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Volumn 29, Issue 7, 1996, Pages 841-851

Oxidative stress in acute intermittent porphyria and lead poisoning may be triggered by 5-aminolevulinic acid

Author keywords

5 aminolevulinic acid; intermittent acute porphyria; lead poisoning; oxidative stress; porphyria; reactive oxygen species

Indexed keywords

AMINOLEVULINIC ACID; FREE RADICAL; REACTIVE OXYGEN METABOLITE;

EID: 0030016990     PISSN: 0100879X     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Review
Times cited : (135)

References (78)
  • 1
    • 0029002081 scopus 로고
    • From free radicals to electronically excited species
    • Adam W & Cilento G (1995). From free radicals to electronically excited species. Free Radical Biology and Medicine, 19: 103-114.
    • (1995) Free Radical Biology and Medicine , vol.19 , pp. 103-114
    • Adam, W.1    Cilento, G.2
  • 2
    • 0022272177 scopus 로고
    • Monosaccharide autoxidation in health and disease
    • Thornalley PJ (1985). Monosaccharide autoxidation in health and disease. Environmental Health Perspectives, 64: 297-307.
    • (1985) Environmental Health Perspectives , vol.64 , pp. 297-307
    • Thornalley, P.J.1
  • 3
    • 0006991476 scopus 로고
    • A free radical hypothesis of porphyria with 5-aminolevulinic acid overload
    • Davis KJA & Ursini F (Editors), CLEUP Press, Padova
    • Bechara EJH (1995). A free radical hypothesis of porphyria with 5-aminolevulinic acid overload. In: Davis KJA & Ursini F (Editors), The Oxygen Paradox. CLEUP Press, Padova, 503-513.
    • (1995) The Oxygen Paradox , pp. 503-513
    • Bechara, E.J.H.1
  • 4
    • 0023333090 scopus 로고
    • Superoxide radical initiates the autoxidation of dihydroxyacetone
    • Mashino T & Fridovich I (1987). Superoxide radical initiates the autoxidation of dihydroxyacetone. Archives of Biochemistry and Biophysics, 254: 547-551.
    • (1987) Archives of Biochemistry and Biophysics , vol.254 , pp. 547-551
    • Mashino, T.1    Fridovich, I.2
  • 5
    • 0024597762 scopus 로고
    • Free radical generation during 6-ammolevulinic acid autoxidation: Induction by hemoglobin and connections with porphyrinpathies
    • Monteiro HP, Abdalla DSP, Auguste O & Bechara EJH (1989). Free radical generation during 6-ammolevulinic acid autoxidation: induction by hemoglobin and connections with porphyrinpathies. Archives of Biochemistry and Biophysics, 271: 206-216.
    • (1989) Archives of Biochemistry and Biophysics , vol.271 , pp. 206-216
    • Monteiro, H.P.1    Abdalla, D.S.P.2    Auguste, O.3    Bechara, E.J.H.4
  • 6
    • 0023028913 scopus 로고
    • Redox cycling of anthracyclines by cardiac mitochondria. Formation of superoxide anion, hydrogen peroxide and hydroxyl radical
    • Doroshow JH & Davies KJA (1986). Redox cycling of anthracyclines by cardiac mitochondria. Formation of superoxide anion, hydrogen peroxide and hydroxyl radical. Journal of Biological Chemistry, 261: 3068-3074.
    • (1986) Journal of Biological Chemistry , vol.261 , pp. 3068-3074
    • Doroshow, J.H.1    Davies, K.J.A.2
  • 7
    • 0022495225 scopus 로고
    • Quinones in biology: Functions in electron transfer, and oxygen activation
    • Nohl H (1986). Quinones in biology: functions in electron transfer, and oxygen activation. Advances in Free Radicals in Biology and Medicine, 2: 211-279.
    • (1986) Advances in Free Radicals in Biology and Medicine , vol.2 , pp. 211-279
    • Nohl, H.1
  • 9
    • 0023708392 scopus 로고
    • Hydroxyl radical production and autoxidative glycosylation. Glucose autoxidation as the cause of protein damage in the experimental glycation model of diabetes mellitus and aging
    • Hunt JV, Dean RT & Wolff SP (1988). Hydroxyl radical production and autoxidative glycosylation. Glucose autoxidation as the cause of protein damage in the experimental glycation model of diabetes mellitus and aging. Biochemical Journal, 256: 205-212.
    • (1988) Biochemical Journal , vol.256 , pp. 205-212
    • Hunt, J.V.1    Dean, R.T.2    Wolff, S.P.3
  • 10
    • 0026073726 scopus 로고
    • Mechanisms of protection against damage mediated by Maillard reaction in aging
    • Monnier VM, Sell DR, Nagaraj RH & Myata S (1991). Mechanisms of protection against damage mediated by Maillard reaction in aging. Gerontology, 37: 152-165.
    • (1991) Gerontology , vol.37 , pp. 152-165
    • Monnier, V.M.1    Sell, D.R.2    Nagaraj, R.H.3    Myata, S.4
  • 11
    • 0023506918 scopus 로고
    • Homogentisic acid autoxidation and oxygen radical generation: Implications for the etiology of alkaptonuric arthritis
    • Martin Jr JP & Batkoff B (1987). Homogentisic acid autoxidation and oxygen radical generation: implications for the etiology of alkaptonuric arthritis. Free Radical Biology and Medicine, 3: 241-250.
    • (1987) Free Radical Biology and Medicine , vol.3 , pp. 241-250
    • Martin Jr., J.P.1    Batkoff, B.2
  • 12
    • 0020400134 scopus 로고
    • The chemistry of favism-inducing compounds. the properties of isouramil and divicine and their reaction with glutathione
    • Chevion M, Navok T, Glaser G & Mager J (1982). The chemistry of favism-inducing compounds. The properties of isouramil and divicine and their reaction with glutathione. European Journal of Biochemistry, 127: 405-409.
    • (1982) European Journal of Biochemistry , vol.127 , pp. 405-409
    • Chevion, M.1    Navok, T.2    Glaser, G.3    Mager, J.4
  • 13
    • 0000016355 scopus 로고
    • The porphyrias
    • Stanbury JB, Wyngaarden JB, Frederickson DS, Goldstein JL & Brown MS (Editors), McGraw-Hill, New York
    • Kappas A, Sassa S & Anderson KE (1983). The porphyrias. In: Stanbury JB, Wyngaarden JB, Frederickson DS, Goldstein JL & Brown MS (Editors), The Metabolic Basis of Inherited Diseases. McGraw-Hill, New York, 1301-1384.
    • (1983) The Metabolic Basis of Inherited Diseases , pp. 1301-1384
    • Kappas, A.1    Sassa, S.2    Anderson, K.E.3
  • 14
    • 0022916740 scopus 로고
    • The porphyrias: Recent advances
    • Hindmarsh JT (1986). The porphyrias: recent advances. Clinical Chemistry, 32: 1255-1263.
    • (1986) Clinical Chemistry , vol.32 , pp. 1255-1263
    • Hindmarsh, J.T.1
  • 15
    • 0020681875 scopus 로고
    • Hereditary tyrosinemia and the heme biosynthetic pathway. Profound inhibition of d-aminolevulinic acid dehydratase activity by succinylacetone?
    • Sassa S & Kappas A (1983). Hereditary tyrosinemia and the heme biosynthetic pathway. Profound inhibition of d-aminolevulinic acid dehydratase activity by succinylacetone? Journal of Clinical Investigation, 71: 625-634.
    • (1983) Journal of Clinical Investigation , vol.71 , pp. 625-634
    • Sassa, S.1    Kappas, A.2
  • 16
    • 0022969487 scopus 로고
    • Measurement of 5-aminolevulinic acid by reverse phase HPLC and fluorescence detection
    • Minder EI (1986). Measurement of 5-aminolevulinic acid by reverse phase HPLC and fluorescence detection. Clinica Chimica Acta, 161: 11-18.
    • (1986) Clinica Chimica Acta , vol.161 , pp. 11-18
    • Minder, E.I.1
  • 17
    • 0023205969 scopus 로고
    • δ-Aminolevulinic acid in plasma, cerebrospinal fluid, saliva and erythrocytes: Studies in normal, uraemic and porphyric subjects
    • Gorchein A & Weber R (1984). δ-Aminolevulinic acid in plasma, cerebrospinal fluid, saliva and erythrocytes: studies in normal, uraemic and porphyric subjects. Clinical Science, 72: 103-112.
    • (1984) Clinical Science , vol.72 , pp. 103-112
    • Gorchein, A.1    Weber, R.2
  • 19
    • 0025080737 scopus 로고
    • Primary liver carcinoma in two sisters with acute intermittent porphyria
    • Gubler JG, Bergetzi MJ & Meyer UA (1990). Primary liver carcinoma in two sisters with acute intermittent porphyria. American Journal of Medicine, 89: 540-541.
    • (1990) American Journal of Medicine , vol.89 , pp. 540-541
    • Gubler, J.G.1    Bergetzi, M.J.2    Meyer, U.A.3
  • 21
    • 0016245366 scopus 로고
    • Hepatic porphyrias. Cytochemical and ultrastructural studies of liver in acute intermittent porphyrias and porphyria tarda
    • Biempica L, Kosower N, Ma MH & Goldfisher S (1974). Hepatic porphyrias. Cytochemical and ultrastructural studies of liver in acute intermittent porphyrias and porphyria tarda. Archives of Pathology, 98: 336-343.
    • (1974) Archives of Pathology , vol.98 , pp. 336-343
    • Biempica, L.1    Kosower, N.2    Ma, M.H.3    Goldfisher, S.4
  • 22
    • 0018375948 scopus 로고
    • δ-Aminolevulinic acid is a potent agonist for GABA receptors
    • Brennan MJW & Cantrill RC (1979). δ-Aminolevulinic acid is a potent agonist for GABA receptors. Nature, 280: 514-515.
    • (1979) Nature , vol.280 , pp. 514-515
    • Brennan, M.J.W.1    Cantrill, R.C.2
  • 24
    • 0022897006 scopus 로고
    • Interaction between L-threonine dehydrogenase and aminoacetone synthetase and mechanism of aminoacetone production
    • Tressel T, Thompson R, Zieske LR, Menendez MITS & Davis L (1986). Interaction between L-threonine dehydrogenase and aminoacetone synthetase and mechanism of aminoacetone production. Journal of Biological Chemistry, 261: 16428-16437.
    • (1986) Journal of Biological Chemistry , vol.261 , pp. 16428-16437
    • Tressel, T.1    Thompson, R.2    Zieske, L.R.3    Menendez, M.I.T.S.4    Davis, L.5
  • 25
    • 0018144622 scopus 로고
    • Threoninemia - A new metabolic defect
    • Reddi OS (1978). Threoninemia - a new metabolic defect. Journal of Pediatrics, 93: 814-816.
    • (1978) Journal of Pediatrics , vol.93 , pp. 814-816
    • Reddi, O.S.1
  • 26
    • 0016139102 scopus 로고
    • Cri-du-chat syndrome with an increased level of proline and threonine
    • Kühner U, Büsse M & Buchinger G (1974). Cri-du-chat syndrome with an increased level of proline and threonine. Zeitschrift für Kinderheilkunde, 117: 259-264.
    • (1974) Zeitschrift für Kinderheilkunde , vol.117 , pp. 259-264
    • Kühner, U.1    Büsse, M.2    Buchinger, G.3
  • 27
    • 0022547219 scopus 로고
    • Generation of active oxygen species during coupled autoxidation of oxyhemoglobin and δ-aminolevulinic acid
    • Monteiro HP, Abdalla DSP, Faljoni-Alario A & Bechara EJH (1986). Generation of active oxygen species during coupled autoxidation of oxyhemoglobin and δ-aminolevulinic acid. Biochimica et Biophysica Acta, 881: 100-106.
    • (1986) Biochimica et Biophysica Acta , vol.881 , pp. 100-106
    • Monteiro, H.P.1    Abdalla, D.S.P.2    Faljoni-Alario, A.3    Bechara, E.J.H.4
  • 29
    • 0001686122 scopus 로고
    • Nuclear magnetic resonance studies of 5-aminolevulinate demonstrate multiple forms in aqueous solutions
    • Jaffe EK & Rajagopalan JS (1990). Nuclear magnetic resonance studies of 5-aminolevulinate demonstrate multiple forms in aqueous solutions. Bioorganic Chemistry, 18: 381-394.
    • (1990) Bioorganic Chemistry , vol.18 , pp. 381-394
    • Jaffe, E.K.1    Rajagopalan, J.S.2
  • 32
    • 0011876687 scopus 로고
    • Generation of reactive oxygen metabolites and oxidative damage in mitochondria. the role of calcium
    • Jones DP & Lash LH (Editors), Academic Press, New York
    • Vercesi AE & Hoffmann ME (1993). Generation of reactive oxygen metabolites and oxidative damage in mitochondria. The role of calcium. In: Jones DP & Lash LH (Editors), Methods in Toxicology, Vol. 2. Academic Press, New York, 256-265.
    • (1993) Methods in Toxicology , vol.2 , pp. 256-265
    • Vercesi, A.E.1    Hoffmann, M.E.2
  • 33
    • 0027180065 scopus 로고
    • 5-Aminolevulinic acid induces lipid peroxidation of cardiolipin-rich liposomes
    • Oteiza P & Bechara EJH (1993). 5-Aminolevulinic acid induces lipid peroxidation of cardiolipin-rich liposomes. Archives of Biochemistry and Biophysics, 305: 282-287.
    • (1993) Archives of Biochemistry and Biophysics , vol.305 , pp. 282-287
    • Oteiza, P.1    Bechara, E.J.H.2
  • 34
    • 8944255851 scopus 로고
    • 2+ in the process of mitochondrial damage associated with oxidative stress
    • 2+ in the process of mitochondrial damage associated with oxidative stress. Quimica Nova, 16: 381-384.
    • (1993) Quimica Nova , vol.16 , pp. 381-384
    • Vercesi, A.E.1
  • 37
    • 0029929578 scopus 로고    scopus 로고
    • The prooxidant effect of 5-aminolevulinic acid in the brain tissue of rats: Implications in neuropsychiatric manifestations in porphyrias
    • Demasi M, Penatti CAA, DeLucia R & Bechara EJH (1996). The prooxidant effect of 5-aminolevulinic acid in the brain tissue of rats: implications in neuropsychiatric manifestations in porphyrias. Free Radical Biology and Medicine, 20: 291-299.
    • (1996) Free Radical Biology and Medicine , vol.20 , pp. 291-299
    • Demasi, M.1    Penatti, C.A.A.2    DeLucia, R.3    Bechara, E.J.H.4
  • 38
    • 0025900187 scopus 로고
    • Are free radicals involved in lead poisoning?
    • Hermes-Lima M, Pereira B & Bechara EJH (1991). Are free radicals involved in lead poisoning? Xenobiotica, 21: 1085-1090.
    • (1991) Xenobiotica , vol.21 , pp. 1085-1090
    • Hermes-Lima, M.1    Pereira, B.2    Bechara, E.J.H.3
  • 42
    • 1542456692 scopus 로고
    • Induction of strand breakage in DNA by hexose derivatives and carbonyl compounds
    • Morita J (1991). Induction of strand breakage in DNA by hexose derivatives and carbonyl compounds. Agricultural and Biological Chemistry, 55: 2407-2408.
    • (1991) Agricultural and Biological Chemistry , vol.55 , pp. 2407-2408
    • Morita, J.1
  • 43
    • 0025814980 scopus 로고
    • Chemistry and biochemistry of 4-hydroxynonenal, malondialdehyde and related aldehydes
    • Esterbauer H, Schaur RJ & Zollner H (1991). Chemistry and biochemistry of 4-hydroxynonenal, malondialdehyde and related aldehydes. Free Radical Biology and Medicine, 11: 81-128.
    • (1991) Free Radical Biology and Medicine , vol.11 , pp. 81-128
    • Esterbauer, H.1    Schaur, R.J.2    Zollner, H.3
  • 44
    • 0022747775 scopus 로고
    • Chemiluminescent aerobic oxidation of protein adducts with glycolaldehyde catalyzed by horseradish peroxidase
    • Medeiros MHG & Bechara EJH (1986). Chemiluminescent aerobic oxidation of protein adducts with glycolaldehyde catalyzed by horseradish peroxidase. Archives of Biochemistry and Biophysics, 248: 435-439.
    • (1986) Archives of Biochemistry and Biophysics , vol.248 , pp. 435-439
    • Medeiros, M.H.G.1    Bechara, E.J.H.2
  • 45
    • 0028152621 scopus 로고
    • 5-Aminolevulinic acid mediates the in vivo and in vitro formation of 8-hydroxy-2′-deoxyguanosine in DNA
    • Fraga C, Onuki J, Lucesoli F, Bechara EJH & Di Mascio P (1994). 5-Aminolevulinic acid mediates the in vivo and in vitro formation of 8-hydroxy-2′-deoxyguanosine in DNA. Carcinogenesis, 15: 2241-2244.
    • (1994) Carcinogenesis , vol.15 , pp. 2241-2244
    • Fraga, C.1    Onuki, J.2    Lucesoli, F.3    Bechara, E.J.H.4    Di Mascio, P.5
  • 46
    • 0026057381 scopus 로고
    • Damage to rat liver mitochondria promoted by 8-aminolevulinic acid-generated reactive oxygen species: Connections with acute intermittent porphyria and lead poisoning
    • Hermes-Lima M, Valle VGR, Vercesi AE & Bechara EJH (1991). Damage to rat liver mitochondria promoted by 8-aminolevulinic acid-generated reactive oxygen species: connections with acute intermittent porphyria and lead poisoning. Biochimica et Biophysics Acta, 1056: 57-63.
    • (1991) Biochimica et Biophysics Acta , vol.1056 , pp. 57-63
    • Hermes-Lima, M.1    Valle, V.G.R.2    Vercesi, A.E.3    Bechara, E.J.H.4
  • 50
    • 0026970483 scopus 로고
    • The role of an endogenous nonheme iron in microsomal redox reactions
    • Minotti G (1992). The role of an endogenous nonheme iron in microsomal redox reactions. Archives of Biochemistry and Biophysics, 297: 189-192.
    • (1992) Archives of Biochemistry and Biophysics , vol.297 , pp. 189-192
    • Minotti, G.1
  • 51
    • 0023814191 scopus 로고
    • Menadione-treated synaptosomes as a model for post-ischemic neuronal damage
    • White EJ & Clark JB (1988). Menadione-treated synaptosomes as a model for post-ischemic neuronal damage. Biochemical Journal, 253: 425-433.
    • (1988) Biochemical Journal , vol.253 , pp. 425-433
    • White, E.J.1    Clark, J.B.2
  • 52
    • 0011396345 scopus 로고
    • Calcium and lipid peroxidation
    • Halliwell B (Editor), UpJohn Co., Michigan
    • Braughler JM (1987). Calcium and lipid peroxidation. In: Halliwell B (Editor), Proceedings of the UpJohn Symposium. UpJohn Co., Michigan, 99-104.
    • (1987) Proceedings of the UpJohn Symposium , pp. 99-104
    • Braughler, J.M.1
  • 53
    • 0002621776 scopus 로고
    • Clinical aspects of the dosage of erythrocuprein
    • Michelson AM, McCord JM & Fridovich I (Editors), Academic Press, New York
    • Michelson AM, Puget K, Durosay P & Bouneau JC (1977). Clinical aspects of the dosage of erythrocuprein. In: Michelson AM, McCord JM & Fridovich I (Editors), Superoxide and Superoxide Dismutases. Academic Press, New York, 467-499
    • (1977) Superoxide and Superoxide Dismutases , pp. 467-499
    • Michelson, A.M.1    Puget, K.2    Durosay, P.3    Bouneau, J.C.4
  • 54
    • 0347077691 scopus 로고
    • Dosage de la superoxyde dismutase plaquettaire dans les psychoses infantiles de développement
    • Glose B, Debray-Ritzen P, Puget K & Michelson AM (1977). Dosage de la superoxyde dismutase plaquettaire dans les psychoses infantiles de développement. Nouvelle Presse Medicale, 6: 2449.
    • (1977) Nouvelle Presse Medicale , vol.6 , pp. 2449
    • Glose, B.1    Debray-Ritzen, P.2    Puget, K.3    Michelson, A.M.4
  • 55
    • 0020006488 scopus 로고
    • Superoxide dismutase, glutathione peroxidase and catalase activities in the erythrocytes of patients with intermittent acute porphyria
    • Medeiros MHG, Marchiori PE & Bechara EJH (1982). Superoxide dismutase, glutathione peroxidase and catalase activities in the erythrocytes of patients with intermittent acute porphyria. Clinical Chemistry, 28: 242.
    • (1982) Clinical Chemistry , vol.28 , pp. 242
    • Medeiros, M.H.G.1    Marchiori, P.E.2    Bechara, E.J.H.3
  • 58
    • 0020033113 scopus 로고
    • Lead-hemoglobin interaction as a possible source of reactive oxygen species - A chemiluminescent study
    • Ribarov SR & Bochev PG (1982). Lead-hemoglobin interaction as a possible source of reactive oxygen species - a chemiluminescent study. Archives of Biochemistry and Biophysics, 213: 288-292.
    • (1982) Archives of Biochemistry and Biophysics , vol.213 , pp. 288-292
    • Ribarov, S.R.1    Bochev, P.G.2
  • 59
    • 0016740142 scopus 로고
    • Lead-induced inhibition of brain adenylcyclase
    • Nathanson JA & Bloom FE (1975). Lead-induced inhibition of brain adenylcyclase. Nature, 255: 419-420.
    • (1975) Nature , vol.255 , pp. 419-420
    • Nathanson, J.A.1    Bloom, F.E.2
  • 60
    • 0023782910 scopus 로고
    • Action of lead(II) and aluminum(III) on iron-stimulated lipid peroxidation in liposomes, erythrocytes and rat liver microsomal fractions
    • Quinlan GJ, Halliwell B, Moorhouse CP & Gutteridge JMC (1988). Action of lead(II) and aluminum(III) on iron-stimulated lipid peroxidation in liposomes, erythrocytes and rat liver microsomal fractions. Biochimica et Biophysics Acta, 962: 196-200.
    • (1988) Biochimica et Biophysics Acta , vol.962 , pp. 196-200
    • Quinlan, G.J.1    Halliwell, B.2    Moorhouse, C.P.3    Gutteridge, J.M.C.4
  • 61
    • 0017927528 scopus 로고
    • Hemes, chlorophylls and related compounds: Biosynthesis
    • Granick S & Beale SI (1978). Hemes, chlorophylls and related compounds: biosynthesis. Advances in Enzymology, 46: 33-203.
    • (1978) Advances in Enzymology , vol.46 , pp. 33-203
    • Granick, S.1    Beale, S.I.2
  • 62
    • 0026547563 scopus 로고
    • 5-Aminolevulinic acid-induced alterations of oxidative metabolism in sedentary and exercise-trained rats
    • Pereira B, Curi R, Kokubun E & Bechara EJH (1992). 5-Aminolevulinic acid-induced alterations of oxidative metabolism in sedentary and exercise-trained rats. Journal of Applied Physiology, 72: 226-230.
    • (1992) Journal of Applied Physiology , vol.72 , pp. 226-230
    • Pereira, B.1    Curi, R.2    Kokubun, E.3    Bechara, E.J.H.4
  • 66
    • 0024520294 scopus 로고
    • On the participation of higher oxidation states of iron and copper in Fenton reactions
    • Sutton HC & Winterbourn CC (1989). On the participation of higher oxidation states of iron and copper in Fenton reactions. Free Radical Biology and Medicine, 6: 53-60.
    • (1989) Free Radical Biology and Medicine , vol.6 , pp. 53-60
    • Sutton, H.C.1    Winterbourn, C.C.2
  • 68
    • 0011222344 scopus 로고
    • Hydroxyl radical formation in biological systems
    • Yamazaki I (1993). Hydroxyl radical formation in biological systems. Química Nova, 16: 365-369.
    • (1993) Química Nova , vol.16 , pp. 365-369
    • Yamazaki, I.1
  • 69
    • 0026673757 scopus 로고
    • Coordination of cellular iron metabolism by posttranscriptional gene regulation
    • Khun LC & Hentze MW (1992). Coordination of cellular iron metabolism by posttranscriptional gene regulation. Journal of Inorganic Chemistry, 47: 183-193.
    • (1992) Journal of Inorganic Chemistry , vol.47 , pp. 183-193
    • Khun, L.C.1    Hentze, M.W.2
  • 70
    • 0027452550 scopus 로고
    • Regulating the fate of mRNA: The control of cellular iron metabolism
    • Klawsner RD, Rovalt TA & Harford JB (1993). Regulating the fate of mRNA: the control of cellular iron metabolism. Cell, 72: 19-28.
    • (1993) Cell , vol.72 , pp. 19-28
    • Klawsner, R.D.1    Rovalt, T.A.2    Harford, J.B.3
  • 71
  • 73
    • 0022899021 scopus 로고
    • Activities of superoxide dismutase and glutathione peroxidase in schizophrenic and manic-depressive patients
    • Abdalla DSP, Monteiro HP, Oliveira JAC & Bechara EJH (1986). Activities of superoxide dismutase and glutathione peroxidase in schizophrenic and manic-depressive patients. Clinical Chemistry, 32: 805-807.
    • (1986) Clinical Chemistry , vol.32 , pp. 805-807
    • Abdalla, D.S.P.1    Monteiro, H.P.2    Oliveira, J.A.C.3    Bechara, E.J.H.4
  • 74
    • 0006480055 scopus 로고
    • Oxidative stress in brain caused by 6-hydroxydopamine: A model for schizophrenia
    • Hayaishi O, Niki E, Kondo M & Yoshikawa T (Editors), Elsevier, Amsterdam
    • Abdalla DSP, Monteiro HP & Bechara EJH (1989). Oxidative stress in brain caused by 6-hydroxydopamine: a model for schizophrenia. In: Hayaishi O, Niki E, Kondo M & Yoshikawa T (Editors), Medical, Biochemical and Chemical Aspects of Free Radicals. Elsevier, Amsterdam, 1245-1248
    • (1989) Medical, Biochemical and Chemical Aspects of Free Radicals , pp. 1245-1248
    • Abdalla, D.S.P.1    Monteiro, H.P.2    Bechara, E.J.H.3
  • 75
    • 0028916715 scopus 로고
    • Free radical-generated neurotoxicity of 6-hydroxydopamine
    • Kumar R, Agarwal AK & Seth PK (1995). Free radical-generated neurotoxicity of 6-hydroxydopamine. Journal of Neurochemistry, 64: 1703-1707.
    • (1995) Journal of Neurochemistry , vol.64 , pp. 1703-1707
    • Kumar, R.1    Agarwal, A.K.2    Seth, P.K.3
  • 76
    • 0026630568 scopus 로고
    • Hydroxylated metabolites of the antimalarial drug primaquine: Oxidation and redox cycling
    • Vásquez Vivar J & Augusto O (1992). Hydroxylated metabolites of the antimalarial drug primaquine: oxidation and redox cycling. Journal of Biological Chemistry, 267: 6848-6854
    • (1992) Journal of Biological Chemistry , vol.267 , pp. 6848-6854
    • Vásquez Vivar, J.1    Augusto, O.2
  • 78
    • 0000201350 scopus 로고
    • Oxidative damage induced by metals without redox capacity in biological systems
    • Oteiza PI, Verstraeten SV & Adonaylo VN (1995). Oxidative damage induced by metals without redox capacity in biological systems. Ciência e Cultura, 47: 330-335.
    • (1995) Ciência e Cultura , vol.47 , pp. 330-335
    • Oteiza, P.I.1    Verstraeten, S.V.2    Adonaylo, V.N.3


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