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Volumn 7, Issue 2, 2008, Pages 129-146

Drug-induced mitochondrial dysfunction in cardiac and skeletal muscle injury

Author keywords

Drug induced toxicity; Heart; Mitochondria; Skeletal muscle

Indexed keywords

ALCOHOL; ALPHA TOCOPHEROL; ANTHRACYCLINE; ATORVASTATIN; BUPIVACAINE; CALCIUM; CARVEDILOL; CERIVASTATIN; CLOFIBRATE; COCAINE; DOXORUBICIN; GLITAZONE DERIVATIVE; HYDROXYMETHYLGLUTARYL COENZYME A REDUCTASE INHIBITOR; LIDOCAINE; LOCAL ANESTHETIC AGENT; MEVINOLIN; NICOTINIC ACID; PRAVASTATIN; REACTIVE OXYGEN METABOLITE; RNA DIRECTED DNA POLYMERASE INHIBITOR; ROSUVASTATIN; SIMVASTATIN; THIAZOLIDINE DERIVATIVE; UBIDECARENONE; UBIQUINONE; ZIDOVUDINE;

EID: 41349119625     PISSN: 14740338     EISSN: None     Source Type: Journal    
DOI: 10.1517/14740338.7.2.129     Document Type: Review
Times cited : (27)

References (163)
  • 2
    • 0022471190 scopus 로고
    • Heterogeneous response of subsarcolemmal heart mitochondria to calcium
    • Palmer JW, Tandler B, Hoppel CL. Heterogeneous response of subsarcolemmal heart mitochondria to calcium. Am J Physiol 1986;250(5 Pt 2):H741-8
    • (1986) Am J Physiol , vol.250 , Issue.5 PART 2
    • Palmer, J.W.1    Tandler, B.2    Hoppel, C.L.3
  • 3
    • 0023010537 scopus 로고
    • Exercise-induced ultrastructural changes in skeletal muscle
    • Hoppeler H. Exercise-induced ultrastructural changes in skeletal muscle. Int J Sports Med 1986;7(4):187-204
    • (1986) Int J Sports Med , vol.7 , Issue.4 , pp. 187-204
    • Hoppeler, H.1
  • 4
    • 0017740356 scopus 로고
    • Biochemical properties of subsarcolemmal and interfibrillar mitochondria isolated from rat cardiac muscle
    • Palmer JW, Tandler B, Hoppel CL. Biochemical properties of subsarcolemmal and interfibrillar mitochondria isolated from rat cardiac muscle. J Biol Chem 1977;252(23):8731-9
    • (1977) J Biol Chem , vol.252 , Issue.23 , pp. 8731-8739
    • Palmer, J.W.1    Tandler, B.2    Hoppel, C.L.3
  • 5
    • 20144374568 scopus 로고    scopus 로고
    • ATP synthesis: The world's smallest wind-up toy
    • Berry RM. ATP synthesis: the world's smallest wind-up toy. Curr Biol 2005;15(10):R385-7
    • (2005) Curr Biol , vol.15 , Issue.10
    • Berry, R.M.1
  • 6
    • 0036137574 scopus 로고    scopus 로고
    • Blachly-Dyson E, Forte M. VDAC channels. IUBMB Life 2001;52(3-5):113-8
    • Blachly-Dyson E, Forte M. VDAC channels. IUBMB Life 2001;52(3-5):113-8
  • 7
    • 33645704767 scopus 로고    scopus 로고
    • Quantitative proteomic comparison of rat mitochondria from muscle, heart, and liver
    • Forner F, Foster LJ, Campanaro S, Valle G, Mann M. Quantitative proteomic comparison of rat mitochondria from muscle, heart, and liver. Mol Cell Proteomics 2006;5(4):608-19
    • (2006) Mol Cell Proteomics , vol.5 , Issue.4 , pp. 608-619
    • Forner, F.1    Foster, L.J.2    Campanaro, S.3    Valle, G.4    Mann, M.5
  • 8
    • 0034986612 scopus 로고    scopus 로고
    • Macrocompartmentation of total creatine in cardiomyocytes revisited
    • Menin L, Panchichkina M, Keriel C, et al. Macrocompartmentation of total creatine in cardiomyocytes revisited. Mol Cell Biochem 2001;220(1-2):149-59
    • (2001) Mol Cell Biochem , vol.220 , Issue.1-2 , pp. 149-159
    • Menin, L.1    Panchichkina, M.2    Keriel, C.3
  • 9
    • 0036037787 scopus 로고    scopus 로고
    • Modeling the energy transfer pathways. creatine kinase activities and heterogeneous distribution of ADP in the perfused heart
    • Joubert F, Hoerter JA, Mazet JL. Modeling the energy transfer pathways. creatine kinase activities and heterogeneous distribution of ADP in the perfused heart. Mol Biol Rep 2002;29(1-2):177-82
    • (2002) Mol Biol Rep , vol.29 , Issue.1-2 , pp. 177-182
    • Joubert, F.1    Hoerter, J.A.2    Mazet, J.L.3
  • 10
    • 0029664623 scopus 로고    scopus 로고
    • The mitochondrial KATP channel as a receptor for potassium channel openers
    • Garlid KD, Paucek P, Yarov-Yarovoy V, Sun X, Schindler PA. The mitochondrial KATP channel as a receptor for potassium channel openers. J Biol Chem 1996;271(15):8796-9
    • (1996) J Biol Chem , vol.271 , Issue.15 , pp. 8796-8799
    • Garlid, K.D.1    Paucek, P.2    Yarov-Yarovoy, V.3    Sun, X.4    Schindler, P.A.5
  • 11
    • 0033022308 scopus 로고    scopus 로고
    • Pharmacological and histochemical distinctions between molecularly defined sarcolemmal KATP channels and native cardiac mitochondrial KATP channels
    • Hu H, Sato T, Seharaseyon J, et al. Pharmacological and histochemical distinctions between molecularly defined sarcolemmal KATP channels and native cardiac mitochondrial KATP channels. Mol Pharmacol 1999;55(6):1000-5
    • (1999) Mol Pharmacol , vol.55 , Issue.6 , pp. 1000-1005
    • Hu, H.1    Sato, T.2    Seharaseyon, J.3
  • 12
    • 0032560651 scopus 로고    scopus 로고
    • Mitochondrial ATP-dependent potassium channels: Novel effectors of cardioprotection?
    • Liu Y, Sato T, O'Rourke B, Marban E. Mitochondrial ATP-dependent potassium channels: novel effectors of cardioprotection? Circulation 1998;97(24):2463-9
    • (1998) Circulation , vol.97 , Issue.24 , pp. 2463-2469
    • Liu, Y.1    Sato, T.2    O'Rourke, B.3    Marban, E.4
  • 13
    • 19944431220 scopus 로고    scopus 로고
    • Mitochondrial KATP channels in hindlimb remote ischemic preconditioning of skeletal muscle against infarction
    • Moses MA, Addison PD, Neligan PC, et al. Mitochondrial KATP channels in hindlimb remote ischemic preconditioning of skeletal muscle against infarction. Am J Physiol Heart Circ Physiol 2005;288(2):H559-67
    • (2005) Am J Physiol Heart Circ Physiol , vol.288 , Issue.2
    • Moses, M.A.1    Addison, P.D.2    Neligan, P.C.3
  • 14
    • 33747630469 scopus 로고    scopus 로고
    • K+-independent actions of diazoxide question the role of inner membrane KATP channels in mitochondrial cytoprotective signaling
    • Drose S, Brandt U, Hanley PJ. K+-independent actions of diazoxide question the role of inner membrane KATP channels in mitochondrial cytoprotective signaling. J Biol Chem 2006;281(33):23733-9
    • (2006) J Biol Chem , vol.281 , Issue.33 , pp. 23733-23739
    • Drose, S.1    Brandt, U.2    Hanley, P.J.3
  • 15
    • 31344444853 scopus 로고    scopus 로고
    • Ischemic preconditioning requires increases in reactive oxygen release independent of mitochondrial K+ channel activity
    • Facundo HT, Carreira RS, de Paula JG, et al. Ischemic preconditioning requires increases in reactive oxygen release independent of mitochondrial K+ channel activity. Free Radic Biol Med 2006;40(3):469-79
    • (2006) Free Radic Biol Med , vol.40 , Issue.3 , pp. 469-479
    • Facundo, H.T.1    Carreira, R.S.2    de Paula, J.G.3
  • 16
    • 0037444667 scopus 로고    scopus 로고
    • Matrix volume measurements challenge the existence of diazoxide/glibencamide-sensitive KATP channels in rat mitochondria
    • Das M, Parker JE, Halestrap AP. Matrix volume measurements challenge the existence of diazoxide/glibencamide-sensitive KATP channels in rat mitochondria. J Physiol 2003;547(Pt 3):893-902
    • (2003) J Physiol , vol.547 , Issue.PART 3 , pp. 893-902
    • Das, M.1    Parker, J.E.2    Halestrap, A.P.3
  • 17
    • 34548217676 scopus 로고    scopus 로고
    • ER-mitochondria communication. How privileged?
    • Franzini-Armstrong C. ER-mitochondria communication. How privileged? Physiology (Bethesda) 2007;22:261-8
    • (2007) Physiology (Bethesda) , vol.22 , pp. 261-268
    • Franzini-Armstrong, C.1
  • 18
    • 0034671162 scopus 로고    scopus 로고
    • Quantification of calcium signal transmission from sarco-endoplasmic reticulum to the mitochondria
    • Pacher P, Csordas P, Schneider T, Hajnoczky G. Quantification of calcium signal transmission from sarco-endoplasmic reticulum to the mitochondria. J Physiol 2000;529(Pt 3):553-64
    • (2000) J Physiol , vol.529 , Issue.PART 3 , pp. 553-564
    • Pacher, P.1    Csordas, P.2    Schneider, T.3    Hajnoczky, G.4
  • 19
    • 17044456631 scopus 로고
    • The role of Ca2+ in the regulation of intramitochondrial energy production in heart
    • McCormack JG, Denton RM. The role of Ca2+ in the regulation of intramitochondrial energy production in heart. Biomed Biochim Acta 1987;46(8-9):S487-92
    • (1987) Biomed Biochim Acta , vol.46 , Issue.8-9
    • McCormack, J.G.1    Denton, R.M.2
  • 20
    • 33644546383 scopus 로고    scopus 로고
    • Mitochondrial matrix phosphoproteome: Effect of extra mitochondrial calcium
    • Hopper RK, Carroll S, Aponte AM, et al. Mitochondrial matrix phosphoproteome: effect of extra mitochondrial calcium. Biochemistry 2006;45(8):2524-36
    • (2006) Biochemistry , vol.45 , Issue.8 , pp. 2524-2536
    • Hopper, R.K.1    Carroll, S.2    Aponte, A.M.3
  • 21
    • 0027234488 scopus 로고    scopus 로고
    • Harris DA. Regulation of the mitochondrial ATP synthase in rat heart. Biochem Soc Trans 1993;21(Pt 3)(3):778-81
    • Harris DA. Regulation of the mitochondrial ATP synthase in rat heart. Biochem Soc Trans 1993;21(Pt 3)(3):778-81
  • 22
    • 33748786501 scopus 로고    scopus 로고
    • ATP regulation in adult rat cardiomyocytes: Time-resolved decoding of rapid mitochondrial calcium spiking imaged with targeted photoproteins
    • Bell CJ, Bright NA, Rutter GA, Griffiths EJ. ATP regulation in adult rat cardiomyocytes: time-resolved decoding of rapid mitochondrial calcium spiking imaged with targeted photoproteins. J Biol Chem 2006;281(38):28058-67
    • (2006) J Biol Chem , vol.281 , Issue.38 , pp. 28058-28067
    • Bell, C.J.1    Bright, N.A.2    Rutter, G.A.3    Griffiths, E.J.4
  • 23
    • 33751077799 scopus 로고    scopus 로고
    • Integration of rapid cytosolic Ca2+ signals by mitochondria in cat ventricular myocytes
    • Sedova M, Dedkova EN, Blatter LA. Integration of rapid cytosolic Ca2+ signals by mitochondria in cat ventricular myocytes. Am J Physiol Cell Physiol 2006;291(5):C840-50
    • (2006) Am J Physiol Cell Physiol , vol.291 , Issue.5
    • Sedova, M.1    Dedkova, E.N.2    Blatter, L.A.3
  • 24
    • 0025292743 scopus 로고
    • Mechanisms by which mitochondria transport calcium
    • Gunter TE, Pfeiffer DR. Mechanisms by which mitochondria transport calcium. Am J Physiol 1990;258(5 Pt 1):C755-86
    • (1990) Am J Physiol , vol.258 , Issue.5 PART 1
    • Gunter, T.E.1    Pfeiffer, D.R.2
  • 25
    • 0033369476 scopus 로고    scopus 로고
    • Mitochondrial oxygen radical generation and leak: Sites of production in states 4 and 3, organ specificity, and relation to aging and longevity
    • Barja G. Mitochondrial oxygen radical generation and leak: sites of production in states 4 and 3, organ specificity, and relation to aging and longevity. J Bioenerg Biomembr 1999;31(4):347-66
    • (1999) J Bioenerg Biomembr , vol.31 , Issue.4 , pp. 347-366
    • Barja, G.1
  • 26
    • 0030068461 scopus 로고    scopus 로고
    • Conditions allowing redox-cycling ubisemiquinone in mitochondria to establish a direct redox couple with molecular oxygen
    • Nohl H, Gille L, Schonheit K, Liu Y. Conditions allowing redox-cycling ubisemiquinone in mitochondria to establish a direct redox couple with molecular oxygen. Free Radic Biol Med 1996;20(2):207-13
    • (1996) Free Radic Biol Med , vol.20 , Issue.2 , pp. 207-213
    • Nohl, H.1    Gille, L.2    Schonheit, K.3    Liu, Y.4
  • 27
    • 0024996681 scopus 로고
    • The oxidative inactivation of mitochondrial electron transport chain components and ATPase
    • Zhang Y, Marcillat O, Giulivi C, Ernster L, Davies KJ. The oxidative inactivation of mitochondrial electron transport chain components and ATPase. J Biol Chem 1990;265(27):16330-6
    • (1990) J Biol Chem , vol.265 , Issue.27 , pp. 16330-16336
    • Zhang, Y.1    Marcillat, O.2    Giulivi, C.3    Ernster, L.4    Davies, K.J.5
  • 28
    • 0032865515 scopus 로고    scopus 로고
    • Reactivity of biologically important thiol compounds with superoxide and hydrogen peroxide
    • Winterbourn CC, Metodiewa D. Reactivity of biologically important thiol compounds with superoxide and hydrogen peroxide. Free Radic Biol Med 1999;27(3-4):322-8
    • (1999) Free Radic Biol Med , vol.27 , Issue.3-4 , pp. 322-328
    • Winterbourn, C.C.1    Metodiewa, D.2
  • 29
    • 0026603840 scopus 로고
    • Cardiolipins and biomembrane function
    • Hoch FL. Cardiolipins and biomembrane function. Biochim Biophys Acta 1992;1113(1):71-133
    • (1992) Biochim Biophys Acta , vol.1113 , Issue.1 , pp. 71-133
    • Hoch, F.L.1
  • 30
    • 33750915424 scopus 로고    scopus 로고
    • Mitochondrial oxidative stress, DNA damage, and heart failure
    • Tsutsui H, Ide T, Kinugawa S. Mitochondrial oxidative stress, DNA damage, and heart failure. Antioxid Redox Signal 2006;8(9-10):1737-44
    • (2006) Antioxid Redox Signal , vol.8 , Issue.9-10 , pp. 1737-1744
    • Tsutsui, H.1    Ide, T.2    Kinugawa, S.3
  • 31
    • 0032827410 scopus 로고    scopus 로고
    • Mitochondrial transport of cations: Channels, exchangers, and permeability transition
    • Bernardi P. Mitochondrial transport of cations: channels, exchangers, and permeability transition. Physiol Rev 1999;79(4):1127-55
    • (1999) Physiol Rev , vol.79 , Issue.4 , pp. 1127-1155
    • Bernardi, P.1
  • 33
    • 0026801183 scopus 로고
    • Modulation of the mitochondrial cyclosporin A-sensitive permeability transition pore by the proton electrochemical gradient. Evidence that the pore can be opened by membrane depolarization
    • Bernardi P. Modulation of the mitochondrial cyclosporin A-sensitive permeability transition pore by the proton electrochemical gradient. Evidence that the pore can be opened by membrane depolarization. J Biol Chem 1992;267(13):8834-9
    • (1992) J Biol Chem , vol.267 , Issue.13 , pp. 8834-8839
    • Bernardi, P.1
  • 34
    • 0031013623 scopus 로고    scopus 로고
    • Oxidative stress, thiol reagents, and membrane potential modulate the mitochondrial permeability transition by affecting nucleotide binding to the adenine nucleotide translocase
    • Halestrap AP, Woodfield KY, Connern CP. Oxidative stress, thiol reagents, and membrane potential modulate the mitochondrial permeability transition by affecting nucleotide binding to the adenine nucleotide translocase. J Biol Chem 1997;272(6):3346-54
    • (1997) J Biol Chem , vol.272 , Issue.6 , pp. 3346-3354
    • Halestrap, A.P.1    Woodfield, K.Y.2    Connern, C.P.3
  • 35
    • 0032503058 scopus 로고    scopus 로고
    • Reconstituted adenine nucleotide translocase forms a channel for small molecules comparable to the mitochondrial permeability transition pore
    • Ruck A, Dolder M, Wallimann T, Brdiczka D. Reconstituted adenine nucleotide translocase forms a channel for small molecules comparable to the mitochondrial permeability transition pore. FEBS Lett 1998;426(1):97-101
    • (1998) FEBS Lett , vol.426 , Issue.1 , pp. 97-101
    • Ruck, A.1    Dolder, M.2    Wallimann, T.3    Brdiczka, D.4
  • 36
    • 0028075423 scopus 로고
    • Recruitment of mitochondrial cyclophilin to the mitochondrial inner membrane under conditions of oxidative stress that enhance the opening of a calcium-sensitive non-specific channel
    • Connern CP, Halestrap AP. Recruitment of mitochondrial cyclophilin to the mitochondrial inner membrane under conditions of oxidative stress that enhance the opening of a calcium-sensitive non-specific channel. Biochem J 1994;302(Pt 2):321-4
    • (1994) Biochem J , vol.302 , Issue.PART 2 , pp. 321-324
    • Connern, C.P.1    Halestrap, A.P.2
  • 37
    • 0027236162 scopus 로고
    • The mitochondrial permeability transition pore may comprise VDAC molecules. II. The electrophysiological properties of VDAC are compatible with those of the mitochondrial megachannel
    • Szabo I, De Pinto V, Zoratti M. The mitochondrial permeability transition pore may comprise VDAC molecules. II. The electrophysiological properties of VDAC are compatible with those of the mitochondrial megachannel. FEBS Lett 1993;330(2):206-10
    • (1993) FEBS Lett , vol.330 , Issue.2 , pp. 206-210
    • Szabo, I.1    De Pinto, V.2    Zoratti, M.3
  • 38
    • 0344653616 scopus 로고    scopus 로고
    • Complexes between porin, hexokinase, mitochondrial creatine kinase and adenylate translocator display properties of the permeability transition pore. Implication for regulation of permeability transition by the kinases
    • Beutner G, Ruck A, Riede B, Brdiczka D. Complexes between porin, hexokinase, mitochondrial creatine kinase and adenylate translocator display properties of the permeability transition pore. Implication for regulation of permeability transition by the kinases. Biochim Biophys Acta 1998;1368(1):7-18
    • (1998) Biochim Biophys Acta , vol.1368 , Issue.1 , pp. 7-18
    • Beutner, G.1    Ruck, A.2    Riede, B.3    Brdiczka, D.4
  • 39
    • 0029953927 scopus 로고    scopus 로고
    • Mitochondrial ADP/ATP carrier can be reversibly converted into a large channel by Ca2+
    • Brustovetsky N, Klingenberg M. Mitochondrial ADP/ATP carrier can be reversibly converted into a large channel by Ca2+. Biochemistry 1996;35(26):8483-8
    • (1996) Biochemistry , vol.35 , Issue.26 , pp. 8483-8488
    • Brustovetsky, N.1    Klingenberg, M.2
  • 40
    • 26444582983 scopus 로고    scopus 로고
    • Genetic dissection of the permeability transition pore
    • Forte M, Bernardi P. Genetic dissection of the permeability transition pore. J Bioenerg Biomembr 2005;37(3):121-8
    • (2005) J Bioenerg Biomembr , vol.37 , Issue.3 , pp. 121-128
    • Forte, M.1    Bernardi, P.2
  • 42
    • 0842307483 scopus 로고    scopus 로고
    • The ADP/ATP translocator is not essential for the mitochondrial permeability transition pore
    • Kokoszka JE, Waymire KG, Levy SE, et al. The ADP/ATP translocator is not essential for the mitochondrial permeability transition pore. Nature 2004;427 (6973):461-5
    • (2004) Nature , vol.427 , Issue.6973 , pp. 461-465
    • Kokoszka, J.E.1    Waymire, K.G.2    Levy, S.E.3
  • 43
    • 0032524667 scopus 로고    scopus 로고
    • Regulation of the permeability transition pore in skeletal muscle mitochondria. Modulation By electron flow through the respiratory chain complex i
    • Fontaine E, Eriksson O, Ichas F, Bernardi P. Regulation of the permeability transition pore in skeletal muscle mitochondria. Modulation By electron flow through the respiratory chain complex i. J Biol Chem 1998;273(20):12662-8
    • (1998) J Biol Chem , vol.273 , Issue.20 , pp. 12662-12668
    • Fontaine, E.1    Eriksson, O.2    Ichas, F.3    Bernardi, P.4
  • 44
    • 0032504717 scopus 로고    scopus 로고
    • From calcium signaling to cell death: Two conformations for the mitochondrial permeability transition pore. Switching from low- to high-conductance state
    • Ichas F, Mazat JP. From calcium signaling to cell death: two conformations for the mitochondrial permeability transition pore. Switching from low- to high-conductance state. Biochim Biophys Acta 1998;1366(1-2):33-50
    • (1998) Biochim Biophys Acta , vol.1366 , Issue.1-2 , pp. 33-50
    • Ichas, F.1    Mazat, J.P.2
  • 45
    • 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(14):7826-30
    • (1989) J Biol Chem , vol.264 , Issue.14 , pp. 7826-7830
    • Broekemeier, K.M.1    Dempsey, M.E.2    Pfeiffer, D.R.3
  • 46
    • 0032557424 scopus 로고    scopus 로고
    • The thiol-specific antioxidant enzyme prevents mitochondrial permeability transition. Evidence for the participation of reactive oxygen species in this mechanism
    • Kowaltowski AJ, Netto LE, Vercesi AE. The thiol-specific antioxidant enzyme prevents mitochondrial permeability transition. Evidence for the participation of reactive oxygen species in this mechanism. J Biol Chem 1998;273(21):12766-9
    • (1998) J Biol Chem , vol.273 , Issue.21 , pp. 12766-12769
    • Kowaltowski, A.J.1    Netto, L.E.2    Vercesi, A.E.3
  • 47
    • 0028239794 scopus 로고
    • The voltage sensor of the mitochondrial permeability transition pore is tuned by the oxidation-reduction state of vicinal thiols. Increase of the gating potential by oxidants and its reversal by reducing agents
    • Petronilli V, Costantini P, Scorrano L, Colonna R, Passamonti S, Bernardi P. The voltage sensor of the mitochondrial permeability transition pore is tuned by the oxidation-reduction state of vicinal thiols. Increase of the gating potential by oxidants and its reversal by reducing agents. J Biol Chem 1994;269(24):16638-42
    • (1994) J Biol Chem , vol.269 , Issue.24 , pp. 16638-16642
    • Petronilli, V.1    Costantini, P.2    Scorrano, L.3    Colonna, R.4    Passamonti, S.5    Bernardi, P.6
  • 48
    • 33745195303 scopus 로고    scopus 로고
    • Muscle denervation promotes opening of the permeability transition pore and increases the expression of cyclophilin D
    • Csukly K, Ascah A, Matas J, Gardiner PF, Fontaine E, Burelle Y. Muscle denervation promotes opening of the permeability transition pore and increases the expression of cyclophilin D. J Physiol 2006;574(Pt 1):319-27
    • (2006) J Physiol , vol.574 , Issue.PART 1 , pp. 319-327
    • Csukly, K.1    Ascah, A.2    Matas, J.3    Gardiner, P.F.4    Fontaine, E.5    Burelle, Y.6
  • 49
    • 19444369714 scopus 로고    scopus 로고
    • Mitochondria-associated apoptotic signalling in denervated rat skeletal muscle
    • S PM, Alway SE. Mitochondria-associated apoptotic signalling in denervated rat skeletal muscle. J Physiol 2005;565(Pt 1):309-23
    • (2005) J Physiol , vol.565 , Issue.PART 1 , pp. 309-323
    • PM, S.1    Alway, S.E.2
  • 50
    • 25444500448 scopus 로고    scopus 로고
    • Differential susceptibility of subsarcolemmal and intermyofibrillar mitochondria to apoptotic stimuli
    • Adhihetty PJ, Ljubicic V, Menzies KJ, Hood DA. Differential susceptibility of subsarcolemmal and intermyofibrillar mitochondria to apoptotic stimuli. Am J Physiol Cell Physiol 2005;289(4):C994-1001
    • (2005) Am J Physiol Cell Physiol , vol.289 , Issue.4
    • Adhihetty, P.J.1    Ljubicic, V.2    Menzies, K.J.3    Hood, D.A.4
  • 51
    • 0032031920 scopus 로고    scopus 로고
    • Induction of the mitochondrial permeability transition causes release of the apoptogenic factor cytochrome c
    • Yang JC, Cortopassi GA. Induction of the mitochondrial permeability transition causes release of the apoptogenic factor cytochrome c. Free Radic Biol Med 1998;24(4):624-31
    • (1998) Free Radic Biol Med , vol.24 , Issue.4 , pp. 624-631
    • Yang, J.C.1    Cortopassi, G.A.2
  • 52
    • 0030724539 scopus 로고    scopus 로고
    • Release of apoptogenic proteins from the mitochondrial intermembrane space during the mitochondrial permeability transition
    • Scarlett JL, Murphy MP. Release of apoptogenic proteins from the mitochondrial intermembrane space during the mitochondrial permeability transition. FEBS Lett 1997;418(3):282-6
    • (1997) FEBS Lett , vol.418 , Issue.3 , pp. 282-286
    • Scarlett, J.L.1    Murphy, M.P.2
  • 53
    • 0029983059 scopus 로고    scopus 로고
    • Inhibitors of permeability transition interfere with the disruption of the mitochondrial transmembrane potential during apoptosis
    • Zamzami N, Marchetti P, Castedo M, et al. Inhibitors of permeability transition interfere with the disruption of the mitochondrial transmembrane potential during apoptosis. FEBS Lett 1996;384(1):53-7
    • (1996) FEBS Lett , vol.384 , Issue.1 , pp. 53-57
    • Zamzami, N.1    Marchetti, P.2    Castedo, M.3
  • 54
    • 0032566649 scopus 로고    scopus 로고
    • Bax and adenine nucleotide translocator cooperate in the mitochondrial control of apoptosis
    • Marzo I, Brenner C, Zamzami N, et al. Bax and adenine nucleotide translocator cooperate in the mitochondrial control of apoptosis. Science 1998;281(5385):2027-31
    • (1998) Science , vol.281 , Issue.5385 , pp. 2027-2031
    • Marzo, I.1    Brenner, C.2    Zamzami, N.3
  • 55
    • 0033611057 scopus 로고    scopus 로고
    • Adenine nucleotide translocase-1, a component of the permeability transition pore, can dominantly induce apoptosis
    • Bauer MK, Schubert A, Rocks O, Grimm S. Adenine nucleotide translocase-1, a component of the permeability transition pore, can dominantly induce apoptosis, J Cell Biol 1999;147(7):1493-1502
    • (1999) J Cell Biol , vol.147 , Issue.7 , pp. 1493-1502
    • Bauer, M.K.1    Schubert, A.2    Rocks, O.3    Grimm, S.4
  • 56
    • 0033891777 scopus 로고    scopus 로고
    • Arcamone F, Cassinelli G, Fantini G, et al. Adriamycin, 14-hydroxydaunomycin, a new antitumor antibiotic from S. peucetius var. caesius. Reprinted from Biotechnology and Bioengineering, XI, Issue 6, Pages 1101-1110 (1969). Biotechnol Bioeng 2000;67(6):704-13
    • Arcamone F, Cassinelli G, Fantini G, et al. Adriamycin, 14-hydroxydaunomycin, a new antitumor antibiotic from S. peucetius var. caesius. Reprinted from Biotechnology and Bioengineering, Vol. XI, Issue 6, Pages 1101-1110 (1969). Biotechnol Bioeng 2000;67(6):704-13
  • 57
    • 0028303762 scopus 로고
    • Anthracycline cardiotoxicity
    • Gasparini M. Anthracycline cardiotoxicity. Pediatr Hematol Oncol 1994;11(3):237-40
    • (1994) Pediatr Hematol Oncol , vol.11 , Issue.3 , pp. 237-240
    • Gasparini, M.1
  • 58
    • 0043237846 scopus 로고    scopus 로고
    • Doxorubicin-induced cardiac mitochondrionopathy
    • Wallace KB. Doxorubicin-induced cardiac mitochondrionopathy. Pharmacol Toxicol 2003;93(3):105-15
    • (2003) Pharmacol Toxicol , vol.93 , Issue.3 , pp. 105-115
    • Wallace, K.B.1
  • 59
    • 0020503635 scopus 로고
    • Anthracycline antibiotic-stimulated superoxide, hydrogen peroxide, and hydroxyl radical production by NADH dehydrogenase
    • Doroshow JH, Anthracycline antibiotic-stimulated superoxide, hydrogen peroxide, and hydroxyl radical production by NADH dehydrogenase. Cancer Res 1983;43(10):4543-51
    • (1983) Cancer Res , vol.43 , Issue.10 , pp. 4543-4551
    • Doroshow, J.H.1
  • 60
    • 0032563825 scopus 로고    scopus 로고
    • Doxorubicin-induced cardiomyopathy
    • Singal PK, Iliskovic N. Doxorubicin-induced cardiomyopathy. N Engl J Med 1998;339(13):900-5
    • (1998) N Engl J Med , vol.339 , Issue.13 , pp. 900-905
    • Singal, P.K.1    Iliskovic, N.2
  • 61
    • 0020530823 scopus 로고
    • Mitochondrial membrane modifications induced by adriamycin-mediated electron transport
    • Goormaghtigh E, Pollakis G, Ruysschaert JM. Mitochondrial membrane modifications induced by adriamycin-mediated electron transport. Biochem Pharmacol 1983;32(5):889-93
    • (1983) Biochem Pharmacol , vol.32 , Issue.5 , pp. 889-893
    • Goormaghtigh, E.1    Pollakis, G.2    Ruysschaert, J.M.3
  • 62
    • 0021023311 scopus 로고
    • Evidence of a covalent linkage in the adriamycin-cardiolipin complex induced by adriamycin-mediated electron transport
    • Goormaghtigh E, Ruysschaert JM. Evidence of a covalent linkage in the adriamycin-cardiolipin complex induced by adriamycin-mediated electron transport. Res Commun Chem Pathol Pharmacol 1983;42(1):149-52
    • (1983) Res Commun Chem Pathol Pharmacol , vol.42 , Issue.1 , pp. 149-152
    • Goormaghtigh, E.1    Ruysschaert, J.M.2
  • 63
    • 0020637503 scopus 로고
    • Enhancement of rat heart microsomal lipid peroxidation following doxorubicin treatment in vivo
    • Mimnaugh EG, Trush MA, Gram TE. Enhancement of rat heart microsomal lipid peroxidation following doxorubicin treatment in vivo. Cancer Treat Rep 1983;67(7-8):731-3
    • (1983) Cancer Treat Rep , vol.67 , Issue.7-8 , pp. 731-733
    • Mimnaugh, E.G.1    Trush, M.A.2    Gram, T.E.3
  • 64
    • 0030880285 scopus 로고    scopus 로고
    • Preferential oxidation of cardiac mitochondrial DNA following acute intoxication with doxorubicin
    • Palmeira CM. Serrano J, Kuehl DW, Wallace KB. Preferential oxidation of cardiac mitochondrial DNA following acute intoxication with doxorubicin. Biochim Biophys Acta 1997;1321(2):101-6
    • (1997) Biochim Biophys Acta , vol.1321 , Issue.2 , pp. 101-106
    • Palmeira, C.M.1    Serrano, J.2    Kuehl, D.W.3    Wallace, K.B.4
  • 65
    • 0028130476 scopus 로고
    • Disruption of mitochondrial calcium homeostasis following chronic doxorubicin administration
    • Solem LE, Henry TR, Wallace KB. Disruption of mitochondrial calcium homeostasis following chronic doxorubicin administration. Toxicol Appl Pharmacol 1994;129(2):214-22
    • (1994) Toxicol Appl Pharmacol , vol.129 , Issue.2 , pp. 214-222
    • Solem, L.E.1    Henry, T.R.2    Wallace, K.B.3
  • 66
    • 33244492919 scopus 로고    scopus 로고
    • Depletion of adenine nucleotide translocator protein in heart mitochondria from doxorubidn-treated rats-relevance for mitochondrial dysfunction
    • Oliveira PJ, Wallace KB. Depletion of adenine nucleotide translocator protein in heart mitochondria from doxorubidn-treated rats-relevance for mitochondrial dysfunction. Toxicology 2006;220(2-3):160-8
    • (2006) Toxicology , vol.220 , Issue.2-3 , pp. 160-168
    • Oliveira, P.J.1    Wallace, K.B.2
  • 67
    • 34548299678 scopus 로고    scopus 로고
    • Adriamycin-induced interference with cardiac mitochondrial calcium homeostasis
    • Wallace KB. Adriamycin-induced interference with cardiac mitochondrial calcium homeostasis. Cardiovasc Toxicol 2007;7(2):101-7
    • (2007) Cardiovasc Toxicol , vol.7 , Issue.2 , pp. 101-107
    • Wallace, K.B.1
  • 68
    • 0027268459 scopus 로고
    • Selective activation of the sodium-independent, cyclosporin A-sensitive calcium pore of cardiac mitochondria by doxorubicin
    • Solem LE, Wallace KB. Selective activation of the sodium-independent, cyclosporin A-sensitive calcium pore of cardiac mitochondria by doxorubicin. Toxicol Appl Pharmacol 1993;121(1):50-7
    • (1993) Toxicol Appl Pharmacol , vol.121 , Issue.1 , pp. 50-57
    • Solem, L.E.1    Wallace, K.B.2
  • 69
    • 0035863469 scopus 로고    scopus 로고
    • Cumulative and irreversible cardiac mitochondrial dysfunction induced by doxorubicin
    • Zhou S, Starkov A, Froberg MK, Leino RL, Wallace KB. Cumulative and irreversible cardiac mitochondrial dysfunction induced by doxorubicin. Cancer Res 2001;61(2):771-7
    • (2001) Cancer Res , vol.61 , Issue.2 , pp. 771-777
    • Zhou, S.1    Starkov, A.2    Froberg, M.K.3    Leino, R.L.4    Wallace, K.B.5
  • 70
    • 0023110485 scopus 로고
    • Effect of adriamycin on electron transport in rat heart, liver, and tumor mitochondria
    • Bianchi C, Bagnato A, Paggi MG, Floridi A. Effect of adriamycin on electron transport in rat heart, liver, and tumor mitochondria. Exp Mol Pathol 1987;46(1):123-35
    • (1987) Exp Mol Pathol , vol.46 , Issue.1 , pp. 123-135
    • Bianchi, C.1    Bagnato, A.2    Paggi, M.G.3    Floridi, A.4
  • 71
    • 0020674160 scopus 로고
    • Inhibition of mitochondrial oxidative phosphorylation by adriamycin
    • Muhammed H, Ramasarma T, Kurup CK. Inhibition of mitochondrial oxidative phosphorylation by adriamycin. Biochim Biophys Acta 1983;722(1):43-50
    • (1983) Biochim Biophys Acta , vol.722 , Issue.1 , pp. 43-50
    • Muhammed, H.1    Ramasarma, T.2    Kurup, C.K.3
  • 72
    • 0017253191 scopus 로고
    • Adriamycin: Energy metabolism and mitochondrial oxidations in the heart of treated rabbits
    • Ferrero ME, Ferrero E, Gaja G, Bernelli-Zazzera A. Adriamycin: energy metabolism and mitochondrial oxidations in the heart of treated rabbits. Biochem Pharmacol 1976;25(2):125-30
    • (1976) Biochem Pharmacol , vol.25 , Issue.2 , pp. 125-130
    • Ferrero, M.E.1    Ferrero, E.2    Gaja, G.3    Bernelli-Zazzera, A.4
  • 73
    • 0016171022 scopus 로고
    • Effects of anticancer agents on the respiration of isolated mitochondria and tumor cells
    • Gosalvez M, Blanco M, Hunter J, Miko M, Chance B. Effects of anticancer agents on the respiration of isolated mitochondria and tumor cells. Eur J Cancer 1974;10(9):567-74
    • (1974) Eur J Cancer , vol.10 , Issue.9 , pp. 567-574
    • Gosalvez, M.1    Blanco, M.2    Hunter, J.3    Miko, M.4    Chance, B.5
  • 74
    • 0041304980 scopus 로고    scopus 로고
    • Doxorubicin-derived metabolites induce release of cytochrome C and inhibition of respiration on cardiac isolated mitochondria
    • Clementi ME, Giardina B, Di Stasio E, Mordente A, Misiti F. Doxorubicin-derived metabolites induce release of cytochrome C and inhibition of respiration on cardiac isolated mitochondria. Anticancer Res 2003;23(3B):2445-50
    • (2003) Anticancer Res , vol.23 , Issue.3 B , pp. 2445-2450
    • Clementi, M.E.1    Giardina, B.2    Di Stasio, E.3    Mordente, A.4    Misiti, F.5
  • 75
    • 5144227343 scopus 로고    scopus 로고
    • Carvedilol-mediated antioxidant protection against doxorubicin-induced cardiac mitochondrial toxicity
    • Oliveira PJ, Bjork JA, Santos MS, et al. Carvedilol-mediated antioxidant protection against doxorubicin-induced cardiac mitochondrial toxicity. Toxicol Appl Pharmacol 2004;200(2):159-68
    • (2004) Toxicol Appl Pharmacol , vol.200 , Issue.2 , pp. 159-168
    • Oliveira, P.J.1    Bjork, J.A.2    Santos, M.S.3
  • 77
  • 79
    • 27144450968 scopus 로고    scopus 로고
    • Dietary vitamin E decreases doxorubicin-induced oxidative stress without preventing mitochondrial dysfunction
    • Berthiaume JM, Oliveira PJ, Fariss MW, Wallace KB. Dietary vitamin E decreases doxorubicin-induced oxidative stress without preventing mitochondrial dysfunction. Cardiovasc Toxicol 2005;5(3):257-67
    • (2005) Cardiovasc Toxicol , vol.5 , Issue.3 , pp. 257-267
    • Berthiaume, J.M.1    Oliveira, P.J.2    Fariss, M.W.3    Wallace, K.B.4
  • 80
    • 33645277082 scopus 로고    scopus 로고
    • Doxorubicin-induced thiol-dependent alteration of cardiac mitochondrial permeability transition and respiration
    • Oliveira PJ, Santos MS, Wallace KB. Doxorubicin-induced thiol-dependent alteration of cardiac mitochondrial permeability transition and respiration. Biochemistry (Mosc) 2006;71(2):194-9
    • (2006) Biochemistry (Mosc) , vol.71 , Issue.2 , pp. 194-199
    • Oliveira, P.J.1    Santos, M.S.2    Wallace, K.B.3
  • 81
    • 0023233821 scopus 로고
    • Effect of adriamycin on heart mitochondrial DNA
    • Ellis CN, Ellis MB, Blakemore WS. Effect of adriamycin on heart mitochondrial DNA. Biochem J 1987;245(1):309-12
    • (1987) Biochem J , vol.245 , Issue.1 , pp. 309-312
    • Ellis, C.N.1    Ellis, M.B.2    Blakemore, W.S.3
  • 82
    • 0027249351 scopus 로고
    • A deletion of mitochondrial DNA in murine doxorubicin-induced cardiotoxicity
    • Adachi K, Fujiura Y, Mayumi F, et al. A deletion of mitochondrial DNA in murine doxorubicin-induced cardiotoxicity. Biochem Biophys Res Commun 1993;195(2):945-51
    • (1993) Biochem Biophys Res Commun , vol.195 , Issue.2 , pp. 945-951
    • Adachi, K.1    Fujiura, Y.2    Mayumi, F.3
  • 83
    • 0036981509 scopus 로고    scopus 로고
    • Increase in DNA polymerase gamma in the hearts of adriamycin-administered rats
    • Ogihara M, Tanno M, Izumiyama N, Nakamura H, Taguchi T. Increase in DNA polymerase gamma in the hearts of adriamycin-administered rats. Exp Mol Pathol 2002;73(3):234-41
    • (2002) Exp Mol Pathol , vol.73 , Issue.3 , pp. 234-241
    • Ogihara, M.1    Tanno, M.2    Izumiyama, N.3    Nakamura, H.4    Taguchi, T.5
  • 84
    • 29744457780 scopus 로고    scopus 로고
    • Tissue-specific mtDNA lesions and radical-associated mitochondrial dysfunction in human hearts exposed to doxorubicin
    • Lebrecht D, Kokkori A, Ketelsen UP, Setzer B, Walker UA, Tissue-specific mtDNA lesions and radical-associated mitochondrial dysfunction in human hearts exposed to doxorubicin. J Pathol 2005;207(4):436-44
    • (2005) J Pathol , vol.207 , Issue.4 , pp. 436-444
    • Lebrecht, D.1    Kokkori, A.2    Ketelsen, U.P.3    Setzer, B.4    Walker, U.A.5
  • 85
    • 0035881024 scopus 로고    scopus 로고
    • Interference with calcium-dependent mitochondrial bioenergetics in cardiac myocytes isolated from doxorubicin-treated rats
    • Zhou S, Heller LJ, Wallace KB. Interference with calcium-dependent mitochondrial bioenergetics in cardiac myocytes isolated from doxorubicin-treated rats. Toxicol Appl Pharmacol 2001;175(1):60-7
    • (2001) Toxicol Appl Pharmacol , vol.175 , Issue.1 , pp. 60-67
    • Zhou, S.1    Heller, L.J.2    Wallace, K.B.3
  • 87
    • 33745067485 scopus 로고    scopus 로고
    • Antiretroviral nucleosides, deoxynucleotide carrier and mitochondrial DNA: Evidence supporting the DNA pol gamma hypothesis
    • Lewis W, Kohler JJ, Hosseini SH, et al. Antiretroviral nucleosides, deoxynucleotide carrier and mitochondrial DNA: evidence supporting the DNA pol gamma hypothesis. AIDS 2006;20(5):675-84
    • (2006) AIDS , vol.20 , Issue.5 , pp. 675-684
    • Lewis, W.1    Kohler, J.J.2    Hosseini, S.H.3
  • 88
    • 6044226886 scopus 로고    scopus 로고
    • Direct, DNA pol-gamma-independent effects of nucleoside reverse transcriptase inhibitors on mitochondrial bioenergetics
    • Lund KC, Wallace KB. Direct, DNA pol-gamma-independent effects of nucleoside reverse transcriptase inhibitors on mitochondrial bioenergetics. Cardiovasc Toxicol 2004;4(3):217-28
    • (2004) Cardiovasc Toxicol , vol.4 , Issue.3 , pp. 217-228
    • Lund, K.C.1    Wallace, K.B.2
  • 89
    • 0028158398 scopus 로고
    • Cardiac mitochondrial DNA polymerase-gamma is inhibited competitively and noncompetitively by phosphorylated zidovudine
    • Lewis W, Simpson JF, Meyer RR. Cardiac mitochondrial DNA polymerase-gamma is inhibited competitively and noncompetitively by phosphorylated zidovudine. Circ Res 1994;74(2):344-8
    • (1994) Circ Res , vol.74 , Issue.2 , pp. 344-348
    • Lewis, W.1    Simpson, J.F.2    Meyer, R.R.3
  • 90
    • 9244222256 scopus 로고    scopus 로고
    • Direct effects of nucleoside reverse transcriptase inhibitors on rat cardiac mitochondrial bioenergetics
    • Lund KC, Wallace KB. Direct effects of nucleoside reverse transcriptase inhibitors on rat cardiac mitochondrial bioenergetics. Mitochondrion 2004;4(2-3):193-202
    • (2004) Mitochondrion , vol.4 , Issue.2-3 , pp. 193-202
    • Lund, K.C.1    Wallace, K.B.2
  • 91
    • 33645124958 scopus 로고    scopus 로고
    • 3′-Azido-3′-deoxythymidine (AZT) inhibits thymidine phosphorylation in isolated rat liver mitochondria: A possible mechanism of AZT hepatotoxicity
    • Lynx MD, Bentley AT, McKee EE. 3′-Azido-3′-deoxythymidine (AZT) inhibits thymidine phosphorylation in isolated rat liver mitochondria: a possible mechanism of AZT hepatotoxicity. Biochem Pharmacol 2006;71(9):1342-8
    • (2006) Biochem Pharmacol , vol.71 , Issue.9 , pp. 1342-1348
    • Lynx, M.D.1    Bentley, A.T.2    McKee, E.E.3
  • 92
    • 33744915313 scopus 로고    scopus 로고
    • 3′-Azido-3′-deoxythymidine (AZT) is a competitive inhibitor of thymidine phosphorylation in isolated rat heart and liver mitochondria
    • Lynx MD, McKee EE. 3′-Azido-3′-deoxythymidine (AZT) is a competitive inhibitor of thymidine phosphorylation in isolated rat heart and liver mitochondria. Biochem Pharmacol 2006;72(2):239-43
    • (2006) Biochem Pharmacol , vol.72 , Issue.2 , pp. 239-243
    • Lynx, M.D.1    McKee, E.E.2
  • 94
    • 0032897990 scopus 로고    scopus 로고
    • Role of reactive oxygen species and poly-ADP-ribose polymerase in the development of AZT-induced cardiomyopathy in rat
    • Szabados E, Fischer GM, Toth K, et al. Role of reactive oxygen species and poly-ADP-ribose polymerase in the development of AZT-induced cardiomyopathy in rat. Free Radic Biol Med 1999;26(3-4):309-17
    • (1999) Free Radic Biol Med , vol.26 , Issue.3-4 , pp. 309-317
    • Szabados, E.1    Fischer, G.M.2    Toth, K.3
  • 95
    • 0034219467 scopus 로고    scopus 로고
    • AZT inhibition of the ADP/ATP antiport in isolated rat heart mitochondria
    • Valenti D, Barile M, Passarella S. AZT inhibition of the ADP/ATP antiport in isolated rat heart mitochondria. Int J Mol Med 2000;6(1):93-6
    • (2000) Int J Mol Med , vol.6 , Issue.1 , pp. 93-96
    • Valenti, D.1    Barile, M.2    Passarella, S.3
  • 96
    • 36849090632 scopus 로고    scopus 로고
    • Adenosine 3′,5′-cyclic monophosphate (cAMP)-dependent phosphoregulation of mitochondrial complex I is inhibited by nucleoside reverse transcriptase inhibitors
    • Lund KC, Wallace KB. Adenosine 3′,5′-cyclic monophosphate (cAMP)-dependent phosphoregulation of mitochondrial complex I is inhibited by nucleoside reverse transcriptase inhibitors. Toxicol Appl Pharmacol 2008;226(1):94-106
    • (2008) Toxicol Appl Pharmacol , vol.226 , Issue.1 , pp. 94-106
    • Lund, K.C.1    Wallace, K.B.2
  • 98
    • 0035479892 scopus 로고    scopus 로고
    • Early effects of AZT on mitochondrial functions in the absence of mitochondrial DNA depletion in rat myotubes
    • Cazzalini O, Lazze MC, Iamele L, et al. Early effects of AZT on mitochondrial functions in the absence of mitochondrial DNA depletion in rat myotubes. Biochem Pharmacol 2001;62(7):893-902
    • (2001) Biochem Pharmacol , vol.62 , Issue.7 , pp. 893-902
    • Cazzalini, O.1    Lazze, M.C.2    Iamele, L.3
  • 99
    • 0026046254 scopus 로고
    • Mitochondrial ultrastructural and molecular changes induced by zidovudine in rat hearts
    • Lewis W, Papoian T, Gonzalez B, et al. Mitochondrial ultrastructural and molecular changes induced by zidovudine in rat hearts. Lab Invest 1991;65(2):228-36
    • (1991) Lab Invest , vol.65 , Issue.2 , pp. 228-236
    • Lewis, W.1    Papoian, T.2    Gonzalez, B.3
  • 100
    • 10044267663 scopus 로고    scopus 로고
    • Effects of alcohol on skeletal and cardiac muscle
    • Urbano-Marquez A, Fernandez-Sola J. Effects of alcohol on skeletal and cardiac muscle. Muscle Nerve 2004;30(6):689-707
    • (2004) Muscle Nerve , vol.30 , Issue.6 , pp. 689-707
    • Urbano-Marquez, A.1    Fernandez-Sola, J.2
  • 101
    • 1542619249 scopus 로고    scopus 로고
    • Ethanol, wine, and experimental cardioprotection in ischemia/reperfusion: Role of the prooxidant/antioxidant balance
    • Rakotovao A, Berthonneche C, Guiraud A, et al. Ethanol, wine, and experimental cardioprotection in ischemia/reperfusion: role of the prooxidant/antioxidant balance. Antioxid Redox Signal 2004;6(2):431-8
    • (2004) Antioxid Redox Signal , vol.6 , Issue.2 , pp. 431-438
    • Rakotovao, A.1    Berthonneche, C.2    Guiraud, A.3
  • 102
    • 0036298643 scopus 로고    scopus 로고
    • Cardioprotection with alcohol: Role of both alcohol and polyphenolic antioxidants
    • Sato M, Maulik N, Das DK. Cardioprotection with alcohol: role of both alcohol and polyphenolic antioxidants. Ann NY Acad Sci 2002;957:122-35
    • (2002) Ann NY Acad Sci , vol.957 , pp. 122-135
    • Sato, M.1    Maulik, N.2    Das, D.K.3
  • 103
    • 0035883495 scopus 로고    scopus 로고
    • Mitochondrial oxidative damage and myocardial fibrosis in rats chronically intoxicated with moderate doses of ethanol
    • Vendemiale G, Grattagliano I, Altomare E, et al. Mitochondrial oxidative damage and myocardial fibrosis in rats chronically intoxicated with moderate doses of ethanol. Toxicol Lett 2001;123(2-3):209-16
    • (2001) Toxicol Lett , vol.123 , Issue.2-3 , pp. 209-216
    • Vendemiale, G.1    Grattagliano, I.2    Altomare, E.3
  • 104
    • 0034913895 scopus 로고    scopus 로고
    • Acute ethanol administration oxidatively damages and depletes mitochondrial DNA in mouse liver, brain, heart, and skeletal muscles: Protective effects of antioxidants
    • Mansouri A, Demeilliers C, Amsellem S, Pessayre D, Fromenty B. Acute ethanol administration oxidatively damages and depletes mitochondrial DNA in mouse liver, brain, heart, and skeletal muscles: protective effects of antioxidants. J Pharmacol Exp Ther 2001;298(2):737-43
    • (2001) J Pharmacol Exp Ther , vol.298 , Issue.2 , pp. 737-743
    • Mansouri, A.1    Demeilliers, C.2    Amsellem, S.3    Pessayre, D.4    Fromenty, B.5
  • 105
    • 0029616381 scopus 로고
    • Heart mitochondria response to alcohol is different than brain and liver
    • Marin-Garcia J, Ananthakrishnan R, Goldenthal MJ. Heart mitochondria response to alcohol is different than brain and liver. Alcohol Clin Exp Res 1995;19(6):1463-6
    • (1995) Alcohol Clin Exp Res , vol.19 , Issue.6 , pp. 1463-1466
    • Marin-Garcia, J.1    Ananthakrishnan, R.2    Goldenthal, M.J.3
  • 106
    • 18844437227 scopus 로고    scopus 로고
    • Alcohol and mitochondria in cardiac apoptosis: Mechanisms and visualization
    • Hajnoczky G, Buzas CJ, Pacher P, Hoek JB, Rubin E, Alcohol and mitochondria in cardiac apoptosis: mechanisms and visualization. Alcohol Clin Exp Res 2005;29(5):693-701
    • (2005) Alcohol Clin Exp Res , vol.29 , Issue.5 , pp. 693-701
    • Hajnoczky, G.1    Buzas, C.J.2    Pacher, P.3    Hoek, J.B.4    Rubin, E.5
  • 108
    • 0026735806 scopus 로고
    • Cardiovascular complications of cocaine
    • Om A. Cardiovascular complications of cocaine. Am J Med Sci 1992;303(5):333-9
    • (1992) Am J Med Sci , vol.303 , Issue.5 , pp. 333-339
    • Om, A.1
  • 109
    • 0032932350 scopus 로고    scopus 로고
    • Effect of cocaine on cardiac biochemical functions
    • Devi BG, Chan AW. Effect of cocaine on cardiac biochemical functions. J Cardiovasc Pharmacol 1999;33(1):1-6
    • (1999) J Cardiovasc Pharmacol , vol.33 , Issue.1 , pp. 1-6
    • Devi, B.G.1    Chan, A.W.2
  • 110
    • 0033962335 scopus 로고    scopus 로고
    • Cocaine induces apoptosis in fetal myocardial cells through a mitochondria-dependent pathway
    • Xiao Y, He J, Gilbert RD, Zhang L. Cocaine induces apoptosis in fetal myocardial cells through a mitochondria-dependent pathway. J Pharmacol Exp Ther 2000;292(1):8-14
    • (2000) J Pharmacol Exp Ther , vol.292 , Issue.1 , pp. 8-14
    • Xiao, Y.1    He, J.2    Gilbert, R.D.3    Zhang, L.4
  • 111
    • 0033572649 scopus 로고    scopus 로고
    • Cocaine and apoptosis in myocardial cells
    • Zhang L, Xiao Y, He J. Cocaine and apoptosis in myocardial cells. Anat Rec 1999;257(6):208-16
    • (1999) Anat Rec , vol.257 , Issue.6 , pp. 208-216
    • Zhang, L.1    Xiao, Y.2    He, J.3
  • 112
    • 0034069847 scopus 로고    scopus 로고
    • Effect of cocaine on mitochondrial electron transport chain evaluated in primary cultures of neonatal rat myocardial cells and in isolated mitochondrial preparations
    • Yuan C, Acosta D Jr. Effect of cocaine on mitochondrial electron transport chain evaluated in primary cultures of neonatal rat myocardial cells and in isolated mitochondrial preparations. Drug Chem Toxicol 2000;23(2):339-48
    • (2000) Drug Chem Toxicol , vol.23 , Issue.2 , pp. 339-348
    • Yuan, C.1    Acosta Jr., D.2
  • 113
    • 29644441890 scopus 로고    scopus 로고
    • Cocaine increases intracellular calcium and reactive oxygen species, depolarizes mitochondria, and activates genes associated with heart failure and remodeling
    • Lattanzio FA Jr, Tiangco D, Osgood C, Beebe S, Kerry J, Hargrave BY. Cocaine increases intracellular calcium and reactive oxygen species, depolarizes mitochondria, and activates genes associated with heart failure and remodeling. Cardiovasc Toxicol 2005;5(4):377-90
    • (2005) Cardiovasc Toxicol , vol.5 , Issue.4 , pp. 377-390
    • Lattanzio Jr, F.A.1    Tiangco, D.2    Osgood, C.3    Beebe, S.4    Kerry, J.5    Hargrave, B.Y.6
  • 114
    • 27144485796 scopus 로고    scopus 로고
    • 3,4-Methylenedioxymethamphetamine activates nuclear factor-kappaB, increases intracellular calcium, and modulates gene transcription in rat heart cells
    • Tiangco DA, Lattanzio FA Jr, Osgood CJ, Beebe SJ, Kerry JA, Hargrave BY. 3,4-Methylenedioxymethamphetamine activates nuclear factor-kappaB, increases intracellular calcium, and modulates gene transcription in rat heart cells. Cardiovasc Toxicol 2005;5(3):301-10
    • (2005) Cardiovasc Toxicol , vol.5 , Issue.3 , pp. 301-310
    • Tiangco, D.A.1    Lattanzio Jr, F.A.2    Osgood, C.J.3    Beebe, S.J.4    Kerry, J.A.5    Hargrave, B.Y.6
  • 115
    • 33749395149 scopus 로고    scopus 로고
    • Statin myopathy: The iceberg or its tip?
    • Campbell WW. Statin myopathy: the iceberg or its tip? Muscle Nerve 2006;34(4):387-90
    • (2006) Muscle Nerve , vol.34 , Issue.4 , pp. 387-390
    • Campbell, W.W.1
  • 116
    • 27744603499 scopus 로고    scopus 로고
    • High-dose atorvastatin vs usual-dose simvastatin for secondary prevention after myocardial infarction: The IDEAL study: a randomized controlled trial
    • Pedersen TR, Faergeman O, Kastelein JJ, et al. High-dose atorvastatin vs usual-dose simvastatin for secondary prevention after myocardial infarction: the IDEAL study: a randomized controlled trial. JAMA 2005;294(19):2437-45
    • (2005) JAMA , vol.294 , Issue.19 , pp. 2437-2445
    • Pedersen, T.R.1    Faergeman, O.2    Kastelein, J.J.3
  • 117
    • 0034046256 scopus 로고    scopus 로고
    • HMG-CoA reductase inhibitors and myotoxicity
    • Ucar M, Mjorndal T, Dahlqvist R. HMG-CoA reductase inhibitors and myotoxicity. Drug Saf 2000;22(6):441-57
    • (2000) Drug Saf , vol.22 , Issue.6 , pp. 441-457
    • Ucar, M.1    Mjorndal, T.2    Dahlqvist, R.3
  • 118
    • 4444254150 scopus 로고    scopus 로고
    • Mitochondrial alterations in muscle biopsies of patients on statin therapy
    • Gambelli S, Dotti MT, Malandrini A, et al. Mitochondrial alterations in muscle biopsies of patients on statin therapy. J Submicrosc Cytol Pathol 2004;36(1):85-9
    • (2004) J Submicrosc Cytol Pathol , vol.36 , Issue.1 , pp. 85-89
    • Gambelli, S.1    Dotti, M.T.2    Malandrini, A.3
  • 119
    • 0018866527 scopus 로고
    • Regulation of hepatic cholesterogenesis
    • Goldfarb S. Regulation of hepatic cholesterogenesis. Int Rev Physiol 1980;21:317-56
    • (1980) Int Rev Physiol , vol.21 , pp. 317-356
    • Goldfarb, S.1
  • 120
    • 0037414218 scopus 로고    scopus 로고
    • Statin-associated myopathy
    • Thompson PD, Clarkson P, Karas RH. Statin-associated myopathy. JAMA 2003;289(13):1681-90
    • (2003) JAMA , vol.289 , Issue.13 , pp. 1681-1690
    • Thompson, P.D.1    Clarkson, P.2    Karas, R.H.3
  • 121
    • 0035197395 scopus 로고    scopus 로고
    • Statin myopathies: Pathophysiologic and clinical perspectives
    • Baker SK, Tarnopolsky MA. Statin myopathies: pathophysiologic and clinical perspectives. Clin Invest Med 2001;24(5):258-72
    • (2001) Clin Invest Med , vol.24 , Issue.5 , pp. 258-272
    • Baker, S.K.1    Tarnopolsky, M.A.2
  • 123
    • 14844327531 scopus 로고    scopus 로고
    • Simvastatin triggers mitochondria-induced Ca2+ signaling alteration in skeletal muscle
    • Sirvent P, Mercier J, Vassort G, Lacampagne A. Simvastatin triggers mitochondria-induced Ca2+ signaling alteration in skeletal muscle. Biochem Biophys Res Commun 2005;329(3):1067-75
    • (2005) Biochem Biophys Res Commun , vol.329 , Issue.3 , pp. 1067-1075
    • Sirvent, P.1    Mercier, J.2    Vassort, G.3    Lacampagne, A.4
  • 124
    • 34248170185 scopus 로고    scopus 로고
    • Coenzyme Q10 and statins: Biochemical and clinical implications
    • Littarru GP, Langsjoen P. Coenzyme Q10 and statins: biochemical and clinical implications. Mitochondrion 2007;7(Suppl):S168-74
    • (2007) Mitochondrion , vol.7 , Issue.SUPPL.
    • Littarru, G.P.1    Langsjoen, P.2
  • 126
    • 0029837064 scopus 로고    scopus 로고
    • Lipid-lowering drugs and mitochondrial function: Effects of HMG-CoA reductase inhibitors on serum ubiquinone and blood lactate/pyruvate ratio
    • De Pinieux G, Chariot P, Ammi-Said M, et al. Lipid-lowering drugs and mitochondrial function: effects of HMG-CoA reductase inhibitors on serum ubiquinone and blood lactate/pyruvate ratio. Br J Clin Pharmacol 1996;42(3):333-7
    • (1996) Br J Clin Pharmacol , vol.42 , Issue.3 , pp. 333-337
    • De Pinieux, G.1    Chariot, P.2    Ammi-Said, M.3
  • 127
    • 0031757804 scopus 로고    scopus 로고
    • Metabolic changes in patients with mitochondrial myopathies and effects of coenzyme Q10 therapy
    • Chan A, Reichmann H, Kogel A, Beck A, Gold R. Metabolic changes in patients with mitochondrial myopathies and effects of coenzyme Q10 therapy. J Neurol 1998;245(10):681-5
    • (1998) J Neurol , vol.245 , Issue.10 , pp. 681-685
    • Chan, A.1    Reichmann, H.2    Kogel, A.3    Beck, A.4    Gold, R.5
  • 131
    • 0032818131 scopus 로고    scopus 로고
    • Gene expression analysis by transcript profiling coupled to a gene database query
    • Shimkets RA, Lowe DG, Tai JT, et al. Gene expression analysis by transcript profiling coupled to a gene database query. Nat Biotechnol 1999;17(8):798-803
    • (1999) Nat Biotechnol , vol.17 , Issue.8 , pp. 798-803
    • Shimkets, R.A.1    Lowe, D.G.2    Tai, J.T.3
  • 132
    • 0031898610 scopus 로고    scopus 로고
    • PPAR-gamma: Adipogenic regulator and thiazolidinedione receptor
    • Spiegelman BM. PPAR-gamma: adipogenic regulator and thiazolidinedione receptor. Diabetes 1998;47(4):507-14
    • (1998) Diabetes , vol.47 , Issue.4 , pp. 507-514
    • Spiegelman, B.M.1
  • 133
    • 20444497357 scopus 로고    scopus 로고
    • Receptor-independent actions of PPAR thiazolidinedione agonists: Is mitochondrial function the key?
    • Feinstein DL, Spagnolo A, Akar C, et al. Receptor-independent actions of PPAR thiazolidinedione agonists: is mitochondrial function the key? Biochem Pharmacol 2005;70(2):177-88
    • (2005) Biochem Pharmacol , vol.70 , Issue.2 , pp. 177-188
    • Feinstein, D.L.1    Spagnolo, A.2    Akar, C.3
  • 134
    • 9644262470 scopus 로고    scopus 로고
    • Mitochondrial dysfunction by synthetic ligands of peroxisome proliferator activated receptors (PPARs)
    • Scatena R, Martorana GE, Bottoni P, Giardina B. Mitochondrial dysfunction by synthetic ligands of peroxisome proliferator activated receptors (PPARs). IUBMB Life 2004;56(8):477-82
    • (2004) IUBMB Life , vol.56 , Issue.8 , pp. 477-482
    • Scatena, R.1    Martorana, G.E.2    Bottoni, P.3    Giardina, B.4
  • 135
    • 0031911722 scopus 로고    scopus 로고
    • Extraperoxisomal targets of peroxisome proliferators: Mitochondrial, microsomal, and cytosolic effects. Implications for health and disease
    • Youssef J, Badr M. Extraperoxisomal targets of peroxisome proliferators: mitochondrial, microsomal, and cytosolic effects. Implications for health and disease. Crit Rev Toxicol 1998;28(1):1-33
    • (1998) Crit Rev Toxicol , vol.28 , Issue.1 , pp. 1-33
    • Youssef, J.1    Badr, M.2
  • 136
    • 12144291275 scopus 로고    scopus 로고
    • Thiazolidinediones, like metformin, inhibit respiratory complex I: A common mechanism contributing to their antidiabetic actions?
    • Brunmair B, Staniek K, Gras F, et al. Thiazolidinediones, like metformin, inhibit respiratory complex I: a common mechanism contributing to their antidiabetic actions? Diabetes 2004;53(4):1052-9
    • (2004) Diabetes , vol.53 , Issue.4 , pp. 1052-1059
    • Brunmair, B.1    Staniek, K.2    Gras, F.3
  • 138
    • 0038650658 scopus 로고    scopus 로고
    • Mechanisms of troglitazone hepatotoxicity
    • Smith MT. Mechanisms of troglitazone hepatotoxicity. Chem Res Toxicol 2003;16(6):679-87
    • (2003) Chem Res Toxicol , vol.16 , Issue.6 , pp. 679-687
    • Smith, M.T.1
  • 139
    • 0037051164 scopus 로고    scopus 로고
    • Myopathy and rhabdomyolysis with lipid-lowering drugs
    • Hodel C. Myopathy and rhabdomyolysis with lipid-lowering drugs. Toxicol Lett 2002;128(1-3):159-68
    • (2002) Toxicol Lett , vol.128 , Issue.1-3 , pp. 159-168
    • Hodel, C.1
  • 140
    • 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, et al. Mitochondrial complex I inhibitor rotenone induces apoptosis through enhancing mitochondrial reactive oxygen species production. J Biol Chem 2003;278(10):8516-25
    • (2003) J Biol Chem , vol.278 , Issue.10 , pp. 8516-8525
    • Li, N.1    Ragheb, K.2    Lawler, G.3
  • 141
    • 34250212715 scopus 로고    scopus 로고
    • Effect of rosiglitazone on the risk of myocardial infarction and death from cardiovascular causes
    • Nissen SE, Wolski K. Effect of rosiglitazone on the risk of myocardial infarction and death from cardiovascular causes. N Engl J Med 2007;356(24):2457-71
    • (2007) N Engl J Med , vol.356 , Issue.24 , pp. 2457-2471
    • Nissen, S.E.1    Wolski, K.2
  • 142
    • 33646071787 scopus 로고    scopus 로고
    • The role of sodium channels in chronic inflammatory and neuropathic pain
    • Amir R, Argoff CE, Bennett GJ, et al. The role of sodium channels in chronic inflammatory and neuropathic pain, J Pain 2006;7(5 Suppl 3):S1-29
    • (2006) J Pain , vol.7 , Issue.5 SUPPL. 3
    • Amir, R.1    Argoff, C.E.2    Bennett, G.J.3
  • 143
    • 0038415732 scopus 로고    scopus 로고
    • Local anesthetics. Differences and similarities in the "-cains
    • Dullenkopf A, Borgeat A. Local anesthetics. Differences and similarities in the "-cains". Anaesthesist 2003;52(4):329-40
    • (2003) Anaesthesist , vol.52 , Issue.4 , pp. 329-340
    • Dullenkopf, A.1    Borgeat, A.2
  • 144
    • 0027403403 scopus 로고
    • The use of antiarrhythmics in advanced cardiac life support
    • Jaffe AS. The use of antiarrhythmics in advanced cardiac life support. Ann Emerg Med 1993;22(2 Pt 2):307-16
    • (1993) Ann Emerg Med , vol.22 , Issue.2 PART 2 , pp. 307-316
    • Jaffe, A.S.1
  • 145
    • 34547398506 scopus 로고    scopus 로고
    • Suicide due to oral ingestion of lidocaine: A case report and review of the literature
    • Centini F, Fiore C, Riezzo I, Rossi G, Fineschi V. Suicide due to oral ingestion of lidocaine: a case report and review of the literature. Forensic Sci Int 2007;171(1):57-62
    • (2007) Forensic Sci Int , vol.171 , Issue.1 , pp. 57-62
    • Centini, F.1    Fiore, C.2    Riezzo, I.3    Rossi, G.4    Fineschi, V.5
  • 146
    • 0018580592 scopus 로고
    • Effects of some antiarrhythmic agents on dog heart mitochondrial oxidative phosphorylation
    • Alto LE, Dhalla NS. Effects of some antiarrhythmic agents on dog heart mitochondrial oxidative phosphorylation. Eur J Pharmacol 1979;59(3-4):311-4
    • (1979) Eur J Pharmacol , vol.59 , Issue.3-4 , pp. 311-314
    • Alto, L.E.1    Dhalla, N.S.2
  • 147
    • 0020332930 scopus 로고
    • Further studies on F 1-ATPase inhibition by local anesthetics
    • Chazotte B, Vanderkooi G, Chignell D. Further studies on F 1-ATPase inhibition by local anesthetics. Biochim Biophys Acta 1982;680(3):310-6
    • (1982) Biochim Biophys Acta , vol.680 , Issue.3 , pp. 310-316
    • Chazotte, B.1    Vanderkooi, G.2    Chignell, D.3
  • 148
    • 0027450348 scopus 로고
    • Investigation of class I anti-arrhythmic drug actions on guinea-pig cardiac mitochondrial lactate dehydrogenase activity
    • Dzimiri N, Almotrefi AA. Investigation of class I anti-arrhythmic drug actions on guinea-pig cardiac mitochondrial lactate dehydrogenase activity. Clin Exp Pharmacol Physiol 1993;20(4):201-6
    • (1993) Clin Exp Pharmacol Physiol , vol.20 , Issue.4 , pp. 201-206
    • Dzimiri, N.1    Almotrefi, A.A.2
  • 149
    • 0034849904 scopus 로고    scopus 로고
    • Lidocaine and mexiletine inhibit mitochondrial oxidation in rat ventricular myocytes
    • Tsutsumi Y, Oshita S, Kawano T, et al. Lidocaine and mexiletine inhibit mitochondrial oxidation in rat ventricular myocytes. Anesthesiology 2001;95(3):766-70
    • (2001) Anesthesiology , vol.95 , Issue.3 , pp. 766-770
    • Tsutsumi, Y.1    Oshita, S.2    Kawano, T.3
  • 150
    • 0036854976 scopus 로고    scopus 로고
    • Cardiac toxicity of local anesthetics in the intact isolated heart model: A review
    • Heavner JE. Cardiac toxicity of local anesthetics in the intact isolated heart model: a review. Reg Anesth Pain Med 2002;27(6):545-55
    • (2002) Reg Anesth Pain Med , vol.27 , Issue.6 , pp. 545-555
    • Heavner, J.E.1
  • 151
    • 34748835906 scopus 로고    scopus 로고
    • Lipid rescue resuscitation from local anaesthetic cardiac toxicity
    • Weinberg G. Lipid rescue resuscitation from local anaesthetic cardiac toxicity. Toxicol Rev 2006;25(3):139-45
    • (2006) Toxicol Rev , vol.25 , Issue.3 , pp. 139-145
    • Weinberg, G.1
  • 152
    • 0026716379 scopus 로고
    • Is bupivacaine a decoupler, a protonophore or a proton-leak-inducer?
    • Schonfeld P, Sztark F, Slimani M, Dabadie P, Mazat JP. Is bupivacaine a decoupler, a protonophore or a proton-leak-inducer? FEBS Lett 1992;304(2-3):273-6
    • (1992) FEBS Lett , vol.304 , Issue.2-3 , pp. 273-276
    • Schonfeld, P.1    Sztark, F.2    Slimani, M.3    Dabadie, P.4    Mazat, J.P.5
  • 153
    • 0030780863 scopus 로고    scopus 로고
    • Effects of the local anesthetic bupivacaine on mitochondrial energy metabolism: Change from uncoupling to decoupling depending on the respiration state
    • Sztark F, Ouhabi R, Dabadie P, Mazat JP. Effects of the local anesthetic bupivacaine on mitochondrial energy metabolism: change from uncoupling to decoupling depending on the respiration state. Biochem Mol Biol Int 1997;43(5):997-1003
    • (1997) Biochem Mol Biol Int , vol.43 , Issue.5 , pp. 997-1003
    • Sztark, F.1    Ouhabi, R.2    Dabadie, P.3    Mazat, J.P.4
  • 154
    • 0031956338 scopus 로고    scopus 로고
    • Comparison of the effects of bupivacaine and ropivacaine on heart cell mitochondrial bioenergetics
    • Sztark F, Malgat M, Dabadie P, Mazat JP. Comparison of the effects of bupivacaine and ropivacaine on heart cell mitochondrial bioenergetics. Anesthesiology 1998;88(5):1340-9
    • (1998) Anesthesiology , vol.88 , Issue.5 , pp. 1340-1349
    • Sztark, F.1    Malgat, M.2    Dabadie, P.3    Mazat, J.P.4
  • 155
    • 3142538596 scopus 로고    scopus 로고
    • Zhang S, Yao S, Li Q. Effects of ropivacaine and bupivacaine on rabbit myocardial energetic metabolism and mitochondria oxidation. J Huazhong Univ Sci Technolog Med Sci 2003;23(2):178-9, 83
    • Zhang S, Yao S, Li Q. Effects of ropivacaine and bupivacaine on rabbit myocardial energetic metabolism and mitochondria oxidation. J Huazhong Univ Sci Technolog Med Sci 2003;23(2):178-9, 83
  • 156
    • 0033853187 scopus 로고    scopus 로고
    • Absence of stereospecific effects of bupivacaine isomers on heart mitochondrial bioenergetics
    • Sztark F, Nouette-Gaulain K, Malgat M, Dabadie P, Mazat JP. Absence of stereospecific effects of bupivacaine isomers on heart mitochondrial bioenergetics. Anesthesiology 2000;93(2):456-62
    • (2000) Anesthesiology , vol.93 , Issue.2 , pp. 456-462
    • Sztark, F.1    Nouette-Gaulain, K.2    Malgat, M.3    Dabadie, P.4    Mazat, J.P.5
  • 158
    • 0018873149 scopus 로고
    • Early ultrastructural changes in skeletal muscle exposed to the local anaesthetic bupivacaine (Marcaine)
    • Hall-Craggs EC. Early ultrastructural changes in skeletal muscle exposed to the local anaesthetic bupivacaine (Marcaine). Br J Exp Pathol 1980;61(2):139-49
    • (1980) Br J Exp Pathol , vol.61 , Issue.2 , pp. 139-149
    • Hall-Craggs, E.C.1
  • 159
    • 0037023786 scopus 로고    scopus 로고
    • Bupivacaine myotoxicity is mediated by mitochondria
    • Irwin W, Fontaine E, Agnolucci L, et al. Bupivacaine myotoxicity is mediated by mitochondria. J Biol Chem 2002;277(14):12221-7
    • (2002) J Biol Chem , vol.277 , Issue.14 , pp. 12221-12227
    • Irwin, W.1    Fontaine, E.2    Agnolucci, L.3
  • 160
    • 37349096665 scopus 로고    scopus 로고
    • Small-scale immunopurification of cytochrome c oxidase for a high-throughput multiplexing analysis of enzyme activity and amount
    • Murray J, Schilling B, Row RH, et al. Small-scale immunopurification of cytochrome c oxidase for a high-throughput multiplexing analysis of enzyme activity and amount. Biotechnol Appl Biochem 2007;48(Pt 4):167-78
    • (2007) Biotechnol Appl Biochem , vol.48 , Issue.PART 4 , pp. 167-178
    • Murray, J.1    Schilling, B.2    Row, R.H.3
  • 161
    • 34147159979 scopus 로고    scopus 로고
    • Analysis of mitochondrial function using phosphorescent oxygen-sensitive probes
    • Will Y, Hynes J, Oguttsov VI, Papkovsky DB. Analysis of mitochondrial function using phosphorescent oxygen-sensitive probes. Nat Protoc 2006;1(6):2563-72
    • (2006) Nat Protoc , vol.1 , Issue.6 , pp. 2563-2572
    • Will, Y.1    Hynes, J.2    Oguttsov, V.I.3    Papkovsky, D.B.4
  • 162
    • 34249890008 scopus 로고    scopus 로고
    • High-throughput identification of inhibitors of human mitochondrial peptide deformylase
    • Antczak C, Shum D, Escobar S, et al. High-throughput identification of inhibitors of human mitochondrial peptide deformylase. J Biomol Screen 2007;12(4):521-35
    • (2007) J Biomol Screen , vol.12 , Issue.4 , pp. 521-535
    • Antczak, C.1    Shum, D.2    Escobar, S.3
  • 163
    • 34047154993 scopus 로고    scopus 로고
    • Strategies to reduce late-stage drug attrition due to mitochondrial toxicity
    • Dykens JA, Marroquin LD, Will Y. Strategies to reduce late-stage drug attrition due to mitochondrial toxicity. Expert Rev Mol Diagn 2007;7(2):161-75
    • (2007) Expert Rev Mol Diagn , vol.7 , Issue.2 , pp. 161-175
    • Dykens, J.A.1    Marroquin, L.D.2    Will, Y.3


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