메뉴 건너뛰기




Volumn 38, Issue 11, 2005, Pages 1458-1470

Erratum: Heterozygous deficiency of manganese superoxide dismutase results in severe lipid peroxidation and spontaneous apoptosis in murine myocardium in vivo (Free Radical Biology and Medicine (2005) 38 (1458-1470) DOI: 10.1016/j.freeradbiomed.2005.02.009);Heterozygous deficiency of manganese superoxide dismutase results in severe lipid peroxidation and spontaneous apoptosis in murine myocardium in vivo

Author keywords

Apoptosis; Copper, zinc superoxide dismutase; Free radicals; Heart tissue; Manganese superoxide dismutase; Mouse model; Reactive oxygen species; Superoxide anion

Indexed keywords

3 NITROTYROSINE; COPPER ZINC SUPEROXIDE DISMUTASE; CYTOKERATIN 14; FAT DROPLET; MANGANESE SUPEROXIDE DISMUTASE; REACTIVE OXYGEN METABOLITE;

EID: 21044450045     PISSN: 08915849     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.freeradbiomed.2005.09.010     Document Type: Erratum
Times cited : (101)

References (72)
  • 4
    • 84985570313 scopus 로고
    • Biochemistry of oxidative stress
    • H. Sies Biochemistry of oxidative stress Angew. Chem. 25 1986 1058 1071
    • (1986) Angew. Chem. , vol.25 , pp. 1058-1071
    • Sies, H.1
  • 6
    • 0036832196 scopus 로고    scopus 로고
    • Oxidative stress, DNA damage, and breast cancer
    • D.H. Kang Oxidative stress, DNA damage, and breast cancer AACN Clin. Issues 13 2002 540 549
    • (2002) AACN Clin. Issues , vol.13 , pp. 540-549
    • Kang, D.H.1
  • 8
    • 0002508819 scopus 로고
    • Antioxidant defences. Protection against oxidants in biological systems: The superoxide theory of oxygen toxicity
    • B. Halliwell J.M.C. Gutteridge Clarendon Oxford
    • B. Halliwell, and J.M.C. Gutteridge Antioxidant defences. Protection against oxidants in biological systems: the superoxide theory of oxygen toxicity B. Halliwell J.M.C. Gutteridge Free radicals in biology and medicine 1995 Clarendon Oxford 86 187
    • (1995) Free Radicals in Biology and Medicine , pp. 86-187
    • Halliwell, B.1    Gutteridge, J.M.C.2
  • 9
    • 0142012094 scopus 로고    scopus 로고
    • Extracellular superoxide dismutase in biology and medicine
    • C.L. Fattman, L.M. Schaefer, and T.D. Oury Extracellular superoxide dismutase in biology and medicine Free Radic. Biol. Med. 35 2003 236 256
    • (2003) Free Radic. Biol. Med. , vol.35 , pp. 236-256
    • Fattman, C.L.1    Schaefer, L.M.2    Oury, T.D.3
  • 10
    • 0034656192 scopus 로고    scopus 로고
    • Oxygen free radicals mediate the induction of manganese superoxide dismutase gene expression by TNF-alpha
    • R. Liu, G.R. Buettner, and L.W. Oberley Oxygen free radicals mediate the induction of manganese superoxide dismutase gene expression by TNF-alpha Free Radic. Biol. Med. 28 2000 1197 1205
    • (2000) Free Radic. Biol. Med. , vol.28 , pp. 1197-1205
    • Liu, R.1    Buettner, G.R.2    Oberley, L.W.3
  • 11
    • 0032171622 scopus 로고    scopus 로고
    • Peroxynitrite modulates MnSOD gene expression in lung epithelial cells
    • R.M. Jackson, G. Parish, and E.S. Helton Peroxynitrite modulates MnSOD gene expression in lung epithelial cells Free Radic. Biol. Med. 25 1998 463 472
    • (1998) Free Radic. Biol. Med. , vol.25 , pp. 463-472
    • Jackson, R.M.1    Parish, G.2    Helton, E.S.3
  • 12
    • 0023190840 scopus 로고
    • Increase in manganese superoxide dismutase activity in the mouse heart after X-irradiation
    • L.W. Oberley, D.K. St. Clair, A.P. Autor, and T.D. Oberley Increase in manganese superoxide dismutase activity in the mouse heart after X-irradiation Arch. Biochem. Biophys. 254 1987 69 80
    • (1987) Arch. Biochem. Biophys. , vol.254 , pp. 69-80
    • Oberley, L.W.1    St. Clair, D.K.2    Autor, A.P.3    Oberley, T.D.4
  • 13
    • 0036846204 scopus 로고    scopus 로고
    • Induction of manganese superoxide dismutase in human dermal fibroblasts: A UV-B-mediated paracrine mechanism with the release of epidermal interleukin 1 alpha, interleukin 1 beta, and tumor necrosis factor alpha
    • L. Naderi-Hachtroudi, T. Peters, P. Brenneisen, C. Meewes, C. Hommel, Z. Razi-Wolf, L.A. Schneider, J. Schueller, M. Wlaschek, and K. Scharffetter-Kochanek Induction of manganese superoxide dismutase in human dermal fibroblasts: a UV-B-mediated paracrine mechanism with the release of epidermal interleukin 1 alpha, interleukin 1 beta, and tumor necrosis factor alpha Arch. Dermatol. 138 2002 1473 1479
    • (2002) Arch. Dermatol. , vol.138 , pp. 1473-1479
    • Naderi-Hachtroudi, L.1    Peters, T.2    Brenneisen, P.3    Meewes, C.4    Hommel, C.5    Razi-Wolf, Z.6    Schneider, L.A.7    Schueller, J.8    Wlaschek, M.9    Scharffetter-Kochanek, K.10
  • 15
    • 0028912663 scopus 로고
    • Antioxidative roles of metallothionein and manganese superoxide dismutase induced by tumor necrosis factor-α and interleukin-6
    • M. Sato, M. Sasaki, and H. Hojo Antioxidative roles of metallothionein and manganese superoxide dismutase induced by tumor necrosis factor-α and interleukin-6 Arch. Biochem. Biophys. 316 1995 738 744
    • (1995) Arch. Biochem. Biophys. , vol.316 , pp. 738-744
    • Sato, M.1    Sasaki, M.2    Hojo, H.3
  • 16
    • 0028973452 scopus 로고
    • Interleukin 1 alpha-induced expression of manganous superoxide dismutase reduces myocardial reperfusion injury in the rat
    • C. Nogae, N. Makino, T. Hata, I. Nogae, S. Takahashi, K. Suzuki, N. Taniguchi, and T. Yanaga Interleukin 1 alpha-induced expression of manganous superoxide dismutase reduces myocardial reperfusion injury in the rat J. Mol. Cell. Cardiol. 27 1995 2091 2099
    • (1995) J. Mol. Cell. Cardiol. , vol.27 , pp. 2091-2099
    • Nogae, C.1    Makino, N.2    Hata, T.3    Nogae, I.4    Takahashi, S.5    Suzuki, K.6    Taniguchi, N.7    Yanaga, T.8
  • 17
    • 0027394553 scopus 로고
    • Overexpression of mitochondrial manganese superoxide dismutase promotes the survival of tumor cells exposed to interleukin-1, tumor necrosis factor, selected anticancer drugs, and ionizing radiation
    • K. Hirose, D.L. Longo, J.J. Oppenheim, and K. Matsushima Overexpression of mitochondrial manganese superoxide dismutase promotes the survival of tumor cells exposed to interleukin-1, tumor necrosis factor, selected anticancer drugs, and ionizing radiation FASEB J. 7 1993 361 368
    • (1993) FASEB J. , vol.7 , pp. 361-368
    • Hirose, K.1    Longo, D.L.2    Oppenheim, J.J.3    Matsushima, K.4
  • 18
    • 0025991016 scopus 로고
    • Manganese superoxide dismutase is induced by IFN-gamma in multiple cell types: Synergistic induction by IFN-gamma and tumor necrosis factor or IL-1
    • C.A. Harris, K.S. Derbin, B. Hunte-McDonough, M.R. Krauss, K.T. Chen, D.M. Smith, and L.B. Epstein Manganese superoxide dismutase is induced by IFN-gamma in multiple cell types: synergistic induction by IFN-gamma and tumor necrosis factor or IL-1 J. Immunol. 147 1991 149 154
    • (1991) J. Immunol. , vol.147 , pp. 149-154
    • Harris, C.A.1    Derbin, K.S.2    Hunte-Mcdonough, B.3    Krauss, M.R.4    Chen, K.T.5    Smith, D.M.6    Epstein, L.B.7
  • 19
    • 0029020434 scopus 로고
    • Irradiation increases manganese superoxide dismutase mRNA levels in human fibroblasts: Possible mechanisms for its accumulation
    • M. Akashi, M. Hachiya, R.L. Paquette, Y. Osawa, S. Shimizu, and G. Suzuki Irradiation increases manganese superoxide dismutase mRNA levels in human fibroblasts: possible mechanisms for its accumulation J. Biol. Chem. 270 1995 15864 15869
    • (1995) J. Biol. Chem. , vol.270 , pp. 15864-15869
    • Akashi, M.1    Hachiya, M.2    Paquette, R.L.3    Osawa, Y.4    Shimizu, S.5    Suzuki, G.6
  • 20
    • 0028329155 scopus 로고
    • Expression of manganese superoxide dismutase promotes cellular differentiation
    • D.K. St Clair, T.D. Oberley, K.E. Muse, and W.H. St Clair Expression of manganese superoxide dismutase promotes cellular differentiation Free Radic. Biol. Med. 16 1994 275 282
    • (1994) Free Radic. Biol. Med. , vol.16 , pp. 275-282
    • St Clair, D.K.1    Oberley, T.D.2    Muse, K.E.3    St Clair, W.H.4
  • 22
    • 0037466652 scopus 로고    scopus 로고
    • DAF-16 target genes that control C. elegans life-span and metabolism
    • S.S. Lee, S. Kennedy, A.C. Tolonen, and G. Ruvkun DAF-16 target genes that control C. elegans life-span and metabolism Science 300 2003 644 647
    • (2003) Science , vol.300 , pp. 644-647
    • Lee, S.S.1    Kennedy, S.2    Tolonen, A.C.3    Ruvkun, G.4
  • 24
    • 0030068056 scopus 로고    scopus 로고
    • Elevation in the ratio of Cu/Zn-superoxide dismutase to glutathione peroxide activity induces features of cellular senescence and this effect is mediated by hydrogen peroxide
    • J.B. de Haan, F. Cristiano, R. Iannello, C. Bladier, M.J. Kelner, and I. Kola Elevation in the ratio of Cu/Zn-superoxide dismutase to glutathione peroxide activity induces features of cellular senescence and this effect is mediated by hydrogen peroxide Hum. Mol. Genet. 5 1996 2832 2892
    • (1996) Hum. Mol. Genet. , vol.5 , pp. 2832-2892
    • De Haan, J.B.1    Cristiano, F.2    Iannello, R.3    Bladier, C.4    Kelner, M.J.5    Kola, I.6
  • 26
    • 0033520497 scopus 로고    scopus 로고
    • Stable overexpression of manganese superoxide dismutase in mitochondria identifies hydrogen peroxide as a major oxidant in the AP-1-mediated induction of matrix-degrading metalloprotease-1
    • J. Wenk, P. Brenneisen, M. Wlaschek, A. Poswig, K. Briviba, T.D. Oberley, and K. Scharffetter-Kochanek Stable overexpression of manganese superoxide dismutase in mitochondria identifies hydrogen peroxide as a major oxidant in the AP-1-mediated induction of matrix-degrading metalloprotease-1 J. Biol. Chem. 274 1999 25869 25876
    • (1999) J. Biol. Chem. , vol.274 , pp. 25869-25876
    • Wenk, J.1    Brenneisen, P.2    Wlaschek, M.3    Poswig, A.4    Briviba, K.5    Oberley, T.D.6    Scharffetter-Kochanek, K.7
  • 27
    • 0029064709 scopus 로고
    • Mice lacking extracellular superoxide dismutase are more sensitive to hyperoxia
    • L.M. Carlsson, J. Jonsson, T. Edlund, and S.L. Marklund Mice lacking extracellular superoxide dismutase are more sensitive to hyperoxia Proc. Natl. Acad. Sci. USA 92 1995 6264 6268
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 6264-6268
    • Carlsson, L.M.1    Jonsson, J.2    Edlund, T.3    Marklund, S.L.4
  • 29
    • 0032571387 scopus 로고    scopus 로고
    • Reduced fertility in female mice lacking copper-zinc superoxide dismutase
    • Y.S. Ho, M. Gargano, J. Cao, R.T. Bronson, I. Heimler, and R.J. Hutz Reduced fertility in female mice lacking copper-zinc superoxide dismutase J. Biol. Chem. 273 1998 7765 7769
    • (1998) J. Biol. Chem. , vol.273 , pp. 7765-7769
    • Ho, Y.S.1    Gargano, M.2    Cao, J.3    Bronson, R.T.4    Heimler, I.5    Hutz, R.J.6
  • 30
    • 0030971057 scopus 로고    scopus 로고
    • Mice deficient in cellular glutathione peroxidase develop normally and show no increased sensitivity to hyperoxia
    • Y.S. Ho, J.L. Magnenat, R.T. Bronson, J. Cao, M. Gargano, M. Sugawara, and C.D. Funk Mice deficient in cellular glutathione peroxidase develop normally and show no increased sensitivity to hyperoxia J. Biol. Chem. 272 1997 16644 16651
    • (1997) J. Biol. Chem. , vol.272 , pp. 16644-16651
    • Ho, Y.S.1    Magnenat, J.L.2    Bronson, R.T.3    Cao, J.4    Gargano, M.5    Sugawara, M.6    Funk, C.D.7
  • 31
    • 0033591310 scopus 로고    scopus 로고
    • Extracellular superoxide dismutase deficiency worsens outcome from focal cerebral ischemia in the mouse
    • H. Sheng, T.C. Brady, R.D. Pearlstein, J.D. Crapo, and D.S. Warner Extracellular superoxide dismutase deficiency worsens outcome from focal cerebral ischemia in the mouse Neurosci. Lett. 267 1999 13 16
    • (1999) Neurosci. Lett. , vol.267 , pp. 13-16
    • Sheng, H.1    Brady, T.C.2    Pearlstein, R.D.3    Crapo, J.D.4    Warner, D.S.5
  • 33
    • 0021288861 scopus 로고
    • Assay of superoxide dismutase activity in tumor tissue
    • L.W. Oberley, and D.R. Spitz Assay of superoxide dismutase activity in tumor tissue Methods Enzymol. 105 1984 457 464
    • (1984) Methods Enzymol. , vol.105 , pp. 457-464
    • Oberley, L.W.1    Spitz, D.R.2
  • 35
    • 0025962976 scopus 로고
    • Use of cyanide and diethyldithiocarbamate in the assay of superoxide dismutase
    • J. Iqbal, and P. Whitney Use of cyanide and diethyldithiocarbamate in the assay of superoxide dismutase Free Radic. Biol. Med. 10 1991 69 77
    • (1991) Free Radic. Biol. Med. , vol.10 , pp. 69-77
    • Iqbal, J.1    Whitney, P.2
  • 36
    • 0000204836 scopus 로고    scopus 로고
    • Assay of superoxide dismutase activity by combining electrophoresis and densitometry
    • C.N. Chen, and S.M. Pan Assay of superoxide dismutase activity by combining electrophoresis and densitometry Bot. Bull. Acad. Sin. 37 1996 107 111
    • (1996) Bot. Bull. Acad. Sin. , vol.37 , pp. 107-111
    • Chen, C.N.1    Pan, S.M.2
  • 37
    • 0022507106 scopus 로고
    • A spectrophotometric assay for superoxide dismutase activities in crude tissue fractions
    • H. Kuthan, H.J. Haussmann, and J. Werringloer A spectrophotometric assay for superoxide dismutase activities in crude tissue fractions Biochem. J. 237 1986 175 180
    • (1986) Biochem. J. , vol.237 , pp. 175-180
    • Kuthan, H.1    Haussmann, H.J.2    Werringloer, J.3
  • 38
    • 0033102629 scopus 로고    scopus 로고
    • Characterization of the antioxidant status of the heterozygous manganese superoxide dismutase knockout mouse
    • H. Van Remmen, C. Salvador, H. Yang, T.T. Huang, C.J. Epstein, and A. Richardson Characterization of the antioxidant status of the heterozygous manganese superoxide dismutase knockout mouse Arch. Biochem. Biophys. 363 1999 91 97
    • (1999) Arch. Biochem. Biophys. , vol.363 , pp. 91-97
    • Van Remmen, H.1    Salvador, C.2    Yang, H.3    Huang, T.T.4    Epstein, C.J.5    Richardson, A.6
  • 39
    • 0019135284 scopus 로고
    • Quantitative resolution of Cu,Zn- and Mn superoxide dismutase activities
    • M. Ysebaert-Vanneste, and W.H. Vanneste Quantitative resolution of Cu,Zn- and Mn superoxide dismutase activities Anal. Biochem. 107 1980 86 95
    • (1980) Anal. Biochem. , vol.107 , pp. 86-95
    • Ysebaert-Vanneste, M.1    Vanneste, W.H.2
  • 40
    • 0027305161 scopus 로고
    • Targeted expression of a dominant-negative FGF receptor mutant in the epidermis of transgenic mice reveals a role of FGF in keratinocyte organization and differentiation
    • S. Werner, W. Weinberg, X. Liao, K.G. Peters, M. Blessing, S.H. Yuspa, R.L. Weiner, and L.T. Williams Targeted expression of a dominant-negative FGF receptor mutant in the epidermis of transgenic mice reveals a role of FGF in keratinocyte organization and differentiation EMBO J. 12 1993 2635 2643
    • (1993) EMBO J. , vol.12 , pp. 2635-2643
    • Werner, S.1    Weinberg, W.2    Liao, X.3    Peters, K.G.4    Blessing, M.5    Yuspa, S.H.6    Weiner, R.L.7    Williams, L.T.8
  • 42
    • 0015153416 scopus 로고
    • Superoxide dismutase: Improved assays and an assay applicable to acrylamide gels
    • C. Beauchamp, and I. Fridovich Superoxide dismutase: improved assays and an assay applicable to acrylamide gels Anal. Biochem. 44 1971 276 287
    • (1971) Anal. Biochem. , vol.44 , pp. 276-287
    • Beauchamp, C.1    Fridovich, I.2
  • 43
    • 0021318441 scopus 로고
    • Catalase in vitro
    • H. Aebi Catalase in vitro Methods Enzymol 105 1984 121 126
    • (1984) Methods Enzymol , vol.105 , pp. 121-126
    • Aebi, H.1
  • 44
    • 0021288821 scopus 로고
    • Assays of glutathione peroxidase
    • L. Flohe, and W.A. Günzler Assays of glutathione peroxidase Methods Enzymol. 105 1984 114 121
    • (1984) Methods Enzymol. , vol.105 , pp. 114-121
    • Flohe, L.1    Günzler, W.A.2
  • 45
    • 0025787017 scopus 로고
    • Phospholipid hydroperoxide glutathione peroxidase is the 18-kDa selenoprotein expressed in human tumor cell lines
    • M. Maiorino, F.F. Chu, F. Ursini, K.J. Davies, J.H. Doroshow, and S.R. Esworthy Phospholipid hydroperoxide glutathione peroxidase is the 18-kDa selenoprotein expressed in human tumor cell lines J. Biol. Chem. 266 1991 7728 7732
    • (1991) J. Biol. Chem. , vol.266 , pp. 7728-7732
    • Maiorino, M.1    Chu, F.F.2    Ursini, F.3    Davies, K.J.4    Doroshow, J.H.5    Esworthy, S.R.6
  • 46
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • M.M. Bradford A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding Anal. Biochem. 72 1976 248 254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 47
    • 10744227003 scopus 로고    scopus 로고
    • N-Acetylcysteine prevents reactive oxygen species-mediated myocardial stress in patients undergoing cardiac surgery: Results of a randomized, double-blind, placebo-controlled clinical trial
    • P. Tossios, W. Bloch, A. Huebner, M.R. Raji, F. Dodos, O. Klass, M. Suedkamp, S.M. Kasper, M. Hellmich, and U. Mehlhorn N-Acetylcysteine prevents reactive oxygen species-mediated myocardial stress in patients undergoing cardiac surgery: results of a randomized, double-blind, placebo-controlled clinical trial J. Thoracic Cardiovasc. Surg. 126 2003 1513 1520
    • (2003) J. Thoracic Cardiovasc. Surg. , vol.126 , pp. 1513-1520
    • Tossios, P.1    Bloch, W.2    Huebner, A.3    Raji, M.R.4    Dodos, F.5    Klass, O.6    Suedkamp, M.7    Kasper, S.M.8    Hellmich, M.9    Mehlhorn, U.10
  • 48
    • 0034652768 scopus 로고    scopus 로고
    • Measurement of F(2)-isoprostanes as an index of oxidative stress in vivo
    • L.J. Roberts, and J.D. Morrow Measurement of F(2)-isoprostanes as an index of oxidative stress in vivo Free Radic. Biol. Med. 28 2000 505 513
    • (2000) Free Radic. Biol. Med. , vol.28 , pp. 505-513
    • Roberts, L.J.1    Morrow, J.D.2
  • 49
    • 0021803196 scopus 로고
    • The selenoenzyme phospholipid hydroperoxide glutathione peroxidase
    • F. Ursini, M. Maiorino, and C. Gregolin The selenoenzyme phospholipid hydroperoxide glutathione peroxidase Biochim. Biophys. Acta 839 1985 62 70
    • (1985) Biochim. Biophys. Acta , vol.839 , pp. 62-70
    • Ursini, F.1    Maiorino, M.2    Gregolin, C.3
  • 50
    • 0029915115 scopus 로고    scopus 로고
    • The selenoenzyme phospholipid hydroperoxide glutathione peroxidase controls the activity of the 15-lipoxygenase with complex substrates and preserves the specificity of the oxygenation products
    • K. Schnurr, J. Belker, F. Ursini, T. Schewe, and H. Kuhn The selenoenzyme phospholipid hydroperoxide glutathione peroxidase controls the activity of the 15-lipoxygenase with complex substrates and preserves the specificity of the oxygenation products J. Biol. Chem. 271 1996 4653 4658
    • (1996) J. Biol. Chem. , vol.271 , pp. 4653-4658
    • Schnurr, K.1    Belker, J.2    Ursini, F.3    Schewe, T.4    Kuhn, H.5
  • 51
    • 0025060737 scopus 로고
    • Protective action of phospholipid hydroperoxide glutathione peroxidase against membrane-damaging lipid peroxidation: In situ reduction of phospholipids and cholesterol hydroperoxides
    • J.P. Thomas, M. Maiorino, F. Ursini, and A.W. Girotti Protective action of phospholipid hydroperoxide glutathione peroxidase against membrane-damaging lipid peroxidation: in situ reduction of phospholipids and cholesterol hydroperoxides J. Biol. Chem. 265 1990 454 461
    • (1990) J. Biol. Chem. , vol.265 , pp. 454-461
    • Thomas, J.P.1    Maiorino, M.2    Ursini, F.3    Girotti, A.W.4
  • 53
    • 0345059129 scopus 로고    scopus 로고
    • The nitric oxide donor S-nitroso-N-acetylpenicillamine (SNAP) increases free radical generation and degrades left ventricular function after ischemia-reperfusion
    • Y. Zhang, L.R. Davies, S.M. Martin, W.J. Coddington, F.J. Miller Jr., G.R. Buettner, and R.E. Kerber The nitric oxide donor S-nitroso-N- acetylpenicillamine (SNAP) increases free radical generation and degrades left ventricular function after ischemia-reperfusion Resuscitation 59 2003 345 352
    • (2003) Resuscitation , vol.59 , pp. 345-352
    • Zhang, Y.1    Davies, L.R.2    Martin, S.M.3    Coddington, W.J.4    Miller Jr., F.J.5    Buettner, G.R.6    Kerber, R.E.7
  • 54
    • 0029862502 scopus 로고    scopus 로고
    • Nitration and inactivation of manganese superoxide dismutase in chronic rejection of human renal allografts
    • L.A. MacMillan-Crow, J.P. Crow, J.D. Kerby, J.S. Beckman, and J.A. Thompson Nitration and inactivation of manganese superoxide dismutase in chronic rejection of human renal allografts Proc. Natl. Acad. Sci. USA 93 1996 11853 11858
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 11853-11858
    • MacMillan-Crow, L.A.1    Crow, J.P.2    Kerby, J.D.3    Beckman, J.S.4    Thompson, J.A.5
  • 56
    • 0003867581 scopus 로고
    • B. Halliwell O.I. Aruoma Ellis Horwood New York
    • K.H. Cheeseman B. Halliwell O.I. Aruoma DNA and free radicals 1993 Ellis Horwood New York 109 144
    • (1993) DNA and Free Radicals , pp. 109-144
    • Cheeseman, K.H.1
  • 57
    • 0026605267 scopus 로고
    • Metals and lipid oxidation: Contemporary issues
    • K.M. Schaich Metals and lipid oxidation: contemporary issues Lipids 27 1992 209 218
    • (1992) Lipids , vol.27 , pp. 209-218
    • Schaich, K.M.1
  • 58
    • 0026597915 scopus 로고
    • Redox cycling of iron and lipid peroxidation
    • G. Minotti, and S.D. Aust Redox cycling of iron and lipid peroxidation Lipids 27 1992 219 226
    • (1992) Lipids , vol.27 , pp. 219-226
    • Minotti, G.1    Aust, S.D.2
  • 59
    • 0027329036 scopus 로고
    • Photodynamic action of merocyanine 540 on leukaemia cells: Iron-stimulated lipid peroxidation and cell killing
    • F. Lin, and A.W. Girotti Photodynamic action of merocyanine 540 on leukaemia cells: iron-stimulated lipid peroxidation and cell killing Arch. Biochem. Biophys. 300 1993 714 723
    • (1993) Arch. Biochem. Biophys. , vol.300 , pp. 714-723
    • Lin, F.1    Girotti, A.W.2
  • 60
    • 0025327637 scopus 로고
    • Stimulation of free radical reactions in biology and medicine: A new two-compartment kinetic model of intracellular lipid peroxidation
    • C.F. Babbs, and M.G. Steiner Stimulation of free radical reactions in biology and medicine: a new two-compartment kinetic model of intracellular lipid peroxidation Free Radic. Biol. Med. 8 1990 471 485
    • (1990) Free Radic. Biol. Med. , vol.8 , pp. 471-485
    • Babbs, C.F.1    Steiner, M.G.2
  • 63
    • 0026327815 scopus 로고
    • Effects of oxidative modification of cholesterol in isolated low density lipoproteins on cultured smooth muscle cells
    • K. Liu, B. Ramjiawan, M.J.B. Kutryk, and G.N. Pierce Effects of oxidative modification of cholesterol in isolated low density lipoproteins on cultured smooth muscle cells Mol. Cell. Biochem. 108 1991 49 56
    • (1991) Mol. Cell. Biochem. , vol.108 , pp. 49-56
    • Liu, K.1    Ramjiawan, B.2    Kutryk, M.J.B.3    Pierce, G.N.4
  • 64
    • 0026737577 scopus 로고
    • Role of lipid peroxidation in enhancement of endotoxin hepatotoxicity
    • Y. Shibayama Role of lipid peroxidation in enhancement of endotoxin hepatotoxicity Exp. Toxicol. Pathol. 44 1992 205 208
    • (1992) Exp. Toxicol. Pathol. , vol.44 , pp. 205-208
    • Shibayama, Y.1
  • 67
    • 0033581904 scopus 로고    scopus 로고
    • Mutant mice live longer
    • L. Guarente Mutant mice live longer Nature 402 1999 243 245
    • (1999) Nature , vol.402 , pp. 243-245
    • Guarente, L.1
  • 72
    • 0035956929 scopus 로고    scopus 로고
    • Increased mitochondrial oxidative stress in the Sod2 (+/-) mouse results in the age-related decline of mitochondrial function culminating in increased apoptosis
    • J.E. Kokoszka, P. Coskun, L.A. Esposito, and D.C. Wallace Increased mitochondrial oxidative stress in the Sod2 (+/-) mouse results in the age-related decline of mitochondrial function culminating in increased apoptosis Proc. Natl. Acad. Sci. USA 98 2001 2278 2283
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 2278-2283
    • Kokoszka, J.E.1    Coskun, P.2    Esposito, L.A.3    Wallace, D.C.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.