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Volumn 45, Issue 5, 2014, Pages 1901-1912

Mitochondrial division inhibitor-1 induces mitochondrial hyperfusion and sensitizes human cancer cells to TRAIL-induced apoptosis

Author keywords

Mitochondrial division inhibitor 1; Mitochondrial fission; ROS; Tumor necrosis factor related apoptosis inducing ligand; Tumor selective killing

Indexed keywords

CARDIOLIPIN; CASPASE 12; CASPASE 3; CASPASE 7; DYNAMIN RELATED PROTEIN 1; MITOCHONDRIAL DIVISION INHIBITOR 1; MITOCHONDRIAL PROTEIN; PROTEIN INHIBITOR; REACTIVE OXYGEN METABOLITE; TUMOR NECROSIS FACTOR RELATED APOPTOSIS INDUCING LIGAND; UNCLASSIFIED DRUG; DNM1L PROTEIN, HUMAN; GUANOSINE TRIPHOSPHATASE; MICROTUBULE ASSOCIATED PROTEIN; TNFSF10 PROTEIN, HUMAN;

EID: 84907190373     PISSN: 10196439     EISSN: 17912423     Source Type: Journal    
DOI: 10.3892/ijo.2014.2608     Document Type: Article
Times cited : (42)

References (48)
  • 1
    • 0038320035 scopus 로고    scopus 로고
    • Apo2L/TRAIL: Apoptosis signaling, biology, and potential for cancer therapy
    • Almasan A and Ashkenazi A: Apo2L/TRAIL: Apoptosis signaling, biology, and potential for cancer therapy. Cytokine Growth Factor Rev 14: 337-348, 2003.
    • (2003) Cytokine Growth Factor Rev , vol.14 , pp. 337-348
    • Almasan, A.1    Ashkenazi, A.2
  • 2
    • 52649109068 scopus 로고    scopus 로고
    • The TRAIL apoptotic pathway in cancer onset, progression and therapy
    • Johnstone RW, Frew AJ and Smyth MJ: The TRAIL apoptotic pathway in cancer onset, progression and therapy. Nat Rev Cancer 8: 782-798, 2008.
    • (2008) Nat Rev Cancer , vol.8 , pp. 782-798
    • Johnstone, R.W.1    Frew, A.J.2    Smyth, M.J.3
  • 3
    • 54249107246 scopus 로고    scopus 로고
    • The promise of cancer therapeutics targeting the TNF-related apoptosis-inducing ligand and TRAIL receptor pathway
    • Wang S: The promise of cancer therapeutics targeting the TNF-related apoptosis-inducing ligand and TRAIL receptor pathway. Oncogene 27: 6207-6215, 2008.
    • (2008) Oncogene , vol.27 , pp. 6207-6215
    • Wang, S.1
  • 4
    • 77956170550 scopus 로고    scopus 로고
    • New insights into apoptosis signaling by Apo2L/TRAIL
    • Gonzalvez F and Ashkenazi A: New insights into apoptosis signaling by Apo2L/TRAIL. Oncogene 29: 4752-4765, 2010.
    • (2010) Oncogene , vol.29 , pp. 4752-4765
    • Gonzalvez, F.1    Ashkenazi, A.2
  • 5
    • 0037273848 scopus 로고    scopus 로고
    • Apo2L/TRAIL and its death and decoy
    • LeBlanc HN and Ashkenazi A: Apo2L/TRAIL and its death and decoy. Cell Death Differ 10: 66-75, 2003.
    • (2003) Cell Death Differ , vol.10 , pp. 66-75
    • LeBlanc, H.N.1    Ashkenazi, A.2
  • 6
    • 0033662433 scopus 로고    scopus 로고
    • Apo2L/TRAIL-dependent recruitment of endogenous FADD and caspase-8 to death receptors 4 and 5
    • Kischkel FC, Lawrence DA, Chuntharapai A, Schow P, Kim KJ and Ashkenazi A: Apo2L/TRAIL-dependent recruitment of endogenous FADD and caspase-8 to death receptors 4 and 5. Immunity 12: 612-620, 2000.
    • (2000) Immunity , vol.12 , pp. 612-620
    • Kischkel, F.C.1    Lawrence, D.A.2    Chuntharapai, A.3    Schow, P.4    Kim, K.J.5    Ashkenazi, A.6
  • 7
    • 35348877298 scopus 로고    scopus 로고
    • Barriers to effective TRAIL-Yargeted therapy of malignancy
    • Dyer MJ, MacFarlane M and Cohen GM: Barriers to effective TRAIL-Yargeted therapy of malignancy. J Clin Oncol 25: 4505-4506, 2007.
    • (2007) J Clin Oncol , vol.25 , pp. 4505-4506
    • Dyer, M.J.1    MacFarlane, M.2    Cohen, G.M.3
  • 8
    • 84875230886 scopus 로고    scopus 로고
    • On the TRAIL to successful cancer therapy? Predicting and counteracting resistance against TRAIL-based therapeutics
    • Dimberg LY, Anderson CK, Camidge R, Behbakht K, Thorburn A and Ford HL: On the TRAIL to successful cancer therapy? Predicting and counteracting resistance against TRAIL-based therapeutics. Oncogene 32: 1341-1350, 2013.
    • (2013) Oncogene , vol.32 , pp. 1341-1350
    • Dimberg, L.Y.1    Anderson, C.K.2    Camidge, R.3    Behbakht, K.4    Thorburn, A.5    Ford, H.L.6
  • 9
    • 79952708659 scopus 로고    scopus 로고
    • Mitochondrial outer membrane permeabilization during apoptosis: The role of mitochondrial fission
    • Landes T and Martinou JC: Mitochondrial outer membrane permeabilization during apoptosis: The role of mitochondrial fission. Biochim Biophys Acta 1813: 540-545, 2011.
    • (2011) Biochim Biophys Acta , vol.1813 , pp. 540-545
    • Landes, T.1    Martinou, J.C.2
  • 10
    • 84871802627 scopus 로고    scopus 로고
    • Recent advances into the understanding of mitochondrial fission
    • Elgass K, Pakay J, Ryan MT and Palmer CS: Recent advances into the understanding of mitochondrial fission. Biochim Biophys Acta 1833: 150-161, 2013.
    • (2013) Biochim Biophys Acta , vol.1833 , pp. 150-161
    • Elgass, K.1    Pakay, J.2    Ryan, M.T.3    Palmer, C.S.4
  • 11
    • 34250204271 scopus 로고    scopus 로고
    • The machines that divide and fuse mitochondria
    • Hoppins S, Lackner L and Nunnari J: The machines that divide and fuse mitochondria. Annu Rev Biochem 76: 751-780, 2007.
    • (2007) Annu Rev Biochem , vol.76 , pp. 751-780
    • Hoppins, S.1    Lackner, L.2    Nunnari, J.3
  • 12
    • 79954571354 scopus 로고    scopus 로고
    • The interplay between mitochondrial dynamics and mitophagy
    • Twig G and Shirihai OS: The interplay between mitochondrial dynamics and mitophagy. Antioxid Redox Signal 14: 1939-1951, 2011.
    • (2011) Antioxid Redox Signal , vol.14 , pp. 1939-1951
    • Twig, G.1    Shirihai, O.S.2
  • 13
    • 84856725391 scopus 로고    scopus 로고
    • The MFN2 gene is responsible for mitochondrial DNA instability and optic atrophy 'plus' phenotype
    • Rouzier C, Bannwarth S, Chaussenot A, et al: The MFN2 gene is responsible for mitochondrial DNA instability and optic atrophy 'plus' phenotype. Brain 135: 23-34, 2012.
    • (2012) Brain , vol.135 , pp. 23-34
    • Rouzier, C.1    Bannwarth, S.2    Chaussenot, A.3
  • 14
    • 22544451586 scopus 로고    scopus 로고
    • Disruption of fusion results in mitochondrial heterogeneity and dysfunction
    • Chen H, Chomyn A and Chan DC: Disruption of fusion results in mitochondrial heterogeneity and dysfunction. J Biol Chem 280: 26185-26192, 2005.
    • (2005) J Biol Chem , vol.280 , pp. 26185-26192
    • Chen, H.1    Chomyn, A.2    Chan, D.C.3
  • 15
    • 77955298543 scopus 로고    scopus 로고
    • Dynamic regulation of mitochondrial fission through modification of the dynamin-related protein Drp1
    • Chang CR and Blackstone C: Dynamic regulation of mitochondrial fission through modification of the dynamin-related protein Drp1. Ann NY Acad Sci 1201: 34-39, 2010.
    • (2010) Ann NY Acad Sci , vol.1201 , pp. 34-39
    • Chang, C.R.1    Blackstone, C.2
  • 16
    • 0035487808 scopus 로고    scopus 로고
    • The role of dynamin-related protein 1, a mediator of mitochondrial fission, in apoptosis
    • Frank S, Gaume B, Bergmann-Leitner ES, et al: The role of dynamin-related protein 1, a mediator of mitochondrial fission, in apoptosis. Dev Cell 1: 515-525, 2001.
    • (2001) Dev Cell , vol.1 , pp. 515-525
    • Frank, S.1    Gaume, B.2    Bergmann-Leitner, E.S.3
  • 17
    • 6344274848 scopus 로고    scopus 로고
    • Roles of the mammalian mitochondrial fission and fusion mediators Fis1, Drp1, and Opa1 in apoptosis
    • Lee YJ, Jeong SY, Karbowski M, Smith CL and Youle RJ: Roles of the mammalian mitochondrial fission and fusion mediators Fis1, Drp1, and Opa1 in apoptosis. Mol Biol Cell 15: 5001-5011, 2004.
    • (2004) Mol Biol Cell , vol.15 , pp. 5001-5011
    • Lee, Y.J.1    Jeong, S.Y.2    Karbowski, M.3    Smith, C.L.4    Youle, R.J.5
  • 18
    • 27444446030 scopus 로고    scopus 로고
    • Release of OPA1 during apoptosis participates in the rapid and complete release of cytochrome c and subsequent mitochondrial fragmentation
    • Arnoult D, Grodet A, Lee YJ, Estaquier J and Blackstone C: Release of OPA1 during apoptosis participates in the rapid and complete release of cytochrome c and subsequent mitochondrial fragmentation. J Biol Chem 280: 35742-35750, 2005.
    • (2005) J Biol Chem , vol.280 , pp. 35742-35750
    • Arnoult, D.1    Grodet, A.2    Lee, Y.J.3    Estaquier, J.4    Blackstone, C.5
  • 19
    • 33750526651 scopus 로고    scopus 로고
    • The mitochondrial fission protein hFis1 requires the endoplasmic reticulum gateway to induce apoptosis
    • Alirol E, James D, Huber D, Marchetto A, Vergani L and Martinou JC: The mitochondrial fission protein hFis1 requires the endoplasmic reticulum gateway to induce apoptosis. Mol Biol Cell 17: 4593-4605, 2006.
    • (2006) Mol Biol Cell , vol.17 , pp. 4593-4605
    • Alirol, E.1    James, D.2    Huber, D.3    Marchetto, A.4    Vergani, L.5    Martinou, J.C.6
  • 20
    • 34249019899 scopus 로고    scopus 로고
    • Inhibiting Drp1-mediated mitochondrial fission selectively prevents the release of cytochrome c during apoptosis
    • Estaquier J and Arnoult D: Inhibiting Drp1-mediated mitochondrial fission selectively prevents the release of cytochrome c during apoptosis. Cell Death Differ 14: 1086-1094, 2007.
    • (2007) Cell Death Differ , vol.14 , pp. 1086-1094
    • Estaquier, J.1    Arnoult, D.2
  • 21
    • 45349094984 scopus 로고    scopus 로고
    • Mitochondrial dynamics and apoptosis
    • Suen DF, Norris KL and Youle RJ: Mitochondrial dynamics and apoptosis. Genes Dev 22: 1577-1590, 2008.
    • (2008) Genes Dev , vol.22 , pp. 1577-1590
    • Suen, D.F.1    Norris, K.L.2    Youle, R.J.3
  • 22
    • 49349105966 scopus 로고    scopus 로고
    • Bax-or Bak-induced mitochondrial fission can be uncoupled from cytochrome c release
    • Sheridan C, Delivani P, Cullen SP and Martin SJ: Bax-or Bak-induced mitochondrial fission can be uncoupled from cytochrome c release. Mol Cell 31: 570-585, 2008.
    • (2008) Mol Cell , vol.31 , pp. 570-585
    • Sheridan, C.1    Delivani, P.2    Cullen, S.P.3    Martin, S.J.4
  • 23
    • 38849099158 scopus 로고    scopus 로고
    • Chemical inhibition of the mitochondrial division dynamin reveals its role in Bax/Bak-dependent mitochondrial outer membrane permeabilization
    • Cassidy-Stone A, Chipuk JE, Ingerman E, et al: Chemical inhibition of the mitochondrial division dynamin reveals its role in Bax/Bak-dependent mitochondrial outer membrane permeabilization. Dev Cell 14: 193-204, 2008.
    • (2008) Dev Cell , vol.14 , pp. 193-204
    • Cassidy-Stone, A.1    Chipuk, J.E.2    Ingerman, E.3
  • 24
    • 84863569591 scopus 로고    scopus 로고
    • Depolarization potentiates TRAIL-induced apoptosis in human melanoma cells: Role for ATP-sensitive K+ channels and endoplasmic reticulum stress
    • Suzuki Y, Inoue T, Murai M, Suzuki-Karasaki M, Ochiai T and Ra C: Depolarization potentiates TRAIL-induced apoptosis in human melanoma cells: Role for ATP-sensitive K+ channels and endoplasmic reticulum stress. Int J Oncol 41: 465-475, 2012.
    • (2012) Int J Oncol , vol.41 , pp. 465-475
    • Suzuki, Y.1    Inoue, T.2    Murai, M.3    Suzuki-Karasaki, M.4    Ochiai, T.5    Ra, C.6
  • 25
    • 84869799967 scopus 로고    scopus 로고
    • Diallyl trisulfide sensitizes human melanoma cells to TRAIL-induced cell death by promoting endoplasmic reticulum-mediated apoptosis
    • Murai M, Inoue T, Suzuki-Karasaki M, Ochiai T, Ra C, Nishida S, et al: Diallyl trisulfide sensitizes human melanoma cells to TRAIL-induced cell death by promoting endoplasmic reticulum-mediated apoptosis. Int J Oncol 41: 2029-2037, 2012.
    • (2012) Int J Oncol , vol.41 , pp. 2029-2037
    • Murai, M.1    Inoue, T.2    Suzuki-Karasaki, M.3    Ochiai, T.4    Ra, C.5    Nishida, S.6
  • 26
    • 84878006508 scopus 로고    scopus 로고
    • Mitochondrial superoxide mediates mitochondrial and endoplasmic reticulum dysfunctions in TRAIL-induced apoptosis in Jurkat cells
    • Inoue T and Suzuki-Karasaki Y: Mitochondrial superoxide mediates mitochondrial and endoplasmic reticulum dysfunctions in TRAIL-induced apoptosis in Jurkat cells. Free Radic Biol Med 61: 273-284, 2013.
    • (2013) Free Radic Biol Med , vol.61 , pp. 273-284
    • Inoue, T.1    Suzuki-Karasaki, Y.2
  • 27
    • 34250888209 scopus 로고    scopus 로고
    • Tunicamycin sensitizes human melanoma cells to tumor necrosis factor-related apoptosis-inducing ligand-induced apoptosis by up-regulation of TRAIL-R2 via the unfolded protein response
    • Jiang CC, Chen LH, Gillespie S, et al: Tunicamycin sensitizes human melanoma cells to tumor necrosis factor-related apoptosis-inducing ligand-induced apoptosis by up-regulation of TRAIL-R2 via the unfolded protein response. Cancer Res 67: 5880-5888, 2007.
    • (2007) Cancer Res , vol.67 , pp. 5880-5888
    • Jiang, C.C.1    Chen, L.H.2    Gillespie, S.3
  • 28
    • 0035830843 scopus 로고    scopus 로고
    • Plasma membrane depolarization without repolarization is an early molecular event in anti-Fas-induced apoptosis
    • Bortner CD, Gomez-Angelats M and Cidlowski JA: Plasma membrane depolarization without repolarization is an early molecular event in anti-Fas-induced apoptosis. J Biol Chem 276: 4304-4314, 2001.
    • (2001) J Biol Chem , vol.276 , pp. 4304-4314
    • Bortner, C.D.1    Gomez-Angelats, M.2    Cidlowski, J.A.3
  • 29
    • 9644262891 scopus 로고    scopus 로고
    • Depolarisation of the plasma membrane in the arsenic trioxide (As2O3)-And anti-CD95-induced apoptosis in myeloid cells
    • Nolte F, Friedrich O, Rojewski M, Fink RH, Schrezenmeier H and Körper S: Depolarisation of the plasma membrane in the arsenic trioxide (As2O3)-And anti-CD95-induced apoptosis in myeloid cells. FEBS Lett 578: 85-89, 2004.
    • (2004) FEBS Lett , vol.578 , pp. 85-89
    • Nolte, F.1    Friedrich, O.2    Rojewski, M.3    Fink, R.H.4    Schrezenmeier, H.5    Körper, S.6
  • 30
    • 65649143561 scopus 로고    scopus 로고
    • Plasma membrane depolarization and Na,K-ATPase impairment induced by mitochondrial toxins augment leukemia cell apoptosis via a novel mitochondrial amplification mechanism
    • Yin W, Li X, Feng S, et al: Plasma membrane depolarization and Na,K-ATPase impairment induced by mitochondrial toxins augment leukemia cell apoptosis via a novel mitochondrial amplification mechanism. Biochem Pharmacol 78: 191-202, 2009.
    • (2009) Biochem Pharmacol , vol.78 , pp. 191-202
    • Yin, W.1    Li, X.2    Feng, S.3
  • 31
    • 84894428398 scopus 로고    scopus 로고
    • Crosstalk between mitochondrial ROS and depolarization in the potentiation of TRAIL-induced apoptosis in human tumor cells
    • Suzuki-Karasaki M, Ochiai T and Suzuki-Karasaki Y: Crosstalk between mitochondrial ROS and depolarization in the potentiation of TRAIL-induced apoptosis in human tumor cells. Int J Oncol 44: 616-628, 2014.
    • (2014) Int J Oncol , vol.44 , pp. 616-628
    • Suzuki-Karasaki, M.1    Ochiai, T.2    Suzuki-Karasaki, Y.3
  • 32
    • 33750063955 scopus 로고    scopus 로고
    • Selective fluorescent imaging of superoxide in vivo using ethidium-based probes
    • Robinson KM, Janes MS, Pehar M, et al: Selective fluorescent imaging of superoxide in vivo using ethidium-based probes. Proc Natl Acad Sci USA 103: 15038-15043, 2006.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 15038-15043
    • Robinson, K.M.1    Janes, M.S.2    Pehar, M.3
  • 34
    • 0026742850 scopus 로고
    • 10-N-nonyl acridine orange interacts with cardiolipin and allows the quantification of this phospholipid in isolated mitochondria
    • Petit JM, Maftah A, Ratinaud MH and Julien R: 10-N-nonyl acridine orange interacts with cardiolipin and allows the quantification of this phospholipid in isolated mitochondria. Eur J Biochem 209: 267-273, 1992.
    • (1992) Eur J Biochem , vol.209 , pp. 267-273
    • Petit, J.M.1    Maftah, A.2    Ratinaud, M.H.3    Julien, R.4
  • 35
    • 0042838291 scopus 로고    scopus 로고
    • Mitochondrial aggregation precedes cytochrome c release from mitochondria during apoptosis
    • Haga N, Fujita N and Tsuruo T: Mitochondrial aggregation precedes cytochrome c release from mitochondria during apoptosis. Oncogene 22: 5579-5585, 2003.
    • (2003) Oncogene , vol.22 , pp. 5579-5585
    • Haga, N.1    Fujita, N.2    Tsuruo, T.3
  • 36
    • 29644436194 scopus 로고    scopus 로고
    • Involvement of mitochondrial aggregation in arsenic trioxide (As2O3)-induced apoptosis in human glioblastoma cells
    • Haga N, Fujita N and Tsuruo T: Involvement of mitochondrial aggregation in arsenic trioxide (As2O3)-induced apoptosis in human glioblastoma cells. Cancer Sci 96: 825-833, 2005.
    • (2005) Cancer Sci , vol.96 , pp. 825-833
    • Haga, N.1    Fujita, N.2    Tsuruo, T.3
  • 37
    • 77953696905 scopus 로고    scopus 로고
    • Small molecule inhibitors of mitochondrial division: Tools that translate basic biological research into medicine
    • Lackner LL and Nunnari J: Small molecule inhibitors of mitochondrial division: Tools that translate basic biological research into medicine. Chem Biol 17: 578-583, 2010.
    • (2010) Chem Biol , vol.17 , pp. 578-583
    • Lackner, L.L.1    Nunnari, J.2
  • 38
    • 84860914473 scopus 로고    scopus 로고
    • Inhibition of mitochondrial fission prevents cell cycle progression in lung cancer
    • Rehman J, Zhang HJ, Toth PT, et al: Inhibition of mitochondrial fission prevents cell cycle progression in lung cancer. FASEB J 26: 2175-2186, 2012.
    • (2012) FASEB J , vol.26 , pp. 2175-2186
    • Rehman, J.1    Zhang, H.J.2    Toth, P.T.3
  • 39
    • 84873679865 scopus 로고    scopus 로고
    • Hydrogen peroxide induces cell death in human TRAIL-resistant melanoma through intracellular superoxide generation
    • Tochigi M, Inoue T, Suzuki-Karasaki M, Ochiai T, Ra C and Suzuki-Karasaki Y: Hydrogen peroxide induces cell death in human TRAIL-resistant melanoma through intracellular superoxide generation. Int J Oncol 42: 863-872, 2013.
    • (2013) Int J Oncol , vol.42 , pp. 863-872
    • Tochigi, M.1    Inoue, T.2    Suzuki-Karasaki, M.3    Ochiai, T.4    Ra, C.5    Suzuki-Karasaki, Y.6
  • 40
    • 0041810128 scopus 로고    scopus 로고
    • The adenine nucleotide translocase: A central component of the mitochondrial permeability transition pore and key player in cell death
    • Halestrap AP and Brennerb C: The adenine nucleotide translocase: A central component of the mitochondrial permeability transition pore and key player in cell death. Curr Med Chem 10: 1507-1525, 2003.
    • (2003) Curr Med Chem , vol.10 , pp. 1507-1525
    • Halestrap, A.P.1    Brennerb, C.2
  • 42
    • 23944478449 scopus 로고    scopus 로고
    • Mitochondria: A novel target for the chemoprevention of cancer
    • Hail N Jr: Mitochondria: A novel target for the chemoprevention of cancer. Apoptosis 10: 687-705, 2005.
    • (2005) Apoptosis , vol.10 , pp. 687-705
    • Hail, N.1
  • 43
    • 70350023058 scopus 로고    scopus 로고
    • Adenine nucleotide translocase: A component of the phylogenetically conserved cell death machinery
    • Zhivotovsky B, Galluzzi L, Kepp O and Kroemer G: Adenine nucleotide translocase: A component of the phylogenetically conserved cell death machinery. Cell Death Differ 16: 1419-1425, 2009.
    • (2009) Cell Death Differ , vol.16 , pp. 1419-1425
    • Zhivotovsky, B.1    Galluzzi, L.2    Kepp, O.3    Kroemer, G.4
  • 44
    • 0030580287 scopus 로고    scopus 로고
    • Why are mitochondria involved in apoptosis? Permeability transition pores and apoptosis as selective mechanisms to eliminate superoxide-producing mitochondria and cell
    • Skulachev VP: Why are mitochondria involved in apoptosis? Permeability transition pores and apoptosis as selective mechanisms to eliminate superoxide-producing mitochondria and cell. FEBS Lett 397: 7-10, 1996.
    • (1996) FEBS Lett , vol.397 , pp. 7-10
    • Skulachev, V.P.1
  • 45
    • 34548451974 scopus 로고    scopus 로고
    • Reactive oxygen species in mitochondria-mediated cell death
    • Orrenius S: Reactive oxygen species in mitochondria-mediated cell death. Drug Metab Rev 39: 443-455, 2007.
    • (2007) Drug Metab Rev , vol.39 , pp. 443-455
    • Orrenius, S.1
  • 47
    • 77649183649 scopus 로고    scopus 로고
    • Bioenergetic pathways in tumor mitochondria as targets for cancer therapy and the importance of the ROS-induced apoptotic trigger
    • Ralph SJ, Rodr íguez-Enr íquez S, Neuzil J and Moreno-Sanchez R: Bioenergetic pathways in tumor mitochondria as targets for cancer therapy and the importance of the ROS-induced apoptotic trigger. Mol Aspects Med 31: 29-59, 2010.
    • (2010) Mol Aspects Med , vol.31 , pp. 29-59
    • Ralph, S.J.1    Rodríguez-Enríquez, S.2    Neuzil, J.3    Moreno-Sanchez, R.4
  • 48
    • 84907223416 scopus 로고    scopus 로고
    • Depolarization controls TRAIL sensitization and tumor-selective killing of cancer cells: Crosstalk with ROS
    • In press
    • Suzuki-Karasaki Y, Suzuki-Karasaki M, Uchida M and Ochiai T: Depolarization controls TRAIL sensitization and tumor-selective killing of cancer cells: Crosstalk with ROS. Front Oncol (In press).
    • Front Oncol
    • Suzuki-Karasaki, Y.1    Suzuki-Karasaki, M.2    Uchida, M.3    Ochiai, T.4


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