메뉴 건너뛰기




Volumn 37, Issue 2, 2005, Pages 311-325

Oxidative stress mediated idiosyncratic drug toxicity

Author keywords

ADMET; Cooxidation; Idiosyncratic drug toxicity; Oxidative stress; Prooxidant

Indexed keywords

CYTOCHROME P450; DICLOFENAC; ENTACAPONE; HYDROGEN PEROXIDE; MEFENAMIC ACID; MYELOPEROXIDASE; PEROXIDASE; PHENYLBUTAZONE; PROSTAGLANDIN SYNTHASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE; TOLCAPONE; TROGLITAZONE; XENOBIOTIC AGENT;

EID: 18744364709     PISSN: 03602532     EISSN: None     Source Type: Journal    
DOI: 10.1081/DMR-200055227     Document Type: Conference Paper
Times cited : (82)

References (55)
  • 1
    • 0030854261 scopus 로고    scopus 로고
    • Human neutrophils employ the myeloperoxidase-hydrogen peroxide-chloride system to convert hydroxy-amino acids into glycolaldehyde, 2-hydroxypropanal, and acrolein. A mechanism for the generation of highly reactive α-hydroxy and α,β-unsaturated aldehydes by phagocytes at sites of inflammation
    • Anderson, M. M., Hazen, S. L., Hsu, F. F., Heinecke, J. W. (1997). Human neutrophils employ the myeloperoxidase-hydrogen peroxide-chloride system to convert hydroxy-amino acids into glycolaldehyde, 2-hydroxypropanal, and acrolein. A mechanism for the generation of highly reactive α-hydroxy and α,β-unsaturated aldehydes by phagocytes at sites of inflammation. J. Clin. Invest. 99:424-432.
    • (1997) J. Clin. Invest. , vol.99 , pp. 424-432
    • Anderson, M.M.1    Hazen, S.L.2    Hsu, F.F.3    Heinecke, J.W.4
  • 3
    • 0019720847 scopus 로고
    • Phenylbutazone liver injury: A clinical-pathologic survey of 23 cases and review of the literature
    • Benjamin, S. B., Ishak, K. G., Zimmerman, H. J., Grushka, A. (1981). Phenylbutazone liver injury: a clinical-pathologic survey of 23 cases and review of the literature. Hepatology 1:255-263.
    • (1981) Hepatology , vol.1 , pp. 255-263
    • Benjamin, S.B.1    Ishak, K.G.2    Zimmerman, H.J.3    Grushka, A.4
  • 5
    • 0035190154 scopus 로고    scopus 로고
    • Immunohistochemical detection of myeloperoxidase and its oxidation products in Kupffer cells of human liver
    • Brown, K. E., Brunt, E. M., Heinecke, J. W. (2001). Immunohistochemical detection of myeloperoxidase and its oxidation products in Kupffer cells of human liver. Am. J. Pathol. 159:2081-2088.
    • (2001) Am. J. Pathol. , vol.159 , pp. 2081-2088
    • Brown, K.E.1    Brunt, E.M.2    Heinecke, J.W.3
  • 6
    • 0030709470 scopus 로고    scopus 로고
    • Anti-thyroid isoflavones from soybean: Isolation, characterization, and mechanisms of action
    • Divi, R. L., Chang, H. C., Doerge, D. R. (1997). Anti-thyroid isoflavones from soybean: isolation, characterization, and mechanisms of action. Biochem. Pharmacol. 54:1087-1096.
    • (1997) Biochem. Pharmacol. , vol.54 , pp. 1087-1096
    • Divi, R.L.1    Chang, H.C.2    Doerge, D.R.3
  • 7
    • 10644226959 scopus 로고    scopus 로고
    • Peroxidase catalysed formation of cytotoxic prooxidant phenothiazine free radicals at physiological pH
    • Eghbal, M. A., Tafazoli, S., Pennefather, P., O'Brien, P. J. (2004). Peroxidase catalysed formation of cytotoxic prooxidant phenothiazine free radicals at physiological pH. Chem. Biol. Interact. 151:43-51.
    • (2004) Chem. Biol. Interact. , vol.151 , pp. 43-51
    • Eghbal, M.A.1    Tafazoli, S.2    Pennefather, P.3    O'Brien, P.J.4
  • 8
    • 1642281756 scopus 로고    scopus 로고
    • Drug-protein adducts: An industry perspective on minimizing the potential for drug bioactivation in drug discovery and development
    • Evans, D. C., Watt, A. P., Nicoll-Griffith, D. A., Baillie, T. A. (2004). Drug-protein adducts: an industry perspective on minimizing the potential for drug bioactivation in drug discovery and development. Chem. Res. Toxicol. 17:3-16.
    • (2004) Chem. Res. Toxicol. , vol.17 , pp. 3-16
    • Evans, D.C.1    Watt, A.P.2    Nicoll-Griffith, D.A.3    Baillie, T.A.4
  • 11
    • 0345130017 scopus 로고    scopus 로고
    • Development of eosinophil peroxidase activity and concomitant alteration of the antioxidant defenses in the liver of mice infected with Schistosoma mansoni
    • Gharib, B., Abdallahi, O. M., Dessein, H., De Reggi, M. (1999). Development of eosinophil peroxidase activity and concomitant alteration of the antioxidant defenses in the liver of mice infected with Schistosoma mansoni. J. Hepatol. 30:594-602.
    • (1999) J. Hepatol. , vol.30 , pp. 594-602
    • Gharib, B.1    Abdallahi, O.M.2    Dessein, H.3    De Reggi, M.4
  • 12
    • 0346731053 scopus 로고    scopus 로고
    • Tyrosine oxidation products: Analysis and biological relevance
    • Giulivi, C., Traaseth, N. J., Davies, K. J. (2003). Tyrosine oxidation products: analysis and biological relevance. Amino Acids 25:227-232.
    • (2003) Amino Acids , vol.25 , pp. 227-232
    • Giulivi, C.1    Traaseth, N.J.2    Davies, K.J.3
  • 13
    • 0031029667 scopus 로고    scopus 로고
    • Roles of efficient substrates in enhancement of peroxidase-catalyzed oxidations
    • Goodwin, D. C., Grover, T. A., Aust, S. D. (1997). Roles of efficient substrates in enhancement of peroxidase-catalyzed oxidations. Biochemistry 36:139-147.
    • (1997) Biochemistry , vol.36 , pp. 139-147
    • Goodwin, D.C.1    Grover, T.A.2    Aust, S.D.3
  • 15
    • 84971586860 scopus 로고
    • Non-steroidal anti-inflammatory drugs in elderly people. Mefenamic acid is more dangerous than most
    • Grant, D. J., MacConnachie, A. M. (1995). Non-steroidal anti-inflammatory drugs in elderly people. Mefenamic acid is more dangerous than most. BMJ 311:392.
    • (1995) BMJ , vol.311 , pp. 392
    • Grant, D.J.1    MacConnachie, A.M.2
  • 16
    • 0037131004 scopus 로고    scopus 로고
    • Effects of entacapone and tolcapone on mitochondrial membrane potential
    • Haasio, K., Koponen, A., Penttila, K. E., Nissinen, E. (2002). Effects of entacapone and tolcapone on mitochondrial membrane potential. Eur. J. Pharmacol. 453:21-26.
    • (2002) Eur. J. Pharmacol. , vol.453 , pp. 21-26
    • Haasio, K.1    Koponen, A.2    Penttila, K.E.3    Nissinen, E.4
  • 17
    • 0036591854 scopus 로고    scopus 로고
    • Oxidized amino acids: Culprits in human atherosclerosis and indicators of oxidative stress
    • Heinecke, J. W. (2002a). Oxidized amino acids: culprits in human atherosclerosis and indicators of oxidative stress. Free Radic. Biol. Med. 32:1090-1101.
    • (2002) Free Radic. Biol. Med. , vol.32 , pp. 1090-1101
    • Heinecke, J.W.1
  • 18
    • 0036679823 scopus 로고    scopus 로고
    • Tyrosyl radical production by myeloperoxidase: A phagocyte pathway for lipid peroxidation and dityrosine cross-linking of proteins
    • Heinecke, J. W. (2002b). Tyrosyl radical production by myeloperoxidase: a phagocyte pathway for lipid peroxidation and dityrosine cross-linking of proteins. Toxicology 177:11-22.
    • (2002) Toxicology , vol.177 , pp. 11-22
    • Heinecke, J.W.1
  • 19
    • 0032457990 scopus 로고    scopus 로고
    • The 1996 Veylien Henderson Award of the Society of Toxicology of Canada. Current concepts: Neutrophils and the activation of carcinogens in the breast and other organs
    • Josephy, P. D., Coomber, B. L. (1998). The 1996 Veylien Henderson Award of the Society of Toxicology of Canada. Current concepts: neutrophils and the activation of carcinogens in the breast and other organs. Can. J. Physiol. Pharm. 76:693-700.
    • (1998) Can. J. Physiol. Pharm. , vol.76 , pp. 693-700
    • Josephy, P.D.1    Coomber, B.L.2
  • 20
    • 0035996570 scopus 로고    scopus 로고
    • Mechanism of idiosyncratic drug reactions: Reactive metabolite formation, protein binding and the regulation of the immune system
    • Ju, C., Uetrecht, J. P. (2002). Mechanism of idiosyncratic drug reactions: reactive metabolite formation, protein binding and the regulation of the immune system. Curr. Drug Metab. 3:367-377.
    • (2002) Curr. Drug Metab. , vol.3 , pp. 367-377
    • Ju, C.1    Uetrecht, J.P.2
  • 22
    • 0028926287 scopus 로고
    • Long-term exposure to the anti-inflammatory agent phenylbutazone induces kidney tumors in rats and liver tumors in mice
    • Kari, F., Bucher, J., Haseman, J., Eustis, S., Huff, J. (1995). Long-term exposure to the anti-inflammatory agent phenylbutazone induces kidney tumors in rats and liver tumors in mice. Jpn. J. Cancer Res. 86:252-263.
    • (1995) Jpn. J. Cancer Res. , vol.86 , pp. 252-263
    • Kari, F.1    Bucher, J.2    Haseman, J.3    Eustis, S.4    Huff, J.5
  • 23
    • 0023266733 scopus 로고
    • Interactions of the antitumor drug, etoposide, with reduced thiols in vitro and in vivo
    • Katki, A. G., Kalyanaraman, B., Sinha, B. K. (1987). Interactions of the antitumor drug, etoposide, with reduced thiols in vitro and in vivo. Chem.-Biol. Interact. 62:231-241.
    • (1987) Chem.-Biol. Interact. , vol.62 , pp. 231-241
    • Katki, A.G.1    Kalyanaraman, B.2    Sinha, B.K.3
  • 24
    • 0033869941 scopus 로고    scopus 로고
    • Regulation of liver inflammatory injury by signal transducer and activator of transcription-6
    • Kato, A., Yoshidome, H., Edwards, M. J., Lentsch, A. B. (2000). Regulation of liver inflammatory injury by signal transducer and activator of transcription-6. Am. J. Pathol. 157:297-302.
    • (2000) Am. J. Pathol. , vol.157 , pp. 297-302
    • Kato, A.1    Yoshidome, H.2    Edwards, M.J.3    Lentsch, A.B.4
  • 25
    • 0033786733 scopus 로고    scopus 로고
    • The specificity of glucuronidation of entacapone and tolcapone by recombinant human UDP-glucuronosyltransferases
    • Lautala, P., Ethell, B. T., Taskinen, J., Burchell, B. (2000). The specificity of glucuronidation of entacapone and tolcapone by recombinant human UDP-glucuronosyltransferases. Drug Metab. Dispos. 28:1385-1389.
    • (2000) Drug Metab. Dispos. , vol.28 , pp. 1385-1389
    • Lautala, P.1    Ethell, B.T.2    Taskinen, J.3    Burchell, B.4
  • 26
    • 0037381306 scopus 로고    scopus 로고
    • In vivo mechanistic studies on the metabolic activation of 2-phenylpropionic acid in rat
    • Li, C., Grillo, M. P., Benet, L. Z. (2003). In vivo mechanistic studies on the metabolic activation of 2-phenylpropionic acid in rat. J. Pharmacol. Exp. Ther. 305:250-256.
    • (2003) J. Pharmacol. Exp. Ther. , vol.305 , pp. 250-256
    • Li, C.1    Grillo, M.P.2    Benet, L.Z.3
  • 27
    • 0021709796 scopus 로고
    • The involvement of endotoxin in halothane-associated liver injury
    • Lind, R. C., Gandolfi, A. J., Sipes, I. G., Brown, B. R. Jr. (1984). The involvement of endotoxin in halothane-associated liver injury. Anesthesiology 61:544-550.
    • (1984) Anesthesiology , vol.61 , pp. 544-550
    • Lind, R.C.1    Gandolfi, A.J.2    Sipes, I.G.3    Brown Jr., B.R.4
  • 29
    • 0035072890 scopus 로고    scopus 로고
    • Phenylbutazone radicals inactivate creatine kinase
    • Miura, T., Muraoka, S., Fujimoto, Y. (2001). Phenylbutazone radicals inactivate creatine kinase. Free Radic. Res. 34:167-175.
    • (2001) Free Radic. Res. , vol.34 , pp. 167-175
    • Miura, T.1    Muraoka, S.2    Fujimoto, Y.3
  • 30
    • 0037134244 scopus 로고    scopus 로고
    • Lipid peroxidation induced by phenylbutazone radicals
    • Miura, T., Muraoka, S., Fujimoto, Y. (2002). Lipid peroxidation induced by phenylbutazone radicals. Life Sci. 70:2611-2621.
    • (2002) Life Sci. , vol.70 , pp. 2611-2621
    • Miura, T.1    Muraoka, S.2    Fujimoto, Y.3
  • 32
    • 0037436733 scopus 로고    scopus 로고
    • Inactivation of creatine kinase during the interaction of mefenamic acid with horseradish peroxidase and hydrogen peroxide: Participation by the mefenamic acid radical
    • Muraoka, S., Miura, T. (2003). Inactivation of creatine kinase during the interaction of mefenamic acid with horseradish peroxidase and hydrogen peroxide: participation by the mefenamic acid radical. Life Sci. 72:1897-1907.
    • (2003) Life Sci. , vol.72 , pp. 1897-1907
    • Muraoka, S.1    Miura, T.2
  • 33
    • 1342284089 scopus 로고    scopus 로고
    • Inactivation of alcohol dehydrogenase by piroxicam-derived radicals
    • Muraoka, S., Miura, T. (2004). Inactivation of alcohol dehydrogenase by piroxicam-derived radicals. Free Radic. Res. 38:217-223.
    • (2004) Free Radic. Res. , vol.38 , pp. 217-223
    • Muraoka, S.1    Miura, T.2
  • 35
    • 0023878505 scopus 로고
    • Radical formation during the peroxidase catalyzed metabolism of carcinogens and xenobiotics: The reactivity of these radicals with GSH, DNA, and unsaturated lipid
    • O'Brien, P. J. (1988). Radical formation during the peroxidase catalyzed metabolism of carcinogens and xenobiotics: the reactivity of these radicals with GSH, DNA, and unsaturated lipid. Free Radic. Biol. Med. 4:169-183.
    • (1988) Free Radic. Biol. Med. , vol.4 , pp. 169-183
    • O'Brien, P.J.1
  • 37
    • 7444245666 scopus 로고    scopus 로고
    • Human and animal hepatocytes in vitro with extrapolation in vivo
    • O'Brien, P. J., Chan, K., Silber, P. M. (2004). Human and animal hepatocytes in vitro with extrapolation in vivo. Chem.-Biol. Interact. 150:97-114.
    • (2004) Chem.-Biol. Interact. , vol.150 , pp. 97-114
    • O'Brien, P.J.1    Chan, K.2    Silber, P.M.3
  • 38
    • 0036310321 scopus 로고    scopus 로고
    • Embryonic prostaglandin H synthase-2 (PHS-2) expression and benzo[a]pyrene teratogenicity in PHS-2 knockout mice
    • Parman, T., Wells, P. G. (2002). Embryonic prostaglandin H synthase-2 (PHS-2) expression and benzo[a]pyrene teratogenicity in PHS-2 knockout mice. FASEB J. 16:1001-1009.
    • (2002) FASEB J. , vol.16 , pp. 1001-1009
    • Parman, T.1    Wells, P.G.2
  • 39
    • 0032920883 scopus 로고    scopus 로고
    • Free radical-mediated oxidative DNA damage in the mechanism of thalidomide teratogenicity
    • Parman, T., Wiley, M. J., Wells, P. G. (1999). Free radical-mediated oxidative DNA damage in the mechanism of thalidomide teratogenicity. Nat. Med. 5:582-585.
    • (1999) Nat. Med. , vol.5 , pp. 582-585
    • Parman, T.1    Wiley, M.J.2    Wells, P.G.3
  • 40
    • 0021247377 scopus 로고
    • Non-steroidal anti-inflammatory agents and hepatic lipid peroxidation in normal- and carrageenin-treated rats
    • Parola, M., Paradisi, L., Torrielli, M. V. (1984). Non-steroidal anti-inflammatory agents and hepatic lipid peroxidation in normal- and carrageenin-treated rats. Res. Commun. Chem. Pathol. Pharmacol. 45:37-53.
    • (1984) Res. Commun. Chem. Pathol. Pharmacol. , vol.45 , pp. 37-53
    • Parola, M.1    Paradisi, L.2    Torrielli, M.V.3
  • 41
    • 0035908632 scopus 로고    scopus 로고
    • C-reactive protein, interleukin 6, and risk of developing type 2 diabetes mellitus
    • Pradhan, A. D., Manson, J. E., Rifai, N., Buring, J. E., Ridker, P. M. (2001). C-reactive protein, interleukin 6, and risk of developing type 2 diabetes mellitus. JAMA 286:327-334.
    • (2001) JAMA , vol.286 , pp. 327-334
    • Pradhan, A.D.1    Manson, J.E.2    Rifai, N.3    Buring, J.E.4    Ridker, P.M.5
  • 42
    • 0019131878 scopus 로고
    • High-performance liquid chromatography analysis of nanomole levels of glutathione, glutathione disulfide, and related thiols and disulfides
    • Reed, D. J., Babson, J. R., Beatty, P. W., Brodie, A. E., Ellis, W. W., Potter, D. W. (1980). High-performance liquid chromatography analysis of nanomole levels of glutathione, glutathione disulfide, and related thiols and disulfides. Anal. Biochem. 106:55-62.
    • (1980) Anal. Biochem. , vol.106 , pp. 55-62
    • Reed, D.J.1    Babson, J.R.2    Beatty, P.W.3    Brodie, A.E.4    Ellis, W.W.5    Potter, D.W.6
  • 43
    • 0015575880 scopus 로고
    • Centrolobular hepatic necrosis related to covalent binding of metabolites of halogenated aromatic hydrocarbons
    • Reid, W. D., Krishna, G. (1973). Centrolobular hepatic necrosis related to covalent binding of metabolites of halogenated aromatic hydrocarbons. Exp. Mol. Pathol. 18:80-99.
    • (1973) Exp. Mol. Pathol. , vol.18 , pp. 80-99
    • Reid, W.D.1    Krishna, G.2
  • 45
    • 0035197972 scopus 로고    scopus 로고
    • In vivo perturbation of rat hepatocyte canalicutar membrane function by diclofenac
    • Sallustio, B. C., Holbrook, F. L. (2001). In vivo perturbation of rat hepatocyte canalicutar membrane function by diclofenac. Drug Metab. Dispos. 29:1535-1538.
    • (2001) Drug Metab. Dispos. , vol.29 , pp. 1535-1538
    • Sallustio, B.C.1    Holbrook, F.L.2
  • 46
    • 0028171376 scopus 로고
    • The metabolism of 17 β-estradiol by lactoperoxidase: A possible source of oxidative stress in breast cancer
    • Sipe, H. J. Jr., Jordan, S. J., Hanna, P. M., Mason, R. P. (1994). The metabolism of 17 β-estradiol by lactoperoxidase: a possible source of oxidative stress in breast cancer. Carcinogenesis 15:2637-2643.
    • (1994) Carcinogenesis , vol.15 , pp. 2637-2643
    • Sipe Jr., H.J.1    Jordan, S.J.2    Hanna, P.M.3    Mason, R.P.4
  • 47
    • 0038650658 scopus 로고    scopus 로고
    • Mechanisms of troglitazone hepatotoxicity
    • Smith, M. T. (2003). Mechanisms of troglitazone hepatotoxicity. Chem. Res. Toxicol. 16:679-687.
    • (2003) Chem. Res. Toxicol. , vol.16 , pp. 679-687
    • Smith, M.T.1
  • 48
    • 0020058754 scopus 로고
    • The measurement of lipid peroxidation in isolated hepatocytes
    • Smith, M. T., Thor, H., Hartizell, P., Orrenius, S. (1982). The measurement of lipid peroxidation in isolated hepatocytes. Biochem. Pharmacol. 31:19-26.
    • (1982) Biochem. Pharmacol. , vol.31 , pp. 19-26
    • Smith, M.T.1    Thor, H.2    Hartizell, P.3    Orrenius, S.4
  • 49
    • 0027787910 scopus 로고
    • Tyrosinase-induced phenoxyl radicals of etoposide (VP-16): Interaction with reductants in model systems, K562 leukemic cell and nuclear homogenates
    • Stoyanovsky, D., Yalowich, J., Gantchev, T., Kagan, V. (1993). Tyrosinase-induced phenoxyl radicals of etoposide (VP-16): interaction with reductants in model systems, K562 leukemic cell and nuclear homogenates. Free Radic. Res. Commun. 19:371-386.
    • (1993) Free Radic. Res. Commun. , vol.19 , pp. 371-386
    • Stoyanovsky, D.1    Yalowich, J.2    Gantchev, T.3    Kagan, V.4
  • 50
    • 0031796531 scopus 로고    scopus 로고
    • Harnessing free radicals: Formation and function of the tyrosyl radical in ribonucleotide reductase
    • Stubbe, J., Riggs-Gelasco, P. (1998). Harnessing free radicals: formation and function of the tyrosyl radical in ribonucleotide reductase. Trends Biochem. Sci. 23:438-443.
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 438-443
    • Stubbe, J.1    Riggs-Gelasco, P.2
  • 51
    • 6344282628 scopus 로고    scopus 로고
    • Prooxidant activity and cytotoxic effects of indole-3-acetic acid derivative radicals
    • Tafazoli, S., O'Brien, P. J. (2004). Prooxidant activity and cytotoxic effects of indole-3-acetic acid derivative radicals. Chem. Res. Toxicol. 17:1350-1355.
    • (2004) Chem. Res. Toxicol. , vol.17 , pp. 1350-1355
    • Tafazoli, S.1    O'Brien, P.J.2
  • 52
    • 0036970711 scopus 로고    scopus 로고
    • Pathogenic importance of intestinal hypermotility in NSAID-induced small intestinal damage in rats
    • Takeuchi, K., Miyazawa, T., Tanaka, A., Kato, S., Kunikata, T. (2002). Pathogenic importance of intestinal hypermotility in NSAID-induced small intestinal damage in rats. Digestion 66:30-41.
    • (2002) Digestion , vol.66 , pp. 30-41
    • Takeuchi, K.1    Miyazawa, T.2    Tanaka, A.3    Kato, S.4    Kunikata, T.5
  • 53
    • 0034868665 scopus 로고    scopus 로고
    • Enzyme-induction dependent bioactivation of troglitazone and troglitazone quinone in vivo
    • Tettey, J. N., Maggs, J. L., Rapeport, W. G., Pirmohamed, M., Park, B. K. (2001). Enzyme-induction dependent bioactivation of troglitazone and troglitazone quinone in vivo. Chem. Res. Toxicol. 14:965-974.
    • (2001) Chem. Res. Toxicol. , vol.14 , pp. 965-974
    • Tettey, J.N.1    Maggs, J.L.2    Rapeport, W.G.3    Pirmohamed, M.4    Park, B.K.5
  • 54
    • 0035142384 scopus 로고    scopus 로고
    • Carcinogen substrate specificity of human COX-1 and COX-2
    • Wiese, F. W., Thompson, P. A., Kadlubar, F. F. (2001). Carcinogen substrate specificity of human COX-1 and COX-2. Carcinogenesis 22:5-10.
    • (2001) Carcinogenesis , vol.22 , pp. 5-10
    • Wiese, F.W.1    Thompson, P.A.2    Kadlubar, F.F.3
  • 55
    • 0031762781 scopus 로고    scopus 로고
    • Assessment of prooxidant activity of vitamin e in human low-density lipoprotein and plasma
    • Witting, P. K., Mohr, D., Stocker, R. (1999). Assessment of prooxidant activity of vitamin E in human low-density lipoprotein and plasma. Methods Enzymol. 299:362-375.
    • (1999) Methods Enzymol. , vol.299 , pp. 362-375
    • Witting, P.K.1    Mohr, D.2    Stocker, R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.