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Volumn 71, Issue 6, 1998, Pages 2497-2504

Protective properties of tin- and manganese-centered porphyrins against hydrogen peroxide-mediated injury in rat astroglial cells

Author keywords

Heme oxygenase; Hydrogen peroxide; Manganese superoxide dismutase mimetic; Metalloporphyrin; Oxidative injury; Superoxide dismutase

Indexed keywords

HEME OXYGENASE; HYDROGEN PEROXIDE; MESOPORPHYRIN TIN; PORPHYRIN DERIVATIVE; SUPEROXIDE DISMUTASE; TETRAKIS(1 METHYL 4 PYRIDYL)PORPHYRIN MANGANESE; UNCLASSIFIED DRUG;

EID: 0031792792     PISSN: 00223042     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1471-4159.1998.71062497.x     Document Type: Article
Times cited : (34)

References (54)
  • 1
    • 0029156942 scopus 로고
    • Transfection of the human heme oxygenase gene into rabbit coronary microvessel endothelial cells: Protective effect against heme and hemoglobin toxicity
    • Abraham N. G., Lavrovsky Y., Schwartzman M. L., Levere R. D., Gerritsen M. E., Shibahara S., and Kappas A. (1995) Transfection of the human heme oxygenase gene into rabbit coronary microvessel endothelial cells: protective effect against heme and hemoglobin toxicity. Proc. Natl. Acad. Sci. USA 92, 6798-6802.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 6798-6802
    • Abraham, N.G.1    Lavrovsky, Y.2    Schwartzman, M.L.3    Levere, R.D.4    Gerritsen, M.E.5    Shibahara, S.6    Kappas, A.7
  • 3
    • 0022361141 scopus 로고
    • Neoplastic transformation of newborn rat astrocytes in culture
    • Bressler J. P. and de Vellis J. (1985) Neoplastic transformation of newborn rat astrocytes in culture. Brain Res. 348, 21-27.
    • (1985) Brain Res. , vol.348 , pp. 21-27
    • Bressler, J.P.1    De Vellis, J.2
  • 5
    • 0029555770 scopus 로고
    • A metalloporphyrin superoxide dismutase mimetic protects against paraquat-induced endothelial cell injury, in vitro
    • Day B. J., Shawen S., Liochev S. I., and Crapo J. D. (1995) A metalloporphyrin superoxide dismutase mimetic protects against paraquat-induced endothelial cell injury, in vitro. J. Pharmacol. Exp. Ther. 275, 1227-1232.
    • (1995) J. Pharmacol. Exp. Ther. , vol.275 , pp. 1227-1232
    • Day, B.J.1    Shawen, S.2    Liochev, S.I.3    Crapo, J.D.4
  • 6
    • 0031573475 scopus 로고    scopus 로고
    • Manganic porphyrins possess catalase activity and protect endothelial cells against hydrogen peroxide-mediated injury
    • Day B. J., Fridovich I., and Crapo J. D. (1997) Manganic porphyrins possess catalase activity and protect endothelial cells against hydrogen peroxide-mediated injury. Arch. Biochem. Biophys. 15, 256-262.
    • (1997) Arch. Biochem. Biophys. , vol.15 , pp. 256-262
    • Day, B.J.1    Fridovich, I.2    Crapo, J.D.3
  • 8
    • 0029990439 scopus 로고    scopus 로고
    • Astrocytes protect neurons from hydrogen peroxide injury
    • Desagher S., Glowinski J., and Premont J. (1996) Astrocytes protect neurons from hydrogen peroxide injury. J. Neurosci. 16, 2553-2562.
    • (1996) J. Neurosci. , vol.16 , pp. 2553-2562
    • Desagher, S.1    Glowinski, J.2    Premont, J.3
  • 9
    • 0023654957 scopus 로고
    • 4 vinyl groups of Sn-protoporphyrin to form Sn-mesoporphyrin markedly enhances the ability of the metalloporphyrin to inhibit in vivo heme catabolism
    • 4 vinyl groups of Sn-protoporphyrin to form Sn-mesoporphyrin markedly enhances the ability of the metalloporphyrin to inhibit in vivo heme catabolism. Arch. Biochem. Biophys. 255, 64-74.
    • (1987) Arch. Biochem. Biophys. , vol.255 , pp. 64-74
    • Drummond, G.S.1    Galbraith, R.A.2    Sardana, M.K.3    Kappas, A.4
  • 10
    • 0024804210 scopus 로고
    • Effects of tin-porphyrins on developmental changes in hepatic cytochrome P450 content, selected P450-dependent drug-metabolizing enzyme activities and brain glutathione levels in the newborn rat
    • Drummond G. S., Rosenberg D. W., Kihlstrom-Johanson A. C., and Kappas A. (1989) Effects of tin-porphyrins on developmental changes in hepatic cytochrome P450 content, selected P450-dependent drug-metabolizing enzyme activities and brain glutathione levels in the newborn rat. Pharmacology 39, 273-284.
    • (1989) Pharmacology , vol.39 , pp. 273-284
    • Drummond, G.S.1    Rosenberg, D.W.2    Kihlstrom-Johanson, A.C.3    Kappas, A.4
  • 11
    • 0026479335 scopus 로고
    • Heme oxygenase is a heat shock protein and PEST protein in rat astroglial cells
    • Dwyer B. E., Nishimura R. N., de Vellis J., and Yoshida T. (1992) Heme oxygenase is a heat shock protein and PEST protein in rat astroglial cells. Glia 5, 300-305.
    • (1992) Glia , vol.5 , pp. 300-305
    • Dwyer, B.E.1    Nishimura, R.N.2    De Vellis, J.3    Yoshida, T.4
  • 12
    • 0028929896 scopus 로고
    • Differential expression of heme oxygenase-1 in cultured cortical neurons and astrocytes determined by the aid of a new heme oxygenase antibody. Response to oxidative stress
    • Dwyer B. E., Nishimura R. N., and Lu S.-Y. (1995a) Differential expression of heme oxygenase-1 in cultured cortical neurons and astrocytes determined by the aid of a new heme oxygenase antibody. Response to oxidative stress. Mol. Brain Res. 30, 37-47.
    • (1995) Mol. Brain Res. , vol.30 , pp. 37-47
    • Dwyer, B.E.1    Nishimura, R.N.2    Lu, S.-Y.3
  • 13
    • 0029040352 scopus 로고
    • Differential localization of heme oxygenase and NADPH-diaphorase in spinal cord neurons
    • Dwyer B. E., Nishimura R. N., and Lu S.-Y. (1995b) Differential localization of heme oxygenase and NADPH-diaphorase in spinal cord neurons. Neuroreport 6, 973-976.
    • (1995) Neuroreport , vol.6 , pp. 973-976
    • Dwyer, B.E.1    Nishimura, R.N.2    Lu, S.-Y.3
  • 14
    • 0029934141 scopus 로고    scopus 로고
    • Transient induction of heme oxygenase after cortical stab wound injury
    • Dwyer B. E., Nishimura R. N., Lu S.-Y., and Alcaraz A. (1996) Transient induction of heme oxygenase after cortical stab wound injury. Mol. Brain Res. 38, 251-259.
    • (1996) Mol. Brain Res. , vol.38 , pp. 251-259
    • Dwyer, B.E.1    Nishimura, R.N.2    Lu, S.-Y.3    Alcaraz, A.4
  • 15
    • 0027054312 scopus 로고
    • In situ hybridization and immunohistochemical localization of heme oxygenase-2 mRNA in normal rat brain: Differential distribution of isozyme 1 and 2
    • Ewing J. F. and Maines M. D. (1992) In situ hybridization and immunohistochemical localization of heme oxygenase-2 mRNA in normal rat brain: differential distribution of isozyme 1 and 2. Mol. Cell. Neurosci. 3, 559-570.
    • (1992) Mol. Cell. Neurosci. , vol.3 , pp. 559-570
    • Ewing, J.F.1    Maines, M.D.2
  • 16
    • 0027989826 scopus 로고
    • Stable Mn(III) porphyrins mimic superoxide dismutase in vitro and substitute for it in vivo
    • Faulkner K. M., Liochev S. I., and Fridovich I. (1994) Stable Mn(III) porphyrins mimic superoxide dismutase in vitro and substitute for it in vivo. J. Biol. Chem. 269, 23471-23476.
    • (1994) J. Biol. Chem. , vol.269 , pp. 23471-23476
    • Faulkner, K.M.1    Liochev, S.I.2    Fridovich, I.3
  • 17
    • 0021288878 scopus 로고
    • Superoxide dismutase assays
    • Flohe L. and Otting F. (1984) Superoxide dismutase assays. Methods Enzymol. 105, 93-104.
    • (1984) Methods Enzymol. , vol.105 , pp. 93-104
    • Flohe, L.1    Otting, F.2
  • 19
    • 0021275463 scopus 로고
    • Regulation of soluble guanylate cyclase activity by porphyrins and metalloporphyrins
    • Ignarro L. J., Ballot B., and Wood K. S. (1984) Regulation of soluble guanylate cyclase activity by porphyrins and metalloporphyrins. J. Biol. Chem. 259, 6201-6207.
    • (1984) J. Biol. Chem. , vol.259 , pp. 6201-6207
    • Ignarro, L.J.1    Ballot, B.2    Wood, K.S.3
  • 20
    • 0029016090 scopus 로고
    • Preischemic but not postischemic zinc protoporphyrin treatment reduces infarct size and edema accumulation after temporary focal cerebral ischemia in rats
    • Kadoya C., Domino E. F., Yang G.-Y., Stern J. D., and Betz A. L. (1995) Preischemic but not postischemic zinc protoporphyrin treatment reduces infarct size and edema accumulation after temporary focal cerebral ischemia in rats. Stroke 26, 1035-1038.
    • (1995) Stroke , vol.26 , pp. 1035-1038
    • Kadoya, C.1    Domino, E.F.2    Yang, G.-Y.3    Stern, J.D.4    Betz, A.L.5
  • 21
    • 0030465238 scopus 로고    scopus 로고
    • Superoxide accelerates DNA damage by elevating free-iron-levels
    • Keyer K. and Imlay J. A. (1996) Superoxide accelerates DNA damage by elevating free-iron-levels. Proc. Natl. Acad. Sci. USA 93, 13635-13640.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 13635-13640
    • Keyer, K.1    Imlay, J.A.2
  • 22
    • 0028871420 scopus 로고
    • Superoxide and the production of oxidative DNA damage
    • Keyer K., Gort A. S., and Imlay J. A. (1995) Superoxide and the production of oxidative DNA damage. J. Bacteriol. 177, 6782-6790.
    • (1995) J. Bacteriol. , vol.177 , pp. 6782-6790
    • Keyer, K.1    Gort, A.S.2    Imlay, J.A.3
  • 23
    • 0029133298 scopus 로고
    • A sensitive microassay reveals marked regional differences in the capacity of rat brain to generate carbon monoxide
    • Laitinen J. T. and Juvonen R. O. (1995) A sensitive microassay reveals marked regional differences in the capacity of rat brain to generate carbon monoxide. Brain Res. 694, 246-252.
    • (1995) Brain Res. , vol.694 , pp. 246-252
    • Laitinen, J.T.1    Juvonen, R.O.2
  • 24
    • 0029814162 scopus 로고    scopus 로고
    • Over-expression of heme oxygenase-1 in human pulmonary epithelial cells results in cell growth arrest and increased resistance to hyperoxia
    • Lee P. J., Alam J., Wiegand G. W., and Choi A. M. K. (1996) Over-expression of heme oxygenase-1 in human pulmonary epithelial cells results in cell growth arrest and increased resistance to hyperoxia. Proc. Natl. Acad. Sci. USA 93, 10393-10398.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 10393-10398
    • Lee, P.J.1    Alam, J.2    Wiegand, G.W.3    Choi, A.M.K.4
  • 26
    • 0028176233 scopus 로고
    • Metalloporphyrins inhibit nitric oxide-dependent cGMP formation in vivo
    • Luo D. and Vincent S. R. (1994) Metalloporphyrins inhibit nitric oxide-dependent cGMP formation in vivo. Eur. J. Pharmacol. 267, 263-267.
    • (1994) Eur. J. Pharmacol. , vol.267 , pp. 263-267
    • Luo, D.1    Vincent, S.R.2
  • 27
    • 0031935122 scopus 로고    scopus 로고
    • Endogenous superoxide dismutase levels regulate iron-dependent hydroxyl radical formation in Escherichia coli exposed to hydrogen peroxide
    • McCormick M. L., Buettner G. R., and Britigan B. E. (1998) Endogenous superoxide dismutase levels regulate iron-dependent hydroxyl radical formation in Escherichia coli exposed to hydrogen peroxide. J. Bacteriol. 180, 622-625.
    • (1998) J. Bacteriol. , vol.180 , pp. 622-625
    • McCormick, M.L.1    Buettner, G.R.2    Britigan, B.E.3
  • 28
    • 0028331627 scopus 로고
    • The structure, organization and differential expression of the gene encoding rat heme oxygenase-2
    • McCoubrey W. K. Jr. and Maines M. D. (1994) The structure, organization and differential expression of the gene encoding rat heme oxygenase-2. Gene 139, 155-161.
    • (1994) Gene , vol.139 , pp. 155-161
    • McCoubrey Jr., W.K.1    Maines, M.D.2
  • 29
    • 8544246393 scopus 로고    scopus 로고
    • Isolation and characterization of a cDNA from the rat brain that encodes hemoprotein heme oxygenase-3
    • McCoubrey W. K. Jr., Huang T. J., and Maines M. D. (1997) Isolation and characterization of a cDNA from the rat brain that encodes hemoprotein heme oxygenase-3. Eur. J. Biochem. 247, 725-732.
    • (1997) Eur. J. Biochem. , vol.247 , pp. 725-732
    • McCoubrey Jr., W.K.1    Huang, T.J.2    Maines, M.D.3
  • 30
    • 0030065052 scopus 로고    scopus 로고
    • NO-mediated activation of heme oxygenase: Endogenous cytoprotection against oxidative stress to endothelium
    • Motterlini M. K., Foresti R., Intaglietta M., and Winslow R. M. (1996) NO-mediated activation of heme oxygenase: endogenous cytoprotection against oxidative stress to endothelium. Am. J. Physiol. 39, H107-H114.
    • (1996) Am. J. Physiol. , vol.39
    • Motterlini, M.K.1    Foresti, R.2    Intaglietta, M.3    Winslow, R.M.4
  • 32
    • 0025128370 scopus 로고
    • Hydrogen peroxide release from human polymorphonuclear leukocytes measured with horseradish peroxidase and o-dianisidine. Effect of various stimulators and cytochalasin B
    • Nowak D. (1990) Hydrogen peroxide release from human polymorphonuclear leukocytes measured with horseradish peroxidase and o-dianisidine. Effect of various stimulators and cytochalasin B. Biomed. Biochim. Acta 5, 353-362.
    • (1990) Biomed. Biochim. Acta , vol.5 , pp. 353-362
    • Nowak, D.1
  • 33
    • 0029984735 scopus 로고    scopus 로고
    • Ultrastructural consequences of radical damage before and after differentiation of neuroblastoma B-104 cells
    • O'Neil B. J., Alousi S. S., White B. C., and Rafols J. A. (1996) Ultrastructural consequences of radical damage before and after differentiation of neuroblastoma B-104 cells. Acta Neuropathol. 92, 75-89.
    • (1996) Acta Neuropathol. , vol.92 , pp. 75-89
    • O'Neil, B.J.1    Alousi, S.S.2    White, B.C.3    Rafols, J.A.4
  • 34
    • 0029410648 scopus 로고
    • Hemoglobin provides protection against lethal endotoxemia in rats: The role of heme oxygenase-1
    • Otterbein L., Sylvester S. L., and Choi A. M. K. (1995) Hemoglobin provides protection against lethal endotoxemia in rats: the role of heme oxygenase-1. Am. J. Respir. Cell Mol. Biol. 13, 595-601.
    • (1995) Am. J. Respir. Cell Mol. Biol. , vol.13 , pp. 595-601
    • Otterbein, L.1    Sylvester, S.L.2    Choi, A.M.K.3
  • 35
    • 0029865404 scopus 로고    scopus 로고
    • Neuroprotection against CA1 injury with metalloporphyrins
    • Panizzon K. L., Dwyer B. E., Nishimura R. N., and Wallis R. A. (1996) Neuroprotection against CA1 injury with metalloporphyrins. Neuroreport 7, 662-666.
    • (1996) Neuroreport , vol.7 , pp. 662-666
    • Panizzon, K.L.1    Dwyer, B.E.2    Nishimura, R.N.3    Wallis, R.A.4
  • 36
  • 37
    • 0031977242 scopus 로고    scopus 로고
    • Molecular actions of a Mn (III) porphyrin superoxide dismutase mimetic and peroxynitrite scavenger: Reaction with nitric oxide and direct inhibition of NO synthase and soluble guanylyl cyclase
    • Pfeiffer S., Schrammel A., Koesling D., Schmidt K., and Mayer B. (1998) Molecular actions of a Mn (III) porphyrin superoxide dismutase mimetic and peroxynitrite scavenger: reaction with nitric oxide and direct inhibition of NO synthase and soluble guanylyl cyclase. Mol. Pharmacol. 53, 795-800.
    • (1998) Mol. Pharmacol. , vol.53 , pp. 795-800
    • Pfeiffer, S.1    Schrammel, A.2    Koesling, D.3    Schmidt, K.4    Mayer, B.5
  • 39
    • 0031579657 scopus 로고    scopus 로고
    • Regulation of heme oxygenase-2 by glucocorticoids in neonatal rat brain: Characterization of a functional glucocorticoid response element
    • Raju V. S., McCoubrey W. K. Jr., and Maines M. D. (1997) Regulation of heme oxygenase-2 by glucocorticoids in neonatal rat brain: characterization of a functional glucocorticoid response element. Biochim. Biophys. Acta 1351, 89-104.
    • (1997) Biochim. Biophys. Acta , vol.1351 , pp. 89-104
    • Raju, V.S.1    McCoubrey Jr., W.K.2    Maines, M.D.3
  • 40
    • 0026526023 scopus 로고
    • Ferritin as a source of iron for oxidative damage
    • Reif D. W. (1992) Ferritin as a source of iron for oxidative damage. Free Radic. Biol. Med. 12, 417-427.
    • (1992) Free Radic. Biol. Med. , vol.12 , pp. 417-427
    • Reif, D.W.1
  • 41
    • 0012151673 scopus 로고
    • Dual control mechanism for heme oxygenase: Tin(IV)-protoporphyrin potently inhibits enzyme activity while markedly increasing content of enzyme protein in liver
    • Sardana M. K. and Kappas A. (1987) Dual control mechanism for heme oxygenase: tin(IV)-protoporphyrin potently inhibits enzyme activity while markedly increasing content of enzyme protein in liver. Proc. Natl. Acad. Sci. USA 84, 2464-2468.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 2464-2468
    • Sardana, M.K.1    Kappas, A.2
  • 42
    • 0024582076 scopus 로고
    • Manipulation of cytochrome P450 dependent renal thromboxane synthase activity in spontaneously hypertensive rats
    • Sessa W. C., Abraham N. G., Escalante B., and Schwartzman M. L. (1989) Manipulation of cytochrome P450 dependent renal thromboxane synthase activity in spontaneously hypertensive rats. J. Hypertens. 7, 37-42.
    • (1989) J. Hypertens. , vol.7 , pp. 37-42
    • Sessa, W.C.1    Abraham, N.G.2    Escalante, B.3    Schwartzman, M.L.4
  • 43
    • 0023665016 scopus 로고
    • Transcriptional control of rat heme oxygenase by heat shock
    • Shibahara S., Muller R. M., and Taguchi H. (1987) Transcriptional control of rat heme oxygenase by heat shock. J. Biol. Chem. 262, 12889-12892.
    • (1987) J. Biol. Chem. , vol.262 , pp. 12889-12892
    • Shibahara, S.1    Muller, R.M.2    Taguchi, H.3
  • 44
    • 0025012990 scopus 로고
    • Manganese-dependent disproportionation of hydrogen peroxide in bicarbonate buffer
    • Stadtman E. R., Berlett B. S., and Chock P. B. (1990) Manganese-dependent disproportionation of hydrogen peroxide in bicarbonate buffer. Proc. Natl. Acad. Sci. USA 87, 384-388.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 384-388
    • Stadtman, E.R.1    Berlett, B.S.2    Chock, P.B.3
  • 45
    • 0028875489 scopus 로고
    • Novel protective effect of manganese against ferrous citrate-induced lipid peroxidation and nigrostriatal neurodegeneration in vivo
    • Sziraki I., Rauhala P., and Chiueh C. C. (1995) Novel protective effect of manganese against ferrous citrate-induced lipid peroxidation and nigrostriatal neurodegeneration in vivo. Brain Res. 698, 285-287.
    • (1995) Brain Res. , vol.698 , pp. 285-287
    • Sziraki, I.1    Rauhala, P.2    Chiueh, C.C.3
  • 46
    • 0029041226 scopus 로고
    • Lethal oxidative damage and mutagenesis are generated by iron in delta fur mutants of Escherichia coli: Protective role for superoxide dismutase
    • Touati D., Jacques M., Tardat B., Bouchard L., and Despied S. (1995) Lethal oxidative damage and mutagenesis are generated by iron in delta fur mutants of Escherichia coli: protective role for superoxide dismutase. J. Bacteriol. 177, 2305-2314.
    • (1995) J. Bacteriol. , vol.177 , pp. 2305-2314
    • Touati, D.1    Jacques, M.2    Tardat, B.3    Bouchard, L.4    Despied, S.5
  • 47
    • 0023831291 scopus 로고
    • Resolution of the rat brain heme oxygenase activity: Absence of a detectable amount of the inducible form (HO-1)
    • Trakshel G. M., Kutty R. K., and Maines M. D. (1988) Resolution of the rat brain heme oxygenase activity: absence of a detectable amount of the inducible form (HO-1). Arch. Biochem. Biophys. 260, 732-739.
    • (1988) Arch. Biochem. Biophys. , vol.260 , pp. 732-739
    • Trakshel, G.M.1    Kutty, R.K.2    Maines, M.D.3
  • 48
    • 0028069329 scopus 로고
    • Control of jaundice in preterm newborns by an inhibitor of bilirubin production: Studies with tin-mesoporphyrin
    • Valaes T., Petmezaki S., Henschke C., Drummond G. S., and Kappas A (1994) Control of jaundice in preterm newborns by an inhibitor of bilirubin production: studies with tin-mesoporphyrin. Pediatrics 93, 1-11.
    • (1994) Pediatrics , vol.93 , pp. 1-11
    • Valaes, T.1    Petmezaki, S.2    Henschke, C.3    Drummond, G.S.4    Kappas, A.5
  • 50
    • 0028300334 scopus 로고
    • Heme oxygenase-1 mediates an adaptive response to oxidative stress in human skin fibroblasts
    • Vile G. F., Basu-Modak S., Waltner C., and Tyrrell R. M. (1994) Heme oxygenase-1 mediates an adaptive response to oxidative stress in human skin fibroblasts. Proc. Natl. Acad. Sci. USA 91, 2607-2610.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 2607-2610
    • Vile, G.F.1    Basu-Modak, S.2    Waltner, C.3    Tyrrell, R.M.4
  • 51
    • 0344367490 scopus 로고    scopus 로고
    • Tin-mesoporphyrin reduces intracerebral "mass" in a pig intracerebral hemorrhage model
    • Wagner K., Dwyer B. E., Hua Y., Cody M., Broderick J., and Brott T (1998) Tin-mesoporphyrin reduces intracerebral "mass" in a pig intracerebral hemorrhage model. (Abstr.) Stroke 29, 332.
    • (1998) Stroke , vol.29 , pp. 332
    • Wagner, K.1    Dwyer, B.E.2    Hua, Y.3    Cody, M.4    Broderick, J.5    Brott, T.6
  • 52
    • 0027936877 scopus 로고
    • Corticosterone regulates heme oxygenase-2 and NO synthase transcription and protein expression in rat brain
    • Weber C. M., Eke B. C., and Maines M. D. (1994) Corticosterone regulates heme oxygenase-2 and NO synthase transcription and protein expression in rat brain. J. Neurochem. 63, 953-962.
    • (1994) J. Neurochem. , vol.63 , pp. 953-962
    • Weber, C.M.1    Eke, B.C.2    Maines, M.D.3
  • 53
    • 0030045835 scopus 로고    scopus 로고
    • Heme oxygenase: A novel target for the modulation of the inflammatory response
    • Willis D., Moore A. R., Frederick R., and Willoughby D. A. (1996) Heme oxygenase: a novel target for the modulation of the inflammatory response. Nat. Med. 2, 87-90.
    • (1996) Nat. Med. , vol.2 , pp. 87-90
    • Willis, D.1    Moore, A.R.2    Frederick, R.3    Willoughby, D.A.4
  • 54
    • 0031032817 scopus 로고    scopus 로고
    • Mitochondrial DNA damage is more extensive and persists longer than nuclear DNA damage in human cells following oxidative stress
    • Yakes F. M. and Van Houten B. (1997) Mitochondrial DNA damage is more extensive and persists longer than nuclear DNA damage in human cells following oxidative stress. Proc. Natl. Acad. Sci. USA 94, 514-519.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 514-519
    • Yakes, F.M.1    Van Houten, B.2


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