.151 , pp. 630-644
    • Mallilankaraman, K.1    Doonan, P.2    Cárdenas, C.3    Chandramoorthy, H.C.4    Müller, M.5    Miller, R.6
  • 174
    • 84883286784 scopus 로고    scopus 로고
    • The mitochondrial calcium uniporter is a multimer that can include a dominantnegative pore-forming subunit
    • Raffaello A, De Stefani D, Sabbadin D, Teardo E, Merli G, Picard A et al. The mitochondrial calcium uniporter is a multimer that can include a dominantnegative pore-forming subunit. EMBO J 2013; 32: 2362-2376.
    • (2013) EMBO J , vol.32 , pp. 2362-2376
    • Raffaello, A.1    De Stefani, D.2    Sabbadin, D.3    Teardo, E.4    Merli, G.5    Picard, A.6
  • 175
  • 176
    • 84880471564 scopus 로고    scopus 로고
    • Mitochondrial calcium uniporter silencing potentiates caspase-independent cell death in MDA-MB-231 breast cancer cells
    • Curry MC, Peters AA, Kenny PA, Roberts-Thomson SJ, Monteith GR. Mitochondrial calcium uniporter silencing potentiates caspase-independent cell death in MDA-MB-231 breast cancer cells. Biochem Biophys Res Commun 2013; 434: 695-700.
    • (2013) Biochem Biophys Res Commun , vol.434 , pp. 695-700
    • Curry, M.C.1    Peters, A.A.2    Kenny, P.A.3    Roberts-Thomson, S.J.4    Monteith, G.R.5
  • 177
    • 84879043626 scopus 로고    scopus 로고
    • Probing novel roles of the mitochondrial uniporter in ovarian cancer cells using nanoparticles
    • Arvizo RR, Moyano DF, Saha S, Thompson MA, Bhattacharya R, Rotello VM et al. Probing novel roles of the mitochondrial uniporter in ovarian cancer cells using nanoparticles. J Biol Chem 2013; 288: 17610-17618.
    • (2013) J Biol Chem , vol.288 , pp. 17610-17618
    • Arvizo, R.R.1    Moyano, D.F.2    Saha, S.3    Thompson, M.A.4    Bhattacharya, R.5    Rotello, V.M.6
  • 178
    • 84880910816 scopus 로고    scopus 로고
    • Assessment of gene expression of intracellular calcium channels, pumps and exchangers with epidermal growth factor-induced epithelial-mesenchymal transition in a breast cancer cell line
    • Davis FM, Parsonage MT, Cabot PJ, Parat MO, Thompson EW, Roberts-Thomson SJ et al. Assessment of gene expression of intracellular calcium channels, pumps and exchangers with epidermal growth factor-induced epithelial-mesenchymal transition in a breast cancer cell line. Cancer Cell Int 2013; 13: 76.
    • (2013) Cancer Cell Int , vol.13 , pp. 76
    • Davis, F.M.1    Parsonage, M.T.2    Cabot, P.J.3    Parat, M.O.4    Thompson, E.W.5    Roberts-Thomson, S.J.6
  • 179
    • 84891393224 scopus 로고    scopus 로고
    • The physiological role of mitochondrial calcium revealed by mice lacking the mitochondrial calcium uniporter
    • Pan X, Liu J, Nguyen T, Liu C, Sun J, Teng Y et al. The physiological role of mitochondrial calcium revealed by mice lacking the mitochondrial calcium uniporter. Nat Cell Biol 2013; 15: 1464-1472.
    • (2013) Nat Cell Biol , vol.15 , pp. 1464-1472
    • Pan, X.1    Liu, J.2    Nguyen, T.3    Liu, C.4    Sun, J.5    Teng, Y.6
  • 181
    • 84879052051 scopus 로고    scopus 로고
    • MCU encodes the pore conducting mitochondrial calcium currents
    • Chaudhuri D, Sancak Y, Mootha VK, Clapham DE. MCU encodes the pore conducting mitochondrial calcium currents. Elife 2013; 2: E00704.
    • (2013) Elife , vol.2 , pp. e00704
    • Chaudhuri, D.1    Sancak, Y.2    Mootha, V.K.3    De, C.4
  • 182
    • 84873572862 scopus 로고    scopus 로고
    • MICU2, a paralog of MICU1, resides within the mitochondrial uniporter complex to regulate calcium handling
    • Plovanich M, Bogorad RL, Sancak Y, Kamer KJ, Strittmatter L, Li AA et al. MICU2, a paralog of MICU1, resides within the mitochondrial uniporter complex to regulate calcium handling. PLoS One 2013; 8: E55785.
    • (2013) PLoS One , vol.8 , pp. e55785
    • Plovanich, M.1    Bogorad, R.L.2    Sancak, Y.3    Kamer, K.J.4    Strittmatter, L.5    Li, A.A.6
  • 183
    • 84883768240 scopus 로고    scopus 로고
    • Intracellular ASIC1a regulates mitochondrial permeability transition-dependent neuronal death
    • Wang YZ, Zeng WZ, Xiao X, Huang Y, Song XL, Yu Z et al. Intracellular ASIC1a regulates mitochondrial permeability transition-dependent neuronal death. Cell Death Differ 2013; 20: 1359-1369.
    • (2013) Cell Death Differ , vol.20 , pp. 1359-1369
    • Wang, Y.Z.1    Zeng, W.Z.2    Xiao, X.3    Huang, Y.4    Song, X.L.5    Yu, Z.6
  • 184
    • 36849009834 scopus 로고    scopus 로고
    • Acidsensing ion channel-1 contributes to axonal degeneration in autoimmune inflammation of the central nervous system
    • Friese MA, Craner MJ, Etzensperger R, Vergo S, Wemmie JA, Welsh MJ et al. Acidsensing ion channel-1 contributes to axonal degeneration in autoimmune inflammation of the central nervous system. Nat Med 2007; 13: 1483-1489.
    • (2007) Nat Med , vol.13 , pp. 1483-1489
    • Friese, M.A.1    Craner, M.J.2    Etzensperger, R.3    Vergo, S.4    Wemmie, J.A.5    Welsh, M.J.6
  • 185
    • 84884302148 scopus 로고    scopus 로고
    • Expression profiling of ion channel genes predicts clinical outcome in breast cancer
    • Ko JH, Ko EA, Gu W, Lim I, Bang H, Zhou T. Expression profiling of ion channel genes predicts clinical outcome in breast cancer. Mol Cancer 2013; 12: 106.
    • (2013) Mol Cancer , vol.12 , pp. 106
    • Ko, J.H.1    Ko, E.A.2    Gu, W.3    Lim, I.4    Bang, H.5    Zhou, T.6
  • 186
    • 80155167926 scopus 로고    scopus 로고
    • Mitochondria-targeted small molecule therapeutics and probes
    • Smith RA, Hartley RC, Murphy MP. Mitochondria-targeted small molecule therapeutics and probes. Antioxid Redox Signal 2011; 15: 3021-3038.
    • (2011) Antioxid Redox Signal , vol.15 , pp. 3021-3038
    • Smith, R.A.1    Hartley, R.C.2    Murphy, M.P.3
  • 188
    • 84883814194 scopus 로고    scopus 로고
    • Classification of mitocans, anti-cancer drugs acting on mitochondria
    • Neuzil J, Dong LF, Rohlena J, Truksa J, Ralph SJ. Classification of mitocans, anti-cancer drugs acting on mitochondria. Mitochondrion 2013; 13: 199-208.
    • (2013) Mitochondrion , vol.13 , pp. 199-208
    • Neuzil, J.1    Dong, L.F.2    Rohlena, J.3    Truksa, J.4    Ralph, S.J.5
  • 192
    • 0026235940 scopus 로고
    • Clinical trial on the effects of shikonin mixture on later stage lung cancer
    • Guo XP, Zhang XY, Zhang SD. Clinical trial on the effects of shikonin mixture on later stage lung cancer. Zhong Xi Yi Jie He Za Zhi 1991; 11: 598-599.
    • (1991) Zhong Xi Yi Jie He Za Zhi , vol.11 , pp. 598-599
    • Guo, X.P.1    Zhang, X.Y.2    Zhang, S.D.3
  • 193
    • 29144474358 scopus 로고    scopus 로고
    • Clinical relevance of ion channels for diagnosis and therapy of cancer
    • Schonherr R. Clinical relevance of ion channels for diagnosis and therapy of cancer. J Membr Biol 2005; 205: 175-184.
    • (2005) J Membr Biol , vol.205 , pp. 175-184
    • Schonherr, R.1
  • 194
    • 0034608869 scopus 로고    scopus 로고
    • Design of a potent and selective inhibitor of the intermediate-conductance Ca2-activated K channel, IKCa1: A potential immunosuppressant
    • Wulff H, Miller MJ, Hansel W, Grissmer S, Cahalan MD, Chandy KG. Design of a potent and selective inhibitor of the intermediate-conductance Ca2-activated K channel, IKCa1: A potential immunosuppressant. Proc Natl Acad Sci USA 2000; 97: 8151-8156.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 8151-8156
    • Wulff, H.1    Miller, M.J.2    Hansel, W.3    Grissmer, S.4    Cahalan, M.D.5    Chandy, K.G.6


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