메뉴 건너뛰기




Volumn 100, Issue 2, 1997, Pages 224-233

Reactive oxygen species and antioxidants: Relationships in green cells

Author keywords

Antioxidants; APX; GR; Oxidative stress; Reactive oxygen specie; SOD; Superoxide

Indexed keywords


EID: 0030970357     PISSN: 00319317     EISSN: None     Source Type: Journal    
DOI: 10.1034/j.1399-3054.1997.1000203.x     Document Type: Article
Times cited : (813)

References (81)
  • 1
    • 0029138945 scopus 로고
    • Dissection of oxidative stress tolerance using transgenic plants
    • Allen, R. D. 1995. Dissection of oxidative stress tolerance using transgenic plants. - Plant Physiol. 107: 1049-1054.
    • (1995) Plant Physiol. , vol.107 , pp. 1049-1054
    • Allen, R.D.1
  • 4
    • 0000459986 scopus 로고
    • Seasonal variation in the antioxidant system of eastern white pine needles. Evidence for thermal dependence
    • Anderson, J. V., Chevone, B. I. & Hess, J. L. 1993. Seasonal variation in the antioxidant system of eastern white pine needles. Evidence for thermal dependence. - Plant Physiol. 98: 501-508.
    • (1993) Plant Physiol. , vol.98 , pp. 501-508
    • Anderson, J.V.1    Chevone, B.I.2    Hess, J.L.3
  • 5
    • 0001537762 scopus 로고
    • Resistance to active oxygen toxicity of transgenic Nicotiana tabacum that expresses the gene for glutathione reductase from Escherichia coli
    • Aono, M., Kubo, A., Saji, H., Natori, T., Tanaka, K. & Kondo, N. 1991. Resistance to active oxygen toxicity of transgenic Nicotiana tabacum that expresses the gene for glutathione reductase from Escherichia coli. - Plant Cell Physiol. 32: 691-697.
    • (1991) Plant Cell Physiol. , vol.32 , pp. 691-697
    • Aono, M.1    Kubo, A.2    Saji, H.3    Natori, T.4    Tanaka, K.5    Kondo, N.6
  • 6
    • 0002844238 scopus 로고
    • Production and action of active oxygen in photosynthetic tissue
    • C. H. Foyer and P. M. Mullineaux, eds, CRC Press, Boca Raton, FL. ISBN 0-8493-5443-9
    • Asada, K. 1994. Production and action of active oxygen in photosynthetic tissue. - In Causes of Photooxidatives Stress and Amelioration of Defense Systems in Plants (C. H. Foyer and P. M. Mullineaux, eds), pp. 77-104. CRC Press, Boca Raton, FL. ISBN 0-8493-5443-9.
    • (1994) Causes of Photooxidatives Stress and Amelioration of Defense Systems in Plants , pp. 77-104
    • Asada, K.1
  • 7
    • 0002698921 scopus 로고
    • Formation of active oxygen and its fate in chloroplasts
    • O. Hayashi and K. Asada, eds, Univ. Park Press, Baltimore, MD. ISBN 0-8391-1204-1
    • _ , Takahashi, M. A., Tanaka, K. & Nakano, Y. 1977. Formation of active oxygen and its fate in chloroplasts. - In Biochemical and Medical Aspects of Active Oxygen (O. Hayashi and K. Asada, eds), pp. 45-62. Univ. Park Press, Baltimore, MD. ISBN 0-8391-1204-1.
    • (1977) Biochemical and Medical Aspects of Active Oxygen , pp. 45-62
    • Takahashi, M.A.1    Tanaka, K.2    Nakano, Y.3
  • 8
    • 0019528608 scopus 로고
    • Isolation and characterization of the cytosolic and mitochondrial superoxide dismutases of maize
    • Baum, J. A. & Scandalios, J. G. 1981. Isolation and characterization of the cytosolic and mitochondrial superoxide dismutases of maize. - Arch. Biochem. Biophys. 206: 249-264.
    • (1981) Arch. Biochem. Biophys. , vol.206 , pp. 249-264
    • Baum, J.A.1    Scandalios, J.G.2
  • 10
    • 0029328498 scopus 로고
    • Peroxisomal copper, zinc superoxide dismutase. Characterization of the isoenzyme from watermelon cotyledons
    • Bueno, P., Varela. J., Gimeenez-Gallego, G. & del Rio, L. A. 1995. Peroxisomal copper, zinc superoxide dismutase. Characterization of the isoenzyme from watermelon cotyledons. - Plant Physiol. 108: 1151-1160.
    • (1995) Plant Physiol. , vol.108 , pp. 1151-1160
    • Bueno, P.1    Varela, J.2    Gimeenez-Gallego, G.3    Del Rio, L.A.4
  • 11
    • 0027976015 scopus 로고
    • Hydroxyl radicals and a thylakoid-bound endopeptidase are involved in light and oxygen-induced proteolysis in oat chloroplasts
    • Casano, L. M., Lascano, H. R. & Trippi, V. S. 1994. Hydroxyl radicals and a thylakoid-bound endopeptidase are involved in light and oxygen-induced proteolysis in oat chloroplasts. - Plant Cell Physiol. 35: 145-152.
    • (1994) Plant Cell Physiol. , vol.35 , pp. 145-152
    • Casano, L.M.1    Lascano, H.R.2    Trippi, V.S.3
  • 12
    • 0000715428 scopus 로고
    • Light activation of fructose bisphosphatase in isolated spinach chloroplasts and deactivation by hydrogen peroxide
    • Charles, S. A. & Halliwell, B. 1981. Light activation of fructose bisphosphatase in isolated spinach chloroplasts and deactivation by hydrogen peroxide. - Planta 151: 242-246.
    • (1981) Planta , vol.151 , pp. 242-246
    • Charles, S.A.1    Halliwell, B.2
  • 13
    • 0029360417 scopus 로고
    • Differential accumulation of antioxidant mRNAs in Arabidopsis thaliana exposed to ozone
    • Conklin, P. L. & Last, R. L. 1995. Differential accumulation of antioxidant mRNAs in Arabidopsis thaliana exposed to ozone. - Plant Physiol. 109: 203-212.
    • (1995) Plant Physiol. , vol.109 , pp. 203-212
    • Conklin, P.L.1    Last, R.L.2
  • 15
    • 0022273073 scopus 로고
    • Coordinate expression of Mn-containing superoxide dismutase and Cu,Zn-containing superoxide dismutase in human fibroblasts with trisomy 21
    • Crosti, N., Bajer, J., Serra, A., Rigo, A., Scarpa, M. & Viglino, P. 1985. Coordinate expression of Mn-containing superoxide dismutase and Cu,Zn-containing superoxide dismutase in human fibroblasts with trisomy 21. - J. Cell Sci. 79: 95-103.
    • (1985) J. Cell Sci. , vol.79 , pp. 95-103
    • Crosti, N.1    Bajer, J.2    Serra, A.3    Rigo, A.4    Scarpa, M.5    Viglino, P.6
  • 16
    • 0030481542 scopus 로고    scopus 로고
    • Death don't have no mercy: Cell death programs in plant-microbe interactions
    • Dangl, J. L., Dietrich, R. A. & Richberg, M. S. 1996. Death don't have no mercy: Cell death programs in plant-microbe interactions. - Plant Cell 8: 1793-1807.
    • (1996) Plant Cell , vol.8 , pp. 1793-1807
    • Dangl, J.L.1    Dietrich, R.A.2    Richberg, M.S.3
  • 17
    • 0023655369 scopus 로고
    • Protein damage and degradation by oxygen radicals
    • Davies, K. J. A. 1987. Protein damage and degradation by oxygen radicals. - J. Biol. Chem. 262: 9895-9901.
    • (1987) J. Biol. Chem. , vol.262 , pp. 9895-9901
    • Davies, K.J.A.1
  • 18
    • 0002892737 scopus 로고
    • The xanthophyll cycle
    • R. G. Alscher and J. L. Hess, eds, CRC Press, Boca Raton, FL. ISBN 0-8493-6328-4
    • Demmig-Adams, B. & Adams, W. 1993. The xanthophyll cycle. - In Antioxidants in Higher Plants (R. G. Alscher and J. L. Hess, eds), pp. 91-110. CRC Press, Boca Raton, FL. ISBN 0-8493-6328-4.
    • (1993) Antioxidants in Higher Plants , pp. 91-110
    • Demmig-Adams, B.1    Adams, W.2
  • 21
    • 0027994964 scopus 로고
    • Synthesis and properties of glutathione reductase in stressed peas
    • Edwards, E., Enard, C., Creissen, G. & Mullineaux, P. 1994. Synthesis and properties of glutathione reductase in stressed peas. - Planta 192: 137-143.
    • (1994) Planta , vol.192 , pp. 137-143
    • Edwards, E.1    Enard, C.2    Creissen, G.3    Mullineaux, P.4
  • 23
    • 0001364802 scopus 로고
    • Seasonal variation of glutathione and glutathione reductase in needles of Picea abies
    • Esterbauer, H. & Grill, D. 1978. Seasonal variation of glutathione and glutathione reductase in needles of Picea abies. - Plant Physiol. 61: 119-121.
    • (1978) Plant Physiol. , vol.61 , pp. 119-121
    • Esterbauer, H.1    Grill, D.2
  • 24
    • 85053492389 scopus 로고
    • Ascorbic acid
    • R.G Alscher and J. L. Hess, eds, CRC Press, Boca Raton, FL. ISBN 0-8493-6328-4
    • Foyer, C. H. 1993. Ascorbic acid. - In Antioxidants in Higher Plants (R.G Alscher and J. L. Hess, eds), pp. 31-58. CRC Press, Boca Raton, FL. ISBN 0-8493-6328-4.
    • (1993) Antioxidants in Higher Plants , pp. 31-58
    • Foyer, C.H.1
  • 26
    • 0028190986 scopus 로고
    • Photooxidative stress in plants
    • _ , Lelandais, M. & Kunert, K. H. 1994. Photooxidative stress in plants. - Physiol. Plant. 92: 696-717.
    • (1994) Physiol. Plant. , vol.92 , pp. 696-717
    • Lelandais, M.1    Kunert, K.H.2
  • 27
    • 0029053451 scopus 로고
    • Superoxide radical and superoxide dismutases
    • Fridovich, I. 1995. Superoxide radical and superoxide dismutases. - Annu. Rev. Biochem. 64: 97-112.
    • (1995) Annu. Rev. Biochem. , vol.64 , pp. 97-112
    • Fridovich, I.1
  • 28
    • 0000412725 scopus 로고
    • Chloroplast superoxide and hydrogen peroxide scavenging systems from pea leaves: Seasonal variations
    • Gilham, D. J. & Dodge, A. D. 1987. Chloroplast superoxide and hydrogen peroxide scavenging systems from pea leaves: Seasonal variations. - Plant Sci. 50: 105-109.
    • (1987) Plant Sci. , vol.50 , pp. 105-109
    • Gilham, D.J.1    Dodge, A.D.2
  • 29
    • 0030478245 scopus 로고    scopus 로고
    • Acclimation of folair antioxidant systems to growth irradiance in three broad-leaved evergreen species
    • Grace, S. C. & Logan, B. A. 1996. Acclimation of folair antioxidant systems to growth irradiance in three broad-leaved evergreen species. - Plant Physiol. 112: 1631-1640.
    • (1996) Plant Physiol. , vol.112 , pp. 1631-1640
    • Grace, S.C.1    Logan, B.A.2
  • 30
    • 0028934243 scopus 로고
    • Formation and decay of monodehydroascorbate radicals in illuminated thylakoids as determined by EPR spectroscopy
    • _ , Pace, R. & Wydrzynski, T. 1995. Formation and decay of monodehydroascorbate radicals in illuminated thylakoids as determined by EPR spectroscopy. - Biochim. Biophys. Acta 1229: 155-165.
    • (1995) Biochim. Biophys. Acta , vol.1229 , pp. 155-165
    • Pace, R.1    Wydrzynski, T.2
  • 31
    • 0003016194 scopus 로고
    • Genetic control of photooxidant tolerance
    • C. H. Foyer and P. Mullineaux, eds, CRC Press, Boca Raton, FL. ISBN 0-8439-5443-9
    • Gressel, J. & Galun, E. 1994. Genetic control of photooxidant tolerance. - In Causes of Photooxidative Stress and Amelioration of Defense Systems in Plants (C. H. Foyer and P. Mullineaux, eds), pp. 237-273. CRC Press, Boca Raton, FL. ISBN 0-8439-5443-9.
    • (1994) Causes of Photooxidative Stress and Amelioration of Defense Systems in Plants , pp. 237-273
    • Gressel, J.1    Galun, E.2
  • 32
    • 0000090225 scopus 로고
    • Changes in glutahione content during cold acclimation in Cornus sericea and Citrus sinensis
    • Guy, C. L., Carter, J. V., Yelenosky, G. & Guy, C. T. 1984. Changes in glutahione content during cold acclimation in Cornus sericea and Citrus sinensis. - Cryobiology 21: 443-453.
    • (1984) Cryobiology , vol.21 , pp. 443-453
    • Guy, C.L.1    Carter, J.V.2    Yelenosky, G.3    Guy, C.T.4
  • 33
    • 0029736434 scopus 로고    scopus 로고
    • Role of reactive oxygen metabolites in DNA damage and cell death in chemical hypoxic injury to LLC-PK1 cells
    • Hagar, H., Ueda, N. & Shah, S. V. 1996. Role of reactive oxygen metabolites in DNA damage and cell death in chemical hypoxic injury to LLC-PK1 cells. - Am. J. Physiol. 271: F209-F215.
    • (1996) Am. J. Physiol. , vol.271
    • Hagar, H.1    Ueda, N.2    Shah, S.V.3
  • 35
    • 0030266346 scopus 로고    scopus 로고
    • Resistance gene-dependent plant defense responses
    • Hammond-Kosack, K. E. & Jones, J. D. G. 1996. Resistance gene-dependent plant defense responses. - Plant Cell 8: 1773-1791.
    • (1996) Plant Cell , vol.8 , pp. 1773-1791
    • Hammond-Kosack, K.E.1    Jones, J.D.G.2
  • 36
    • 0028809394 scopus 로고
    • Pseudomonas aeruginosa sodA and sodB mutants defective in manganese- And iron-cofactored superoxide dismutase activity demonstrate the importance of the iron-cofactored form in aerobic metabolism
    • Hassett, D. J., Schweizer, H. P. & Ohman. D. E. 1995. Pseudomonas aeruginosa sodA and sodB mutants defective in manganese-and iron-cofactored superoxide dismutase activity demonstrate the importance of the iron-cofactored form in aerobic metabolism. - J. Bacteriol. 177: 6330-6337.
    • (1995) J. Bacteriol. , vol.177 , pp. 6330-6337
    • Hassett, D.J.1    Schweizer, H.P.2    Ohman, D.E.3
  • 37
    • 85053516230 scopus 로고
    • Glutathione
    • R. G. Alscher and J. L. Hess, eds, CRC Press, Boca Raton, FL. ISBN 0-8493-6328-4
    • Hausladen, A. & Alscher, R. G. 1993. Glutathione. - In Antioxidants in Higher Plants (R. G. Alscher and J. L. Hess, eds), pp. 1-30. CRC Press, Boca Raton, FL. ISBN 0-8493-6328-4.
    • (1993) Antioxidants in Higher Plants , pp. 1-30
    • Hausladen, A.1    Alscher, R.G.2
  • 38
    • 0028427877 scopus 로고
    • Purification and characterization of glutathione reductase isozymes specific for the state of cold hardiness of red spruce
    • _ & Alscher, R. G. 1994a. Purification and characterization of glutathione reductase isozymes specific for the state of cold hardiness of red spruce. - Plant Physiol. 105: 205-213.
    • (1994) Plant Physiol. , vol.105 , pp. 205-213
    • Alscher, R.G.1
  • 39
    • 0028425499 scopus 로고
    • Cold-hardiness specific glutathione reductase isozymes in red spruce. Thermal dependence of kinetic parameters and possible regulatory mechanisms
    • _ & Alscher, R. G. 1994b. Cold-hardiness specific glutathione reductase isozymes in red spruce. Thermal dependence of kinetic parameters and possible regulatory mechanisms. - Plant Physiol. 105: 215-223.
    • (1994) Plant Physiol. , vol.105 , pp. 215-223
    • Alscher, R.G.1
  • 40
    • 85053562294 scopus 로고
    • Vitamin E, alpha-tocopherol
    • R. G. Alscher and J. L. Hess, eds, CRC Press, Boca Raton, FL. ISBN 0-8493-6328-4
    • Hess, J. L. 1993. Vitamin E, alpha-tocopherol. - In Antioxidants in Higher Plants (R. G. Alscher and J. L. Hess, eds), pp. 111-134. CRC Press, Boca Raton, FL. ISBN 0-8493-6328-4.
    • (1993) Antioxidants in Higher Plants , pp. 111-134
    • Hess, J.L.1
  • 41
    • 0026443939 scopus 로고
    • Functional differences between manganese and iron superoxide dismutases in Escherichia coli K-12
    • Hopkin, K. A., Papazian, M. A. & Steinman, H. M. 1992. Functional differences between manganese and iron superoxide dismutases in Escherichia coli K-12. - J. Biol. Chem. 267: 24253-24258.
    • (1992) J. Biol. Chem. , vol.267 , pp. 24253-24258
    • Hopkin, K.A.1    Papazian, M.A.2    Steinman, H.M.3
  • 42
    • 0029865598 scopus 로고    scopus 로고
    • cDNAs encoding spinach stromal and thylakoid-bound ascorbate peroxidase, differing in the presence or absence of their 3'-coding regions
    • Ishikawa, T., Sakai, K., Yoshimura, K., Takeda, T. & Shigeoka, S. 1996. cDNAs encoding spinach stromal and thylakoid-bound ascorbate peroxidase, differing in the presence or absence of their 3'-coding regions. - FEBS Lett. 384: 289-293.
    • (1996) FEBS Lett. , vol.384 , pp. 289-293
    • Ishikawa, T.1    Sakai, K.2    Yoshimura, K.3    Takeda, T.4    Shigeoka, S.5
  • 43
    • 0002879407 scopus 로고
    • Characteristic amino acid sequences of chloroplast and cytosol isozymes of CuZn-superoxide dismutase in spinach, rice and horsetail
    • Kanematsu, S. & Asada, K. 1990. Characteristic amino acid sequences of chloroplast and cytosol isozymes of CuZn-superoxide dismutase in spinach, rice and horsetail. - Plant Cell Physiol. 31: 99-112.
    • (1990) Plant Cell Physiol. , vol.31 , pp. 99-112
    • Kanematsu, S.1    Asada, K.2
  • 44
    • 0028486025 scopus 로고
    • The tomato gene for the chloroplastic Cu,Zn superoxide dismutase regulation of expression imposed in transgenic tobacco plants by a short promoter
    • Kardish, N., Magal, N., Aviv, D. & Galun, E. 1994. The tomato gene for the chloroplastic Cu,Zn superoxide dismutase regulation of expression imposed in transgenic tobacco plants by a short promoter. - Plant Mol. Biol. 25: 887-897.
    • (1994) Plant Mol. Biol. , vol.25 , pp. 887-897
    • Kardish, N.1    Magal, N.2    Aviv, D.3    Galun, E.4
  • 45
    • 0026815923 scopus 로고
    • Characterization of cDNAs encoding CuZn-superoxide dismutases in Scots pine
    • Karpinski, S., Wingsle, G., Olsson, O. & Hällgren, J. E. 1992. Characterization of cDNAs encoding CuZn-superoxide dismutases in Scots pine. - Plant Mol. Biol. 18: 545-555.
    • (1992) Plant Mol. Biol. , vol.18 , pp. 545-555
    • Karpinski, S.1    Wingsle, G.2    Olsson, O.3    Hällgren, J.E.4
  • 46
    • 0002977772 scopus 로고    scopus 로고
    • Glutathione, a regulator of chloroplast transcription
    • K. K. Hatzios, ed.. Kluwer Academic Publishers, Dordrecht. (In press)
    • Link, G., Tiller, K. & Baginsky, S. 1997. Glutathione, a regulator of chloroplast transcription. - In Regulation of Enzymatic Systems Detoxifying Xenobiotics in Plants (K. K. Hatzios, ed.). Kluwer Academic Publishers, Dordrecht. (In press).
    • (1997) Regulation of Enzymatic Systems Detoxifying Xenobiotics in Plants
    • Link, G.1    Tiller, K.2    Baginsky, S.3
  • 47
    • 12044253736 scopus 로고
    • Metabolic bases for differences in sensitivity of two pea cultivars to sulfur dioxide
    • Madamanchi, N. R. & Alscher, R. G. 1991. Metabolic bases for differences in sensitivity of two pea cultivars to sulfur dioxide. - Plant Physiol. 97: 88-93.
    • (1991) Plant Physiol. , vol.97 , pp. 88-93
    • Madamanchi, N.R.1    Alscher, R.G.2
  • 48
    • 0028001977 scopus 로고
    • Acquired resistance to herbicides in pea cultivars by exposure to sulfur dioxide
    • _ , Alscher, R., Hatzios, K. & Cramer, C. 1994a. Acquired resistance to herbicides in pea cultivars by exposure to sulfur dioxide. - Pestic. Biochem. Physiol. 48: 31-40.
    • (1994) Pestic. Biochem. Physiol. , vol.48 , pp. 31-40
    • Alscher, R.1    Hatzios, K.2    Cramer, C.3
  • 49
    • 0028518593 scopus 로고
    • Differential response of Cu,Zn superoxide dismutase in two pea cultivars during a short term exposure to sulfur dioxide
    • _ , Donahue, J., Cramer, C., Alscher, R. & Pedersen, K. 1994b. Differential response of Cu,Zn superoxide dismutase in two pea cultivars during a short term exposure to sulfur dioxide. - Plant Mol. Biol. 26: 95-103.
    • (1994) Plant Mol. Biol. , vol.26 , pp. 95-103
    • Donahue, J.1    Cramer, C.2    Alscher, R.3    Pedersen, K.4
  • 50
    • 0000338463 scopus 로고
    • Correlation between CuZn superoxide dismutase and glutahtione reductase, and environmental and xenobiotic stress tolerance in maize inbreds
    • Malan, C., Greyling, M. M. & Gressel, J. 1990. Correlation between CuZn superoxide dismutase and glutahtione reductase, and environmental and xenobiotic stress tolerance in maize inbreds. - Plant Sci. 69: 157-166.
    • (1990) Plant Sci. , vol.69 , pp. 157-166
    • Malan, C.1    Greyling, M.M.2    Gressel, J.3
  • 51
    • 0022504269 scopus 로고
    • Effect of the free radical-generating herbicide paraquat on the expression of the superoxide dismutase (SOD) genes in maize
    • Matters, G. L. & Scandalios, J. G. 1986. Effect of the free radical-generating herbicide paraquat on the expression of the superoxide dismutase (SOD) genes in maize. - Biochim. Biophys. Acta 882: 29-38.
    • (1986) Biochim. Biophys. Acta , vol.882 , pp. 29-38
    • Matters, G.L.1    Scandalios, J.G.2
  • 53
    • 0029824775 scopus 로고    scopus 로고
    • Water-deficit tolerance and field performance of transgenic alfalfa overexpressing superoxide dismutase
    • McKersie, B. D., Bowley, S. R., Harjanto, E. & Leprince, O. 1996. Water-deficit tolerance and field performance of transgenic alfalfa overexpressing superoxide dismutase. - Plant Physiol. 111: 1177-1181.
    • (1996) Plant Physiol. , vol.111 , pp. 1177-1181
    • McKersie, B.D.1    Bowley, S.R.2    Harjanto, E.3    Leprince, O.4
  • 54
    • 0003092129 scopus 로고
    • Studies on reactions of illuminated chloroplasts. 10. Mechanics of the reduction of oxygen and other Hill reagents
    • Mehler, A. H. 1951. Studies on reactions of illuminated chloroplasts. 10. Mechanics of the reduction of oxygen and other Hill reagents. - Arch. Biochem. Biophys. 33: 65-77.
    • (1951) Arch. Biochem. Biophys. , vol.33 , pp. 65-77
    • Mehler, A.H.1
  • 55
    • 84989683640 scopus 로고
    • Electron spin resonance evidence for the formation of free radicals in plants exposed to ozone
    • Mehlhorn, H., Tabner, B. J. & Wellburn, A. R. 1990. Electron spin resonance evidence for the formation of free radicals in plants exposed to ozone. - Physiol. Plant. 79: 377-383.
    • (1990) Physiol. Plant. , vol.79 , pp. 377-383
    • Mehlhorn, H.1    Tabner, B.J.2    Wellburn, A.R.3
  • 56
    • 0026793997 scopus 로고
    • Molecular cloning and characterization of a gene encoding pea cytosolic ascorbate peroxidase
    • Mittler, R. & Zilinskas, B. A. 1992. Molecular cloning and characterization of a gene encoding pea cytosolic ascorbate peroxidase. - J. Biol. Chem. 267: 21802-21807.
    • (1992) J. Biol. Chem. , vol.267 , pp. 21802-21807
    • Mittler, R.1    Zilinskas, B.A.2
  • 57
    • 0028385024 scopus 로고
    • Regulation of pea cytosolic ascorbate peroxidase and other antioxidant enzymes during the progression of drought stress and following recovery from drought
    • _ & Zilinskas, B. 1994. Regulation of pea cytosolic ascorbate peroxidase and other antioxidant enzymes during the progression of drought stress and following recovery from drought. - Plant J. 5: 397-405.
    • (1994) Plant J. , vol.5 , pp. 397-405
    • Zilinskas, B.1
  • 58
    • 0028801954 scopus 로고
    • Attachment of Cu,Zn SOD to thylakoid membranes at the site of superoxide generation (PSI) in spincah chloroplasts: Detection by immunogold labeling after rapid freezing
    • Ogawa, K., Kanematsu, S., Takebe, K. & Asada, K. 1995. Attachment of Cu,Zn SOD to thylakoid membranes at the site of superoxide generation (PSI) in spincah chloroplasts: Detection by immunogold labeling after rapid freezing. - Plant Cell Phvsiol. 36: 565-573.
    • (1995) Plant Cell Phvsiol. , vol.36 , pp. 565-573
    • Ogawa, K.1    Kanematsu, S.2    Takebe, K.3    Asada, K.4
  • 59
    • 0029802169 scopus 로고    scopus 로고
    • Physiological, biochemical and molecular effects of sulfur dioxide
    • Okpodu, C. M., Alscher, R. G., Grabau, E. A. & Cramer, C. L. 1996. Physiological, biochemical and molecular effects of sulfur dioxide. - J. Plant Physiol. 148: 309-316.
    • (1996) J. Plant Physiol. , vol.148 , pp. 309-316
    • Okpodu, C.M.1    Alscher, R.G.2    Grabau, E.A.3    Cramer, C.L.4
  • 60
    • 0001453595 scopus 로고
    • Perspectives on photoinhibition and photorespiration in the field: Quintessential inefficiencies of the light and dark reactions of photosynthesis?
    • Osmond, C. B. & Grace, S. C. 1995. Perspectives on photoinhibition and photorespiration in the field: Quintessential inefficiencies of the light and dark reactions of photosynthesis? -J. Exp. Bot. 46: 1351-1362.
    • (1995) J. Exp. Bot. , vol.46 , pp. 1351-1362
    • Osmond, C.B.1    Grace, S.C.2
  • 61
    • 0027324284 scopus 로고
    • Hydophobicity as the signal for selective degradation of hydroxyl radical-modified hemoglobin by the multicatalytic proteinase complex, proteasome
    • Pacifici, R. E., Kono, Y. & Davies, K. J. A. 1993. Hydophobicity as the signal for selective degradation of hydroxyl radical-modified hemoglobin by the multicatalytic proteinase complex, proteasome. - J. Biol. Chem. 268: 15405-15411.
    • (1993) J. Biol. Chem. , vol.268 , pp. 15405-15411
    • Pacifici, R.E.1    Kono, Y.2    Davies, K.J.A.3
  • 62
    • 0000211650 scopus 로고
    • Enhanced oxidative stress defence in transgenic potato expressing tomato Cu,Zn superoxide dismutases
    • Perl, A., Perl-Treves, R., Galili, S., Aviv, D., Shalgi, E., Malkin, S. & Galun, E. 1993. Enhanced oxidative stress defence in transgenic potato expressing tomato Cu,Zn superoxide dismutases. - Theor. Appl. Genet. 85: 568-576.
    • (1993) Theor. Appl. Genet. , vol.85 , pp. 568-576
    • Perl, A.1    Perl-Treves, R.2    Galili, S.3    Aviv, D.4    Shalgi, E.5    Malkin, S.6    Galun, E.7
  • 63
    • 0026245748 scopus 로고
    • The tomato Cu,Zn superoxide dismutase genes are developmentally regulated and respond to light and stress
    • Perl-Treves, R. & Galun, E. 1991. The tomato Cu,Zn superoxide dismutase genes are developmentally regulated and respond to light and stress. - Plant Mol. Biol. 17: 745-760.
    • (1991) Plant Mol. Biol. , vol.17 , pp. 745-760
    • Perl-Treves, R.1    Galun, E.2
  • 64
    • 0000988360 scopus 로고
    • The antiozonant ethylenediurea does not act via superoxide dismutase induction in bean
    • Pitcher, L. H., Brennan, E. & Zilinskas. B. A. 1992. The antiozonant ethylenediurea does not act via superoxide dismutase induction in bean. - Plant Physiol. 99: 1388-1392.
    • (1992) Plant Physiol. , vol.99 , pp. 1388-1392
    • Pitcher, L.H.1    Brennan, E.2    Zilinskas, B.A.3
  • 65
    • 0027954797 scopus 로고
    • Evidence for chilling-induced oxidative stress in maize seedlings and a regulatory role for hydrogen peroxide
    • Prasad, T. K., Anderson, M. D., Martin, B. A. & Stewart, C. R. 1994. Evidence for chilling-induced oxidative stress in maize seedlings and a regulatory role for hydrogen peroxide. - Plant Cell 6: 65-74.
    • (1994) Plant Cell , vol.6 , pp. 65-74
    • Prasad, T.K.1    Anderson, M.D.2    Martin, B.A.3    Stewart, C.R.4
  • 66
    • 0001389865 scopus 로고
    • Plasma membrane redox activity: Components and role in plant processes
    • Rubinstein, B. & Luster, D. G. 1993. Plasma membrane redox activity: Components and role in plant processes. - Annu. Rev. Plant Physiol. Plant Mol. Biol. 44: 131-155.
    • (1993) Annu. Rev. Plant Physiol. Plant Mol. Biol. , vol.44 , pp. 131-155
    • Rubinstein, B.1    Luster, D.G.2
  • 67
    • 0025358959 scopus 로고
    • Superoxide dismutase undergoes proteolysis and fragmentation following oxidative modification and inactivation
    • Salo, D. C., Pacifici, R. E., Lin, S. W., Guilivi, C. & Davies, K. J. A. 1990. Superoxide dismutase undergoes proteolysis and fragmentation following oxidative modification and inactivation. - J. Biol. Chem. 265: 11919-11927.
    • (1990) J. Biol. Chem. , vol.265 , pp. 11919-11927
    • Salo, D.C.1    Pacifici, R.E.2    Lin, S.W.3    Guilivi, C.4    Davies, K.J.A.5
  • 69
    • 0002702237 scopus 로고    scopus 로고
    • Molecular biology of the antioxidant defense genes encoding catalases and superoxide dismutases in maize
    • K. K. Hatzios, ed.. Kluwer Academic Publishers, Dordrecht. (In press)
    • _ 1997. Molecular biology of the antioxidant defense genes encoding catalases and superoxide dismutases in maize. - In Regulation of Enzymatic Systems Detoxifying Xenobiotics in Plants (K. K. Hatzios, ed.). Kluwer Academic Publishers, Dordrecht. (In press).
    • (1997) Regulation of Enzymatic Systems Detoxifying Xenobiotics in Plants
  • 70
    • 0027511499 scopus 로고
    • Increased resistance to oxidative stress in transgenic plants that overexpress chloroplastic Cu/Zn superoxide dismutase
    • Sen Gupta, A., Heinen, J. L., Holaday, A. S., Burke, J. J. & Allen, R. D. 1993. Increased resistance to oxidative stress in transgenic plants that overexpress chloroplastic Cu/Zn superoxide dismutase. - Proc. Natl. Acad. Sci. USA 90: 1629-1633.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 1629-1633
    • Sen Gupta, A.1    Heinen, J.L.2    Holaday, A.S.3    Burke, J.J.4    Allen, R.D.5
  • 71
    • 0026633193 scopus 로고
    • A comparison of evolutionary rates of the two major kinds of superoxide dismutase
    • Smith, M. W. & Doolittle, R. F. 1992. A comparison of evolutionary rates of the two major kinds of superoxide dismutase. - J. Mol. Evol. 34: 175-184.
    • (1992) J. Mol. Evol. , vol.34 , pp. 175-184
    • Smith, M.W.1    Doolittle, R.F.2
  • 72
    • 0025417768 scopus 로고
    • Transformed plants with elevated levels of chloroplastic SOD are not more resistant to superoxide toxicity
    • Tepperman, J. M. & Dunsmuir, P. 1990. Transformed plants with elevated levels of chloroplastic SOD are not more resistant to superoxide toxicity. - Plant Mol. Biol. 14: 501-511.
    • (1990) Plant Mol. Biol. , vol.14 , pp. 501-511
    • Tepperman, J.M.1    Dunsmuir, P.2
  • 73
    • 0026200486 scopus 로고
    • Differential regulation of superoxide dismutases in plants exposed to environmental stress
    • Tsang, E. W., Bowler, C., Herouart, D., Van Camp, W. & Inzé, D. 1991. Differential regulation of superoxide dismutases in plants exposed to environmental stress. - Plant Cell 3: 783-792.
    • (1991) Plant Cell , vol.3 , pp. 783-792
    • Tsang, E.W.1    Bowler, C.2    Herouart, D.3    Van Camp, W.4    Inzé, D.5
  • 74
    • 0025686977 scopus 로고
    • Characterization of iron superoxide dismutase cDNAs from plants obtained by genetic complementation in Escherichia coli
    • Van Camp, W., Bowler, C., Villaroel, R., Tsang, E. W. T., Van Montagu, M. & Inzé, D. 1991. Characterization of iron superoxide dismutase cDNAs from plants obtained by genetic complementation in Escherichia coli. - Proc. Natl. Acad. Sci. USA 87: 9903-9907.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 9903-9907
    • Van Camp, W.1    Bowler, C.2    Villaroel, R.3    Tsang, E.W.T.4    Van Montagu, M.5    Inzé, D.6
  • 76
    • 0030452648 scopus 로고    scopus 로고
    • Enhancement of oxidative stress tolerance in transgenic tobacco plants overproducing Fe-superoxide dismutase in chloroplasts
    • _ , Capiau, K., Van Montagu, M., Inzé, D. & Slooten, L. 1996. Enhancement of oxidative stress tolerance in transgenic tobacco plants overproducing Fe-superoxide dismutase in chloroplasts. - Plant Physiol. 112: 1703-1714.
    • (1996) Plant Physiol. , vol.112 , pp. 1703-1714
    • Capiau, K.1    Van Montagu, M.2    Inzé, D.3    Slooten, L.4
  • 77
    • 0030033982 scopus 로고    scopus 로고
    • Arabidopsis MBP1 gene encodes a conserved ubiquitin recognition component of the 26S proteasome
    • Van Nocker, S., Deveraux, Q., Rechsteiner, M. & Viestra, R. D. 1996. Arabidopsis MBP1 gene encodes a conserved ubiquitin recognition component of the 26S proteasome. - Proc. Natl. Acad. Sci. USA 93: 856-860.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 856-860
    • Van Nocker, S.1    Deveraux, Q.2    Rechsteiner, M.3    Viestra, R.D.4
  • 78
    • 0028254307 scopus 로고
    • Ozone, sulfur dioxide, and ultraviolet B have similar effects on mRNA accumulation of antioxidant genes in Nicotiana plumbaginifolia L
    • Willekens, H., Van Camp, W., Van Montagu, M., Inzé, D., Langebartels, C. & Sandermann, H. Jr. 1994. Ozone, sulfur dioxide, and ultraviolet B have similar effects on mRNA accumulation of antioxidant genes in Nicotiana plumbaginifolia L. - Plant Physiol. 106: 1007-1014.
    • (1994) Plant Physiol. , vol.106 , pp. 1007-1014
    • Willekens, H.1    Van Camp, W.2    Van Montagu, M.3    Inzé, D.4    Langebartels, C.5    Sandermann Jr., H.6
  • 79
    • 0026865453 scopus 로고
    • Differential response of maize catalases and superoxide dismutases to the photoactivated fungal toxin cercosporin
    • Williamson, J. D. & Scandalios, J. G. 1992. Differential response of maize catalases and superoxide dismutases to the photoactivated fungal toxin cercosporin. - Plant J. 2: 351-358.
    • (1992) Plant J. , vol.2 , pp. 351-358
    • Williamson, J.D.1    Scandalios, J.G.2
  • 80
    • 0027935268 scopus 로고
    • The redox couple between glutathione and ascorbic acid: A chemical and physiology perspective
    • Winkler, B. S., Orselli, S. M. & Tonia, S. 1994. The redox couple between glutathione and ascorbic acid: A chemical and physiology perspective. - Free Radic. Biol. Med. 17: 333-349.
    • (1994) Free Radic. Biol. Med. , vol.17 , pp. 333-349
    • Winkler, B.S.1    Orselli, S.M.2    Tonia, S.3
  • 81
    • 0029914038 scopus 로고    scopus 로고
    • Photoinhibition of photosystem II from higher plants. Effect of copper inhibition
    • Yruela, I., Pueyo, J. J., Alonso, P. J. & Picorel, R. 1996. Photoinhibition of photosystem II from higher plants. Effect of copper inhibition. - J. Biol. Chem. 271: 27408-27415.
    • (1996) J. Biol. Chem. , vol.271 , pp. 27408-27415
    • Yruela, I.1    Pueyo, J.J.2    Alonso, P.J.3    Picorel, R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.