메뉴 건너뛰기




Volumn 46, Issue 9, 2008, Pages 2972-2983

Identification of superoxide dismutase as a potential urinary marker of carbon tetrachloride-induced hepatic toxicity

Author keywords

Carbon tetrachloride; Liver; Rat; Superoxide dismutase; Toxicity; Urine

Indexed keywords

CARBON TETRACHLORIDE; COPPER ZINC SUPEROXIDE DISMUTASE; SUPEROXIDE DISMUTASE;

EID: 50249130695     PISSN: 02786915     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.fct.2008.05.041     Document Type: Article
Times cited : (15)

References (54)
  • 1
    • 0032702434 scopus 로고    scopus 로고
    • Oxidative damage to the lipids and proteins of the lungs, testis and kidney of rats during carbon tetrachloride intoxication
    • Abraham P., Wilfred G., and Cathrine X. Oxidative damage to the lipids and proteins of the lungs, testis and kidney of rats during carbon tetrachloride intoxication. Clin. Chim. Acta 289 (1999) 177-179
    • (1999) Clin. Chim. Acta , vol.289 , pp. 177-179
    • Abraham, P.1    Wilfred, G.2    Cathrine, X.3
  • 2
    • 0036005658 scopus 로고    scopus 로고
    • Level of superoxide dismutase, glutiathione peroxidase and uric acid in thioacetamide-induced cirrhotic rats
    • Abul H., Mathew T.C., Dashti H.M., and Al-Bader A. Level of superoxide dismutase, glutiathione peroxidase and uric acid in thioacetamide-induced cirrhotic rats. Anat. Histol. Embryol. 31 (2002) 66-71
    • (2002) Anat. Histol. Embryol. , vol.31 , pp. 66-71
    • Abul, H.1    Mathew, T.C.2    Dashti, H.M.3    Al-Bader, A.4
  • 3
    • 12444342983 scopus 로고    scopus 로고
    • Urinary hydrogen peroxide: a probable marker of oxidative stress in malignancy
    • Banerjee D., Madhusoodana U.K., Nayak S., and Jacob J. Urinary hydrogen peroxide: a probable marker of oxidative stress in malignancy. Clin. Chim. Acta 334 (2003) 205-209
    • (2003) Clin. Chim. Acta , vol.334 , pp. 205-209
    • Banerjee, D.1    Madhusoodana, U.K.2    Nayak, S.3    Jacob, J.4
  • 4
    • 34548359247 scopus 로고    scopus 로고
    • Urine proteomics: the present and future of measuring urinary protein components in disease
    • Barratt J., and Topham P. Urine proteomics: the present and future of measuring urinary protein components in disease. CMAJ 177 (2007) 361-368
    • (2007) CMAJ , vol.177 , pp. 361-368
    • Barratt, J.1    Topham, P.2
  • 6
    • 0346880053 scopus 로고    scopus 로고
    • Hyaluronic acid and chondroitin-4-sulphate treatment reduces damage in carbon tetrachloride-induced acute rat liver injury
    • Campo G.M., Avenoso A., Campo S., Ferlazzo A.M., Micali C., Zanghi L., and Calatroni A. Hyaluronic acid and chondroitin-4-sulphate treatment reduces damage in carbon tetrachloride-induced acute rat liver injury. Life Sci. 74 (2004) 1289-1305
    • (2004) Life Sci. , vol.74 , pp. 1289-1305
    • Campo, G.M.1    Avenoso, A.2    Campo, S.3    Ferlazzo, A.M.4    Micali, C.5    Zanghi, L.6    Calatroni, A.7
  • 7
    • 0036747317 scopus 로고    scopus 로고
    • Application of surface-enhanced laser desorption/ionizaton technology to the detection and identification of urinary parvalbumin-α: a biomarker of compound-induced skeletal muscle toxicity in the rat
    • Dare T.O., Davies H.A., Turton J.A., Lomas L., Williams T.C., and York M.J. Application of surface-enhanced laser desorption/ionizaton technology to the detection and identification of urinary parvalbumin-α: a biomarker of compound-induced skeletal muscle toxicity in the rat. Electrophoresis 23 (2002) 3241-3251
    • (2002) Electrophoresis , vol.23 , pp. 3241-3251
    • Dare, T.O.1    Davies, H.A.2    Turton, J.A.3    Lomas, L.4    Williams, T.C.5    York, M.J.6
  • 8
    • 0034670151 scopus 로고    scopus 로고
    • Antioxidant properties of colchicines in acute carbon tetrachloride induced rat liver injury and its role in the resolution of established cirrhosis
    • Das D., Pemberton P.W., Burrows P.C., Gordon C., Smith A., McMahon R.F., and Warnes T.W. Antioxidant properties of colchicines in acute carbon tetrachloride induced rat liver injury and its role in the resolution of established cirrhosis. Biochim. Biophys. Acta 1502 (2000) 351-362
    • (2000) Biochim. Biophys. Acta , vol.1502 , pp. 351-362
    • Das, D.1    Pemberton, P.W.2    Burrows, P.C.3    Gordon, C.4    Smith, A.5    McMahon, R.F.6    Warnes, T.W.7
  • 10
    • 0024505693 scopus 로고
    • Comparative study of cytotoxicity, tumour necrosis factor, and prostaglandin release after stimulation of rat Kupffer cells, murine Kupffer cells, and murine inflammatory liver macrophages
    • Decker T., Lohmann-Matthes M.L., Karck U., Peters T., and Decker K. Comparative study of cytotoxicity, tumour necrosis factor, and prostaglandin release after stimulation of rat Kupffer cells, murine Kupffer cells, and murine inflammatory liver macrophages. J. Leukoc. Biol. 45 (1989) 139-146
    • (1989) J. Leukoc. Biol. , vol.45 , pp. 139-146
    • Decker, T.1    Lohmann-Matthes, M.L.2    Karck, U.3    Peters, T.4    Decker, K.5
  • 11
    • 0015935503 scopus 로고
    • On the stability of bovine superoxide dismutase. The effects of metals
    • Forman H.J., and Fridovich I. On the stability of bovine superoxide dismutase. The effects of metals. J. Biol. Chem. 248 (1973) 2645-2649
    • (1973) J. Biol. Chem. , vol.248 , pp. 2645-2649
    • Forman, H.J.1    Fridovich, I.2
  • 12
    • 0029859930 scopus 로고    scopus 로고
    • Localization of superoxide dismutase activity in rat tissues
    • Frederiks W.M., and Bosch K.S. Localization of superoxide dismutase activity in rat tissues. Free Radic. Biol. Med. 22 (1997) 241-248
    • (1997) Free Radic. Biol. Med. , vol.22 , pp. 241-248
    • Frederiks, W.M.1    Bosch, K.S.2
  • 13
    • 0037220482 scopus 로고    scopus 로고
    • Liver fibrosis - from bench to bedside
    • Friedman S. Liver fibrosis - from bench to bedside. J. Hepatol. 38 (2003) S38-S53
    • (2003) J. Hepatol. , vol.38
    • Friedman, S.1
  • 14
    • 0000074107 scopus 로고
    • Oxygen radical, hydrogen peroxide and oxygen toxicity
    • Pryor W. (Ed), Academic Press, New York
    • Fridovich I. Oxygen radical, hydrogen peroxide and oxygen toxicity. In: Pryor W. (Ed). Free Radicals in Biology vol. I (1982), Academic Press, New York 239-271
    • (1982) Free Radicals in Biology , vol.I , pp. 239-271
    • Fridovich, I.1
  • 16
    • 0019907606 scopus 로고
    • Rat liver Cu,Zn-superoxide dismutase. Subcellular location in lysosomes
    • Geller B.L., and Winge D.R. Rat liver Cu,Zn-superoxide dismutase. Subcellular location in lysosomes. J. Biol. Chem. 257 (1982) 8945-8952
    • (1982) J. Biol. Chem. , vol.257 , pp. 8945-8952
    • Geller, B.L.1    Winge, D.R.2
  • 20
    • 0032575136 scopus 로고    scopus 로고
    • Ultrastructural changes in liver damage induce by carbon tetrachloride in spontaneously hypertensive rats and Wistar-Kyotot rats
    • Hsu C.T. Ultrastructural changes in liver damage induce by carbon tetrachloride in spontaneously hypertensive rats and Wistar-Kyotot rats. J. Auton. Nerv. Syst. 70 (1998) 79-83
    • (1998) J. Auton. Nerv. Syst. , vol.70 , pp. 79-83
    • Hsu, C.T.1
  • 21
    • 0036079692 scopus 로고    scopus 로고
    • The SELDI-TOF MS approach to proteomics: protein profiling and biomarker identification
    • Issaq H.J., Veenstra T.D., Conrads T.P., and Felschow D. The SELDI-TOF MS approach to proteomics: protein profiling and biomarker identification. Biochem. Biophys. Res. Commun. 292 (2002) 587-592
    • (2002) Biochem. Biophys. Res. Commun. , vol.292 , pp. 587-592
    • Issaq, H.J.1    Veenstra, T.D.2    Conrads, T.P.3    Felschow, D.4
  • 22
    • 11144356519 scopus 로고    scopus 로고
    • Identification by proteomic analysis of calreticulin as a marker for bladder cancer and evaluation of the diagnostic accuracy of its detection in urine
    • Kageyama S., Isono T., Iwaki H., Wakabayashi Y., Okada Y., Kontani K., Yoshimura K., Terai A., Arai Y., and Yoshiki T. Identification by proteomic analysis of calreticulin as a marker for bladder cancer and evaluation of the diagnostic accuracy of its detection in urine. Clin. Chem. 50 (2004) 857-866
    • (2004) Clin. Chem. , vol.50 , pp. 857-866
    • Kageyama, S.1    Isono, T.2    Iwaki, H.3    Wakabayashi, Y.4    Okada, Y.5    Kontani, K.6    Yoshimura, K.7    Terai, A.8    Arai, Y.9    Yoshiki, T.10
  • 23
    • 0037186348 scopus 로고    scopus 로고
    • The effect of 2,3,7,8-tetrachlorodibenzo-p-dioxin (TCDD) on oxidative enzymes in adipocytes and liver
    • Kern P.A., Fishman R.B., Song W., Brown A.D., and Fonseca V. The effect of 2,3,7,8-tetrachlorodibenzo-p-dioxin (TCDD) on oxidative enzymes in adipocytes and liver. Toxicology 171 (2002) 117-125
    • (2002) Toxicology , vol.171 , pp. 117-125
    • Kern, P.A.1    Fishman, R.B.2    Song, W.3    Brown, A.D.4    Fonseca, V.5
  • 24
    • 0031586757 scopus 로고    scopus 로고
    • Oxidative stress to DNA, protein and antioxidant enzymes (superoxide dismutase and catalase) in rats treated with benzo(a)pyrene
    • Kim K.B., and Lee B.M. Oxidative stress to DNA, protein and antioxidant enzymes (superoxide dismutase and catalase) in rats treated with benzo(a)pyrene. Cancer Lett. 113 (1997) 205-212
    • (1997) Cancer Lett. , vol.113 , pp. 205-212
    • Kim, K.B.1    Lee, B.M.2
  • 26
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 27
    • 0029591778 scopus 로고
    • Lobar variation of carbon tetrachloride hepatotoxicity in the rat
    • Low D., Thomas N.W., and Fry J.R. Lobar variation of carbon tetrachloride hepatotoxicity in the rat. Toxicol. Lett. 81 (1995) 1-4
    • (1995) Toxicol. Lett. , vol.81 , pp. 1-4
    • Low, D.1    Thomas, N.W.2    Fry, J.R.3
  • 28
    • 0014691242 scopus 로고
    • Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein)
    • McCord J.M., and Fridovich I. Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein). J. Biol. Chem. 244 (1969) 6049-6055
    • (1969) J. Biol. Chem. , vol.244 , pp. 6049-6055
    • McCord, J.M.1    Fridovich, I.2
  • 29
    • 0015056379 scopus 로고
    • An enzyme-based theory of obligate anaerobiosis: the physiological function of superoxide dismutase
    • McCord J.M., Keele B.B., and Fridovich I. An enzyme-based theory of obligate anaerobiosis: the physiological function of superoxide dismutase. Proc. Natl. Acad. Sci. USA 68 (1971) 1024-1027
    • (1971) Proc. Natl. Acad. Sci. USA , vol.68 , pp. 1024-1027
    • McCord, J.M.1    Keele, B.B.2    Fridovich, I.3
  • 30
    • 0029921975 scopus 로고    scopus 로고
    • Effects of chloroquine treatment on antioxidant enzymes in rat liver and kidney
    • Magwere T., Naik Y.S., and Hasler J.A. Effects of chloroquine treatment on antioxidant enzymes in rat liver and kidney. Free Radic. Biol. Med. 22 (1997) 321-327
    • (1997) Free Radic. Biol. Med. , vol.22 , pp. 321-327
    • Magwere, T.1    Naik, Y.S.2    Hasler, J.A.3
  • 31
    • 0036066905 scopus 로고    scopus 로고
    • Advantages of glutamate dehydrogenase as a biomarker of acute hepatic injury in rats
    • O'Brien P.J., Slaughter M.R., Polley S.R., and Kramer K. Advantages of glutamate dehydrogenase as a biomarker of acute hepatic injury in rats. Lab. Anim. 36 (2002) 313-321
    • (2002) Lab. Anim. , vol.36 , pp. 313-321
    • O'Brien, P.J.1    Slaughter, M.R.2    Polley, S.R.3    Kramer, K.4
  • 32
    • 0034283863 scopus 로고    scopus 로고
    • Smoking and oxidant stress: assay of isoprostane in human urine by gas chromatography-mass spectrometry
    • Obata T., Tomaru K., Nagakura T., Izumi Y., and Kawamoto T. Smoking and oxidant stress: assay of isoprostane in human urine by gas chromatography-mass spectrometry. J. Chromatogr. B: Biomed. Sci. Appl. 746 (2000) 11-15
    • (2000) J. Chromatogr. B: Biomed. Sci. Appl. , vol.746 , pp. 11-15
    • Obata, T.1    Tomaru, K.2    Nagakura, T.3    Izumi, Y.4    Kawamoto, T.5
  • 33
    • 0032756387 scopus 로고    scopus 로고
    • Change in hepatic antioxidant defense system with liver injury development in rats with a single alpha-naphthylisothiocyanate intoxication
    • Ohta Y., Kongo M., Sasaki E., and Harada N. Change in hepatic antioxidant defense system with liver injury development in rats with a single alpha-naphthylisothiocyanate intoxication. Toxicology 139 (1999) 265-275
    • (1999) Toxicology , vol.139 , pp. 265-275
    • Ohta, Y.1    Kongo, M.2    Sasaki, E.3    Harada, N.4
  • 34
    • 0035914342 scopus 로고    scopus 로고
    • Subcellular distribution of superoxide dismutases (SOD) in rat liver: Cu,Zn-SOD in mitochondria
    • Okado-Matsumoto A., and Fridovich I. Subcellular distribution of superoxide dismutases (SOD) in rat liver: Cu,Zn-SOD in mitochondria. J. Biol. Chem. 276 (2001) 38388-38393
    • (2001) J. Biol. Chem. , vol.276 , pp. 38388-38393
    • Okado-Matsumoto, A.1    Fridovich, I.2
  • 35
    • 0042123515 scopus 로고    scopus 로고
    • Carbon tetrachloride-induced nephrotoxicity and protective effect of betaine in Sprague-Dawley rats
    • Ozturk F., Ucar M., Ozturk I.C., Vardi N., and Batcioglu K. Carbon tetrachloride-induced nephrotoxicity and protective effect of betaine in Sprague-Dawley rats. Urology 62 (2003) 353-356
    • (2003) Urology , vol.62 , pp. 353-356
    • Ozturk, F.1    Ucar, M.2    Ozturk, I.C.3    Vardi, N.4    Batcioglu, K.5
  • 36
    • 1842525727 scopus 로고    scopus 로고
    • Liver necrosis and fulminant hepatic failure in rats: protection by oxyanionic form of tungsten
    • Pawa S., and Ali S. Liver necrosis and fulminant hepatic failure in rats: protection by oxyanionic form of tungsten. Biochim. Biophys. Acta 1688 (2004) 210-222
    • (2004) Biochim. Biophys. Acta , vol.1688 , pp. 210-222
    • Pawa, S.1    Ali, S.2
  • 37
    • 4444226979 scopus 로고    scopus 로고
    • Identification and proteomic profiling of exosomes in human urine
    • Pisitkun T., Shen R.F., and Knepper M.A. Identification and proteomic profiling of exosomes in human urine. Proc. Natl. Acad. Sci. USA 101 (2004) 13368-13373
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 13368-13373
    • Pisitkun, T.1    Shen, R.F.2    Knepper, M.A.3
  • 39
    • 0001791671 scopus 로고
    • Chemical mechanisms in carbon tetrachloride toxicity
    • Pryor W.A. (Ed), Academic Press, New York (Chapter 3)
    • Recknagel R.O., Glende Jr. E.A., and Hruskewycz A. Chemical mechanisms in carbon tetrachloride toxicity. In: Pryor W.A. (Ed). Free Radicals in Biology vol. III (1977), Academic Press, New York 97-130 (Chapter 3)
    • (1977) Free Radicals in Biology , vol.III , pp. 97-130
    • Recknagel, R.O.1    Glende Jr., E.A.2    Hruskewycz, A.3
  • 40
    • 0037150281 scopus 로고    scopus 로고
    • Hepatotoxicity and aging: endogenous antioxidant systems in hepatocytes from 2-, 6-, 12-, 18- and 30-month-old rats following a necrogenic dose of thioacetamide
    • Sanz N., Diez-Fernandez C., Andres D., and Cascales M. Hepatotoxicity and aging: endogenous antioxidant systems in hepatocytes from 2-, 6-, 12-, 18- and 30-month-old rats following a necrogenic dose of thioacetamide. Biochim. Biophys. Acta 1587 (2002) 12-20
    • (2002) Biochim. Biophys. Acta , vol.1587 , pp. 12-20
    • Sanz, N.1    Diez-Fernandez, C.2    Andres, D.3    Cascales, M.4
  • 41
    • 0035861399 scopus 로고    scopus 로고
    • Carbon tetrachloride changes the activity of cytochrome P450 system in the liver of male rats: role of antioxidants
    • Sheweita S.A., El-Gabar M.A., and Bastawy M. Carbon tetrachloride changes the activity of cytochrome P450 system in the liver of male rats: role of antioxidants. Toxicology 169 (2001) 83-92
    • (2001) Toxicology , vol.169 , pp. 83-92
    • Sheweita, S.A.1    El-Gabar, M.A.2    Bastawy, M.3
  • 42
    • 0031876158 scopus 로고    scopus 로고
    • Evidence of hepatocytes apoptosis in rat liver after the administration of carbon tetrachloride
    • Shi J., Aisaki K., Ikawa Y., and Wake K. Evidence of hepatocytes apoptosis in rat liver after the administration of carbon tetrachloride. Am. J. Pathol. 153 (1998) 515-525
    • (1998) Am. J. Pathol. , vol.153 , pp. 515-525
    • Shi, J.1    Aisaki, K.2    Ikawa, Y.3    Wake, K.4
  • 43
    • 0035184151 scopus 로고    scopus 로고
    • Gender difference in cytoprotection induced by estrogen on female and male bovine aortic endothelial cells
    • Si M.L., Al-Sharafi B., Lai C.C., Khardori R., Chang C., and Su C.Y. Gender difference in cytoprotection induced by estrogen on female and male bovine aortic endothelial cells. Endocrine 15 (2001) 255-262
    • (2001) Endocrine , vol.15 , pp. 255-262
    • Si, M.L.1    Al-Sharafi, B.2    Lai, C.C.3    Khardori, R.4    Chang, C.5    Su, C.Y.6
  • 44
    • 0030885361 scopus 로고    scopus 로고
    • Antioxidant status of liver, erythrocytes, and blood serum of rats in acute methanol intoxication
    • Skrzydlewska E., and Farbiszewski R. Antioxidant status of liver, erythrocytes, and blood serum of rats in acute methanol intoxication. Alcohol 14 (1997) 431-437
    • (1997) Alcohol , vol.14 , pp. 431-437
    • Skrzydlewska, E.1    Farbiszewski, R.2
  • 45
    • 0013872594 scopus 로고
    • Necrogenic action of carbon tetrachloride in the rat: a speculative mechanism based on activation
    • Slater T.F. Necrogenic action of carbon tetrachloride in the rat: a speculative mechanism based on activation. Nature 209 (1966) 36-40
    • (1966) Nature , vol.209 , pp. 36-40
    • Slater, T.F.1
  • 46
    • 0018261942 scopus 로고
    • Mechanisms of protection against the damage produced in biological systems by oxygen-derived free radicals
    • Slater T.F. Mechanisms of protection against the damage produced in biological systems by oxygen-derived free radicals. Ciba Found. Symp. 65 (1978) 143-176
    • (1978) Ciba Found. Symp. , vol.65 , pp. 143-176
    • Slater, T.F.1
  • 47
    • 0013292906 scopus 로고    scopus 로고
    • The role of nitric oxide in multiple sclerosis
    • Smith K.J., and Lassmann H. The role of nitric oxide in multiple sclerosis. Lancet Neurol. 1 (2002) 232-241
    • (2002) Lancet Neurol. , vol.1 , pp. 232-241
    • Smith, K.J.1    Lassmann, H.2
  • 48
    • 34548674191 scopus 로고    scopus 로고
    • Comprehensive characterisation of serum clinical chemistry parameters and the identification of urinary superoxide dismutase in a carbon tetrachloride-induced model of hepatic fibrosis in the female Hanover Wistar rat
    • Smyth R., Munday M.R., Clarke C.J., York M.J., Dare T.O., and Turton J.A. Comprehensive characterisation of serum clinical chemistry parameters and the identification of urinary superoxide dismutase in a carbon tetrachloride-induced model of hepatic fibrosis in the female Hanover Wistar rat. Int. J. Exp. Pathol. 88 (2007) 361-376
    • (2007) Int. J. Exp. Pathol. , vol.88 , pp. 361-376
    • Smyth, R.1    Munday, M.R.2    Clarke, C.J.3    York, M.J.4    Dare, T.O.5    Turton, J.A.6
  • 49
    • 0016264038 scopus 로고
    • Bovine erythrocyte superoxide dismutase. Complete amino acid sequence
    • Steinman H.M., Naik V.R., Abernethy J.L., and Hill R.L. Bovine erythrocyte superoxide dismutase. Complete amino acid sequence. J. Biol. Chem. 249 (1974) 7326-7338
    • (1974) J. Biol. Chem. , vol.249 , pp. 7326-7338
    • Steinman, H.M.1    Naik, V.R.2    Abernethy, J.L.3    Hill, R.L.4
  • 51
    • 0020374498 scopus 로고
    • Determination and analysis of the 2 A-structure of copper, zinc superoxide dismutase
    • Tainer J.A., Getzoff E.D., Beem K.M., Richardson J.S., and Richardson D.C. Determination and analysis of the 2 A-structure of copper, zinc superoxide dismutase. J. Mol. Biol. 160 (1982) 181-217
    • (1982) J. Mol. Biol. , vol.160 , pp. 181-217
    • Tainer, J.A.1    Getzoff, E.D.2    Beem, K.M.3    Richardson, J.S.4    Richardson, D.C.5
  • 52
    • 0034630204 scopus 로고    scopus 로고
    • Prolonged phenobarbital pre-treatment abolishes the early oxidative stress component induced in the liver by acute lindane intoxication
    • Videla L.A., Arisi A.C., Fuzaro A.P., Koch O.R., and Junqueira V.B. Prolonged phenobarbital pre-treatment abolishes the early oxidative stress component induced in the liver by acute lindane intoxication. Toxicol. Lett. 115 (2000) 45-51
    • (2000) Toxicol. Lett. , vol.115 , pp. 45-51
    • Videla, L.A.1    Arisi, A.C.2    Fuzaro, A.P.3    Koch, O.R.4    Junqueira, V.B.5
  • 53
    • 0015848173 scopus 로고
    • Superoxide dismutase. Organelle specificity
    • Weisiger R.A., and Fridovich I. Superoxide dismutase. Organelle specificity. J. Biol. Chem. 248 (1973) 3582-3592
    • (1973) J. Biol. Chem. , vol.248 , pp. 3582-3592
    • Weisiger, R.A.1    Fridovich, I.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.