메뉴 건너뛰기




Volumn 7, Issue 6, 2008, Pages 647-662

A systems biology based integrative framework to enhance the predictivity of in vitro methods for drug-induced liver injury

Author keywords

Drug induced liver injury; Hepatotoxicity; In silico; In vitro; Integrative; Predictive; Systems biology; Systems modelling

Indexed keywords

AMIODARONE; BUTHIONINE SULFOXIMINE; ETACRYNIC ACID; NONSTEROID ANTIINFLAMMATORY AGENT; PERHEXILINE;

EID: 57049095489     PISSN: 14740338     EISSN: None     Source Type: Journal    
DOI: 10.1517/14740330802501211     Document Type: Article
Times cited : (17)

References (111)
  • 1
    • 0030886937 scopus 로고    scopus 로고
    • Managing the drug discovery/development interface
    • Kennedy T. Managing the drug discovery/development interface. Drug Discov Today 1997;2:436-44
    • (1997) Drug Discov Today , vol.2 , pp. 436-444
    • Kennedy, T.1
  • 2
    • 35548954739 scopus 로고    scopus 로고
    • Improving early drug discovery through ADME modelling: An overview
    • Wishart DS. Improving early drug discovery through ADME modelling: an overview. Drugs RD 2007;8:349-62
    • (2007) Drugs RD , vol.8 , pp. 349-362
    • Wishart, D.S.1
  • 3
    • 33747814785 scopus 로고    scopus 로고
    • Subramanian K. truPK-human pharmacokinetic models for quantitative ADME prediction. Expert Opin Drug Metab Toxicol 2005;1(3):555-64
    • Subramanian K. truPK-human pharmacokinetic models for quantitative ADME prediction. Expert Opin Drug Metab Toxicol 2005;1(3):555-64
  • 4
    • 0025804183 scopus 로고
    • Correlation between oral drug absorption in humans and apparent drug permeability coefficients in human intestinal epithelial (CACO-2) cells
    • Artursson P, Karlsson J. Correlation between oral drug absorption in humans and apparent drug permeability coefficients in human intestinal epithelial (CACO-2) cells. Biochem Biophys Res Comm 1991;175:880-5
    • (1991) Biochem Biophys Res Comm , vol.175 , pp. 880-885
    • Artursson, P.1    Karlsson, J.2
  • 5
    • 0024533366 scopus 로고
    • In vivo and in vitro pharmacokinetic differences between four structurally closely related anthracyclines in hematopoietic cell subtypes in humans
    • Speth PA, Linssen PC, Termond EF, et al. In vivo and in vitro pharmacokinetic differences between four structurally closely related anthracyclines in hematopoietic cell subtypes in humans. Drug Metab Dispos 1989;17:98-105
    • (1989) Drug Metab Dispos , vol.17 , pp. 98-105
    • Speth, P.A.1    Linssen, P.C.2    Termond, E.F.3
  • 7
    • 33845712413 scopus 로고    scopus 로고
    • Clinical implications of CYP3A polymorphisms. Expert Opin Drug Metab
    • Wojnowski L, Kamdem LK. Clinical implications of CYP3A polymorphisms. Expert Opin Drug Metab Toxicol 2006;2:171-82
    • (2006) Toxicol , vol.2 , pp. 171-182
    • Wojnowski, L.1    Kamdem, L.K.2
  • 9
    • 0041342015 scopus 로고    scopus 로고
    • Drug-induced hepatotoxicity
    • Lee WJ. Drug-induced hepatotoxicity. N Engl J Med 2003;349:474-85
    • (2003) N Engl J Med , vol.349 , pp. 474-485
    • Lee, W.J.1
  • 10
    • 40649116713 scopus 로고    scopus 로고
    • Differential response of human and rat epoxide hydrolase to polycyclic aromatic hydrocarbon exposure: Studies using precision-cut tissue slices
    • Pushparajah DS, Umachandran M, Plant KE, et al. Differential response of human and rat epoxide hydrolase to polycyclic aromatic hydrocarbon exposure: studies using precision-cut tissue slices. Mutat Res 2008;640(1-2):153-61
    • (2008) Mutat Res , vol.640 , Issue.1-2 , pp. 153-161
    • Pushparajah, D.S.1    Umachandran, M.2    Plant, K.E.3
  • 11
    • 0030799001 scopus 로고    scopus 로고
    • The prediction of human pharmacokinetic parameters from preclinical and in vitro metabolism data
    • Obach RS, Baxter JG, Liston TE, et al. The prediction of human pharmacokinetic parameters from preclinical and in vitro metabolism data. J Pharmacol Exp Ther 1997;283(1):46-58
    • (1997) J Pharmacol Exp Ther , vol.283 , Issue.1 , pp. 46-58
    • Obach, R.S.1    Baxter, J.G.2    Liston, T.E.3
  • 12
    • 33747833384 scopus 로고    scopus 로고
    • Comparison of intrinsic clearance in liver microsomes and hepatocytes from rats and humans: Evaluation of free fraction and uptake in hepatocytes
    • Lu C, Li P, Gallegos R, et al. Comparison of intrinsic clearance in liver microsomes and hepatocytes from rats and humans: evaluation of free fraction and uptake in hepatocytes. Drug Metab Dispos 2006;34(9):1600-5
    • (2006) Drug Metab Dispos , vol.34 , Issue.9 , pp. 1600-1605
    • Lu, C.1    Li, P.2    Gallegos, R.3
  • 13
    • 84934441733 scopus 로고    scopus 로고
    • Predictive toxicogenomics in preclinical discovery
    • Barros SA, Martin RB. Predictive toxicogenomics in preclinical discovery. Methods Mol Biol 2008;460:89-112
    • (2008) Methods Mol Biol , vol.460 , pp. 89-112
    • Barros, S.A.1    Martin, R.B.2
  • 15
    • 0036186560 scopus 로고    scopus 로고
    • Role of mitochondrial permeability transition in diclofenac-induced hepatocyte injury in rats
    • Masubuchi Y, Nakayama S, Horie T. Role of mitochondrial permeability transition in diclofenac-induced hepatocyte injury in rats. Hepatology 2002;35:544-51
    • (2002) Hepatology , vol.35 , pp. 544-551
    • Masubuchi, Y.1    Nakayama, S.2    Horie, T.3
  • 16
    • 0033179481 scopus 로고    scopus 로고
    • Top-down control analysis of ATP turnover, glycolysis and oxidative phophorylation in rat hepatocytes
    • Ainscow EK, Brand MD. Top-down control analysis of ATP turnover, glycolysis and oxidative phophorylation in rat hepatocytes. Eur J Biochem 1999;263:671-85
    • (1999) Eur J Biochem , vol.263 , pp. 671-685
    • Ainscow, E.K.1    Brand, M.D.2
  • 17
    • 0031036081 scopus 로고    scopus 로고
    • Uncoupling effects of diclofenac and aspirin in the perfused liver and isolated hepatic mitochondria of rat
    • Petrescu I, Tarba C. Uncoupling effects of diclofenac and aspirin in the perfused liver and isolated hepatic mitochondria of rat. Biochem Biophys Acta 1997;1318:385-94
    • (1997) Biochem Biophys Acta , vol.1318 , pp. 385-394
    • Petrescu, I.1    Tarba, C.2
  • 18
    • 0344097396 scopus 로고    scopus 로고
    • Inhibition and uncoupling of oxidative phosphorylation by non-steroidal anti-inflammatory drugs
    • Moreno-Sanchez R, Bravo C, Vasquez C, et al. Inhibition and uncoupling of oxidative phosphorylation by non-steroidal anti-inflammatory drugs Biochem Pharmacol 1999;57:743-52
    • (1999) Biochem Pharmacol , vol.57 , pp. 743-752
    • Moreno-Sanchez, R.1    Bravo, C.2    Vasquez, C.3
  • 19
    • 85009593103 scopus 로고    scopus 로고
    • Potential cholestatic activity of various therapeutic agents assessed by bile canalicular membrane vesicles isolated from rats and humans
    • Horikawa M, Kato Y, Tyson CA, et al. Potential cholestatic activity of various therapeutic agents assessed by bile canalicular membrane vesicles isolated from rats and humans. Drug Metab Pharmacokin 2003;18:16-22
    • (2003) Drug Metab Pharmacokin , vol.18 , pp. 16-22
    • Horikawa, M.1    Kato, Y.2    Tyson, C.A.3
  • 20
    • 0019475767 scopus 로고
    • Effect of bile duct ligation on bile acid metabolism in rats
    • Kinugasa T, Uchida K, Kadowaki M, et al. Effect of bile duct ligation on bile acid metabolism in rats. J Lipid Res 1981;22(2):201-7
    • (1981) J Lipid Res , vol.22 , Issue.2 , pp. 201-207
    • Kinugasa, T.1    Uchida, K.2    Kadowaki, M.3
  • 21
    • 0029924518 scopus 로고    scopus 로고
    • Ion transport in hepatocytes: Mechanisms and correlations to cell volume, hormone actions and metabolism
    • Graf J, Häussinger D. Ion transport in hepatocytes: mechanisms and correlations to cell volume, hormone actions and metabolism. J Hepatol 1996;24:53-77
    • (1996) J Hepatol , vol.24 , pp. 53-77
    • Graf, J.1    Häussinger, D.2
  • 22
    • 0025720142 scopus 로고
    • Motility of bile canaliculi in the living animal: Implications for bile flow
    • Watanabe N, Tsukada N, Smith CR, Phillips MJ. Motility of bile canaliculi in the living animal: implications for bile flow. J Cell Biol 1991;113:1069-80
    • (1991) J Cell Biol , vol.113 , pp. 1069-1080
    • Watanabe, N.1    Tsukada, N.2    Smith, C.R.3    Phillips, M.J.4
  • 23
    • 0025317268 scopus 로고
    • Glutathione: Toxicological implications
    • Reed DJ. Glutathione: toxicological implications. Ann Rev Pharmacol Toxicol 1990;30:603-31
    • (1990) Ann Rev Pharmacol Toxicol , vol.30 , pp. 603-631
    • Reed, D.J.1
  • 24
    • 0032774131 scopus 로고    scopus 로고
    • Bimolecular glutathione conjugation kinetics of ethacrynic acid in the rat liver: In vitro and perfusion studies
    • Tirona RG, Pang KS. Bimolecular glutathione conjugation kinetics of ethacrynic acid in the rat liver: in vitro and perfusion studies. J Pharmacol Exper Ther 1999;290:1230-40
    • (1999) J Pharmacol Exper Ther , vol.290 , pp. 1230-1240
    • Tirona, R.G.1    Pang, K.S.2
  • 25
    • 9744256972 scopus 로고    scopus 로고
    • Daphnetoxin interacts with mitochondrial oxidative phosphorylation and induces membrane permeability transition in rat liver
    • Peixoto F, Carvalho MJ, Almeida J, et al. Daphnetoxin interacts with mitochondrial oxidative phosphorylation and induces membrane permeability transition in rat liver. Planta Med 2004;70:1-5
    • (2004) Planta Med , vol.70 , pp. 1-5
    • Peixoto, F.1    Carvalho, M.J.2    Almeida, J.3
  • 26
    • 0028302917 scopus 로고
    • Inhibition by perhexiline of oxidative phosphorylation and the beta-oxidation of fatty acids: Possible role in pseudoalcoholic liver lesions
    • Deschamps D, DeBeco V, Fisch C, et al. Inhibition by perhexiline of oxidative phosphorylation and the beta-oxidation of fatty acids: possible role in pseudoalcoholic liver lesions. Hepatology 1994;19:948-61
    • (1994) Hepatology , vol.19 , pp. 948-961
    • Deschamps, D.1    DeBeco, V.2    Fisch, C.3
  • 27
    • 0025677186 scopus 로고
    • Amiodarone inhibits the mitochondrial beta-oxidation of fatty acids and produces microvesicular steatosis of the liver in mice
    • Fromenty B, Fisch C, Labbe G, et al. Amiodarone inhibits the mitochondrial beta-oxidation of fatty acids and produces microvesicular steatosis of the liver in mice. J Pharmacol Exp Ther 1990;225:1371-6
    • (1990) J Pharmacol Exp Ther , vol.225 , pp. 1371-1376
    • Fromenty, B.1    Fisch, C.2    Labbe, G.3
  • 28
    • 34249284163 scopus 로고    scopus 로고
    • Genetic polymorphisms of manganese superoxide dismurase, NAD(P)H:quinone oxidoreduccase, glutathione S-transferase M1 and T1, and the susceptibility to drug-induced liver injury
    • Huang YS, Su WJ, Huang YH, et al. Genetic polymorphisms of manganese superoxide dismurase, NAD(P)H:quinone oxidoreduccase, glutathione S-transferase M1 and T1, and the susceptibility to drug-induced liver injury. J Hepatol 2007;47(1):128-34
    • (2007) J Hepatol , vol.47 , Issue.1 , pp. 128-134
    • Huang, Y.S.1    Su, W.J.2    Huang, Y.H.3
  • 29
    • 0037134782 scopus 로고    scopus 로고
    • Coherent and robust modulation of a metabolic network by cytoskeletal organization and dynamics
    • Aon MA, Cortassa S. Coherent and robust modulation of a metabolic network by cytoskeletal organization and dynamics. Biophys chem 2002;97:213-31
    • (2002) Biophys chem , vol.97 , pp. 213-231
    • Aon, M.A.1    Cortassa, S.2
  • 30
    • 0035982810 scopus 로고    scopus 로고
    • A computational model for glycogenolysis in skeletal muscle
    • Lambeth MJ, Kushmerick MJ. A computational model for glycogenolysis in skeletal muscle. Ann Biomed Eng 2002;30(6):808-27
    • (2002) Ann Biomed Eng , vol.30 , Issue.6 , pp. 808-827
    • Lambeth, M.J.1    Kushmerick, M.J.2
  • 31
    • 0037380954 scopus 로고    scopus 로고
    • An integrated model of cardiac mitochondrial energy metabolism and calcium dynamics
    • Cortassa S, Aon MA, Marbán E, et al. An integrated model of cardiac mitochondrial energy metabolism and calcium dynamics. Biophys J 2003;84(4):2734-55
    • (2003) Biophys J , vol.84 , Issue.4 , pp. 2734-2755
    • Cortassa, S.1    Aon, M.A.2    Marbán, E.3
  • 33
    • 3042647922 scopus 로고    scopus 로고
    • Theoretical studies on the regulation of anaerobic glycolysis and its influence on oxidative phosphorylation in skeletal muscle
    • Korzeniewski B, Liguzinski P. Theoretical studies on the regulation of anaerobic glycolysis and its influence on oxidative phosphorylation in skeletal muscle. Biophys Chem 2004;110(1-2):147-69
    • (2004) Biophys Chem , vol.110 , Issue.1-2 , pp. 147-169
    • Korzeniewski, B.1    Liguzinski, P.2
  • 34
    • 0035283048 scopus 로고    scopus 로고
    • Theoretical studies on the regulation of oxidative phosphorylation in intact tissues
    • Korzeniewski B. Theoretical studies on the regulation of oxidative phosphorylation in intact tissues. Biochim Biophys Acta 2001;1504(1):31-45
    • (2001) Biochim Biophys Acta , vol.1504 , Issue.1 , pp. 31-45
    • Korzeniewski, B.1
  • 35
    • 0035975695 scopus 로고    scopus 로고
    • A model of oxidative phosphorylation in mammalian skeletal muscle
    • Korzeniewski B, Zoladz JA. A model of oxidative phosphorylation in mammalian skeletal muscle. Biophys Chem 2001;92(1-2):17-34
    • (2001) Biophys Chem , vol.92 , Issue.1-2 , pp. 17-34
    • Korzeniewski, B.1    Zoladz, J.A.2
  • 36
    • 0030026579 scopus 로고    scopus 로고
    • Simulation of oxidative phosphorylation in hepatocytes
    • Korzeniewski B. Simulation of oxidative phosphorylation in hepatocytes. Biophys Chem 1996;58(3):215-24
    • (1996) Biophys Chem , vol.58 , Issue.3 , pp. 215-224
    • Korzeniewski, B.1
  • 37
    • 0019003787 scopus 로고
    • Rat liver phosphofructokinase: Kinetic activity under near-physiological conditions
    • Reinhart GD, Lardy HA. Rat liver phosphofructokinase: kinetic activity under near-physiological conditions. Biochemistry 1980;19(7):1477-84
    • (1980) Biochemistry , vol.19 , Issue.7 , pp. 1477-1484
    • Reinhart, G.D.1    Lardy, H.A.2
  • 38
    • 0019005411 scopus 로고
    • Rat liver pliosphofructokinase: Use of fluorescence polarization to study aggregation at low protein concentration
    • Reinhart GD, Lardy HA. Rat liver pliosphofructokinase: use of fluorescence polarization to study aggregation at low protein concentration. Biochemistry 1980;19(7):1484-90
    • (1980) Biochemistry , vol.19 , Issue.7 , pp. 1484-1490
    • Reinhart, G.D.1    Lardy, H.A.2
  • 39
    • 0019003969 scopus 로고
    • Rat liver phosphofructokinase: Kinetic and physiological ramifications of the aggregation behavior
    • Reinhart GD, Lardy HA. Rat liver phosphofructokinase: kinetic and physiological ramifications of the aggregation behavior. Biochemistry 1980;19(7):1491-5
    • (1980) Biochemistry , vol.19 , Issue.7 , pp. 1491-1495
    • Reinhart, G.D.1    Lardy, H.A.2
  • 40
    • 0342485742 scopus 로고
    • An activation factor of liver phosphofructokinase
    • Furuya E, Uyeda K. An activation factor of liver phosphofructokinase. Proc Natl Acad Sci USA 1980;77(10):5861-4
    • (1980) Proc Natl Acad Sci USA , vol.77 , Issue.10 , pp. 5861-5864
    • Furuya, E.1    Uyeda, K.2
  • 41
    • 0025276048 scopus 로고
    • Cellular concentrations of enzymes and their substrates
    • Albe KR, Butler MH, Wright BE. Cellular concentrations of enzymes and their substrates. J Theor Biol 1990;143(2):163-95
    • (1990) J Theor Biol , vol.143 , Issue.2 , pp. 163-195
    • Albe, K.R.1    Butler, M.H.2    Wright, B.E.3
  • 43
    • 0032169351 scopus 로고    scopus 로고
    • Integrating cytosolic calcium signals into mitochondrial metabolic responses
    • Robb-Gaspers LD, Burnett P, Rutter GA, et al. Integrating cytosolic calcium signals into mitochondrial metabolic responses. EMBO J 1998;17(17):4987-5000
    • (1998) EMBO J , vol.17 , Issue.17 , pp. 4987-5000
    • Robb-Gaspers, L.D.1    Burnett, P.2    Rutter, G.A.3
  • 44
    • 0017187544 scopus 로고
    • The kinetic mechanisms of rat kidney gamma glutamyl cysteine synthetase
    • Yip B, Rudolph FB. The kinetic mechanisms of rat kidney gamma glutamyl cysteine synthetase. J Biol Chem 1976;251:3563-8
    • (1976) J Biol Chem , vol.251 , pp. 3563-3568
    • Yip, B.1    Rudolph, F.B.2
  • 46
    • 0015207580 scopus 로고
    • Isolation of highly purified gamma glutamyl cysteine synthetase from rat kidney
    • Orlowski M, Meister A. Isolation of highly purified gamma glutamyl cysteine synthetase from rat kidney. Biochemistry 1971;10:(3)372-80
    • (1971) Biochemistry , vol.10 , Issue.3 , pp. 372-380
    • Orlowski, M.1    Meister, A.2
  • 47
    • 0034726737 scopus 로고    scopus 로고
    • Novel kinetics of mammalian glutathione synthetase: Characterization of gamma glutamyl substrate cooperative binding
    • Luo J, Huang CS, Babaoglu K, et al. Novel kinetics of mammalian glutathione synthetase: characterization of gamma glutamyl substrate cooperative binding, Biochem Biochem Res Comm 2000;275:577-81
    • (2000) Biochem Biochem Res Comm , vol.275 , pp. 577-581
    • Luo, J.1    Huang, C.S.2    Babaoglu, K.3
  • 48
    • 0001547757 scopus 로고
    • Origin and turnover of mitochondrial glutathione
    • Griffith OW, Meister A. Origin and turnover of mitochondrial glutathione. Proc Natl Acad Sci 1985;82:4668-72
    • (1985) Proc Natl Acad Sci , vol.82 , pp. 4668-4672
    • Griffith, O.W.1    Meister, A.2
  • 49
    • 0016808562 scopus 로고
    • Purification and characterization of the flavoenzyme glutathione reductase from rat liver
    • Carlberg I, Mannervik B. Purification and characterization of the flavoenzyme glutathione reductase from rat liver. J Biol chem 1975;250(14):5475-80
    • (1975) J Biol chem , vol.250 , Issue.14 , pp. 5475-5480
    • Carlberg, I.1    Mannervik, B.2
  • 50
    • 0029908304 scopus 로고    scopus 로고
    • A mathematical model for lipid peroxidation in inner mitochondrial membranes. I an integrative kinetic model
    • Antunes F, Salvador A, Marinho HS, et al. A mathematical model for lipid peroxidation in inner mitochondrial membranes. I an integrative kinetic model. Free Radic Biol Med 1996;21(7):917-43
    • (1996) Free Radic Biol Med , vol.21 , Issue.7 , pp. 917-943
    • Antunes, F.1    Salvador, A.2    Marinho, H.S.3
  • 51
    • 0019740344 scopus 로고
    • Glutathione peroxidase
    • Wendel A. Glutathione peroxidase. Methods Enzymol 1981;77:325-33
    • (1981) Methods Enzymol , vol.77 , pp. 325-333
    • Wendel, A.1
  • 52
    • 0021923561 scopus 로고
    • Sinusoidal efflux of glutathione in the perfused rat liver - evidence for a carrier mediated process
    • Ookhtens M, Hobdy K, Corvasce MC, et al. Sinusoidal efflux of glutathione in the perfused rat liver - evidence for a carrier mediated process. J Clin Invest 1985;75:258-65
    • (1985) J Clin Invest , vol.75 , pp. 258-265
    • Ookhtens, M.1    Hobdy, K.2    Corvasce, M.C.3
  • 53
    • 0024446703 scopus 로고
    • Transport of glutathione, glutathione disulfide and glutathione conjugates across the plasma membrane
    • Akerboom TPM, Sies H. Transport of glutathione, glutathione disulfide and glutathione conjugates across the plasma membrane. Methods Enzymol 1989;173:523-34
    • (1989) Methods Enzymol , vol.173 , pp. 523-534
    • Akerboom, T.P.M.1    Sies, H.2
  • 54
    • 0019948316 scopus 로고
    • The relationship of biliary glutathione disulfide efflux and intracellular glutathione disulfide content in the perfused rat liver
    • Akerboom TPM, Bilzer M, Sies H. The relationship of biliary glutathione disulfide efflux and intracellular glutathione disulfide content in the perfused rat liver. J Biol Chem 1982;257(8):4248-52
    • (1982) J Biol Chem , vol.257 , Issue.8 , pp. 4248-4252
    • Akerboom, T.P.M.1    Bilzer, M.2    Sies, H.3
  • 55
    • 0036785479 scopus 로고    scopus 로고
    • Reactive intermediates and the dynamics of glutathione-S-transferases
    • Rinaldi R, Eliasson E, Swedmark S, Morgenstern R. Reactive intermediates and the dynamics of glutathione-S-transferases. Drug Metab Dispos 2002;30(10):1053-8
    • (2002) Drug Metab Dispos , vol.30 , Issue.10 , pp. 1053-1058
    • Rinaldi, R.1    Eliasson, E.2    Swedmark, S.3    Morgenstern, R.4
  • 56
    • 0025979356 scopus 로고
    • Impaired uptake of glutathione by hepatic mitochondria from chronic ethanol fed rats
    • Fernandez-Checa JC, Garcia Ruiz C, Ookhtens M, Kaplowitz N. Impaired uptake of glutathione by hepatic mitochondria from chronic ethanol fed rats. J Clin Invest 1991;87:397-405
    • (1991) J Clin Invest , vol.87 , pp. 397-405
    • Fernandez-Checa, J.C.1    Garcia Ruiz, C.2    Ookhtens, M.3    Kaplowitz, N.4
  • 57
    • 0025049139 scopus 로고
    • High affinity transport of glutathione is a part of a multicomponent system essential for mitochondrial function
    • Martensson J, Lai JCK, Meister A. High affinity transport of glutathione is a part of a multicomponent system essential for mitochondrial function. Proc Natl Acad Sci 1990;87:7185-9
    • (1990) Proc Natl Acad Sci , vol.87 , pp. 7185-7189
    • Martensson, J.1    Lai, J.C.K.2    Meister, A.3
  • 58
    • 33646839278 scopus 로고    scopus 로고
    • Increased hepatocellular uptake of long chain fatty acids occurs by difference mechanisms in fatty livers due to obesity or excess ethanol use, contributing to the development of steatohepatitis in both settings
    • Berk PD, Zhou S, Bradbury MW. Increased hepatocellular uptake of long chain fatty acids occurs by difference mechanisms in fatty livers due to obesity or excess ethanol use, contributing to the development of steatohepatitis in both settings. Trans Am Clin Clim Assoc 2005;116:335-45
    • (2005) Trans Am Clin Clim Assoc , vol.116 , pp. 335-345
    • Berk, P.D.1    Zhou, S.2    Bradbury, M.W.3
  • 59
    • 0018787590 scopus 로고
    • Isolation and purification of long chain fatty acyl coenzyme a ligase from rat liver mitochondria
    • Philipp DP, Parsons P. Isolation and purification of long chain fatty acyl coenzyme a ligase from rat liver mitochondria. J Biol Chem 1979;254:10776-84
    • (1979) J Biol Chem , vol.254 , pp. 10776-10784
    • Philipp, D.P.1    Parsons, P.2
  • 60
    • 0014216622 scopus 로고
    • The mechanism of substrate inhibition of palmityl coenzyme A: Carnitine palmityltransferase by palmityl coenzyme A
    • Bremer J, Norum KR. The mechanism of substrate inhibition of palmityl coenzyme A: carnitine palmityltransferase by palmityl coenzyme A. J Biol Chem 1967;242(8):1744-8
    • (1967) J Biol Chem , vol.242 , Issue.8 , pp. 1744-1748
    • Bremer, J.1    Norum, K.R.2
  • 61
    • 0023220660 scopus 로고
    • Purification and properties of the soluble carnitine palmitoyltransferase from bovine liver mitochondria
    • Ramsay RR, Derrick JP, Friend AS, Tubbs PK. Purification and properties of the soluble carnitine palmitoyltransferase from bovine liver mitochondria. Biochem J 1987;244:271-8
    • (1987) Biochem J , vol.244 , pp. 271-278
    • Ramsay, R.R.1    Derrick, J.P.2    Friend, A.S.3    Tubbs, P.K.4
  • 62
    • 0018800786 scopus 로고
    • General acyl-CoA dehydrogenase from pig liver kinetic and binding studies
    • McKean MC, Herman FE, Mielke DM. General acyl-CoA dehydrogenase from pig liver kinetic and binding studies. J Biol Chem 1979;254:2730-5
    • (1979) J Biol Chem , vol.254 , pp. 2730-2735
    • McKean, M.C.1    Herman, F.E.2    Mielke, D.M.3
  • 63
    • 0023664837 scopus 로고
    • Kinetics of coupled enzyme reactions
    • Yang SY, Schulz H. Kinetics of coupled enzyme reactions. Biochemistry 1987;26(17):5579-84
    • (1987) Biochemistry , vol.26 , Issue.17 , pp. 5579-5584
    • Yang, S.Y.1    Schulz, H.2
  • 64
    • 0019605416 scopus 로고
    • Properties of peroxisomal 3-ketoacyl-CoA thiolase from rat liver
    • Miyazawa S, Furuta S, Osumi T, et al. Properties of peroxisomal 3-ketoacyl-CoA thiolase from rat liver. J Biochem 1981;90:511-9
    • (1981) J Biochem , vol.90 , pp. 511-519
    • Miyazawa, S.1    Furuta, S.2    Osumi, T.3
  • 65
    • 0014578265 scopus 로고
    • The kinetic properties of citrate synthase from rat liver mitochondria
    • Shepherd D, Garland PB. The kinetic properties of citrate synthase from rat liver mitochondria. Biochem J 1969;114:597-610
    • (1969) Biochem J , vol.114 , pp. 597-610
    • Shepherd, D.1    Garland, P.B.2
  • 66
    • 0015987790 scopus 로고
    • The kinetic mechanism and properties of the cytoplasmic acetoacetyl-coenzyme A thiolase from rat liver
    • Middleton B. The kinetic mechanism and properties of the cytoplasmic acetoacetyl-coenzyme A thiolase from rat liver. Biochem J 1974;139:109-21
    • (1974) Biochem J , vol.139 , pp. 109-121
    • Middleton, B.1
  • 67
    • 0021876885 scopus 로고
    • 3-Hydroxy-3-methylglutaryl-coenzyme A synthase from ox liver purification, molecular and catalytic properties
    • Lowe DM, Tubbs PK. 3-Hydroxy-3-methylglutaryl-coenzyme A synthase from ox liver purification, molecular and catalytic properties Biochem J 1985;227:591-9
    • (1985) Biochem J , vol.227 , pp. 591-599
    • Lowe, D.M.1    Tubbs, P.K.2
  • 68
    • 0014430171 scopus 로고
    • Stereospecificity and other properties, of highly purified beta-hydroxy-P-methylglutaryl coenzyme A cleavage enzyme from bovine liver
    • Stegink LD, Coon MJ. Stereospecificity and other properties, of highly purified beta-hydroxy-P-methylglutaryl coenzyme A cleavage enzyme from bovine liver. J Biol Chem 1968;243:5272-9
    • (1968) J Biol Chem , vol.243 , pp. 5272-5279
    • Stegink, L.D.1    Coon, M.J.2
  • 69
    • 0018396515 scopus 로고
    • The kinetics of rat liver and heart mitochondrial P-hydroxybutyrate dehydrogenase
    • Tucker GA, Dawson AP. The kinetics of rat liver and heart mitochondrial P-hydroxybutyrate dehydrogenase. Biochem J 1979;179:579-581
    • (1979) Biochem J , vol.179 , pp. 579-581
    • Tucker, G.A.1    Dawson, A.P.2
  • 70
    • 0020160249 scopus 로고
    • Model of the kinetics of ketone bodies in humans
    • Cobelli C, Nosadini R, Toffolo G, et al Model of the kinetics of ketone bodies in humans Am J Physiol 1982;243(1):R7-17
    • (1982) Am J Physiol , vol.243 , Issue.1
    • Cobelli, C.1    Nosadini, R.2    Toffolo, G.3
  • 71
    • 0015141467 scopus 로고
    • Kinetics of ketone body metabolism in fasted and diabetic rats
    • Bates MW. Kinetics of ketone body metabolism in fasted and diabetic rats. Am J Physiol 1971;221(4):984-91
    • (1971) Am J Physiol , vol.221 , Issue.4 , pp. 984-991
    • Bates, M.W.1
  • 72
    • 0015015088 scopus 로고
    • Kinetic Studies on the reaction mechanism and the citrate activation of liver acetyl coenzyme A carboxylase
    • Hashimoto T, Numa S. Kinetic Studies on the reaction mechanism and the citrate activation of liver acetyl coenzyme A carboxylase. Eur J Biochem 1971;18:319-31
    • (1971) Eur J Biochem , vol.18 , pp. 319-331
    • Hashimoto, T.1    Numa, S.2
  • 73
    • 57049118897 scopus 로고    scopus 로고
    • Assay of the activity of malonyl-CoA decarboxylase by gas chromatography-mass spectrometry
    • Wang X, Stanley WC, Brunengraber H, Kasumov T. Assay of the activity of malonyl-CoA decarboxylase by gas chromatography-mass spectrometry. Anal Biochem 2001;298(1):69-75
    • (2001) Anal Biochem , vol.298 , Issue.1 , pp. 69-75
    • Wang, X.1    Stanley, W.C.2    Brunengraber, H.3    Kasumov, T.4
  • 74
    • 0020560104 scopus 로고
    • Steady-state kinetic study of fatty acid synthase from chicken liver(enzyme kinetics/multienzyme complex/enzymc mechanism)
    • Cox BG, Hammes GG. Steady-state kinetic study of fatty acid synthase from chicken liver(enzyme kinetics/multienzyme complex/enzymc mechanism). Proc Natl Acad Sci USA 1983;80:4233-7
    • (1983) Proc Natl Acad Sci USA , vol.80 , pp. 4233-4237
    • Cox, B.G.1    Hammes, G.G.2
  • 75
    • 0028104966 scopus 로고
    • Purification and characterizatioonf glycerophosphate acyltransferase from rat liver mitochondria
    • Vancura A, Haldar D. Purification and characterizatioonf glycerophosphate acyltransferase from rat liver mitochondria. J Biol Chem 1994;269:27209-15
    • (1994) J Biol Chem , vol.269 , pp. 27209-27215
    • Vancura, A.1    Haldar, D.2
  • 76
    • 0028039202 scopus 로고
    • Fatty acids as determinants of triglyceride and cholesteryl ester synthesis by isolated hepatocytes:kinetics as a function of various fatty acids
    • Kvilekval K, Lin J, Cheng W, Abumrad N. Fatty acids as determinants of triglyceride and cholesteryl ester synthesis by isolated hepatocytes:kinetics as a function of various fatty acids. J Lipid Res 1994;35:1786-94
    • (1994) J Lipid Res , vol.35 , pp. 1786-1794
    • Kvilekval, K.1    Lin, J.2    Cheng, W.3    Abumrad, N.4
  • 77
    • 0015844399 scopus 로고
    • Acyl-donor specificities of partially purified 1-acylglycerophosphate acyltransferase, 2-acylglycerophosphate acyltransferase and 1-acylglycerophosphorylcholine acyltransferase from rat-liver microsomes
    • Yamashita S, Hosaka K, Numa S. Acyl-donor specificities of partially purified 1-acylglycerophosphate acyltransferase, 2-acylglycerophosphate acyltransferase and 1-acylglycerophosphorylcholine acyltransferase from rat-liver microsomes. Eur J Biochem 1973;38(1):25-31
    • (1973) Eur J Biochem , vol.38 , Issue.1 , pp. 25-31
    • Yamashita, S.1    Hosaka, K.2    Numa, S.3
  • 78
    • 0024978898 scopus 로고
    • Activation of rat liver cytosolic phosphatidic acid phosphatase by nucleoside diphosphates
    • Berglund L, Björkhem I, Angelin B, Einarsson K. Activation of rat liver cytosolic phosphatidic acid phosphatase by nucleoside diphosphates. Biochim et Biophys Acta 1989;1002(3):382-7
    • (1989) Biochim et Biophys Acta , vol.1002 , Issue.3 , pp. 382-387
    • Berglund, L.1    Björkhem, I.2    Angelin, B.3    Einarsson, K.4
  • 79
    • 0022387519 scopus 로고
    • Studies on enzyme-substrate interactions of cholinephosphotransferase from rat liver
    • Pontoni G, Manna C, Salluzzo A, et al. Studies on enzyme-substrate interactions of cholinephosphotransferase from rat liver. Biochim et Biophys Acta 1985;836(2):222-32
    • (1985) Biochim et Biophys Acta , vol.836 , Issue.2 , pp. 222-232
    • Pontoni, G.1    Manna, C.2    Salluzzo, A.3
  • 80
    • 0028323262 scopus 로고
    • Purification of diacylglycerol acyl transferase from rat liver to near homogeneity
    • Anderson M, Wettesten M, Borén J, et al. Purification of diacylglycerol acyl transferase from rat liver to near homogeneity. J Lipid Res 1994;35(3):535-45
    • (1994) J Lipid Res , vol.35 , Issue.3 , pp. 535-545
    • Anderson, M.1    Wettesten, M.2    Borén, J.3
  • 81
    • 0033178534 scopus 로고    scopus 로고
    • Insulin stimulates triacylglycerol secretion by perfused livers from fed rats but inhibits it in livers from fasted or insulin-deficient rats. Implications for the relationship between hyperinsulinaemia and hypertriglyceridaemia
    • Zammit VA, Lankester DJ, Brown AM, Park BS. Insulin stimulates triacylglycerol secretion by perfused livers from fed rats but inhibits it in livers from fasted or insulin-deficient rats. Implications for the relationship between hyperinsulinaemia and hypertriglyceridaemia. Eur J Biochem 1999;263:859-64
    • (1999) Eur J Biochem , vol.263 , pp. 859-864
    • Zammit, V.A.1    Lankester, D.J.2    Brown, A.M.3    Park, B.S.4
  • 82
    • 0023833533 scopus 로고
    • The active synthesis of phosphatidylcholine is required for very low density lipoprotein secretion from rat hepatocytes
    • Yao Z, Vance DE. The active synthesis of phosphatidylcholine is required for very low density lipoprotein secretion from rat hepatocytes. J Biol Chem 1988;263(6):2998-3004
    • (1988) J Biol Chem , vol.263 , Issue.6 , pp. 2998-3004
    • Yao, Z.1    Vance, D.E.2
  • 83
    • 0027512952 scopus 로고
    • Taurine conjugate of 3 alpha, 6 beta, 7 beta trihydroxy-5 beta, 22-cholen-24-oic acid (tauro delta 22-beta-muricholate): The major bile acid in the serum of female rats treated with alpha-naphthylisothiocyanate and its secretion by liver slices
    • Thompson MB, Davis DG, Morris RW. Taurine conjugate of 3 alpha, 6 beta, 7 beta trihydroxy-5 beta, 22-cholen-24-oic acid (tauro delta 22-beta-muricholate): the major bile acid in the serum of female rats treated with alpha-naphthylisothiocyanate and its secretion by liver slices. J Lipid Res 1993;34:553-61
    • (1993) J Lipid Res , vol.34 , pp. 553-561
    • Thompson, M.B.1    Davis, D.G.2    Morris, R.W.3
  • 84
    • 0142151027 scopus 로고    scopus 로고
    • Substrate specificities of rat oatp1 and ntcp: Implications for hepatic organic anion uptake
    • Hata S, Wang P, Eftychiou N, et al. Substrate specificities of rat oatp1 and ntcp: implications for hepatic organic anion uptake. Am J Physiol Gastrointest Liver Physiol 2003;285(5):G829-39
    • (2003) Am J Physiol Gastrointest Liver Physiol , vol.285 , Issue.5
    • Hata, S.1    Wang, P.2    Eftychiou, N.3
  • 85
    • 0021961581 scopus 로고
    • Blood volume in the rat
    • Lee HB, Blaufox MD. Blood volume in the rat. J Nucl Med 1985;25:72-6
    • (1985) J Nucl Med , vol.25 , pp. 72-76
    • Lee, H.B.1    Blaufox, M.D.2
  • 86
    • 0034723163 scopus 로고    scopus 로고
    • ATP-dependent transport of bile salts by rat multidrug resistance-associated protein 3 (Mrp3)
    • Hirohashi T, Suzuki H, Takikawa H, Sugiyama Y. ATP-dependent transport of bile salts by rat multidrug resistance-associated protein 3 (Mrp3). J Biol Chem 2000;275(4):2905-10
    • (2000) J Biol Chem , vol.275 , Issue.4 , pp. 2905-2910
    • Hirohashi, T.1    Suzuki, H.2    Takikawa, H.3    Sugiyama, Y.4
  • 87
    • 0015415160 scopus 로고
    • Hepatic synthesis of bile acids. Biochemical steps and mechanisms of rate control
    • Mosbach EH. Hepatic synthesis of bile acids. Biochemical steps and mechanisms of rate control. Arch Intern Med 1972;130(4):478-87
    • (1972) Arch Intern Med , vol.130 , Issue.4 , pp. 478-487
    • Mosbach, E.H.1
  • 88
    • 0017839644 scopus 로고
    • Distribution of bile acids in rats
    • Uchida K, Okuno I, Takase H, et al. Distribution of bile acids in rats. Lipids 1978;13(1):42-8
    • (1978) Lipids , vol.13 , Issue.1 , pp. 42-48
    • Uchida, K.1    Okuno, I.2    Takase, H.3
  • 89
    • 20944450029 scopus 로고    scopus 로고
    • Protective effects of 6-ethyl chenodeoxycholic acid, a farnesoid X receptor, ligand, in estrogen-induced cholestasis
    • Fiorucci S, Clerici C, Antonelli E, et al. Protective effects of 6-ethyl chenodeoxycholic acid, a farnesoid X receptor, ligand, in estrogen-induced cholestasis. J Pharmacol Exp Ther 2005;313(2):604-12
    • (2005) J Pharmacol Exp Ther , vol.313 , Issue.2 , pp. 604-612
    • Fiorucci, S.1    Clerici, C.2    Antonelli, E.3
  • 90
    • 33646785035 scopus 로고    scopus 로고
    • Galactosamine prevents ethinylestradiol-induced cholestasis
    • Crocenzi FA, Pellegrino JM, Catania VA, et al. Galactosamine prevents ethinylestradiol-induced cholestasis. Drug Metab Dispos 2006;34(6):993-7
    • (2006) Drug Metab Dispos , vol.34 , Issue.6 , pp. 993-997
    • Crocenzi, F.A.1    Pellegrino, J.M.2    Catania, V.A.3
  • 91
    • 0018140509 scopus 로고
    • Age-related changes in cholesterol and bile acid metabolism in rats
    • Uchida K, Nomura Y, Kadowaki M, et al. Age-related changes in cholesterol and bile acid metabolism in rats. J Lipid Res 1978;19:544-52
    • (1978) J Lipid Res , vol.19 , pp. 544-552
    • Uchida, K.1    Nomura, Y.2    Kadowaki, M.3
  • 92
    • 0023280162 scopus 로고
    • Biochemistry of bile secretion
    • Colman R. Biochemistry of bile secretion. Biochem J 1987;244:249-61
    • (1987) Biochem J , vol.244 , pp. 249-261
    • Colman, R.1
  • 93
    • 0023900477 scopus 로고
    • Separate transport systems for biliary secretion of sulfated and unsulfated bile acids in the rat
    • Kuipers F, Enserink M, Havinga R, et al. Separate transport systems for biliary secretion of sulfated and unsulfated bile acids in the rat. J Clin Invest 1988;81(5):1593-9
    • (1988) J Clin Invest , vol.81 , Issue.5 , pp. 1593-1599
    • Kuipers, F.1    Enserink, M.2    Havinga, R.3
  • 94
    • 0017713544 scopus 로고
    • The role of tubular reabsorption in the renal excretion of bile acids
    • Barnes S, Gollan JL, Billing BH. The role of tubular reabsorption in the renal excretion of bile acids. Biochem J 1977;166(1):65-73
    • (1977) Biochem J , vol.166 , Issue.1 , pp. 65-73
    • Barnes, S.1    Gollan, J.L.2    Billing, B.H.3
  • 95
    • 0345258429 scopus 로고    scopus 로고
    • Regulation of renal tubular bile acid transport in the early phase of an obstructive cholestasis in the rat
    • Schlattjan JH, Winter C, Greven J. Regulation of renal tubular bile acid transport in the early phase of an obstructive cholestasis in the rat. Nephron Physiol 2003;95(3):49-56
    • (2003) Nephron Physiol , vol.95 , Issue.3 , pp. 49-56
    • Schlattjan, J.H.1    Winter, C.2    Greven, J.3
  • 96
    • 0022069481 scopus 로고
    • Measurement of glomerular filtration rate in conscious unrestrained rats with inulin infused by implanted osmotic pumps
    • Jobin J, Bonjour JP. Measurement of glomerular filtration rate in conscious unrestrained rats with inulin infused by implanted osmotic pumps. Am J Physiol Renal Physiol 1985;248:F734-8
    • (1985) Am J Physiol Renal Physiol , vol.248
    • Jobin, J.1    Bonjour, J.P.2
  • 97
    • 0027104517 scopus 로고
    • The control of actin nucleotide exchange by thymosin beta 4 and profilin. A potential regulatory mechanism for actin polymerization in cells
    • Goldschmidt-Clermont PJ, Furman MI, Safer D, et al. The control of actin nucleotide exchange by thymosin beta 4 and profilin. A potential regulatory mechanism for actin polymerization in cells. Mol Bio Cell 1992;3:1015-24
    • (1992) Mol Bio Cell , vol.3 , pp. 1015-1024
    • Goldschmidt-Clermont, P.J.1    Furman, M.I.2    Safer, D.3
  • 98
    • 0022881322 scopus 로고
    • Rate constants for the reactions of ATP and ADP actin with the ends of actin filaments
    • Pollard TD. Rate constants for the reactions of ATP and ADP actin with the ends of actin filaments. J Cell Biol 1986;103:2747-54
    • (1986) J Cell Biol , vol.103 , pp. 2747-2754
    • Pollard, T.D.1
  • 99
    • 4444297060 scopus 로고    scopus 로고
    • A signal transduction pathway model prototype I: From agonist to cellular endpoint
    • Lukas TJ. A signal transduction pathway model prototype I: from agonist to cellular endpoint. Biophys J 2004;87:1406-16
    • (2004) Biophys J , vol.87 , pp. 1406-1416
    • Lukas, T.J.1
  • 100
    • 23644453449 scopus 로고    scopus 로고
    • Theoretical model of the interactions between Ca2+, calmodulin and myosin light chain kinase
    • Fajmut A, Brumen M, Schuster S. Theoretical model of the interactions between Ca2+, calmodulin and myosin light chain kinase. FEBS Lett 2005;579(20):4361-6
    • (2005) FEBS Lett , vol.579 , Issue.20 , pp. 4361-4366
    • Fajmut, A.1    Brumen, M.2    Schuster, S.3
  • 101
    • 4444277780 scopus 로고    scopus 로고
    • A signal transduction pathway model prototype II: Application to Ca2+-calmodulin signaling and myosin light chain phosphorylation
    • Lukas, TJ. A signal transduction pathway model prototype II: application to Ca2+-calmodulin signaling and myosin light chain phosphorylation. Biophys J 2004;87:1417-25
    • (2004) Biophys J , vol.87 , pp. 1417-1425
    • Lukas, T.J.1
  • 103
    • 0036708440 scopus 로고    scopus 로고
    • Simulations of inositol phosphate metabolism and Its Interaction with InsP3-mediated calcium release
    • Mishra J, Bhalla US. Simulations of inositol phosphate metabolism and Its Interaction with InsP3-mediated calcium release. Biophys J 2002;83(3):1298-316
    • (2002) Biophys J , vol.83 , Issue.3 , pp. 1298-1316
    • Mishra, J.1    Bhalla, U.S.2
  • 104
    • 0015522788 scopus 로고
    • Metabolism of free fatty acids in isolated liver cells
    • Ontko JA. Metabolism of free fatty acids in isolated liver cells. J Biol Chem 1972;247:1788-800
    • (1972) J Biol Chem , vol.247 , pp. 1788-1800
    • Ontko, J.A.1
  • 105
    • 0014082605 scopus 로고
    • The redox state of free nicotinamide adenine dinucleotide in the cytoplasm and mitochondria of rat liver
    • Williamson DH, Lund P, Krebs HA. The redox state of free nicotinamide adenine dinucleotide in the cytoplasm and mitochondria of rat liver. Biochem J 1967;103:514-27
    • (1967) Biochem J , vol.103 , pp. 514-527
    • Williamson, D.H.1    Lund, P.2    Krebs, H.A.3
  • 106
    • 0015524030 scopus 로고
    • The concentration of malonyl coenzyme A and the control of fatty acid synthesis in vivo
    • Guynn RW, Veloso D, Veech RL. The concentration of malonyl coenzyme A and the control of fatty acid synthesis in vivo. J Biol Chem 1972;247:7325-31
    • (1972) J Biol Chem , vol.247 , pp. 7325-7331
    • Guynn, R.W.1    Veloso, D.2    Veech, R.L.3
  • 107
    • 0014124478 scopus 로고
    • Internal standards in the estimation of acetyl CoA in liver extracts
    • Herrera E, Freinkel N. Internal standards in the estimation of acetyl CoA in liver extracts. J Lipid Res 1967;8:515-8
    • (1967) J Lipid Res , vol.8 , pp. 515-518
    • Herrera, E.1    Freinkel, N.2
  • 108
    • 0018320433 scopus 로고
    • Hepatic mitochondrial and cytosolic glutathione content and the subcellular distribution of GSH-S-transferases
    • Wahllander A, Soboll S, Sies H, et al. Hepatic mitochondrial and cytosolic glutathione content and the subcellular distribution of GSH-S-transferases. FEBS Lett 1979;97:138-40
    • (1979) FEBS Lett , vol.97 , pp. 138-140
    • Wahllander, A.1    Soboll, S.2    Sies, H.3
  • 109
    • 0018776894 scopus 로고
    • Hydroperoxide metabolism in mammalian organs
    • Chance B, Sies H, Boveris A. Hydroperoxide metabolism in mammalian organs. Physiol Rev 1979;59:527-605
    • (1979) Physiol Rev , vol.59 , pp. 527-605
    • Chance, B.1    Sies, H.2    Boveris, A.3
  • 110
    • 0017854835 scopus 로고
    • Intramitochondrial and extramitochondrial concentrations of adenine nucleotides and inorganic phosphate in isolated hepatocytes from fasted rats
    • Akerboom TP, Bookelman H, Zuurendonk PF, et al. Intramitochondrial and extramitochondrial concentrations of adenine nucleotides and inorganic phosphate in isolated hepatocytes from fasted rats. Eur J Biochem 1978;84:413-20
    • (1978) Eur J Biochem , vol.84 , pp. 413-420
    • Akerboom, T.P.1    Bookelman, H.2    Zuurendonk, P.F.3
  • 111
    • 0020444895 scopus 로고
    • Mechanism of action, metabolism and toxicity of buthionine sulfoximine and its higher homologs, potent inhibitors of glutathione synthesis
    • Griffith, OW. Mechanism of action, metabolism and toxicity of buthionine sulfoximine and its higher homologs, potent inhibitors of glutathione synthesis. J Biol Chem 1982;257(22):13704-12
    • (1982) J Biol Chem , vol.257 , Issue.22 , pp. 13704-13712
    • Griffith, O.W.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.