메뉴 건너뛰기




Volumn 256, Issue 1-2, 2009, Pages 128-134

Naringenin protects against cadmium-induced oxidative renal dysfunction in rats

Author keywords

Cadmium; Kidney; Naringenin; Oxidative stress; Rats

Indexed keywords

ALPHA TOCOPHEROL; ASCORBIC ACID; CADMIUM CHLORIDE; CARBONYL DERIVATIVE; CATALASE; CREATININE; GLUTATHIONE; GLUTATHIONE 6 PHOSPHATE DEHYDROGENASE; GLUTATHIONE DERIVATIVE; GLUTATHIONE PEROXIDASE; GLUTATHIONE REDUCTASE; GLUTATHIONE TRANSFERASE; LIPID HYDROPEROXIDE; NARINGENIN; SUPEROXIDE DISMUTASE; THIOBARBITURIC ACID REACTIVE SUBSTANCE; THIOL DERIVATIVE; UNCLASSIFIED DRUG; UREA; URIC ACID;

EID: 58149233844     PISSN: 0300483X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tox.2008.11.012     Document Type: Article
Times cited : (250)

References (63)
  • 1
    • 0344197165 scopus 로고    scopus 로고
    • Cadmium binding and sodium dependent solute transport in renal brush border membrane vesicles
    • Ahn D.W., Kim M.Y., Kim K.R., and Park P.S. Cadmium binding and sodium dependent solute transport in renal brush border membrane vesicles. Toxicol. Appl. Pharmacol. 154 (1999) 212-218
    • (1999) Toxicol. Appl. Pharmacol. , vol.154 , pp. 212-218
    • Ahn, D.W.1    Kim, M.Y.2    Kim, K.R.3    Park, P.S.4
  • 2
    • 1542475977 scopus 로고    scopus 로고
    • Structure radical scavenging activity and relationships of flavonoids
    • Amic D., Amic D.D., Beslo D., and Trinajstic N. Structure radical scavenging activity and relationships of flavonoids. Clin. Chim. Acta 76 (2003) 55-61
    • (2003) Clin. Chim. Acta , vol.76 , pp. 55-61
    • Amic, D.1    Amic, D.D.2    Beslo, D.3    Trinajstic, N.4
  • 3
    • 13844272440 scopus 로고    scopus 로고
    • Naringenin attenuates cisplatin nephrotoxicity in rats
    • Badary O.A., Maksoud S.A., Ahmed W.A., and Owieda G.H. Naringenin attenuates cisplatin nephrotoxicity in rats. Life Sci. 76 (2005) 2125-2135
    • (2005) Life Sci. , vol.76 , pp. 2125-2135
    • Badary, O.A.1    Maksoud, S.A.2    Ahmed, W.A.3    Owieda, G.H.4
  • 4
    • 0002663724 scopus 로고
    • Active transport of glutathione disulfide from erythrocytes
    • Larson A., Orrenius S., Holmgren A., and Mannerwik B. (Eds), Raven Press, NY, USA
    • Beutler E. Active transport of glutathione disulfide from erythrocytes. In: Larson A., Orrenius S., Holmgren A., and Mannerwik B. (Eds). Functions of Glutathione-Biochemical, Physiological, Toxicological and Clinical Aspects (1983), Raven Press, NY, USA 65
    • (1983) Functions of Glutathione-Biochemical, Physiological, Toxicological and Clinical Aspects , pp. 65
    • Beutler, E.1
  • 5
    • 0032408711 scopus 로고    scopus 로고
    • Structural and functional changes in proteins induced by radical mediated oxidative stress and protective action of antioxidants N-tert-butyl-alpha-phenylnitrone and vitamin E
    • Butterfield D.A., Koppal T., Howard B., Subramanian R., Hall N., Hensley K., Yatin S., Allen K., Aksenova M., and Carney J. Structural and functional changes in proteins induced by radical mediated oxidative stress and protective action of antioxidants N-tert-butyl-alpha-phenylnitrone and vitamin E. Ann. N. Y. Acad. Sci. 854 (1998) 448-462
    • (1998) Ann. N. Y. Acad. Sci. , vol.854 , pp. 448-462
    • Butterfield, D.A.1    Koppal, T.2    Howard, B.3    Subramanian, R.4    Hall, N.5    Hensley, K.6    Yatin, S.7    Allen, K.8    Aksenova, M.9    Carney, J.10
  • 6
    • 0034669717 scopus 로고    scopus 로고
    • Cadmium dependent enzyme activity alteration is not imputable to lipid peroxidation
    • Casalino E., Calzaretti G., Sblano L., and Landriscina C. Cadmium dependent enzyme activity alteration is not imputable to lipid peroxidation. Arch. Biochem. Biophys. 383 (2000) 288-295
    • (2000) Arch. Biochem. Biophys. , vol.383 , pp. 288-295
    • Casalino, E.1    Calzaretti, G.2    Sblano, L.3    Landriscina, C.4
  • 7
    • 0034054733 scopus 로고    scopus 로고
    • On the ability of four flavonoids, baicilein, luteolin, naringenin and quercetin to suppress the Fenton reaction of the iron ATP complex
    • Cheng F., and Breen K. On the ability of four flavonoids, baicilein, luteolin, naringenin and quercetin to suppress the Fenton reaction of the iron ATP complex. Biometals 13 (2000) 77-83
    • (2000) Biometals , vol.13 , pp. 77-83
    • Cheng, F.1    Breen, K.2
  • 8
    • 0028420282 scopus 로고
    • Antimutagenic effect of plant flavonoids in the salmonella assay system
    • Choi J.S., Park K.Y., Moon S.H., Rhee S.H., and Young H.S. Antimutagenic effect of plant flavonoids in the salmonella assay system. Arch. Pharm. Res. 17 (1994) 71-75
    • (1994) Arch. Pharm. Res. , vol.17 , pp. 71-75
    • Choi, J.S.1    Park, K.Y.2    Moon, S.H.3    Rhee, S.H.4    Young, H.S.5
  • 10
    • 0021288822 scopus 로고
    • Vitamin E analysis method for animal tissues
    • Desai I.D. Vitamin E analysis method for animal tissues. Method Enzymol. 105 (1984) 138-143
    • (1984) Method Enzymol. , vol.105 , pp. 138-143
    • Desai, I.D.1
  • 11
    • 0031473475 scopus 로고    scopus 로고
    • Creatinine clearance predicted from body cells mass is a good indicator of renal function
    • Donadio C., Lucchesi A., Tramonti G., and Bianchi C. Creatinine clearance predicted from body cells mass is a good indicator of renal function. Kidney Int. 52 (1997) 166-168
    • (1997) Kidney Int. , vol.52 , pp. 166-168
    • Donadio, C.1    Lucchesi, A.2    Tramonti, G.3    Bianchi, C.4
  • 13
    • 0035750172 scopus 로고    scopus 로고
    • Toxic metals and oxidative stress. Part I. Mechanisms involved in metal induced oxidative damage
    • Ercal N., Gurrer-Orhan H., and Aykin-Burns N. Toxic metals and oxidative stress. Part I. Mechanisms involved in metal induced oxidative damage. Curr. Top. Med. Chem. 1 (2001) 529-539
    • (2001) Curr. Top. Med. Chem. , vol.1 , pp. 529-539
    • Ercal, N.1    Gurrer-Orhan, H.2    Aykin-Burns, N.3
  • 14
    • 34247623143 scopus 로고    scopus 로고
    • Biomonitoring of the adverse effects induced by the chronic exposure to lead and cadmium on kidney function: usefulness of alpha-glutathione S-transferase
    • Garcon G., Leleu B., Marez T., Zerimech F., Mariehaguenoer J., Furon D., and Shirali P. Biomonitoring of the adverse effects induced by the chronic exposure to lead and cadmium on kidney function: usefulness of alpha-glutathione S-transferase. Sci. Total Environ. 377 (2007) 165-172
    • (2007) Sci. Total Environ. , vol.377 , pp. 165-172
    • Garcon, G.1    Leleu, B.2    Marez, T.3    Zerimech, F.4    Mariehaguenoer, J.5    Furon, D.6    Shirali, P.7
  • 15
    • 0021338273 scopus 로고
    • Differences in the uptake of cadmium and mercury by the rat hepatocyte primary cultures - role of sulfhydryl carrier
    • Gerson R.J., and Shaikh Z.A. Differences in the uptake of cadmium and mercury by the rat hepatocyte primary cultures - role of sulfhydryl carrier. Biochem. Pharmacol. 33 (1984) 199-203
    • (1984) Biochem. Pharmacol. , vol.33 , pp. 199-203
    • Gerson, R.J.1    Shaikh, Z.A.2
  • 16
    • 0016275313 scopus 로고
    • Glutathione transferase: a first enzymatic step in mercapturic acid formation
    • Habig W.H., Pabst M.J., and Jakpoly W.B. Glutathione transferase: a first enzymatic step in mercapturic acid formation. J. Biol. Chem. 249 (1974) 7130-7139
    • (1974) J. Biol. Chem. , vol.249 , pp. 7130-7139
    • Habig, W.H.1    Pabst, M.J.2    Jakpoly, W.B.3
  • 17
    • 0025126555 scopus 로고
    • Free radicals and catalytic metal ions in human disease. An overview
    • Halliwell B., and Gutteridge J.M.C. Free radicals and catalytic metal ions in human disease. An overview. Method Enzymol. 186 (1990) 1-85
    • (1990) Method Enzymol. , vol.186 , pp. 1-85
    • Halliwell, B.1    Gutteridge, J.M.C.2
  • 18
    • 0030565592 scopus 로고    scopus 로고
    • Cadmium induced production of superoxide anion and nitric oxide. DNA single strand breaks and lactate dehydrogenase leakage in J774A1 cell cultures
    • Hassoun E.A., and Stohs S.J. Cadmium induced production of superoxide anion and nitric oxide. DNA single strand breaks and lactate dehydrogenase leakage in J774A1 cell cultures. Toxicology 112 (1996) 219-226
    • (1996) Toxicology , vol.112 , pp. 219-226
    • Hassoun, E.A.1    Stohs, S.J.2
  • 19
    • 0035793127 scopus 로고    scopus 로고
    • The integrity of renal cortical brush-border and basolateral membrane vesicles is damaged in vitro by nephrotoxic heavy metals
    • Herak-Kramberger C.M., and Sabolic I. The integrity of renal cortical brush-border and basolateral membrane vesicles is damaged in vitro by nephrotoxic heavy metals. Toxicology 156 (2001) 139-147
    • (2001) Toxicology , vol.156 , pp. 139-147
    • Herak-Kramberger, C.M.1    Sabolic, I.2
  • 21
    • 0031930043 scopus 로고    scopus 로고
    • Uric acid, a natural scavenger of peroxynitrite, in experimental allergic encephalomyelitis and multiple sclerosis
    • Hooper D.C., Spitsin S., Kean R.B., Champion J.M., Dickson G.M., and Chaudhry I. Uric acid, a natural scavenger of peroxynitrite, in experimental allergic encephalomyelitis and multiple sclerosis. Proc. Natl. Acad. Sci. U.S.A. 95 (1998) 675-680
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 675-680
    • Hooper, D.C.1    Spitsin, S.2    Kean, R.B.3    Champion, J.M.4    Dickson, G.M.5    Chaudhry, I.6
  • 22
    • 0000091713 scopus 로고
    • Assay of glutathione reductase activity
    • Bergmeyer H.V. (Ed), Academic Press, New York, USA
    • Horn H.D., and Burns F.H. Assay of glutathione reductase activity. In: Bergmeyer H.V. (Ed). Methods of Enzymatic Analysis (1978), Academic Press, New York, USA 142-146
    • (1978) Methods of Enzymatic Analysis , pp. 142-146
    • Horn, H.D.1    Burns, F.H.2
  • 23
    • 0034537505 scopus 로고    scopus 로고
    • Exposure to metals
    • Hu H. Exposure to metals. Primary Care 27 (2000) 983-996
    • (2000) Primary Care , vol.27 , pp. 983-996
    • Hu, H.1
  • 25
    • 0026632930 scopus 로고
    • Ferrous ion oxidation in the presence of xylenol orange for detection of lipid hydroperoxide in low density lipoprotein
    • Jiang Z.Y., Hunt J.V., and Wolff S.D. Ferrous ion oxidation in the presence of xylenol orange for detection of lipid hydroperoxide in low density lipoprotein. Anal. Biochem. 202 (1992) 384-389
    • (1992) Anal. Biochem. , vol.202 , pp. 384-389
    • Jiang, Z.Y.1    Hunt, J.V.2    Wolff, S.D.3
  • 26
    • 0021681627 scopus 로고
    • A modified spectrophotometric assay of superoxide dismutase
    • Kakkar P., Das B., and Viswanathan P.N. A modified spectrophotometric assay of superoxide dismutase. Indian J. Biochem. Biophys. 21 (1984) 130-132
    • (1984) Indian J. Biochem. Biophys. , vol.21 , pp. 130-132
    • Kakkar, P.1    Das, B.2    Viswanathan, P.N.3
  • 27
    • 0034813893 scopus 로고    scopus 로고
    • Anti-atherogenic effect of citrus flavonoid, naringin and naringenin associated with hepatic ACAT and acrotic VCAM-1 and MCP-1 in high cholesterol fed rabbits
    • Lee C.H., Jeong T.S., Choi Y.K., Hyun B.H., Oh G.T., Kim E.H., and Bok S.H. Anti-atherogenic effect of citrus flavonoid, naringin and naringenin associated with hepatic ACAT and acrotic VCAM-1 and MCP-1 in high cholesterol fed rabbits. Biochem. Biophys. Res. Commun. 284 (2001) 681-688
    • (2001) Biochem. Biophys. Res. Commun. , vol.284 , pp. 681-688
    • Lee, C.H.1    Jeong, T.S.2    Choi, Y.K.3    Hyun, B.H.4    Oh, G.T.5    Kim, E.H.6    Bok, S.H.7
  • 28
    • 3442892728 scopus 로고    scopus 로고
    • The flavonoid naringenin inhibits dimethylnitrosamine induced liver damage in rats
    • Lee M.H., Soon S., and Moon J.O. The flavonoid naringenin inhibits dimethylnitrosamine induced liver damage in rats. Biol. Pharm. Bull. 27 (2004) 72-76
    • (2004) Biol. Pharm. Bull. , vol.27 , pp. 72-76
    • Lee, M.H.1    Soon, S.2    Moon, J.O.3
  • 32
    • 0033637140 scopus 로고    scopus 로고
    • The effects of plant flavonoids on mammalian cells. Implication for inflammation, heart disease and cancer
    • Middleton E., Kandaswami C., and Theoharides T.C. The effects of plant flavonoids on mammalian cells. Implication for inflammation, heart disease and cancer. Pharmacol. Rev. 52 (2000) 673-751
    • (2000) Pharmacol. Rev. , vol.52 , pp. 673-751
    • Middleton, E.1    Kandaswami, C.2    Theoharides, T.C.3
  • 33
    • 0036827673 scopus 로고    scopus 로고
    • Interaction of flavonoids with iron and copper ions, a mechanism for their antioxidant activity
    • Mira L., Fernandez M.T., Santos M., Rocha R., Florencio M.H., and Jennings K.R. Interaction of flavonoids with iron and copper ions, a mechanism for their antioxidant activity. Free Radical Res. 36 (2002) 1199-1208
    • (2002) Free Radical Res. , vol.36 , pp. 1199-1208
    • Mira, L.1    Fernandez, M.T.2    Santos, M.3    Rocha, R.4    Florencio, M.H.5    Jennings, K.R.6
  • 34
    • 0242331583 scopus 로고    scopus 로고
    • Sodium fluoride ion and renal function after prolonged sevoflurane or isoflurane anaesthesia
    • Mohamed M., Abdellatif M.D., Sabar A., and Elglammal M.D. Sodium fluoride ion and renal function after prolonged sevoflurane or isoflurane anaesthesia. Eng. J. Anaesth. 19 (2003) 79-83
    • (2003) Eng. J. Anaesth. , vol.19 , pp. 79-83
    • Mohamed, M.1    Abdellatif, M.D.2    Sabar, A.3    Elglammal, M.D.4
  • 35
    • 33749558205 scopus 로고    scopus 로고
    • Protective effect of quercetin on experimental chronic cadmium nephrotoxicity in rats is based on its antioxidant properties
    • Morales A.I., Vicente-Sanchez C., Egido J., Arevalo M.A., and Lopeznovoa J.M. Protective effect of quercetin on experimental chronic cadmium nephrotoxicity in rats is based on its antioxidant properties. Food Chem. Toxicol. 44 (2006) 2092-2100
    • (2006) Food Chem. Toxicol. , vol.44 , pp. 2092-2100
    • Morales, A.I.1    Vicente-Sanchez, C.2    Egido, J.3    Arevalo, M.A.4    Lopeznovoa, J.M.5
  • 36
    • 0018327389 scopus 로고
    • Levels of glutathione, glutathione reductase and glutathione S-transferase activities in rat lung and liver
    • Moron M.S., Despierre J.W., and Minnervik B. Levels of glutathione, glutathione reductase and glutathione S-transferase activities in rat lung and liver. Biochim. Biophys. Acta 582 (1979) 67-78
    • (1979) Biochim. Biophys. Acta , vol.582 , pp. 67-78
    • Moron, M.S.1    Despierre, J.W.2    Minnervik, B.3
  • 38
    • 0014421644 scopus 로고
    • Formation of malondialdehyde from phospholipid arachidonate during microsomal lipid peroxidation
    • Niehiaus W.G., and Samuelsson D. Formation of malondialdehyde from phospholipid arachidonate during microsomal lipid peroxidation. Eur. J. Biochem. 6 (1968) 126-130
    • (1968) Eur. J. Biochem. , vol.6 , pp. 126-130
    • Niehiaus, W.G.1    Samuelsson, D.2
  • 39
    • 0018369625 scopus 로고
    • Selected methods for the determination of ascorbic acid in animal cells, tissues and fluids
    • Omaye S.T., Turbull J.D., and Sauberlich H.E. Selected methods for the determination of ascorbic acid in animal cells, tissues and fluids. Method Enzymol. 62 (1979) 3-11
    • (1979) Method Enzymol. , vol.62 , pp. 3-11
    • Omaye, S.T.1    Turbull, J.D.2    Sauberlich, H.E.3
  • 40
    • 33646258956 scopus 로고    scopus 로고
    • Influence of naringenin on oxytetracycline mediated oxidative damage in rat liver
    • Pari L., and Gnanasoundari M. Influence of naringenin on oxytetracycline mediated oxidative damage in rat liver. Basic Clin. Pharmacol. Toxicol. 98 (2006) 1-6
    • (2006) Basic Clin. Pharmacol. Toxicol. , vol.98 , pp. 1-6
    • Pari, L.1    Gnanasoundari, M.2
  • 41
    • 24944447847 scopus 로고    scopus 로고
    • Role of diallyl tetrasulfide in ameliorating the cadmium induced biochemical changes in rats
    • Pari L., and Murugavel P. Role of diallyl tetrasulfide in ameliorating the cadmium induced biochemical changes in rats. Environ. Toxicol. Pharmacol. 20 (2005) 493-500
    • (2005) Environ. Toxicol. Pharmacol. , vol.20 , pp. 493-500
    • Pari, L.1    Murugavel, P.2
  • 42
    • 33846070110 scopus 로고    scopus 로고
    • Cytoprotective and antioxidant role of diallyl tetrasulfide on cadmium induced renal injury. An in vivo and in vitro study
    • Pari L., Murugavel P., Sitasawad S.L., and Sandeep Kumar K. Cytoprotective and antioxidant role of diallyl tetrasulfide on cadmium induced renal injury. An in vivo and in vitro study. Life Sci. 80 (2007) 650-658
    • (2007) Life Sci. , vol.80 , pp. 650-658
    • Pari, L.1    Murugavel, P.2    Sitasawad, S.L.3    Sandeep Kumar, K.4
  • 43
    • 0032135465 scopus 로고    scopus 로고
    • Cysteine metabolism and metal toxicity
    • Quig D. Cysteine metabolism and metal toxicity. Altern. Med. Rev. 3 (1998) 262-270
    • (1998) Altern. Med. Rev. , vol.3 , pp. 262-270
    • Quig, D.1
  • 44
    • 0015918166 scopus 로고
    • Selenium: biochemical role as a component of glutathione peroxidase purification assay
    • Rotruck J.T., Pope A.L., and Ganther H.E. Selenium: biochemical role as a component of glutathione peroxidase purification assay. Science 179 (1973) 588-590
    • (1973) Science , vol.179 , pp. 588-590
    • Rotruck, J.T.1    Pope, A.L.2    Ganther, H.E.3
  • 45
    • 0035964436 scopus 로고    scopus 로고
    • Subchronic cadmium treatment affects the abundance and arrangement of cytoskeletal proteins in rat renal proximal tubule cells
    • Sabolic I., Herak-Kramberger C.M., and Brown D. Subchronic cadmium treatment affects the abundance and arrangement of cytoskeletal proteins in rat renal proximal tubule cells. Toxicology 165 (2001) 205-216
    • (2001) Toxicology , vol.165 , pp. 205-216
    • Sabolic, I.1    Herak-Kramberger, C.M.2    Brown, D.3
  • 46
    • 0032786872 scopus 로고    scopus 로고
    • Hypolipidemic effects of naringenin, rutin, nicotinic acid and their association
    • Santos K.F., Oliveria T.T., Nagem T.J., Pinto A.S., and Oliveria M.G. Hypolipidemic effects of naringenin, rutin, nicotinic acid and their association. Pharmacol. Res. 40 (1999) 493-496
    • (1999) Pharmacol. Res. , vol.40 , pp. 493-496
    • Santos, K.F.1    Oliveria, T.T.2    Nagem, T.J.3    Pinto, A.S.4    Oliveria, M.G.5
  • 47
    • 0023835083 scopus 로고
    • Kidney synthesizes less metallothionein then liver in response to cadmium chloride and cadmium metallothionein
    • Sendelbach L.E., and Klaassen C.D. Kidney synthesizes less metallothionein then liver in response to cadmium chloride and cadmium metallothionein. Toxicol. Appl. Pharmacol. 92 (1988) 95-102
    • (1988) Toxicol. Appl. Pharmacol. , vol.92 , pp. 95-102
    • Sendelbach, L.E.1    Klaassen, C.D.2
  • 48
    • 0033012168 scopus 로고    scopus 로고
    • Oxidative stress as a mechanism of chronic cadmium induced hepatotoxicity and renal toxicity and protection by antioxidants
    • Shaikh Z.A., Vu T.T., and Zaman K. Oxidative stress as a mechanism of chronic cadmium induced hepatotoxicity and renal toxicity and protection by antioxidants. Toxicol. Appl. Pharmacol. 154 (1999) 256-263
    • (1999) Toxicol. Appl. Pharmacol. , vol.154 , pp. 256-263
    • Shaikh, Z.A.1    Vu, T.T.2    Zaman, K.3
  • 49
    • 0015353270 scopus 로고
    • Calorimetric assay of catalase
    • Sinha A.K. Calorimetric assay of catalase. Anal. Biochem. 47 (1972) 389-394
    • (1972) Anal. Biochem. , vol.47 , pp. 389-394
    • Sinha, A.K.1
  • 50
    • 0031590969 scopus 로고    scopus 로고
    • Inhibition of proliferation of estrogen receptor-positive MCF-7 human
    • So F.V., Guthrie N., Chambers A.F., and Carroll K.K. Inhibition of proliferation of estrogen receptor-positive MCF-7 human. Cancer Lett. 112 (1997) 127-133
    • (1997) Cancer Lett. , vol.112 , pp. 127-133
    • So, F.V.1    Guthrie, N.2    Chambers, A.F.3    Carroll, K.K.4
  • 52
    • 0028798434 scopus 로고
    • Oxidative mechanisms in the toxicity of metal ions
    • Stohs S.J., and Bagchi D. Oxidative mechanisms in the toxicity of metal ions. Free Radical Biol. Med. 18 (1995) 321-336
    • (1995) Free Radical Biol. Med. , vol.18 , pp. 321-336
    • Stohs, S.J.1    Bagchi, D.2
  • 54
    • 0034950809 scopus 로고    scopus 로고
    • Hepatoprotective effect of lupeol and lupeol linoleate on tissue antioxidant defense system in cadmium induced hepatotoxicity in rats
    • Sunitha S., Nagaraj M., and Varalkshmi P. Hepatoprotective effect of lupeol and lupeol linoleate on tissue antioxidant defense system in cadmium induced hepatotoxicity in rats. Fitoterapia 72 (2001) 516-523
    • (2001) Fitoterapia , vol.72 , pp. 516-523
    • Sunitha, S.1    Nagaraj, M.2    Varalkshmi, P.3
  • 56
    • 0033527677 scopus 로고    scopus 로고
    • In vitro and in vivo effects of naringin on cytochrome P450-dependent monooxygenase in mouse liver
    • Ueng Y.F., Chang Y.L., Oda Y., Park S.S., Liao J.F., Lin M.F., and Chen C.F. In vitro and in vivo effects of naringin on cytochrome P450-dependent monooxygenase in mouse liver. Life Sci. 65 (1999) 2591-2602
    • (1999) Life Sci. , vol.65 , pp. 2591-2602
    • Ueng, Y.F.1    Chang, Y.L.2    Oda, Y.3    Park, S.S.4    Liao, J.F.5    Lin, M.F.6    Chen, C.F.7
  • 57
  • 58
    • 0015462313 scopus 로고
    • Biochemical effects of mercury, cadmium and lead
    • Vallee B.L., and Ulmer D.D. Biochemical effects of mercury, cadmium and lead. Annu. Rev. Biochem. 41 (1972) 91-128
    • (1972) Annu. Rev. Biochem. , vol.41 , pp. 91-128
    • Vallee, B.L.1    Ulmer, D.D.2
  • 60
    • 0142219722 scopus 로고    scopus 로고
    • Molecular mechanisms of cadmium carcinogenesis
    • Waisberg M., Joseph P., Hale B., and Beyersmann D. Molecular mechanisms of cadmium carcinogenesis. Toxicology 192 (2003) 95-117
    • (2003) Toxicology , vol.192 , pp. 95-117
    • Waisberg, M.1    Joseph, P.2    Hale, B.3    Beyersmann, D.4
  • 61
    • 2342646206 scopus 로고    scopus 로고
    • Cadmium inhibits electron transfer chain and induced reactive oxygen species
    • Wang Y., Fang J., Leonard S.S., and Rao K.M.K. Cadmium inhibits electron transfer chain and induced reactive oxygen species. Free Radical Biol. Med. 36 (2004) 1434-1443
    • (2004) Free Radical Biol. Med. , vol.36 , pp. 1434-1443
    • Wang, Y.1    Fang, J.2    Leonard, S.S.3    Rao, K.M.K.4
  • 62
    • 0142171680 scopus 로고    scopus 로고
    • Cadmium induced apoptosis in C6 gliomacells. Influence of oxidative stress
    • Watjen W., and Beyermann D. Cadmium induced apoptosis in C6 gliomacells. Influence of oxidative stress. Biometals 17 (2004) 65-78
    • (2004) Biometals , vol.17 , pp. 65-78
    • Watjen, W.1    Beyermann, D.2
  • 63
    • 0002553168 scopus 로고
    • Structure of human glucose-6-phosphate dehydrogenase
    • Yoshida A., and Beutler E. (Eds), Academic Press, New York
    • Yoshida A., and Huang I.Y. Structure of human glucose-6-phosphate dehydrogenase. In: Yoshida A., and Beutler E. (Eds). Glucose-6-phosphate Dehydrogenase (1986), Academic Press, New York 473-482
    • (1986) Glucose-6-phosphate Dehydrogenase , pp. 473-482
    • Yoshida, A.1    Huang, I.Y.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.