메뉴 건너뛰기




Volumn 14, Issue 3, 2013, Pages 377-389

Targeting the mitochondrial electron transport chain complexes for the induction of apoptosis and cancer treatment

Author keywords

Cancer; Electron transport chain; Mitochondria; Oxidative stress

Indexed keywords

1 METHYL 4 PHENYLPYRIDINIUM; 3,3' DIINDOLYLMETHANE; ADAPHOSTIN; ALPHA TOCOPHEROL; ALPHA TOCOPHEROL SUCCINATE; ANTIMYCIN A1; BENZYL ISOTHIOCYANATE; BUTYLATED HYDROXYANISOLE; DEGUELIN; DOXORUBICIN; FENRETINIDE; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; MALONIC ACID; MITOGEN ACTIVATED PROTEIN KINASE; NITRIC OXIDE; OLIGOMYCIN; OXIDOREDUCTASE; PHENETHYL ISOTHIOCYANATE; PORPHYRIN DERIVATIVE; PROTEIN KINASE B; RESVERATROL; RHODAMINE 123; ROTENONE; SPHINGOMYELIN PHOSPHODIESTERASE; SUPEROXIDE; TAMOXIFEN; THENOYLTRIFLUOROACETONE; TROGLITAZONE; UNINDEXED DRUG; XANTHOHUMOL;

EID: 84875284814     PISSN: 13892010     EISSN: 18734316     Source Type: Journal    
DOI: 10.2174/1389201011314030011     Document Type: Article
Times cited : (34)

References (187)
  • 1
    • 38949192547 scopus 로고    scopus 로고
    • Targeted cancer therapy: Conferring specificity to cytotoxic drugs
    • Chari, R. V. Targeted cancer therapy: conferring specificity to cytotoxic drugs. Acc. Chem. Res., 2008, 41, 98-107.
    • (2008) Acc. Chem. Res , vol.41 , pp. 98-107
    • Chari, R.V.1
  • 2
    • 9244222261 scopus 로고    scopus 로고
    • Targeted cancer therapy
    • Sawyers, C. Targeted cancer therapy. Nature, 2004, 432, 294-297.
    • (2004) Nature , vol.432 , pp. 294-297
    • Sawyers, C.1
  • 3
    • 0036216405 scopus 로고    scopus 로고
    • STI571 (Gleevec) as a paradigm for cancer therapy
    • Druker, B. J. STI571 (Gleevec) as a paradigm for cancer therapy. Trends Mol. Med., 2002, 8, S14-18.
    • (2002) Trends Mol. Med , vol.8
    • Druker, B.J.1
  • 4
    • 51649089553 scopus 로고    scopus 로고
    • Cancer complexity slows quest for cure
    • Check Hayden, E. Cancer complexity slows quest for cure. Nature, 2008, 455, 148.
    • (2008) Nature , vol.455 , pp. 148
    • Check, H.E.1
  • 7
    • 47949089077 scopus 로고    scopus 로고
    • VEGF-targeted therapy: Mechanisms of anti-tumour activity
    • Ellis, L. M.; Hicklin, D. J. VEGF-targeted therapy: mechanisms of anti-tumour activity. Nat. Rev. Cancer, 2008, 8, 579-591.
    • (2008) Nat. Rev. Cancer , vol.8 , pp. 579-591
    • Ellis, L.M.1    Hicklin, D.J.2
  • 8
    • 0004235430 scopus 로고    scopus 로고
    • John Wiley & Sons, Inc.: Hoboken, New Jersey, USA
    • Scheffler, I. Mitochondria, Second Edition, John Wiley & Sons, Inc.: Hoboken, New Jersey, USA, 2008.
    • (2008) Mitochondria, Second Edition
    • Scheffler, I.1
  • 9
    • 66249108601 scopus 로고    scopus 로고
    • Understanding the Warburg effect: The metabolic requirements of cell proliferation
    • Vander Heiden, M. G.; Cantley, L. C.; Thompson, C. B. Understanding the Warburg effect: the metabolic requirements of cell proliferation. Science, 2009, 324, 1029-1033.
    • (2009) Science , vol.324 , pp. 1029-1033
    • Vander Heiden, M.G.1    Cantley, L.C.2    Thompson, C.B.3
  • 10
    • 60249085118 scopus 로고    scopus 로고
    • Mitochondria in cancer: Not just innocent bystanders
    • Frezza, C.; Gottlieb, E. Mitochondria in cancer: not just innocent bystanders. Semin. Cancer Biol., 2009, 19, 4-11.
    • (2009) Semin. Cancer Biol , vol.19 , pp. 4-11
    • Frezza, C.1    Gottlieb, E.2
  • 11
    • 43049109160 scopus 로고    scopus 로고
    • Aerobic glycolysis in cancers: Implications for the usability of oxygen-responsive genes and fluorodeoxyglucose-PET as markers of tissue hypoxia
    • Busk, M.; Horsman, M. R.; Kristjansen, P. E.; van der Kogel, A. J.; Bussink, J.; Overgaard, J. Aerobic glycolysis in cancers: implications for the usability of oxygen-responsive genes and fluorodeoxyglucose-PET as markers of tissue hypoxia. Int. J. Cancer, 2008, 122, 2726-2734.
    • (2008) Int. J. Cancer , vol.122 , pp. 2726-2734
    • Busk, M.1    Horsman, M.R.2    Kristjansen, P.E.3    van der Kogel, A.J.4    Bussink, J.5    Overgaard, J.6
  • 13
    • 35448937135 scopus 로고    scopus 로고
    • A message emerging from development: The repression of mitochondrial beta-F1-ATPase expression in cancer
    • Cuezva, J. M.; Sanchez-Arago, M.; Sala, S.; Blanco-Rivero, A.; Ortega, A. D. A message emerging from development: the repression of mitochondrial beta-F1-ATPase expression in cancer. J. Bioenerg. Biomembr., 2007, 39, 259-265.
    • (2007) J. Bioenerg. Biomembr , vol.39 , pp. 259-265
    • Cuezva, J.M.1    Sanchez-Arago, M.2    Sala, S.3    Blanco-Rivero, A.4    Ortega, A.D.5
  • 15
    • 73249137166 scopus 로고    scopus 로고
    • Mitochondrial Complex I decrease is responsible for bioenergetic dysfunction in K-ras transformed cells
    • Baracca, A.; Chiaradonna, F.; Sgarbi, G.; Solaini, G.; Alberghina, L.; Lenaz, G. Mitochondrial Complex I decrease is responsible for bioenergetic dysfunction in K-ras transformed cells. Biochim. Biophys., Acta, 2010, 1797, 314-323.
    • (2010) Biochim. Biophys., Acta , vol.1797 , pp. 314-323
    • Baracca, A.1    Chiaradonna, F.2    Sgarbi, G.3    Solaini, G.4    Alberghina, L.5    Lenaz, G.6
  • 16
    • 0023227833 scopus 로고
    • Basis for the selective cytotoxicity of rhodamine 123
    • Modica-Napolitano, J. S.; Aprille, J. R. Basis for the selective cytotoxicity of rhodamine 123. Cancer Res., 1987, 47, 4361-4365.
    • (1987) Cancer Res , vol.47 , pp. 4361-4365
    • Modica-Napolitano, J.S.1    Aprille, J.R.2
  • 17
    • 0022344345 scopus 로고
    • Mitochondrial and plasma membrane potentials cause unusual accumulation and retention of rhodamine 123 by human breast adenocarcinoma-derived MCF-7 cells
    • Davis, S.; Weiss, M. J.; Wong, J. R.; Lampidis, T. J.; Chen, L. B. Mitochondrial and plasma membrane potentials cause unusual accumulation and retention of rhodamine 123 by human breast adenocarcinoma-derived MCF-7 cells. J. Biol. Chem., 1985, 260, 13844-13850.
    • (1985) J. Biol. Chem , vol.260 , pp. 13844-13850
    • Davis, S.1    Weiss, M.J.2    Wong, J.R.3    Lampidis, T.J.4    Chen, L.B.5
  • 19
    • 57049167019 scopus 로고    scopus 로고
    • Regulation of oxidative phosphorylation, the mitochondrial membrane potential, and their role in human disease
    • Huttemann, M.; Lee, I.; Pecinova, A.; Pecina, P.; Przyklenk, K.; Doan, J. W. Regulation of oxidative phosphorylation, the mitochondrial membrane potential, and their role in human disease. J. Bioenerg. Biomembr., 2008, 40, 445-456.
    • (2008) J. Bioenerg. Biomembr , vol.40 , pp. 445-456
    • Huttemann, M.1    Lee, I.2    Pecinova, A.3    Pecina, P.4    Przyklenk, K.5    Doan, J.W.6
  • 21
    • 67749111889 scopus 로고    scopus 로고
    • Membrane potential greatly enhances superoxide generation by the cytochrome bc1 complex reconstituted into phospholipid vesicles
    • Rottenberg, H.; Covian, R.; Trumpower, B. L. Membrane potential greatly enhances superoxide generation by the cytochrome bc1 complex reconstituted into phospholipid vesicles. J. Biol. Chem., 2009, 284, 19203-19210.
    • (2009) J. Biol. Chem , vol.284 , pp. 19203-19210
    • Rottenberg, H.1    Covian, R.2    Trumpower, B.L.3
  • 22
    • 76749091531 scopus 로고    scopus 로고
    • New extension of the Mitchell Theory for oxidative phosphorylation in mitochondria of living organisms
    • Kadenbach, B.; Ramzan, R.; Wen, L.; Vogt, S. New extension of the Mitchell Theory for oxidative phosphorylation in mitochondria of living organisms. Biochim. Biophys. Acta, 2010, 1800, 205-212.
    • (2010) Biochim. Biophys. Acta , vol.1800 , pp. 205-212
    • Kadenbach, B.1    Ramzan, R.2    Wen, L.3    Vogt, S.4
  • 25
    • 41149105722 scopus 로고    scopus 로고
    • Mitochondria in cancer cells: What is so special about them?
    • Gogvadze, V.; Orrenius, S.; Zhivotovsky, B. Mitochondria in cancer cells: what is so special about them? Trends Cell Biol., 2008, 18, 165-173.
    • (2008) Trends Cell Biol , vol.18 , pp. 165-173
    • Gogvadze, V.1    Orrenius, S.2    Zhivotovsky, B.3
  • 26
    • 33746895175 scopus 로고    scopus 로고
    • Mitochondria as therapeutic targets for cancer chemotherapy
    • Galluzzi, L.; Larochette, N.; Zamzami, N.; Kroemer, G. Mitochondria as therapeutic targets for cancer chemotherapy. Oncogene, 2006, 25, 4812-4830.
    • (2006) Oncogene , vol.25 , pp. 4812-4830
    • Galluzzi, L.1    Larochette, N.2    Zamzami, N.3    Kroemer, G.4
  • 27
    • 77953131908 scopus 로고    scopus 로고
    • Targeting mitochondria for cancer therapy
    • Fulda, S.; Galluzzi, L.; Kroemer, G. Targeting mitochondria for cancer therapy. Nat. Rev. Drug Discov., 2010, 010, 9, 447-464.
    • (2010) Nat. Rev. Drug Discov , vol.10 , Issue.9 , pp. 447-464
    • Fulda, S.1    Galluzzi, L.2    Kroemer, G.3
  • 28
    • 77649188789 scopus 로고    scopus 로고
    • Small mitochondriatargeting molecules as anti-cancer agents
    • Wang, F.; Ogasawara, M. A.; Huang, P. Small mitochondriatargeting molecules as anti-cancer agents. Mol. Aspects Med., 2010, 31, 75-92.
    • (2010) Mol. Aspects Med , vol.31 , pp. 75-92
    • Wang, F.1    Ogasawara, M.A.2    Huang, P.3
  • 30
    • 65549144609 scopus 로고    scopus 로고
    • Mitochondria as targets for cancer therapy
    • Ralph, S. J.; Neuzil, J. Mitochondria as targets for cancer therapy. Mol. Nutr. Food Res., 2009, 53, 9-28.
    • (2009) Mol. Nutr. Food Res , vol.53 , pp. 9-28
    • Ralph, S.J.1    Neuzil, J.2
  • 31
    • 0033525924 scopus 로고    scopus 로고
    • Oxidative phosphorylation at the fin de siecle
    • Saraste, M. Oxidative phosphorylation at the fin de siecle. Science, 1999, 283, 1488-1493.
    • (1999) Science , vol.283 , pp. 1488-1493
    • Saraste, M.1
  • 32
    • 33751072935 scopus 로고    scopus 로고
    • Bioenergetics and the formation of mitochondrial reactive oxygen species
    • Adam-Vizi, V.; Chinopoulos, C. Bioenergetics and the formation of mitochondrial reactive oxygen species. Trends Pharmacol. Sci., 2006, 27, 639-645.
    • (2006) Trends Pharmacol. Sci , vol.27 , pp. 639-645
    • Adam-Vizi, V.1    Chinopoulos, C.2
  • 33
    • 58249093939 scopus 로고    scopus 로고
    • How mitochondria produce reactive oxygen species
    • Murphy, M. P. How mitochondria produce reactive oxygen species. Biochem. J., 2009, 417, 1-13.
    • (2009) Biochem. J , vol.417 , pp. 1-13
    • Murphy, M.P.1
  • 34
    • 33847349283 scopus 로고    scopus 로고
    • Reactive oxygen species: A breath of life or death?
    • Fruehauf, J. P.; Meyskens, F. L. Jr. Reactive oxygen species: a breath of life or death?, Clin. Cancer Res., 2007, 13, 789-794.
    • (2007) Clin. Cancer Res , vol.13 , pp. 789-794
    • Fruehauf, J.P.1    Meyskens Jr., F.L.2
  • 35
    • 0035842896 scopus 로고    scopus 로고
    • VDAC-dependent permeabilization of the outer mitochondrial membrane by superoxide induces rapid and massive cytochrome c release
    • Madesh, M.; Hajnoczky, G. VDAC-dependent permeabilization of the outer mitochondrial membrane by superoxide induces rapid and massive cytochrome c release. J. Cell Biol., 2001, 155, 1003-1015.
    • (2001) J. Cell Biol , vol.155 , pp. 1003-1015
    • Madesh, M.1    Hajnoczky, G.2
  • 36
    • 37249087334 scopus 로고    scopus 로고
    • The mitochondrial respiratory chain is a modulator of apoptosis
    • Kwong, J. Q.; Henning, M. S.; Starkov, A. A.; Manfredi, G. The mitochondrial respiratory chain is a modulator of apoptosis. J. Cell Biol., 2007, 179, 1163-1177.
    • (2007) J. Cell Biol , vol.179 , pp. 1163-1177
    • Kwong, J.Q.1    Henning, M.S.2    Starkov, A.A.3    Manfredi, G.4
  • 37
    • 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
  • 38
    • 77952979824 scopus 로고    scopus 로고
    • The architecture of respiratory complex I
    • Efremov, R. G.; Baradaran, R.; Sazanov, L. A. The architecture of respiratory complex I. Nature, 2010, 465, 441-445.
    • (2010) Nature , vol.465 , pp. 441-445
    • Efremov, R.G.1    Baradaran, R.2    Sazanov, L.A.3
  • 39
    • 70350351403 scopus 로고    scopus 로고
    • Structural basis for the mechanism of respiratory complex I
    • Berrisford, J. M.; Sazanov, L. A. Structural basis for the mechanism of respiratory complex I. J. Biol. Chem., 2009, 284, 29773-29783.
    • (2009) J. Biol. Chem , vol.284 , pp. 29773-29783
    • Berrisford, J.M.1    Sazanov, L.A.2
  • 40
    • 56349113200 scopus 로고    scopus 로고
    • Generation of reactive oxygen species by mitochondrial complex I: Implications in neurodegeneration
    • Fato, R.; Bergamini, C.; Leoni, S.; Strocchi, P.; Lenaz, G. Generation of reactive oxygen species by mitochondrial complex I: implications in neurodegeneration. Neurochem. Res., 2008, 33, 2487-2501.
    • (2008) Neurochem. Res , vol.33 , pp. 2487-2501
    • Fato, R.1    Bergamini, C.2    Leoni, S.3    Strocchi, P.4    Lenaz, G.5
  • 41
    • 33745628757 scopus 로고    scopus 로고
    • Generation of superoxide by the mitochondrial Complex I
    • Grivennikova, V. G.; Vinogradov, A. D. Generation of superoxide by the mitochondrial Complex I. Biochim. Biophys. Acta, 2006, 1757, 553-561.
    • (2006) Biochim. Biophys. Acta , vol.1757 , pp. 553-561
    • Grivennikova, V.G.1    Vinogradov, A.D.2
  • 42
    • 1042301416 scopus 로고    scopus 로고
    • Characterization of superoxide-producing sites in isolated brain mitochondria
    • Kudin, A. P.; Bimpong-Buta, N. Y.; Vielhaber, S.; Elger, C. E.; Kunz, W. S. Characterization of superoxide-producing sites in isolated brain mitochondria. J. Biol. Chem., 2004, 279, 4127-4135.
    • (2004) J. Biol. Chem , vol.279 , pp. 4127-4135
    • Kudin, A.P.1    Bimpong-Buta, N.Y.2    Vielhaber, S.3    Elger, C.E.4    Kunz, W.S.5
  • 43
    • 33646716659 scopus 로고    scopus 로고
    • The mechanism of superoxide production by NADH:Ubiquinone oxidoreductase (complex I) from bovine heart mitochondria
    • Kussmaul, L.; Hirst, J. The mechanism of superoxide production by NADH:ubiquinone oxidoreductase (complex I) from bovine heart mitochondria. Proc. Natl. Acad. Sci. USA, 2006, 103, 7607-7612.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 7607-7612
    • Kussmaul, L.1    Hirst, J.2
  • 44
    • 4544354262 scopus 로고    scopus 로고
    • Inhibitors of the quinone-binding site allow rapid superoxide production from mitochondrial NADH:Ubiquinone oxidoreductase (complex I)
    • Lambert, A. J.; Brand, M. D. Inhibitors of the quinone-binding site allow rapid superoxide production from mitochondrial NADH:ubiquinone oxidoreductase (complex I). J. Biol. Chem., 2004, 279, 39414-39420.
    • (2004) J. Biol. Chem , vol.279 , pp. 39414-39420
    • Lambert, A.J.1    Brand, M.D.2
  • 45
    • 0032490114 scopus 로고    scopus 로고
    • Inhibitors of NADH-ubiquinone reductase: An overview
    • Degli Esposti, M. Inhibitors of NADH-ubiquinone reductase: an overview. Biochim. Biophys. Acta, 1998, 1364, 222-235.
    • (1998) Biochim. Biophys. Acta , vol.1364 , pp. 222-235
    • Degli, E.M.1
  • 46
    • 0344820721 scopus 로고    scopus 로고
    • Three classes of inhibitors share a common binding domain in mitochondrial complex I (NADH:Ubiquinone oxidoreductase)
    • Okun, J. G.; Lummen, P.; Brandt, U. Three classes of inhibitors share a common binding domain in mitochondrial complex I (NADH:ubiquinone oxidoreductase). J. Biol. Chem., 1999, 274, 2625-2630.
    • (1999) J. Biol. Chem , vol.274 , pp. 2625-2630
    • Okun, J.G.1    Lummen, P.2    Brandt, U.3
  • 47
    • 35748979985 scopus 로고    scopus 로고
    • Exploring the ubiquinone binding cavity of respiratory complex I
    • Tocilescu, M. A.; Fendel, U.; Zwicker, K.; Kerscher, S.; Brandt, U. Exploring the ubiquinone binding cavity of respiratory complex I. J. Biol. Chem., 2007, 282, 29514-29520.
    • (2007) J. Biol. Chem , vol.282 , pp. 29514-29520
    • Tocilescu, M.A.1    Fendel, U.2    Zwicker, K.3    Kerscher, S.4    Brandt, U.5
  • 48
  • 49
    • 0042521076 scopus 로고    scopus 로고
    • The environment and Parkinson's disease: Is the nigrostriatal system preferentially targeted by neurotoxins?
    • Di Monte, D. A. The environment and Parkinson's disease: is the nigrostriatal system preferentially targeted by neurotoxins?. Lancet Neurol., 2003, 2, 531-538.
    • (2003) Lancet Neurol , vol.2 , pp. 531-538
    • Di Monte, D.A.1
  • 50
    • 43049175139 scopus 로고    scopus 로고
    • Role of reactive oxygen species in the neurotoxicity of environmental agents implicated in Parkinson's disease
    • Drechsel, D. A.; Patel, M. Role of reactive oxygen species in the neurotoxicity of environmental agents implicated in Parkinson's disease. Free Radic. Biol. Med., 2008, 44, 1873-1886.
    • (2008) Free Radic. Biol. Med , vol.44 , pp. 1873-1886
    • Drechsel, D.A.1    Patel, M.2
  • 54
    • 0037424245 scopus 로고    scopus 로고
    • Mitochondrial complex I inhibitor rotenone induces apoptosis through enhancing mitochondrial reactive oxygen species production
    • Li, N.; Ragheb, K.; Lawler, G.; Sturgis, J.; Rajwa, B.; Melendez, J. A.; Robinson, J. P. Mitochondrial complex I inhibitor rotenone induces apoptosis through enhancing mitochondrial reactive oxygen species production. J. Biol. Chem., 2003, 278, 8516-8525.
    • (2003) J. Biol. Chem , vol.278 , pp. 8516-8525
    • Li, N.1    Ragheb, K.2    Lawler, G.3    Sturgis, J.4    Rajwa, B.5    Melendez, J.A.6    Robinson, J.P.7
  • 55
    • 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, J. S.; Hileman, E. O.; Plunkett, W.; Keating, M. J.; Huang, P. 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    Keating, M.J.7    Huang, P.8
  • 56
    • 0035930930 scopus 로고    scopus 로고
    • Rotenone-induced G2/M cell cycle arrest and apoptosis in a human B lymphoma cell line PW
    • Armstrong, J. S.; Hornung, B.; Lecane, P.; Jones, D. P.; Knox, S. J. Rotenone-induced G2/M cell cycle arrest and apoptosis in a human B lymphoma cell line PW. Biochem. Biophys. Res. Commun., 2001, 289, 973-978.
    • (2001) Biochem. Biophys. Res. Commun , vol.289 , pp. 973-978
    • Armstrong, J.S.1    Hornung, B.2    Lecane, P.3    Jones, D.P.4    Knox, S.J.5
  • 57
    • 75849160168 scopus 로고    scopus 로고
    • Rotenone induces apoptosis in MCF-7 human breast cancer cell-mediated ROS through JNK and p38 signaling
    • Deng, Y. T.; Huang, H. C.; Lin, J. K. Rotenone induces apoptosis in MCF-7 human breast cancer cell-mediated ROS through JNK and p38 signaling. Mol. Carcinog, 2010, 49, 141-151.
    • (2010) Mol. Carcinog , vol.49 , pp. 141-151
    • Deng, Y.T.1    Huang, H.C.2    Lin, J.K.3
  • 58
    • 0037453909 scopus 로고    scopus 로고
    • Effects of deguelin on the phosphatidylinositol 3-kinase/Akt pathway and apoptosis in premalignant human bronchial epithelial cells
    • Chun, K. H.; Kosmeder, J. W., 2nd; Sun, S.; Pezzuto, J. M.; Lotan, R.; Hong, W. K.; Lee, H. Y. Effects of deguelin on the phosphatidylinositol 3-kinase/Akt pathway and apoptosis in premalignant human bronchial epithelial cells. J. Natl. Cancer Inst., 2003, 95, 291-302.
    • (2003) J. Natl. Cancer Inst , vol.95 , pp. 291-302
    • Chun, K.H.1    Kosmeder II, J.W.2    Sun, S.3    Pezzuto, J.M.4    Lotan, R.5    Hong, W.K.6    Lee, H.Y.7
  • 60
    • 36749072578 scopus 로고    scopus 로고
    • Identification of novel antiangiogenic anticancer activities of deguelin targeting hypoxia-inducible factor-1 alpha
    • Oh, S. H.; Woo, J. K.; Jin, Q.; Kang, H. J.; Jeong, J. W.; Kim, K. W.; Hong, W. K.; Lee, H. Y. Identification of novel antiangiogenic anticancer activities of deguelin targeting hypoxia-inducible factor-1 alpha. Int. J. Cancer, 2008, 122, 5-14.
    • (2008) Int. J. Cancer , vol.122 , pp. 5-14
    • Oh, S.H.1    Woo, J.K.2    Jin, Q.3    Kang, H.J.4    Jeong, J.W.5    Kim, K.W.6    Hong, W.K.7    Lee, H.Y.8
  • 62
    • 33847259309 scopus 로고    scopus 로고
    • The Akt inhibitor deguelin, is an angiopreventive agent also acting on the NF-kappaB pathway
    • Dell'Eva, R.; Ambrosini, C.; Minghelli, S.; Noonan, D. M.; Albini, A.; Ferrari, N. The Akt inhibitor deguelin, is an angiopreventive agent also acting on the NF-kappaB pathway. Carcinogenesis, 2007, 28, 404-413.
    • (2007) Carcinogenesis , vol.28 , pp. 404-413
    • Dell'eva, R.1    Ambrosini, C.2    Minghelli, S.3    Noonan, D.M.4    Albini, A.5    Ferrari, N.6
  • 63
    • 33749524818 scopus 로고    scopus 로고
    • Deguelin, an Akt inhibitor, suppresses IkappaBalpha kinase activation leading to suppression of NF-kappaBregulated gene expression, potentiation of apoptosis, and inhibition of cellular invasion
    • Nair, A. S.; Shishodia, S.; Ahn, K. S.; Kunnumakkara, A. B.; Sethi, G.; Aggarwal, B. B. Deguelin, an Akt inhibitor, suppresses IkappaBalpha kinase activation leading to suppression of NF-kappaBregulated gene expression, potentiation of apoptosis, and inhibition of cellular invasion. J. Immunol., 2006, 177, 5612-5622.
    • (2006) J. Immunol , vol.177 , pp. 5612-5622
    • Nair, A.S.1    Shishodia, S.2    Ahn, K.S.3    Kunnumakkara, A.B.4    Sethi, G.5    Aggarwal, B.B.6
  • 64
    • 2442669734 scopus 로고    scopus 로고
    • Apoptosis induction by the natural product cancer chemopreventive agent deguelin is mediated through the inhibition of mitochondrial bioenergetics
    • Hail, N., Jr.; Lotan, R. Apoptosis induction by the natural product cancer chemopreventive agent deguelin is mediated through the inhibition of mitochondrial bioenergetics. Apoptosis, 2004, 9, 437-447.
    • (2004) Apoptosis , vol.9 , pp. 437-447
    • Hail Jr., N.1    Lotan, R.2
  • 65
    • 60549083336 scopus 로고    scopus 로고
    • Targeting heat shock protein 90 overrides the resistance of lung cancer cells by blocking radiation-induced stabilization of hypoxiainducible factor-1alpha
    • Kim, W. Y.; Oh, S. H.; Woo, J. K.; Hong, W. K.; Lee, H. Y. Targeting heat shock protein 90 overrides the resistance of lung cancer cells by blocking radiation-induced stabilization of hypoxiainducible factor-1alpha. Cancer Res., 2009, 69, 1624-1632.
    • (2009) Cancer Res , vol.69 , pp. 1624-1632
    • Kim, W.Y.1    Oh, S.H.2    Woo, J.K.3    Hong, W.K.4    Lee, H.Y.5
  • 68
    • 33744518169 scopus 로고    scopus 로고
    • Tamoxifen and estradiol interact with the flavin mononucleotide site of complex I leading to mitochondrial failure
    • Moreira, P. I.; Custodio, J.; Moreno, A.; Oliveira, C. R.; Santos, M. S. Tamoxifen and estradiol interact with the flavin mononucleotide site of complex I leading to mitochondrial failure. J. Biol. Chem., 2006, 281, 10143-10152.
    • (2006) J. Biol. Chem , vol.281 , pp. 10143-10152
    • Moreira, P.I.1    Custodio, J.2    Moreno, A.3    Oliveira, C.R.4    Santos, M.S.5
  • 71
    • 18044398983 scopus 로고    scopus 로고
    • Reversal of tamoxifen resistant breast cancer by low dose estrogen therapy
    • Osipo, C.; Gajdos, C.; Cheng, D.; Jordan, V. C. Reversal of tamoxifen resistant breast cancer by low dose estrogen therapy. J. Steroid Biochem. Mol. Biol., 2005, 93, 249-256.
    • (2005) J. Steroid Biochem. Mol. Biol , vol.93 , pp. 249-256
    • Osipo, C.1    Gajdos, C.2    Cheng, D.3    Jordan, V.C.4
  • 72
    • 34247096170 scopus 로고    scopus 로고
    • Target identification of drug induced mitochondrial toxicity using immunocapture based OXPHOS activity assays
    • Nadanaciva, S.; Bernal, A.; Aggeler, R.; Capaldi, R.; Will, Y. Target identification of drug induced mitochondrial toxicity using immunocapture based OXPHOS activity assays. Toxicol In Vitro, 2007, 21, 902-911.
    • (2007) Toxicol In Vitro , vol.21 , pp. 902-911
    • Nadanaciva, S.1    Bernal, A.2    Aggeler, R.3    Capaldi, R.4    Will, Y.5
  • 74
    • 21244503033 scopus 로고    scopus 로고
    • Crystal structure of mitochondrial respiratory membrane protein complex II
    • Sun, F.; Huo, X.; Zhai, Y.; Wang, A.; Xu, J.; Su, D.; Bartlam, M.; Rao, Z. Crystal structure of mitochondrial respiratory membrane protein complex II. Cell, 2005, 121, 1043-1057.
    • (2005) Cell , vol.121 , pp. 1043-1057
    • Sun, F.1    Huo, X.2    Zhai, Y.3    Wang, A.4    Xu, J.5    Su, D.6    Bartlam, M.7    Rao, Z.8
  • 75
    • 78149465602 scopus 로고    scopus 로고
    • The quinone-binding and catalytic site of complex II
    • in press
    • Maklashina, E.; Cecchini, G. The quinone-binding and catalytic site of complex II. Biochim. Biophys. Acta, 2010, in press.
    • (2010) Biochim. Biophys. Acta
    • Maklashina, E.1    Cecchini, G.2
  • 78
    • 21844469713 scopus 로고    scopus 로고
    • Alpha-tocopheryl succinate inhibits malignant mesothelioma by disrupting the fibroblast growth factor autocrine loop: Mechanism and the role of oxidative stress
    • Stapelberg, M.; Gellert, N.; Swettenham, E.; Tomasetti, M.; Witting, P. K.; Procopio, A.; Neuzil, J. Alpha-tocopheryl succinate inhibits malignant mesothelioma by disrupting the fibroblast growth factor autocrine loop: mechanism and the role of oxidative stress. J. Biol. Chem., 2005, 280, 25369-76.
    • (2005) J. Biol. Chem , vol.280 , pp. 25369-25376
    • Stapelberg, M.1    Gellert, N.2    Swettenham, E.3    Tomasetti, M.4    Witting, P.K.5    Procopio, A.6    Neuzil, J.7
  • 79
    • 33748423217 scopus 로고    scopus 로고
    • Vitamin E analogues as anticancer agents: Lessons from studies with alpha-tocopheryl succinate
    • Wang, X. F.; Dong, L.; Zhao, Y.; Tomasetti, M.; Wu, K.; Neuzil, J. Vitamin E analogues as anticancer agents: lessons from studies with alpha-tocopheryl succinate. Mol. Nutr. Food Res., 2006, 50, 675-685.
    • (2006) Mol. Nutr. Food Res , vol.50 , pp. 675-685
    • Wang, X.F.1    Dong, L.2    Zhao, Y.3    Tomasetti, M.4    Wu, K.5    Neuzil, J.6
  • 80
    • 0035137727 scopus 로고    scopus 로고
    • Selective cancer cell killing by alpha-tocopheryl succinate
    • Neuzil, J.; Weber, T.; Gellert, N.; Weber, C. Selective cancer cell killing by alpha-tocopheryl succinate. Br. J. Cancer, 2001, 84, 87-89.
    • (2001) Br. J. Cancer , vol.84 , pp. 87-89
    • Neuzil, J.1    Weber, T.2    Gellert, N.3    Weber, C.4
  • 82
    • 1642501556 scopus 로고    scopus 로고
    • A vitamin E analogue suppresses malignant mesothelioma in a preclinical model: A future drug against a fatal neoplastic disease?
    • Tomasetti, M.; Gellert, N.; Procopio, A.; Neuzil, J. A vitamin E analogue suppresses malignant mesothelioma in a preclinical model: a future drug against a fatal neoplastic disease? Int. J. Cancer, 2004, 109, 641-642.
    • (2004) Int. J. Cancer , vol.109 , pp. 641-642
    • Tomasetti, M.1    Gellert, N.2    Procopio, A.3    Neuzil, J.4
  • 84
    • 77956997398 scopus 로고    scopus 로고
    • Involvement of Ca(2+) and ROS in alpha-tocopheryl succinate-induced mitochondrial permeabilization
    • Gogvadze, V.; Norberg, E.; Orrenius, S.; Zhivotovsky, B. Involvement of Ca(2+) and ROS in alpha-tocopheryl succinate-induced mitochondrial permeabilization. Int. J. Cancer, 2010, 2010, 127, 1823-1832.
    • (2010) Int. J. Cancer , vol.2010 , Issue.127 , pp. 1823-1832
    • Gogvadze, V.1    Norberg, E.2    Orrenius, S.3    Zhivotovsky, B.4
  • 86
    • 77954570017 scopus 로고    scopus 로고
    • Alpha-Tocopheryl succinate causes mitochondrial permeabilization by preferential formation of Bak channels
    • Prochazka, L.; Dong, L. F.; Valis, K.; Freeman, R.; Ralph, S. J.; Turanek, J.; Neuzil, J. Alpha-Tocopheryl succinate causes mitochondrial permeabilization by preferential formation of Bak channels. Apoptosis, 2010, 15, 782-794.
    • (2010) Apoptosis , vol.15 , pp. 782-794
    • Prochazka, L.1    Dong, L.F.2    Valis, K.3    Freeman, R.4    Ralph, S.J.5    Turanek, J.6    Neuzil, J.7
  • 87
    • 33744959427 scopus 로고    scopus 로고
    • Alpha-Tocopheryl succinate induces apoptosis in prostate cancer cells in part through inhibition of BclxL/ Bcl-2 function
    • Shiau, C. W.; Huang, J. W.; Wang, D. S.; Weng, J. R.; Yang, C. C.; Lin, C. H.; Li, C.; Chen, C.S. Alpha-Tocopheryl succinate induces apoptosis in prostate cancer cells in part through inhibition of BclxL/ Bcl-2 function, J. Biol. Chem., 2006, 281, 11819-11825.
    • (2006) J. Biol. Chem , vol.281 , pp. 11819-11825
    • Shiau, C.W.1    Huang, J.W.2    Wang, D.S.3    Weng, J.R.4    Yang, C.C.5    Lin, C.H.6    Li, C.7    Chen, C.S.8
  • 89
  • 91
    • 77951668551 scopus 로고    scopus 로고
    • Downregulation of Epidermal Growth Factor Receptor Expression Contributes to alpha-TEA's Proapoptotic Effects in Human Ovarian Cancer Cell Lines
    • Shun, M. C.; Yu, W.; Park, S. K.; Sanders, B. G.; Kline, K. Downregulation of Epidermal Growth Factor Receptor Expression Contributes to alpha-TEA's Proapoptotic Effects in Human Ovarian Cancer Cell Lines. J. Oncol., 2010, 2010, 824-571.
    • (2010) J. Oncol , vol.2010 , pp. 571-824
    • Shun, M.C.1    Yu, W.2    Park, S.K.3    Sanders, B.G.4    Kline, K.5
  • 94
    • 34548791268 scopus 로고    scopus 로고
    • Alpha-Tocopheryl succinate inhibits angiogenesis by disrupting paracrine FGF2 signalling
    • Neuzil, J.; Swettenham, E.; Wang, X. F.; Dong, L. F.; Stapelberg, M. alpha-Tocopheryl succinate inhibits angiogenesis by disrupting paracrine FGF2 signalling. FEBS Lett., 2007, 581, 4611-4615.
    • (2007) FEBS Lett , vol.581 , pp. 4611-4615
    • Neuzil, J.1    Swettenham, E.2    Wang, X.F.3    Dong, L.F.4    Stapelberg, M.5
  • 96
    • 0035930395 scopus 로고    scopus 로고
    • Vitamin E succinate protects hepatocytes against the toxic effect of reactive oxygen species generated at mitochondrial complexes I and III by alkylating agents
    • Zhang, J. G.; Nicholls-Grzemski, F. A.; Tirmenstein, M. A.; Fariss, M. W. Vitamin E succinate protects hepatocytes against the toxic effect of reactive oxygen species generated at mitochondrial complexes I and III by alkylating agents. Chem. Biol. Interact, 2001, 138, 267-284.
    • (2001) Chem. Biol. Interact , vol.138 , pp. 267-284
    • Zhang, J.G.1    Nicholls-Grzemski, F.A.2    Tirmenstein, M.A.3    Fariss, M.W.4
  • 97
    • 12344254836 scopus 로고    scopus 로고
    • Hepatic processing determines dual activity of alpha-tocopheryl succinate: A novel paradigm for a shift in biological activity due to pro-vitamin-to-vitamin conversion
    • Neuzil, J.; Massa, H. Hepatic processing determines dual activity of alpha-tocopheryl succinate: a novel paradigm for a shift in biological activity due to pro-vitamin-to-vitamin conversion. Biochem. Biophys. Res. Commun., 2005, 327, 1024-1027.
    • (2005) Biochem. Biophys. Res. Commun , vol.327 , pp. 1024-1027
    • Neuzil, J.1    Massa, H.2
  • 98
    • 1642441930 scopus 로고    scopus 로고
    • Apoptotic death in Leishmania donovani promastigotes in response to respiratory chain inhibition: Complex II inhibition results in increased pentamidine cytotoxicity
    • Mehta, A.; Shaha, C. Apoptotic death in Leishmania donovani promastigotes in response to respiratory chain inhibition: complex II inhibition results in increased pentamidine cytotoxicity. J. Biol. Chem., 2004, 279, 11798-11813.
    • (2004) J. Biol. Chem , vol.279 , pp. 11798-11813
    • Mehta, A.1    Shaha, C.2
  • 99
    • 0035450853 scopus 로고    scopus 로고
    • Mitochondrial electron transport inhibitors cause lipid peroxidation-dependent and-independent cell death: Protective role of antioxidants
    • Zhang, J. G.; Tirmenstein, M. A.; Nicholls-Grzemski, F. A.; Fariss, M. W. Mitochondrial electron transport inhibitors cause lipid peroxidation-dependent and-independent cell death: protective role of antioxidants. Arch. Biochem. Biophys., 2001, 393, 87-96.
    • (2001) Arch. Biochem. Biophys , vol.393 , pp. 87-96
    • Zhang, J.G.1    Tirmenstein, M.A.2    Nicholls-Grzemski, F.A.3    Fariss, M.W.4
  • 100
    • 34347345089 scopus 로고    scopus 로고
    • Mechanism of thiazolidinedione-dependent cell death in Jurkat T cells
    • Soller, M.; Drose, S.; Brandt, U.; Brune, B.; von Knethen, A. Mechanism of thiazolidinedione-dependent cell death in Jurkat T cells, Mol Pharmacol, 2007, 71, 1535-44.
    • (2007) Mol Pharmacol , vol.71 , pp. 1535-1544
    • Soller, M.1    Drose, S.2    Brandt, U.3    Brune, B.4    von Knethen, A.5
  • 101
    • 0037353404 scopus 로고    scopus 로고
    • Troglitazoneinduced liver failure: A case study
    • Graham, D. J.; Green, L.; Senior, J. R.; Nourjah, P. Troglitazoneinduced liver failure: a case study. Am. J. Med., 2003, 114, 299-306.
    • (2003) Am. J. Med , vol.114 , pp. 299-306
    • Graham, D.J.1    Green, L.2    Senior, J.R.3    Nourjah, P.4
  • 103
  • 104
    • 33847109840 scopus 로고    scopus 로고
    • Reactive oxygen species and p38 mitogen-activated protein kinase activate Bax to induce mito chondrial cytochrome c release and apoptosis in response to malonate
    • Gomez-Lazaro, M.; Galindo, M. F.; Melero-Fernandez de Mera, R. M.; Fernandez-Gomez, F. J.; Concannon, C. G.; Segura, M. F.; Comella, J. X.; Prehn, J. H.; Jordan, J. Reactive oxygen species and p38 mitogen-activated protein kinase activate Bax to induce mito chondrial cytochrome c release and apoptosis in response to malonate, Mol. Pharmacol., 2007, 71, 736-743.
    • (2007) Mol. Pharmacol , vol.71 , pp. 736-743
    • Gomez-Lazaro, M.1    Galindo, M.F.2    de mera, R.M.M.-F.3    Fernandez-Gomez, F.J.4    Concannon, C.G.5    Segura, M.F.6    Comella, J.X.7    Prehn, J.H.8    Jordan, J.9
  • 105
    • 33646846683 scopus 로고    scopus 로고
    • 3-nitropropionic acid is a suicide inhibitor of mitochondrial respiration that, upon oxidation by complex II, forms a covalent adduct with a catalytic base arginine in the active site of the enzyme
    • Huang, L. S.; Sun, G.; Cobessi, D.; Wang, A. C.; Shen, J. T.; Tung, E. Y.; Anderson, V. E.; Berry, E.A. 3-nitropropionic acid is a suicide inhibitor of mitochondrial respiration that, upon oxidation by complex II, forms a covalent adduct with a catalytic base arginine in the active site of the enzyme, J. Biol. Chem., 2006, 281, 5965-5972.
    • (2006) J. Biol. Chem , vol.281 , pp. 5965-5972
    • Huang, L.S.1    Sun, G.2    Cobessi, D.3    Wang, A.C.4    Shen, J.T.5    Tung, E.Y.6    Anderson, V.E.7    Berry, E.A.8
  • 106
    • 67349120572 scopus 로고    scopus 로고
    • Complex II inhibition by 3-NP causes mitochondrial fragmentation and neuronal cell death via an NMDA-and ROSdependent pathway
    • Liot, G.; Bossy, B.; Lubitz, S.; Kushnareva, Y.; Sejbuk, N.; Bossy-Wetzel, E. Complex II inhibition by 3-NP causes mitochondrial fragmentation and neuronal cell death via an NMDA-and ROSdependent pathway. Cell Death Differ., 2009, 16, 899-909.
    • (2009) Cell Death Differ , vol.16 , pp. 899-909
    • Liot, G.1    Bossy, B.2    Lubitz, S.3    Kushnareva, Y.4    Sejbuk, N.5    Bossy-Wetzel, E.6
  • 110
    • 0030867866 scopus 로고    scopus 로고
    • Crystal structure of the cytochrome bc1 complex from bovine heart mitochondria
    • Xia, D.; Yu, C. A.; Kim, H.; Xia, J. Z.; Kachurin, A. M.; Zhang, L.; Yu, L.; Deisenhofer, J. Crystal structure of the cytochrome bc1 complex from bovine heart mitochondria. Science, 1997, 277, 60-66.
    • (1997) Science , vol.277 , pp. 60-66
    • Xia, D.1    Yu, C.A.2    Kim, H.3    Xia, J.Z.4    Kachurin, A.M.5    Zhang, L.6    Yu, L.7    Deisenhofer, J.8
  • 111
    • 52049104467 scopus 로고    scopus 로고
    • The mechanism of mitochondrial superoxide production by the cytochrome bc1 complex
    • Drose, S.; Brandt, U. The mechanism of mitochondrial superoxide production by the cytochrome bc1 complex. J. Biol. Chem., 2008, 283, 21649-21654.
    • (2008) J. Biol. Chem , vol.283 , pp. 21649-21654
    • Drose, S.1    Brandt, U.2
  • 112
    • 0141815741 scopus 로고    scopus 로고
    • Production of reactive oxygen species by mitochondria: Central role of complex III
    • Chen, Q.; Vazquez, E. J.; Moghaddas, S.; Hoppel, C. L.; Lesnefsky, E. J. Production of reactive oxygen species by mitochondria: central role of complex III. J. Biol. Chem., 2003, 278, 36027-31.
    • (2003) J. Biol. Chem , vol.278 , pp. 36027-36031
    • Chen, Q.1    Vazquez, E.J.2    Moghaddas, S.3    Hoppel, C.L.4    Lesnefsky, E.J.5
  • 113
    • 1942447877 scopus 로고    scopus 로고
    • The cytochrome bc1 complex: Function in the context of structure
    • Crofts, A. R. The cytochrome bc1 complex: function in the context of structure. Annu. Rev. Physiol., 2004, 66, 689-733.
    • (2004) Annu. Rev. Physiol , vol.66 , pp. 689-733
    • Crofts, A.R.1
  • 118
    • 14944349512 scopus 로고    scopus 로고
    • Adaphostin-induced apoptosis in CLL B cells is associated with induction of oxidative stress and exhibits synergy with fludarabine
    • Shanafelt, T. D.; Lee, Y. K.; Bone, N. D.; Strege, A. K.; Narayanan, V. L.; Sausville, E. A.; Geyer, S. M.; Kaufmann, S. H.; Kay, N. E. Adaphostin-induced apoptosis in CLL B cells is associated with induction of oxidative stress and exhibits synergy with fludarabine. Blood, 2005, 105, 2099-2106.
    • (2005) Blood , vol.105 , pp. 2099-2106
    • Shanafelt, T.D.1    Lee, Y.K.2    Bone, N.D.3    Strege, A.K.4    Narayanan, V.L.5    Sausville, E.A.6    Geyer, S.M.7    Kaufmann, S.H.8    Kay, N.E.9
  • 119
    • 33746638536 scopus 로고    scopus 로고
    • Adaphostin and bortezomib induce oxidative injury and apoptosis in imatinib mesylate-resistant hematopoietic cells expressing mutant forms of Bcr/Abl
    • Dasmahapatra, G.; Nguyen, T. K.; Dent, P.; Grant, S. Adaphostin and bortezomib induce oxidative injury and apoptosis in imatinib mesylate-resistant hematopoietic cells expressing mutant forms of Bcr/Abl. Leuk Res., 2006, 30, 1263-1272.
    • (2006) Leuk Res , vol.30 , pp. 1263-1272
    • Dasmahapatra, G.1    Nguyen, T.K.2    Dent, P.3    Grant, S.4
  • 122
    • 1442308361 scopus 로고    scopus 로고
    • Induction of apoptosis in human leukemia cells by the tyrosine kinase inhibitor adaphostin proceeds through a RAF-1/MEK/ERK-and AKT-dependent process
    • Yu, C.; Rahmani, M.; Almenara, J.; Sausville, E. A.; Dent, P.; Grant, S. Induction of apoptosis in human leukemia cells by the tyrosine kinase inhibitor adaphostin proceeds through a RAF-1/MEK/ERK-and AKT-dependent process Oncogene, 2004, 23, 1364-1376.
    • (2004) Oncogene , vol.23 , pp. 1364-1376
    • Yu, C.1    Rahmani, M.2    Almenara, J.3    Sausville, E.A.4    Dent, P.5    Grant, S.6
  • 123
    • 33846012546 scopus 로고    scopus 로고
    • Molecular mechanism of adaphostin-mediated G1 arrest in prostate cancer (PC-3) cells: Signaling events mediated by hepatocyte growth factor receptor, c-Met, and p38 MAPK pathways
    • Mukhopadhyay, I.; Sausville, E. A.; Doroshow, J. H.; Roy, K. K. Molecular mechanism of adaphostin-mediated G1 arrest in prostate cancer (PC-3) cells: signaling events mediated by hepatocyte growth factor receptor, c-Met, and p38 MAPK pathways, J. Biol. Chem., 2006, 281, 37330-37344.
    • (2006) J. Biol. Chem , vol.281 , pp. 37330-37344
    • Mukhopadhyay, I.1    Sausville, E.A.2    Doroshow, J.H.3    Roy, K.K.4
  • 125
    • 0035408191 scopus 로고    scopus 로고
    • Resveratrol, a tumor-suppressive compound from grapes, induces apoptosis via a novel mitochondrial pathway controlled by Bcl-2
    • Tinhofer, I.; Bernhard, D.; Senfter, M.; Anether, G.; Loeffler, M.; Kroemer, G.; Kofler, R.; Csordas, A.; Greil, R. Resveratrol, a tumor-suppressive compound from grapes, induces apoptosis via a novel mitochondrial pathway controlled by Bcl-2. FASEB J., 2001, 15, 1613-1615.
    • (2001) FASEB J , vol.15 , pp. 1613-1615
    • Tinhofer, I.1    Bernhard, D.2    Senfter, M.3    Anether, G.4    Loeffler, M.5    Kroemer, G.6    Kofler, R.7    Csordas, A.8    Greil, R.9
  • 127
    • 43549088782 scopus 로고    scopus 로고
    • Resveratrol: A multitargeted agent for age-associated chronic diseases
    • Harikumar, K. B.; Aggarwal, B. B. Resveratrol: a multitargeted agent for age-associated chronic diseases. Cell Cycle, 2008, 7, 1020-1035.
    • (2008) Cell Cycle , vol.7 , pp. 1020-1035
    • Harikumar, K.B.1    Aggarwal, B.B.2
  • 128
    • 77955839687 scopus 로고    scopus 로고
    • Xanthohumol-induced transient superoxide anion radical formation triggers cancer cells into apoptosis via a mitochondria-mediated mechanism
    • Strathmann, J.; Klimo, K.; Sauer, S. W.; Okun, J. G.; Prehn, J. H.; Gerhauser, C. Xanthohumol-induced transient superoxide anion radical formation triggers cancer cells into apoptosis via a mitochondria-mediated mechanism. FASEB J., 2010.
    • (2010) FASEB J
    • Strathmann, J.1    Klimo, K.2    Sauer, S.W.3    Okun, J.G.4    Prehn, J.H.5    Gerhauser, C.6
  • 129
    • 33845611585 scopus 로고    scopus 로고
    • Xanthohumol, a prenylflavonoid derived from hops induces apoptosis and inhibits NF-kappaB activation in prostate epithelial cells
    • Colgate, E. C.; Miranda, C. L.; Stevens, J. F.; Bray, T. M.; Ho, E. Xanthohumol, a prenylflavonoid derived from hops induces apoptosis and inhibits NF-kappaB activation in prostate epithelial cells. Cancer Lett., 2007, 246, 201-209.
    • (2007) Cancer Lett , vol.246 , pp. 201-209
    • Colgate, E.C.1    Miranda, C.L.2    Stevens, J.F.3    Bray, T.M.4    Ho, E.5
  • 130
    • 33645814383 scopus 로고    scopus 로고
    • Mechanisms of the antiangiogenic activity by the hop flavonoid xanthohumol: NF-kappaB and Akt as targets
    • Albini, A.; Dell'Eva, R.; Vene, R.; Ferrari, N.; Buhler, D. R.; Noonan, D. M.; Fassina, G. Mechanisms of the antiangiogenic activity by the hop flavonoid xanthohumol: NF-kappaB and Akt as targets. FASEB J., 2006, 20, 527-529.
    • (2006) FASEB J , vol.20 , pp. 527-529
    • Albini, A.1    Dell'eva, R.2    Vene, R.3    Ferrari, N.4    Buhler, D.R.5    Noonan, D.M.6    Fassina, G.7
  • 132
    • 61949193344 scopus 로고    scopus 로고
    • Modification of the cysteine residues in IkappaBalpha kinase and NF-kappaB (p65) by xanthohumol leads to suppression of NF-kappaB-regulated gene products and potentiation of apoptosis in leukemia cells
    • Harikumar, K. B.; Kunnumakkara, A. B.; Ahn, K. S.; Anand, P.; Krishnan, S.; Guha, S.; Aggarwal, B. B. Modification of the cysteine residues in IkappaBalpha kinase and NF-kappaB (p65) by xanthohumol leads to suppression of NF-kappaB-regulated gene products and potentiation of apoptosis in leukemia cells. Blood, 2009, 113, 2003-2013.
    • (2009) Blood , vol.113 , pp. 2003-2013
    • Harikumar, K.B.1    Kunnumakkara, A.B.2    Ahn, K.S.3    Anand, P.4    Krishnan, S.5    Guha, S.6    Aggarwal, B.B.7
  • 135
    • 57649174596 scopus 로고    scopus 로고
    • Benzyl isothiocyanate targets mitochondrial respiratory chain to trigger reactive oxygen species-dependent apoptosis in human breast cancer cells
    • Xiao, D.; Powolny, A. A.; Singh, S. V. Benzyl isothiocyanate targets mitochondrial respiratory chain to trigger reactive oxygen species-dependent apoptosis in human breast cancer cells. J. Biol. Chem., 2008, 283, 30151-30163.
    • (2008) J. Biol. Chem , vol.283 , pp. 30151-30163
    • Xiao, D.1    Powolny, A.A.2    Singh, S.V.3
  • 136
    • 70349989502 scopus 로고    scopus 로고
    • Benzyl isothiocyanate-mediated generation of reactive oxygen species causes cell cycle arrest and induces apoptosis via activation of MAPK in human pancreatic cancer cells
    • Sahu, R. P.; Zhang, R.; Batra, S.; Shi, Y.; Srivastava, S. K. Benzyl isothiocyanate-mediated generation of reactive oxygen species causes cell cycle arrest and induces apoptosis via activation of MAPK in human pancreatic cancer cells. Carcinogenesis, 2009, 30, 1744-1753.
    • (2009) Carcinogenesis , vol.30 , pp. 1744-1753
    • Sahu, R.P.1    Zhang, R.2    Batra, S.3    Shi, Y.4    Srivastava, S.K.5
  • 137
    • 0037040918 scopus 로고    scopus 로고
    • Involvement of the mitochondrial death pathway in chemopreventive benzyl isothiocyanate-induced apoptosis
    • Nakamura, Y.; Kawakami, M.; Yoshihiro, A.; Miyoshi, N.; Ohigashi, H.; Kawai, K.; Osawa, T.; Uchida, K. Involvement of the mitochondrial death pathway in chemopreventive benzyl isothiocyanate-induced apoptosis. J. Biol. Chem., 2002, 277, 8492-8499.
    • (2002) J. Biol. Chem , vol.277 , pp. 8492-8499
    • Nakamura, Y.1    Kawakami, M.2    Yoshihiro, A.3    Miyoshi, N.4    Ohigashi, H.5    Kawai, K.6    Osawa, T.7    Uchida, K.8
  • 138
    • 77953037528 scopus 로고    scopus 로고
    • Inhibition of human breast cancer xenograft growth by cruciferous vegetable constituent benzyl isothiocyanate
    • Warin, R.; Xiao, D.; Arlotti, J. A.; Bommareddy, A.; Singh, S. V. Inhibition of human breast cancer xenograft growth by cruciferous vegetable constituent benzyl isothiocyanate. Mol. Carcinog, 2010, 49, 500-507.
    • (2010) Mol. Carcinog , vol.49 , pp. 500-507
    • Warin, R.1    Xiao, D.2    Arlotti, J.A.3    Bommareddy, A.4    Singh, S.V.5
  • 139
    • 0036142924 scopus 로고    scopus 로고
    • Inhibition of benzo(a)pyrene-induced lung tumorigenesis in A/J mice by dietary N-acetylcysteine conjugates of benzyl and phenethyl isothiocyanates during the postinitiation phase is associated with activation of mitogen-activated protein kinases and p53 activity and induction of apoptosis
    • Yang, Y. M.; Conaway, C. C.; Chiao, J. W.; Wang, C. X.; Amin, S.; Whysner, J.; Dai, W.; Reinhardt, J.; Chung, F. L. Inhibition of benzo(a)pyrene-induced lung tumorigenesis in A/J mice by dietary N-acetylcysteine conjugates of benzyl and phenethyl isothiocyanates during the postinitiation phase is associated with activation of mitogen-activated protein kinases and p53 activity and induction of apoptosis. Cancer Res., 2002, 62, 2-7.
    • (2002) Cancer Res , vol.62 , pp. 2-7
    • Yang, Y.M.1    Conaway, C.C.2    Chiao, J.W.3    Wang, C.X.4    Amin, S.5    Whysner, J.6    Dai, W.7    Reinhardt, J.8    Chung, F.L.9
  • 140
    • 73649091148 scopus 로고    scopus 로고
    • Prevention of mammary carcinogenesis in MMTV-neu mice by cruciferous vegetable constituent benzyl isothiocyanate
    • Warin, R.; Chambers, W. H.; Potter, D. M.; Singh, S. V. Prevention of mammary carcinogenesis in MMTV-neu mice by cruciferous vegetable constituent benzyl isothiocyanate. Cancer Res., 2009, 69, 9473-9480.
    • (2009) Cancer Res , vol.69 , pp. 9473-9480
    • Warin, R.1    Chambers, W.H.2    Potter, D.M.3    Singh, S.V.4
  • 142
    • 77950370157 scopus 로고    scopus 로고
    • Mitochondrial respiratory chain involvement in peroxiredoxin 3 oxidation by phenethyl isothiocyanate and auranofin
    • Brown, K. K.; Cox, A. G.; Hampton, M. B. Mitochondrial respiratory chain involvement in peroxiredoxin 3 oxidation by phenethyl isothiocyanate and auranofin. FEBS Lett., 2010, 584, 1257-1262.
    • (2010) FEBS Lett , vol.584 , pp. 1257-1262
    • Brown, K.K.1    Cox, A.G.2    Hampton, M.B.3
  • 144
    • 0032891198 scopus 로고    scopus 로고
    • New lamellarin alkaloids from the australian ascidian, didemnum chartaceum
    • Davis, R. A.; Carroll, A. R.; Pierens, G. K.; Quinn, R. J. New lamellarin alkaloids from the australian ascidian, didemnum chartaceum. J. Nat. Prod., 1999, 62, 419-424.
    • (1999) J. Nat. Prod , vol.62 , pp. 419-424
    • Davis, R.A.1    Carroll, A.R.2    Pierens, G.K.3    Quinn, R.J.4
  • 149
    • 33947724515 scopus 로고    scopus 로고
    • HIF-1 regulates cytochrome oxidase subunits to optimize efficiency of respiration in hypoxic cells
    • Fukuda, R.; Zhang, H.; Kim, J. W.; Shimoda, L.; Dang, C. V.; Semenza, G. L. HIF-1 regulates cytochrome oxidase subunits to optimize efficiency of respiration in hypoxic cells. Cell, 2007, 129, 111-122.
    • (2007) Cell , vol.129 , pp. 111-122
    • Fukuda, R.1    Zhang, H.2    Kim, J.W.3    Shimoda, L.4    Dang, C.V.5    Semenza, G.L.6
  • 150
    • 0036513249 scopus 로고    scopus 로고
    • Does nitric oxide modulate mitochondrial energy generation and apoptosis?
    • Moncada, S.; Erusalimsky, J. D. Does nitric oxide modulate mitochondrial energy generation and apoptosis? Nat. Rev. Mol. Cell Biol., 2002, 3, 214-220.
    • (2002) Nat. Rev. Mol. Cell Biol , vol.3 , pp. 214-220
    • Moncada, S.1    Erusalimsky, J.D.2
  • 151
    • 0021017718 scopus 로고
    • Lung strips from guinea pigs as test system for lipoxygenase inhibitors. Inhibition of arachidonic acid-induced contractions by 3-t-butyl-4-hydroxyanisole and nordihydroguaiaretic acid
    • Slapke, J.; Schewe, T.; Hummel, S.; Winkler, J.; Kopf, M. Lung strips from guinea pigs as test system for lipoxygenase inhibitors. Inhibition of arachidonic acid-induced contractions by 3-t-butyl-4-hydroxyanisole and nordihydroguaiaretic acid. Biomed. Biochim. Acta, 1983, 42, 1309-1318.
    • (1983) Biomed. Biochim. Acta , vol.42 , pp. 1309-1318
    • Slapke, J.1    Schewe, T.2    Hummel, S.3    Winkler, J.4    Kopf, M.5
  • 152
    • 13844260816 scopus 로고    scopus 로고
    • Molecular mechanism of cell death induced by the antioxidant tertbutylhydroxyanisole in human monocytic leukemia U937 cells
    • Okubo, T.; Yokoyama, Y.; Kano, K.; Kano, I. Molecular mechanism of cell death induced by the antioxidant tertbutylhydroxyanisole in human monocytic leukemia U937 cells. Biol. Pharm. Bull, 2004, 27, 295-302.
    • (2004) Biol. Pharm. Bull , vol.27 , pp. 295-302
    • Okubo, T.1    Yokoyama, Y.2    Kano, K.3    Kano, I.4
  • 154
    • 0035476327 scopus 로고    scopus 로고
    • Cytochrome c oxidase inhibition by N-retinyl-N-retinylidene ethanolamine, a compound suspected to cause age-related macula degeneration
    • Shaban, H.; Gazzotti, P.; Richter, C. Cytochrome c oxidase inhibition by N-retinyl-N-retinylidene ethanolamine, a compound suspected to cause age-related macula degeneration. Arch Biochem. Biophys., 2001, 394, 111-116.
    • (2001) Arch Biochem. Biophys , vol.394 , pp. 111-116
    • Shaban, H.1    Gazzotti, P.2    Richter, C.3
  • 155
    • 0034671726 scopus 로고    scopus 로고
    • Age-related macular degeneration. The lipofusion component N-retinyl-N-retinylidene ethanolamine detaches proapoptotic proteins from mitochondria and induces apoptosis in mammalian retinal pigment epithelial cells
    • Suter, M.; Reme, C.; Grimm, C.; Wenzel, A.; Jaattela, M.; Esser, P.; Kociok, N.; Leist, M.; Richter, C. Age-related macular degeneration. The lipofusion component N-retinyl-N-retinylidene ethanolamine detaches proapoptotic proteins from mitochondria and induces apoptosis in mammalian retinal pigment epithelial cells. J. Biol. Chem., 2000, 275, 39625-39630.
    • (2000) J. Biol. Chem , vol.275 , pp. 39625-39630
    • Suter, M.1    Reme, C.2    Grimm, C.3    Wenzel, A.4    Jaattela, M.5    Esser, P.6    Kociok, N.7    Leist, M.8    Richter, C.9
  • 156
    • 34249941838 scopus 로고    scopus 로고
    • Mitochondria are targets of photodynamic therapy
    • Hilf, R. Mitochondria are targets of photodynamic therapy. J. Bioenerg Biomembr., 2007, 39, 85-9.
    • (2007) J. Bioenerg Biomembr , vol.39 , pp. 85-89
    • Hilf, R.1
  • 157
    • 0037040169 scopus 로고    scopus 로고
    • Cytochrome c oxidase subunit III: A molecular marker for N-(4-hydroxyphenyl) retinamise-induced oxidative stress in hepatoma cells
    • You, K. R.; Wen, J.; Lee, S. T.; Kim, D. G. Cytochrome c oxidase subunit III: a molecular marker for N-(4-hydroxyphenyl) retinamise-induced oxidative stress in hepatoma cells. J. Biol. Chem., 2002, 277, 3870-3877.
    • (2002) J. Biol. Chem , vol.277 , pp. 3870-3877
    • You, K.R.1    Wen, J.2    Lee, S.T.3    Kim, D.G.4
  • 159
    • 0027477389 scopus 로고
    • Mitochondrial cytochrome c oxidase as a target site for daunomycin in K-562 cells and heart tissue
    • Papadopoulou, L. C.; Tsiftsoglou, A. S. Mitochondrial cytochrome c oxidase as a target site for daunomycin in K-562 cells and heart tissue. Cancer Res., 1993, 53, 1072-1078.
    • (1993) Cancer Res , vol.53 , pp. 1072-1078
    • Papadopoulou, L.C.1    Tsiftsoglou, A.S.2
  • 160
    • 48949095741 scopus 로고    scopus 로고
    • The structure and function of mitochondrial F1F0-ATP synthases
    • Devenish, R. J.; Prescott, M.; Rodgers, A. J. The structure and function of mitochondrial F1F0-ATP synthases. Int. Rev. Cell Mol. Biol., 2008, 267, 1-58.
    • (2008) Int. Rev. Cell Mol. Biol , vol.267 , pp. 1-58
    • Devenish, R.J.1    Prescott, M.2    Rodgers, A.J.3
  • 161
    • 66249132322 scopus 로고    scopus 로고
    • Torque generation and elastic power transmission in the rotary F(O)F(1)-ATPase
    • Junge, W.; Sielaff, H.; Engelbrecht, S. Torque generation and elastic power transmission in the rotary F(O)F(1)-ATPase. Nature, 2009, 459, 364-370.
    • (2009) Nature , vol.459 , pp. 364-370
    • Junge, W.1    Sielaff, H.2    Engelbrecht, S.3
  • 162
    • 0035116589 scopus 로고    scopus 로고
    • Apoptolidin, a selective cytotoxic agent, is an inhibitor of F0F1-ATPase
    • Salomon, A. R.; Voehringer, D. W.; Herzenberg, L. A.; Khosla, C. Apoptolidin, a selective cytotoxic agent, is an inhibitor of F0F1-ATPase. Chem. Biol., 2001, 8, 71-80.
    • (2001) Chem. Biol , vol.8 , pp. 71-80
    • Salomon, A.R.1    Voehringer, D.W.2    Herzenberg, L.A.3    Khosla, C.4
  • 163
    • 0034687837 scopus 로고    scopus 로고
    • Understanding and exploiting the mechanistic basis for selectivity of polyketide inhibitors of F(0)F(1)-ATPase
    • Salomon, A. R.; Voehringer, D. W.; Herzenberg, L. A.; Khosla, C. Understanding and exploiting the mechanistic basis for selectivity of polyketide inhibitors of F(0)F(1)-ATPase. Proc. Natl. Acad Sci. USA, 2000, 97, 14766-14771.
    • (2000) Proc. Natl. Acad Sci. USA , vol.97 , pp. 14766-14771
    • Salomon, A.R.1    Voehringer, D.W.2    Herzenberg, L.A.3    Khosla, C.4
  • 164
    • 46749100904 scopus 로고    scopus 로고
    • Poly (ADP-ribose) polymerase activity regulates apoptosis in HeLa cells after alkylating DNA damage
    • Liu, X.; Luo, X.; Shi, Y.; Zhu, G. D.; Penning, T.; Giranda, V. L.; Luo, Y. Poly (ADP-ribose) polymerase activity regulates apoptosis in HeLa cells after alkylating DNA damage. Cancer Biol. Ther., 2008, 7, 934-941.
    • (2008) Cancer Biol. Ther , vol.7 , pp. 934-941
    • Liu, X.1    Luo, X.2    Shi, Y.3    Zhu, G.D.4    Penning, T.5    Giranda, V.L.6    Luo, Y.7
  • 165
    • 27344438327 scopus 로고    scopus 로고
    • Cells die with increased cytosolic ATP during apoptosis: A bioluminescence study with intracellular luciferase
    • Zamaraeva, M. V.; Sabirov, R. Z.; Maeno, E.; Ando-Akatsuka, Y.; Bessonova, S. V.; Okada, Y. Cells die with increased cytosolic ATP during apoptosis: a bioluminescence study with intracellular luciferase. Cell Death Differ., 2005, 12, 1390-1397.
    • (2005) Cell Death Differ , vol.12 , pp. 1390-1397
    • Zamaraeva, M.V.1    Sabirov, R.Z.2    Maeno, E.3    Ando-Akatsuka, Y.4    Bessonova, S.V.5    Okada, Y.6
  • 166
    • 0030915587 scopus 로고    scopus 로고
    • Intracellular ATP levels determine cell death fate by apoptosis or necrosis
    • Eguchi, Y.; Shimizu, S.; Tsujimoto, Y. Intracellular ATP levels determine cell death fate by apoptosis or necrosis. Cancer Res., 1997, 57, 1835-1840.
    • (1997) Cancer Res , vol.57 , pp. 1835-1840
    • Eguchi, Y.1    Shimizu, S.2    Tsujimoto, Y.3
  • 167
    • 0030900980 scopus 로고    scopus 로고
    • Intracellular adenosine triphosphate (ATP) concentration: A switch in the decision between apoptosis and necrosis
    • Leist, M.; Single, B.; Castoldi, A. F.; Kuhnle, S.; Nicotera, P. Intracellular adenosine triphosphate (ATP) concentration: a switch in the decision between apoptosis and necrosis. J. Exp. Med., 1997, 185, 1481-1486.
    • (1997) J. Exp. Med , vol.185 , pp. 1481-1486
    • Leist, M.1    Single, B.2    Castoldi, A.F.3    Kuhnle, S.4    Nicotera, P.5
  • 168
    • 0033776271 scopus 로고    scopus 로고
    • Changes in intramitochondrial and cytosolic pH: Early events that modulate caspase activation during apoptosis
    • Matsuyama, S.; Llopis, J.; Deveraux, Q. L.; Tsien, R. Y.; Reed, J. C. Changes in intramitochondrial and cytosolic pH: early events that modulate caspase activation during apoptosis. Nat. Cell Biol., 2000, 2, 318-325.
    • (2000) Nat. Cell Biol , vol.2 , pp. 318-325
    • Matsuyama, S.1    Llopis, J.2    Deveraux, Q.L.3    Tsien, R.Y.4    Reed, J.C.5
  • 169
    • 0033922250 scopus 로고    scopus 로고
    • Inhibition of mitochondrial proton F0F1-ATPase/ATP synthase by polyphenolic phytochemicals
    • Zheng, J.; Ramirez, V. D. Inhibition of mitochondrial proton F0F1-ATPase/ATP synthase by polyphenolic phytochemicals. Br. J. Pharmacol., 2000, 130, 1115-1123.
    • (2000) Br. J. Pharmacol , vol.130 , pp. 1115-1123
    • Zheng, J.1    Ramirez, V.D.2
  • 170
    • 35348865444 scopus 로고    scopus 로고
    • Mechanism of inhibition of bovine F1-ATPase by resveratrol and related polyphenols
    • Gledhill, J. R.; Montgomery, M. G.; Leslie, A. G.; Walker, J. E. Mechanism of inhibition of bovine F1-ATPase by resveratrol and related polyphenols. Proc. Natl. Acad Sci. USA, 2007, 104, 13632-13637.
    • (2007) Proc. Natl. Acad Sci. USA , vol.104 , pp. 13632-13637
    • Gledhill, J.R.1    Montgomery, M.G.2    Leslie, A.G.3    Walker, J.E.4
  • 171
    • 33646428633 scopus 로고    scopus 로고
    • F. 3,3'-Diindolylmethane is a novel mitochondrial H(+)-ATP synthase inhibitor that can induce p21(Cip1/Waf1) expression by induction of oxidative stress in human breast cancer cells
    • Gong, Y.; Sohn, H.; Xue, L.; Firestone, G. L.; Bjeldanes, L. F. 3,3'-Diindolylmethane is a novel mitochondrial H(+)-ATP synthase inhibitor that can induce p21(Cip1/Waf1) expression by induction of oxidative stress in human breast cancer cells. Cancer Res., 2006, 66, 4880-4887.
    • (2006) Cancer Res , vol.66 , pp. 4880-4887
    • Gong, Y.1    Sohn, H.2    Xue, L.3    Firestone, G.L.4    Bjeldanes, L.5
  • 172
    • 51549095960 scopus 로고    scopus 로고
    • Cancer chemotherapy with indole-3-carbinol, bis(3'-indolyl)methane and synthetic analogs
    • Safe, S.; Papineni, S.; Chintharlapalli, S. Cancer chemotherapy with indole-3-carbinol, bis(3'-indolyl)methane and synthetic analogs. Cancer Lett., 2008, 269, 326-338.
    • (2008) Cancer Lett , vol.269 , pp. 326-338
    • Safe, S.1    Papineni, S.2    Chintharlapalli, S.3
  • 174
    • 0344553280 scopus 로고    scopus 로고
    • Overview of recurrent respiratory papillomatosis
    • Wiatrak, B. J. Overview of recurrent respiratory papillomatosis. Curr. Opin. Otolaryngol. Head Neck Surg., 2003, 11, 433-441.
    • (2003) Curr. Opin. Otolaryngol. Head Neck Surg , vol.11 , pp. 433-441
    • Wiatrak, B.J.1
  • 175
    • 35548958999 scopus 로고    scopus 로고
    • Mechanistic basis for therapeutic targeting of the mitochondrial F1F0-ATPase
    • Johnson, K. M.; Cleary, J.; Fierke, C. A.; Opipari, A. W., Jr.; Glick, G. D. Mechanistic basis for therapeutic targeting of the mitochondrial F1F0-ATPase. ACS Chem. Biol., 2006, 1, 304-308.
    • (2006) ACS Chem. Biol , vol.1 , pp. 304-308
    • Johnson, K.M.1    Cleary, J.2    Fierke, C.A.3    Opipari Jr., A.W.4    Glick, G.D.5
  • 176
    • 17844366842 scopus 로고    scopus 로고
    • Identification and validation of the mitochondrial F1F0-ATPase as the molecular target of the immunomodulatory benzodiazepine Bz-423
    • Johnson, K. M.; Chen, X.; Boitano, A.; Swenson, L.; Opipari, A. W., Jr.; Glick, G. D. Identification and validation of the mitochondrial F1F0-ATPase as the molecular target of the immunomodulatory benzodiazepine Bz-423. Chem. Biol., 2005, 12, 485-496.
    • (2005) Chem. Biol , vol.12 , pp. 485-496
    • Johnson, K.M.1    Chen, X.2    Boitano, A.3    Swenson, L.4    Opipari Jr., A.W.5    Glick, G.D.6
  • 177
    • 0142219875 scopus 로고    scopus 로고
    • The proapoptotic benzodiazepine Bz-423 affects the growth and survival of malignant B cells
    • Boitano, A.; Ellman, J. A.; Glick, G. D.; Opipari, A. W. Jr. The proapoptotic benzodiazepine Bz-423 affects the growth and survival of malignant B cells. Cancer Res., 2003, 63, 6870-6876.
    • (2003) Cancer Res , vol.63 , pp. 6870-6876
    • Boitano, A.1    Ellman, J.A.2    Glick, G.D.3    Opipari Jr., A.W.4
  • 179
    • 0024347890 scopus 로고
    • Inhibition of the bovine-heart mitochondrial F1-ATPase by cationic dyes and amphipathic peptides
    • Bullough, D. A.; Ceccarelli, E. A.; Roise, D.; Allison, W. S. Inhibition of the bovine-heart mitochondrial F1-ATPase by cationic dyes and amphipathic peptides. Biochim. Biophys. Acta, 1989, 975, 377-383.
    • (1989) Biochim. Biophys. Acta , vol.975 , pp. 377-383
    • Bullough, D.A.1    Ceccarelli, E.A.2    Roise, D.3    Allison, W.S.4
  • 180
    • 0020561660 scopus 로고
    • Anticarcinoma activity in vivo of rhodamine 123, a mitochondrialspecific dye
    • Bernal, S. D.; Lampidis, T. J.; McIsaac, R. M.; Chen, L. B. Anticarcinoma activity in vivo of rhodamine 123, a mitochondrialspecific dye. Science, 1983, 222, 169-172.
    • (1983) Science , vol.222 , pp. 169-172
    • Bernal, S.D.1    Lampidis, T.J.2    McIsaac, R.M.3    Chen, L.B.4
  • 181
    • 0020428221 scopus 로고
    • Rhodamine-123 selectively reduces clonal growth of carcinoma cells
    • Bernal, S. D.; Lampidis, T. J.; Summerhayes, I. C.; Chen, L. B. Rhodamine-123 selectively reduces clonal growth of carcinoma cells in vitro. Science, 1982, 218, 1117-1119.
    • (1982) In Vitro. Science , vol.218 , pp. 1117-1119
    • Bernal, S.D.1    Lampidis, T.J.2    Summerhayes, I.C.3    Chen, L.B.4
  • 183
    • 24644499548 scopus 로고    scopus 로고
    • Rhodamine-123: Therapy for hormone refractory prostate cancer, a phase I clinical trial
    • Jones, L. W.; Narayan, K. S.; Shapiro, C. E.; Sweatman, T. W. Rhodamine-123: therapy for hormone refractory prostate cancer, a phase I clinical trial. J. Chemother., 2005, 17, 435-440.
    • (2005) J. Chemother , vol.17 , pp. 435-440
    • Jones, L.W.1    Narayan, K.S.2    Shapiro, C.E.3    Sweatman, T.W.4
  • 186
    • 28544446058 scopus 로고    scopus 로고
    • Mitochondrial tumour suppressors: A genetic and biochemical update
    • Gottlieb, E.; Tomlinson, I. P. Mitochondrial tumour suppressors: a genetic and biochemical update. Nat. Rev. Cancer, 2005, 5, 857-866.
    • (2005) Nat. Rev. Cancer , vol.5 , pp. 857-866
    • Gottlieb, E.1    Tomlinson, I.P.2
  • 187
    • 68149169947 scopus 로고    scopus 로고
    • Mitochondrial electron transport chain blockers enhance 2-deoxy-D-glucose induced oxidative stress and cell killing in human colon carcinoma cells
    • Fath, M. A.; Diers, A. R.; Aykin-Burns, N.; Simons, A. L.; Hua, L.; Spitz, D. R. Mitochondrial electron transport chain blockers enhance 2-deoxy-D-glucose induced oxidative stress and cell killing in human colon carcinoma cells. Cancer Biol. Ther., 2009, 8, 1228-1236.
    • (2009) Cancer Biol. Ther , vol.8 , pp. 1228-1236
    • Fath, M.A.1    Diers, A.R.2    Aykin-Burns, N.3    Simons, A.L.4    Hua, L.5    Spitz, D.R.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.