메뉴 건너뛰기




Volumn 11, Issue 2, 2005, Pages 187-198

Superoxide dismutase and abiotic stress tolerance

Author keywords

[No Author keywords available]

Indexed keywords


EID: 30444446828     PISSN: 09715894     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Review
Times cited : (7)

References (103)
  • 1
    • 0034940405 scopus 로고    scopus 로고
    • Arabidopsis thaliiana Cvi shows an increased tolerance to photooxidative stress and contains a new chloroplastic copper/ zinc superoxide dismutase isozyme
    • Abarca, D., Roldan, M., Martin, M., and Sabater, B. (2001) Arabidopsis thaliiana Cvi shows an increased tolerance to photooxidative stress and contains a new chloroplastic copper/ zinc superoxide dismutase isozyme. J. Exp. Bot, 52:1417-1425.
    • (2001) J. Exp. Bot , vol.52 , pp. 1417-1425
    • Abarca, D.1    Roldan, M.2    Martin, M.3    Sabater, B.4
  • 2
    • 30444437701 scopus 로고    scopus 로고
    • Impact o f climate change on Indian agriculture
    • Aggarwal, P.K. (2003) Impact o f climate change on Indian agriculture. J. plant. Biol, 30(2):189-198.
    • (2003) J Plant Biol , vol.30 , Issue.2 , pp. 189-198
    • Aggarwal, P.K.1
  • 3
    • 0033620622 scopus 로고    scopus 로고
    • Gene structure and expression of the aspen cytosolic Cu/Zn superoxide dismutase
    • Akkapeddi, N., Karnosky, D., Podila, G. K. (1999) Gene structure and expression of the aspen cytosolic Cu/Zn superoxide dismutase. Plant Science, 143: 151-162.
    • (1999) Plant Science , vol.143 , pp. 151-162
    • Akkapeddi, N.1    Karnosky, D.2    Podila, G.K.3
  • 4
    • 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
  • 5
    • 0036001083 scopus 로고    scopus 로고
    • Role of superoxide dismutases in controlling oxidative stress in plants
    • Alscher, R.G., Neval, E., and Heath, L.S. (2002) Role of superoxide dismutases in controlling oxidative stress in plants. J Exp. Bot, 53 (372): 1331-1341.
    • (2002) J Exp Bot , vol.53 , Issue.372 , pp. 1331-1341
    • Alscher, R.G.1    Neval, E.2    Heath, L.S.3
  • 6
    • 0033513358 scopus 로고    scopus 로고
    • The water -water cycle in chloroplasts: Scavenging of active oxygens and dissipation of excess photons
    • Asada, K. (1999) The water -water cycle in chloroplasts: Scavenging of active oxygens and dissipation of excess photons. Annul Rev Plant Physiol Plant Mol Biol. 601-639.
    • (1999) Annul Rev Plant Physiol Plant Mol Biol , pp. 601-639
    • Asada, K.1
  • 7
    • 0035665413 scopus 로고    scopus 로고
    • Purification and partial characterization of superoxide dismutase from chicken erytrocytes
    • Aydemir, T. and Tarhan, L. (2001) Purification and partial characterization of superoxide dismutase from chicken erytrocytes. Turk J Chem, 25: 451-459.
    • (2001) Turk J Chem , vol.25 , pp. 451-459
    • Aydemir, T.1    Tarhan, L.2
  • 8
    • 0037008216 scopus 로고    scopus 로고
    • AtCOX17, an Arabidopsis Homolog of the Yeast Copper Chaperone COX17
    • Balandin, T and Castresana, C. (2002) AtCOX17, an Arabidopsis Homolog of the Yeast Copper Chaperone COX17. Plant Physiol, 129: 1852-1857.
    • (2002) Plant Physiol , vol.129 , pp. 1852-1857
    • Balandin, T.1    Castresana, C.2
  • 10
    • 0023463279 scopus 로고
    • Aspects of the structure, function and applications of superoxide dismutase
    • Bannister, J.V., Bannister, W.H., Rotilio, G. (1987). Aspects of the structure, function and applications of superoxide dismutase. Critical Reviews in Biochemistry, 22:111-180.
    • (1987) Critical Reviews in Biochemistry , vol.22 , pp. 111-180
    • Bannister, J.V.1    Bannister, W.H.2    Rotilio, G.3
  • 11
    • 0000118235 scopus 로고
    • Inhibition of photosynthetic reactions by light. A study with isolated spinach chloroplasts
    • Barenyi, B. and Krause, G.H. (1985) Inhibition of photosynthetic reactions by light. A study with isolated spinach chloroplasts. Planta, 163:218-226.
    • (1985) Planta , vol.163 , pp. 218-226
    • Barenyi, B.1    Krause, G.H.2
  • 12
    • 0028841185 scopus 로고
    • Isolation of an active and heat stable monomeric form of Cu/Zn superoxide dismutase from the periplasmic space of Escherichia coli
    • Battistoni, A and Rotilio, G. (1995) Isolation of an active and heat stable monomeric form of Cu/Zn superoxide dismutase from the periplasmic space of Escherichia coli FEBS Lett, 374: 199-202.
    • (1995) FEBS Lett , vol.374 , pp. 199-202
    • Battistoni, A.1    Rotilio, G.2
  • 13
    • 0019528608 scopus 로고
    • Isolation and characterization of the cytosolic and mitochondrial superoxide dismutase of maize
    • Baum, J.A. and Scandalious, J.G. (1981) Isolation and characterization of the cytosolic and mitochondrial superoxide dismutase of maize. Arch Biochem Biophys 206: 249-264.
    • (1981) Arch Biochem Biophys , vol.206 , pp. 249-264
    • Baum, J.A.1    Scandalious, J.G.2
  • 14
    • 0034055539 scopus 로고    scopus 로고
    • Expression and activity of isoenzymes of superoxide dismutase in in wheat roots in response to hyopxia and anoxia
    • Biemelt, S., Keetman, U., Mock, H.P., and Grimm, B. (2000) Expression and activity of isoenzymes of superoxide dismutase in in wheat roots in response to hyopxia and anoxia; Plant Cell Environ, 23 : 135-144.
    • (2000) Plant Cell Environ , vol.23 , pp. 135-144
    • Biemelt, S.1    Keetman, U.2    Mock, H.P.3    Grimm, B.4
  • 15
    • 0037237973 scopus 로고    scopus 로고
    • Antioxidants, oxidative damage and oxygen deprivation stress: A review
    • Blokhina, O., Virolainen, E. and Fagerstedt, K. V. (2003) Antioxidants, oxidative damage and oxygen deprivation stress: a review; Ann Bot, 91 : 179-194.
    • (2003) Ann Bot , vol.91 , pp. 179-194
    • Blokhina, O.1    Virolainen, E.2    Fagerstedt, K.V.3
  • 16
    • 0345540683 scopus 로고    scopus 로고
    • Water deficit-induced oxidative stress and antioxidative defenses in rice plants
    • Boo, Y. C. and Jung, J. (1999) Water deficit-induced oxidative stress and antioxidative defenses in rice plants; J Plant Physiol, 155 : 255-261.
    • (1999) J Plant Physiol , vol.155 , pp. 255-261
    • Boo, Y.C.1    Jung, J.2
  • 17
    • 0028228085 scopus 로고
    • Conserved patterns in the Cu/Zn superoxide dismutase family
    • Bordo, D., Djinovic, K and Bolognesi, M. (1994).Conserved patterns in the Cu/Zn superoxide dismutase family. J. Mol. Biol, 238: 366-386.
    • (1994) J Mol Biol , vol.238 , pp. 366-386
    • Bordo, D.1    Djinovic, K.2    Bolognesi, M.3
  • 19
    • 0028112660 scopus 로고
    • Cold acclimation increases tolerance of activated oxygen in winter cereals
    • Bridger, G.M., Yang, W., Falk, D.E., McKersie, B.D. (1994). Cold acclimation increases tolerance of activated oxygen in winter cereals. J Plant Physiol, 144: 235-240.
    • (1994) J Plant Physiol , vol.144 , pp. 235-240
    • Bridger, G.M.1    Yang, W.2    Falk, D.E.3    McKersie, B.D.4
  • 20
    • 0034711245 scopus 로고    scopus 로고
    • Tobacco Nectarin I. Purification and characterization as germ-like manganese superoxide dismutase implicated in the defense of floral reproductive tisues
    • Carter, C. and Thornburg, R.W. (2000) Tobacco Nectarin I. Purification and characterization as germ-like manganese superoxide dismutase implicated in the defense of floral reproductive tisues. J. Biol Chem, 275 (47): 36726-36733.
    • (2000) J Biol Chem , vol.275 , Issue.47 , pp. 36726-36733
    • Carter, C.1    Thornburg, R.W.2
  • 22
    • 0035112618 scopus 로고    scopus 로고
    • Differential response of antioxidant enzymes in leaves of necrotic wheat hybrids and their parents
    • Dalal, M., and Khanna-Chopra, R. (2001) Differential response of antioxidant enzymes in leaves of necrotic wheat hybrids and their parents. Physiol Plant, 111 : 297-304.
    • (2001) Physiol Plant , vol.111 , pp. 297-304
    • Dalal, M.1    Khanna-Chopra, R.2
  • 23
    • 0000576780 scopus 로고
    • Isozymes of superoxide dismutase in mitochondria and in peroxisomes isolated from petals of carnation during senescence
    • Droillard, M.J and Paulin, A. (1990) Isozymes of superoxide dismutase in mitochondria and in peroxisomes isolated from petals of carnation during senescence. Plant Physiol, 94: 1187-1192.
    • (1990) Plant Physiol , vol.94 , pp. 1187-1192
    • Droillard, M.J.1    Paulin, A.2
  • 24
    • 0000027474 scopus 로고
    • Metabolism of activated oxygen species
    • Eds Davies, D,D, London: Academic Press
    • Elstner, E.F. (1987) Metabolism of activated oxygen species. In: Biochemistry of Plants, (Eds Davies, D,D,) Vol.11.London: Academic Press, pp235-315.
    • (1987) Biochemistry of Plants , vol.11 , pp. 235-315
    • Elstner, E.F.1
  • 25
    • 1242270806 scopus 로고    scopus 로고
    • Isolation of full length cDNA clone encoding a cytosolic Cu/Zn Superoxide dismutase from the common ice plant, Mesembryanthemum crystallinum
    • Emig, I., Owens, K., Ratajezak, R., Luetge, U and Cushman, J.C (1998) Isolation of full length cDNA clone encoding a cytosolic Cu/Zn Superoxide dismutase from the common ice plant, Mesembryanthemum crystallinum. Plant Physiol, 116: 868-872
    • (1998) Plant Physiol , vol.116 , pp. 868-872
    • Emig, I.1    Owens, K.2    Ratajezak, R.3    Luetge, U.4    Cushman, J.C.5
  • 26
    • 0002841178 scopus 로고
    • Superoxide dismutase from Lens esculenta: Purification and properties
    • Federico, R., Medda, R. and Floris, G. (1985) Superoxide dismutase from Lens esculenta :purification and properties. Plant Physiol, 78: 357-358.
    • (1985) Plant Physiol , vol.78 , pp. 357-358
    • Federico, R.1    Medda, R.2    Floris, G.3
  • 28
    • 0015935503 scopus 로고
    • On the Stability of Bovine Superoxide Dismutase. The Effects of Metals
    • Forman, H. and Fridovich, I (1973) On the Stability of Bovine Superoxide Dismutase. The Effects of Metals. J.Biol.Chem 248: 2645-2649.
    • (1973) J.Biol.Chem , vol.248 , pp. 2645-2649
    • Forman, H.1    Fridovich, I.2
  • 29
    • 0016414528 scopus 로고
    • Superoxide dismutases
    • Fridovich, I. (1975) Superoxide dismutases, Annu Rev Biochem, 44: 147-159.
    • (1975) Annu Rev Biochem , vol.44 , pp. 147-159
    • Fridovich, I.1
  • 30
    • 0022480378 scopus 로고
    • Superoxide dismutases
    • Fridovich, I. (1986) Superoxide dismutases, Adv.Enzymol, 58: 62-97.
    • (1986) Adv.Enzymol , vol.58 , pp. 62-97
    • Fridovich, I.1
  • 31
    • 0032006077 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae LYS7 gene is involved in oxidative stress protection
    • Gamonet, F. and Lauquin, G.J.M (1998) The Saccharomyces cerevisiae LYS7 gene is involved in oxidative stress protection. Eur J Biochem, 251: 716-723.
    • (1998) Eur J Biochem , vol.251 , pp. 716-723
    • Gamonet, F.1    Lauquin, G.J.M.2
  • 32
    • 15844421373 scopus 로고    scopus 로고
    • Characterisation of COX17, a yeast gene in copper metabolism and assembly of cytochrome oxidase
    • Glerum, D.M., Shtanko, A., Tzagoloff, A. (1996) Characterisation of COX17, a yeast gene in copper metabolism and assembly of cytochrome oxidase. J Biol Chem, 271: 14504-14509.
    • (1996) J Biol Chem , vol.271 , pp. 14504-14509
    • Glerum, D.M.1    Shtanko, A.2    Tzagoloff, A.3
  • 33
    • 0000617154 scopus 로고
    • Oxidative damage, lipid peroxidation and antioxidant protection in chloroplast
    • Halliwell, B (1987) Oxidative damage, lipid peroxidation and antioxidant protection in chloroplast. Chem.Phys.Lipids, 44: 327-340.
    • (1987) Chem.Phys.Lipids , vol.44 , pp. 327-340
    • Halliwell, B.1
  • 38
    • 0032134438 scopus 로고    scopus 로고
    • Identification of a functional homolog of the yeast copper homeostasis gene ATX1 from Arabidopsis
    • Himelblau, E., Mira, H., Lin, S.J., Culotta, V.C., Peñarrubia, L., Amasino, R.M. (1998) Identification of a functional homolog of the yeast copper homeostasis gene ATX1 from Arabidopsis. Plant Physiol, 117: 1227-1234
    • (1998) Plant Physiol , vol.117 , pp. 1227-1234
    • Himelblau, E.1    Mira, H.2    Lin, S.J.3    Culotta, V.C.4    Peñarrubia, L.5    Amasino, R.M.6
  • 39
    • 1842709537 scopus 로고
    • Isolation and sequence of complementary DNA encoding human extra-cellular superoxide dismutase
    • USA
    • Hjalmarsson, K., Marklund, S.L., Engstrom, A. and Edlund, T. (1987) Isolation and sequence of complementary DNA encoding human extra-cellular superoxide dismutase. Proc.Natl. Acad.Sci. (USA), 84: 6340-6344.
    • (1987) Proc.Natl. Acad.Sci. , vol.84 , pp. 6340-6344
    • Hjalmarsson, K.1    Marklund, S.L.2    Engstrom, A.3    Edlund, T.4
  • 40
    • 0003459120 scopus 로고    scopus 로고
    • Inter-govermental panel on climate change, report of working group II, Cambridge,UK
    • IPCC 2001.Climate Change (2001) Impact, adaptation and vulnerability; Inter-govermental panel on climate change, report of working group II, Cambridge,UK, 967.
    • (2001) Climate Change (2001) Impact, Adaptation and Vulnerability , pp. 967
  • 41
    • 0002879407 scopus 로고
    • Characteristic amino acid sequences of chloroplast and cytosol isozymes of Cu/Zn superoixde dismutase in spinach, rice and horse tail
    • Kanematsu, S. and Asada, K. (1990) characteristic amino acid sequences of chloroplast and cytosol isozymes of Cu/Zn superoixde dismutase in spinach, rice and horse tail. Plant cell physiol, 31: 99-112
    • (1990) Plant Cell Physiol , vol.31 , pp. 99-112
    • Kanematsu, S.1    Asada, K.2
  • 42
    • 0002879408 scopus 로고
    • Cu/Zn SOD in Rice; Occurrence of an active monomeric enzyme and two types of isozyme in leaf and non photosynthetic tissue
    • Kanesmatsu, S and Asada, K. (1989) Cu/Zn SOD in Rice; Occurrence of an active monomeric enzyme and two types of isozyme in leaf and non photosynthetic tissue. Plant Cell Physiol, 30: 381-391.
    • (1989) Plant Cell Physiol , vol.30 , pp. 381-391
    • Kanesmatsu, S.1    Asada, K.2
  • 43
    • 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 and 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
  • 44
    • 0034863923 scopus 로고    scopus 로고
    • A novel superoxide dismutase with high isoelectric point in higher plants: Expression, regulation, and Protein localization
    • Karpinska, M., Schinkel, K.H., Streller, S., Suss, K.H and Wingle, G. (2001). A novel superoxide dismutase with high isoelectric point in higher plants: Expression, regulation, and Protein localization. Plant Physiol, 126: 1668-1677.
    • (2001) Plant Physiol , vol.126 , pp. 1668-1677
    • Karpinska, M.1    Schinkel, K.H.2    Streller, S.3    Suss, K.H.4    Wingle, G.5
  • 45
    • 84989712875 scopus 로고
    • Free radical and freezing injury to cell membranes of winter wheat
    • Kendall, E.J., McKersie, B.D. (1989) Free radical and freezing injury to cell membranes of winter wheat. Physiol Plant, 76: 86-94.
    • (1989) Physiol Plant , vol.76 , pp. 86-94
    • Kendall, E.J.1    McKersie, B.D.2
  • 46
    • 3142709437 scopus 로고    scopus 로고
    • Heat stable Chloroplastic Cu/Zn SOD in C.murale
    • Khanna Chopra, R and Sabarinath, S. (2004) Heat stable Chloroplastic Cu/Zn SOD in C.murale. Biochem Biophy Res Comm. 321: 1187-1191.
    • (2004) Biochem Biophy Res Comm , vol.321 , pp. 1187-1191
    • Khanna Chopra, R.1    Sabarinath, S.2
  • 47
    • 0026021532 scopus 로고
    • Three dimensional structure of Cu/Zn Superoxide dismutase from spinach at 2.0 A. resolution
    • Kitagawa, Y., Yasuo, N.T., Kusunoki, H.M., Asada, K and Morita, Y. (1991) Three dimensional structure of Cu/Zn Superoxide dismutase from spinach at 2.0 A. resolution. J Biochem, 109: 477-485.
    • (1991) J Biochem , vol.109 , pp. 477-485
    • Kitagawa, Y.1    Yasuo, N.T.2    Kusunoki, H.M.3    Asada, K.4    Morita, Y.5
  • 48
    • 0032187235 scopus 로고    scopus 로고
    • Superoxide dismutase in Arabidopsis: An eclectic enzyme family with disparate regulation and protein Localization
    • Kliebenstein, D. J., Monde, R. A., and Last, R. L. (1998) Superoxide dismutase in Arabidopsis: An eclectic enzyme family with disparate regulation and protein Localization; Plant Physiol, 118 : 637-650.
    • (1998) Plant Physiol , vol.118 , pp. 637-650
    • Kliebenstein, D.J.1    Monde, R.A.2    Last, R.L.3
  • 49
    • 0000531523 scopus 로고
    • The antioxidants of higher plants
    • Larson, R.A.(1988) The antioxidants of higher plants. Phytochemistry 27:969-978.
    • (1988) Phytochemistry , vol.27 , pp. 969-978
    • Larson, R.A.1
  • 50
    • 0029039920 scopus 로고
    • The ATX1 Gene of Saccharomyces cerevisiae encodes a small metal homeostasis factor that protects cells against reactive oxygen toxicity
    • Lin, S., Culotta, V.C. (1995) The ATX1 Gene of Saccharomyces cerevisiae encodes a small metal homeostasis factor that protects cells against reactive oxygen toxicity. Proc Natl Acad Sci (USA), 92: 3784-3788.
    • (1995) Proc Natl Acad Sci (USA) , vol.92 , pp. 3784-3788
    • Lin, S.1    Culotta, V.C.2
  • 51
    • 0029294031 scopus 로고
    • Subunit interaction enhances enzymatic activity and stability of sweet potato cytosolic Cu/Zn superoxide dismutase purified by a His-tagged recombinant protein method
    • Lin, C. T., Lin, M. T., Chen, Yu-T and Shaw, J.F. (1995) Subunit interaction enhances enzymatic activity and stability of sweet potato cytosolic Cu/Zn superoxide dismutase purified by a His-tagged recombinant protein method. Plant. Mol. Biol., 28: 305-311
    • (1995) Plant Mol Biol , vol.28 , pp. 305-311
    • Lin, C.T.1    Lin, M.T.2    Chen, Y.-T.3    Shaw, J.F.4
  • 52
    • 0034624001 scopus 로고    scopus 로고
    • Copper and Zinc containing superoxide dismutase can act as superoxide reductase and a superoxide oxidase
    • Liochev, S.I. and Fridovich, I. (2000) Copper and Zinc containing superoxide dismutase can act as superoxide reductase and a superoxide oxidase. J.Biol.Chem, 275: 38482-38485.
    • (2000) J.Biol.Chem. , vol.275 , pp. 38482-38485
    • Liochev, S.I.1    Fridovich, I.2
  • 53
    • 0025847723 scopus 로고
    • Manganese SOD from Thermus thermophilus. A structural model refined at 1.8A resolution
    • Ludwig, M.L., Metzger, A.L., Pattridge, K.A., and Stallings, W.C. (1991) Manganese SOD from Thermus thermophilus. A structural model refined at 1.8A resolution. J.Mol.Biol 219:335-358.
    • (1991) J.Mol.Biol , vol.219 , pp. 335-358
    • Ludwig, M.L.1    Metzger, A.L.2    Pattridge, K.A.3    Stallings, W.C.4
  • 54
    • 0032793927 scopus 로고    scopus 로고
    • Winter Survival of Transgenic Alfalfa Overexpressing Superoxide Dismutase
    • McKersie Bryan, D, Stephen, R., Bowley, and Kim, S. Jones. (1999) Winter Survival of Transgenic Alfalfa Overexpressing Superoxide Dismutase. Plant Physiol, 119: 839-848.
    • (1999) Plant Physiol , vol.119 , pp. 839-848
    • McKersie Bryan, D.1    Stephen, R.2    Bowley3    Jones, K.S.4
  • 55
    • 0029824775 scopus 로고    scopus 로고
    • Water deficit tolerance and field performance of transgenic alfalfa overexpressing superoxide dismutase
    • McKersie, B.D., Bowley, S., Harjanto, E., Leprince, R. (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.2    Harjanto, E.3    Leprince, R.4
  • 56
  • 57
    • 0034001533 scopus 로고    scopus 로고
    • Iron-superoxide dismutase expression in transgenic alfalfa increases winter survival without a detectable increase in photosynthetic oxidative stress tolerance
    • McKersie, B. D., Murnaghan, J., Jones, K. S., and Bowley, S. R. (2000) Iron-superoxide dismutase expression in transgenic alfalfa increases winter survival without a detectable increase in photosynthetic oxidative stress tolerance. Plant Physiol, 122 : 1427-1438.
    • (2000) Plant Physiol , vol.122 , pp. 1427-1438
    • McKersie, B.D.1    Murnaghan, J.2    Jones, K.S.3    Bowley, S.R.4
  • 58
    • 17744391056 scopus 로고    scopus 로고
    • Evidence for the plant-specific intercellular transport of the Arabidopsis copper chaperone CCH
    • Mira, H., Martinez-Garcia, F., Peñarrubia, L. (2001b) Evidence for the plant-specific intercellular transport of the Arabidopsis copper chaperone CCH. Plant J, 25: 521-528.
    • (2001) Plant J , vol.25 , pp. 521-528
    • Mira, H.1    Martinez-Garcia, F.2    Peñarrubia, L.3
  • 59
    • 0035878742 scopus 로고    scopus 로고
    • Functional and conformational properties of the exclusive C-domain from the Arabidopsis copper chaperone (CCH)
    • Mira, H., Vilar, M., Péres-Payá, E., Peñarrubia, L. (2001a) Functional and conformational properties of the exclusive C-domain from the Arabidopsis copper chaperone (CCH). Biochem J, 357: 545-549.
    • (2001) Biochem J , vol.357 , pp. 545-549
    • Mira, H.1    Vilar, M.2    Péres-Payá, E.3    Peñarrubia, L.4
  • 60
    • 3543019650 scopus 로고    scopus 로고
    • Oxidative DNA Damage Associated with Combination of Guanine and Superoxide Radicals and Repair Mechanisms via Radical Trapping
    • Misiaszek, R., Crean, C., Joffe, A. Geacintov,N. and Shafirovich,V.(2004) Oxidative DNA Damage Associated with Combination of Guanine and Superoxide Radicals and Repair Mechanisms via Radical Trapping. J. Biol. Chem, 279: 32106-32115
    • (2004) J Biol Chem , vol.279 , pp. 32106-32115
    • Misiaszek, R.1    Crean, C.2    Joffe, A.3    Geacintov, N.4    Shafirovich, V.5
  • 61
    • 0036728244 scopus 로고    scopus 로고
    • Oxidative stress, antioxidants and stress tolerance
    • Mitller, R. (2002) Oxidative stress, antioxidants and stress tolerance; Trends Plant Sci, 7 : 405-410.
    • (2002) Trends Plant Sci , vol.7 , pp. 405-410
    • Mitller, R.1
  • 62
    • 0035086009 scopus 로고    scopus 로고
    • Living under a 'dormant' canopy: A molecular acclimation of the desert plant Retama raetam
    • Mitller, R., Merquiol, E., Hallak-Herr, E., Rachmilevitch, S., Kaplan, A., and Cohen, M. (2001) Living under a 'dormant' canopy: a molecular acclimation of the desert plant Retama raetam; Plant J, 25 : 407-416.
    • (2001) Plant J , vol.25 , pp. 407-416
    • Mitller, R.1    Merquiol, E.2    Hallak-Herr, E.3    Rachmilevitch, S.4    Kaplan, A.5    Cohen, M.6
  • 63
    • 0028385024 scopus 로고
    • Regulation of pea cytosolic ascorbate peroxidase and other antioxidant enzymes during the progression of drought and following recovery from drought
    • Mittler, R. and Zilinskas, B.A. (1994) Regulation of pea cytosolic ascorbate peroxidase and other antioxidant enzymes during the progression of drought and following recovery from drought. Plant J, 5:397-405.
    • (1994) Plant J , vol.5 , pp. 397-405
    • Mittler, R.1    Zilinskas, B.A.2
  • 64
    • 0035781005 scopus 로고    scopus 로고
    • Plant mitochondria and oxidative stress: Electron transport, NADPH turnover, and metabolism of reactive oxygen species
    • Möller, I. M. (2001) Plant mitochondria and oxidative stress: electron transport, NADPH turnover, and metabolism of reactive oxygen species; Annu Rev Plant Physiol Plant. Mol. Biol, 52 : 561-591.
    • (2001) Annu Rev Plant Physiol Plant Mol Biol , vol.52 , pp. 561-591
    • Möller, I.M.1
  • 65
    • 0036007031 scopus 로고    scopus 로고
    • Signal transduction in response to excess light: Getting out of the chloroplast
    • Mullineaux, P. M. and Karpinski, S. (2002) Signal transduction in response to excess light: getting out of the chloroplast; Curr Opin Plant Biol, 5 : 43-48.
    • (2002) Curr Opin Plant Biol , vol.5 , pp. 43-48
    • Mullineaux, P.M.1    Karpinski, S.2
  • 66
    • 0031569326 scopus 로고    scopus 로고
    • A critical assessment of the evidence from XAFS and crystallography for the breakage of the imidazolate bridge during catalysis in Cu/Zn superoxide dismutase
    • Murphy, L.M., Strange,R.W. and Hasnain,S.S. (1997) A critical assessment of the evidence from XAFS and crystallography for the breakage of the imidazolate bridge during catalysis in Cu/Zn superoxide dismutase. Structure, 5: 2371-379.
    • (1997) Structure , vol.5 , pp. 2371-2379
    • Murphy, L.M.1    Strange, R.W.2    Hasnain, S.S.3
  • 67
    • 0032466812 scopus 로고    scopus 로고
    • Thylakoid-bound and stromal antioxidative enzymes in wheat treated with excess copper
    • Navari-Izzo, F., Quartacci, M. F., Pinzino, C., Vecchia, F. D., and Sgherri, L. M. C. (1998) Thylakoid-bound and stromal antioxidative enzymes in wheat treated with excess copper. Physiol Plant, 104: 630-638.
    • (1998) Physiol Plant , vol.104 , pp. 630-638
    • Navari-Izzo, F.1    Quartacci, M.F.2    Pinzino, C.3    Vecchia, F.D.4    Sgherri, L.M.C.5
  • 69
    • 0028801954 scopus 로고
    • Attachment of Cu/Zn SOD to thylakoid membranes at the site of superoxide generation (PSI) in spinach chloroplast: Detection by immuno-gold labeling after rapid freezing and subtitution method
    • Ogawa, K., Kanesmatsu, S., Takabe, K. and Asada, K. (1995) Attachment of Cu/Zn SOD to thylakoid membranes at the site of superoxide generation (PSI) in spinach chloroplast: detection by immuno-gold labeling after rapid freezing and subtitution method. Plant Cell Physiol. 36:565-573.
    • (1995) Plant Cell Physiol , vol.36 , pp. 565-573
    • Ogawa, K.1    Kanesmatsu, S.2    Takabe, K.3    Asada, K.4
  • 70
    • 0026711256 scopus 로고
    • Atomic structure of wild type and thermostable mutant recombinant human Cu/Zn superoxide dismutase
    • USA
    • Parege, H. E., Hallewell, R.A and Tainer, J.A (1992) Atomic structure of wild type and thermostable mutant recombinant human Cu/Zn superoxide dismutase. Proc. Natl. Acad. Sci. (USA), 89: 6109-6113.
    • (1992) Proc Natl Acad Sci , vol.89 , pp. 6109-6113
    • Parege, H.E.1    Hallewell, R.A.2    Tainer, J.A.3
  • 72
    • 0034973677 scopus 로고    scopus 로고
    • Dissecting the superoxide dismutase-ascorbate-glutathione-pathway in chloroplasts by metabolic modeling. Computer simulations as a step towards flux analysis
    • Polle, A. (2001) Dissecting the superoxide dismutase-ascorbate- glutathione-pathway in chloroplasts by metabolic modeling. Computer simulations as a step towards flux analysis; Plant Physiol, 126 : 445-462.
    • (2001) Plant Physiol , vol.126 , pp. 445-462
    • Polle, A.1
  • 74
    • 0033785074 scopus 로고    scopus 로고
    • Jasmonic acid signalling modulates ozone-induced hypersensitive cell death
    • Rao, M.V., Lee H., Creelman, R.A., Mullet, J.E., and Davis,K.R. (2000) Jasmonic acid signalling modulates ozone-induced hypersensitive cell death. The Plant Cell, 12: 1633-1646.
    • (2000) The Plant Cell , vol.12 , pp. 1633-1646
    • Rao, M.V.1    Lee, H.2    Creelman, R.A.3    Mullet, J.E.4    Davis, K.R.5
  • 75
    • 0027762219 scopus 로고
    • Cloning and sequencing analysis of a cDNA for manganese superoxide dismutase from rice
    • Sakamoto, A., Yasuhoto, N. and Tanaka, K. (1993) Cloning and sequencing analysis of a cDNA for manganese superoxide dismutase from rice. Plant Physiol, 103:1477-1478.
    • (1993) Plant Physiol , vol.103 , pp. 1477-1478
    • Sakamoto, A.1    Yasuhoto, N.2    Tanaka, K.3
  • 76
    • 0028816621 scopus 로고
    • Effect of chilling on activated oxygen-scavenging enzymes in low temperature-sensitive and -tolerant cultivars of rice (Oryza sativa L.)
    • Saruyama, H., and Tanida, M. (1995) Effect of chilling on activated oxygen-scavenging enzymes in low temperature-sensitive and -tolerant cultivars of rice (Oryza sativa L.). Plant Sci, 109 : 105-113.
    • (1995) Plant Sci , vol.109 , pp. 105-113
    • Saruyama, H.1    Tanida, M.2
  • 77
    • 0002696602 scopus 로고
    • Oxygen stress and superoxide dismutases
    • Scandalious, J.G (1993) Oxygen stress and superoxide dismutases. Plant Physiol, 101:7-12.
    • (1993) Plant Physiol , vol.101 , pp. 7-12
    • Scandalious, J.G.1
  • 78
    • 0031810627 scopus 로고    scopus 로고
    • Multiple forms of extracellular superoxide dismutase in needles,stem tissues and seeds of scots pine
    • Schinkel,H., Streller,S. And Wingsle,G. (1998) Multiple forms of extracellular superoxide dismutase in needles,stem tissues and seeds of scots pine. J.Exp.Bot, 49: 931-936.
    • (1998) J.Exp.Bot , vol.49 , pp. 931-936
    • Schinkel, H.1    Streller, S.2    Wingsle, G.3
  • 79
    • 0024095632 scopus 로고
    • Cloning and characterization of cDNA encoding the chloroplastic Cu/Zn superoxide dismutase from pea
    • USA
    • Scioli, J.R., and Zilinskas, B.A. (1988) Cloning and characterization of cDNA encoding the chloroplastic Cu/Zn superoxide dismutase from pea. Proc Natl Acad Sci (USA), 85:7661-7665.
    • (1988) Proc Natl Acad Sci , vol.85 , pp. 7661-7665
    • Scioli, J.R.1    Zilinskas, B.A.2
  • 80
    • 0027141553 scopus 로고
    • Over expression of superoxide dismutase protects plants from oxidative stress
    • SenGupta, A., Webb, R.P., Holaday, A.S, Allen, R.D (1993b) Over expression of superoxide dismutase protects plants from oxidative stress. Plant Physiol, 103:1067-1073.
    • (1993) Plant Physiol , vol.103 , pp. 1067-1073
    • SenGupta, A.1    Webb, R.P.2    Holaday, A.S.3    Allen, R.D.4
  • 81
    • 0027511499 scopus 로고
    • Increased resistance to oxidative stress in transgenic plants that overexpress chloroplastic Cu/Zn superoxide dimsutase
    • USA
    • SenGupta, A., Heinon J.L., Holaday,A.S., Burke,J.J., and Allen R.D. (1993a) Increased resistance to oxidative stress in transgenic plants that overexpress chloroplastic Cu/Zn superoxide dimsutase. Proc.Natl.Aca.Sci.(USA), 90:1629-1633.
    • (1993) Proc.Natl.Aca.Sci. , vol.90 , pp. 1629-1633
    • Sengupta, A.1    Heinon, J.L.2    Holaday, A.S.3    Burke, J.J.4    Allen, R.D.5
  • 83
    • 0033555968 scopus 로고    scopus 로고
    • Bicarbonate is required for the peroxidase function of Cu/Zn Superoxide dismutase at physiological pH
    • Shankarapandi, S and Zweier, J.L. (1999) Bicarbonate is required for the peroxidase function of Cu/Zn Superoxide dismutase at physiological pH. J Biol Chem, 274: 1226-1232.
    • (1999) J Biol Chem , vol.274 , pp. 1226-1232
    • Shankarapandi, S.1    Zweier, J.L.2
  • 85
    • 84987012931 scopus 로고
    • The role of active oxygen in the response of plants to water deficit and desiccation
    • Smirnoff, N. (1993) The role of active oxygen in the response of plants to water deficit and desiccation. New Phytol, 125: 27-58.
    • (1993) New Phytol , vol.125 , pp. 27-58
    • Smirnoff, N.1
  • 86
    • 0035834564 scopus 로고    scopus 로고
    • Induction of new isoforms of Superoxide dismutase and catalase enzymes in flag leaf of wheat during monocarpic senescence
    • Srivalli, B and Khanna-Chopra, R. (2001) Induction of new isoforms of Superoxide dismutase and catalase enzymes in flag leaf of wheat during monocarpic senescence. Biochem.Biophy Res Comm, 288:1307-1042.
    • (2001) Biochem.Biophy Res Comm , vol.288 , pp. 1307-11042
    • Srivalli, B.1    Khanna-Chopra, R.2
  • 87
    • 0345526533 scopus 로고    scopus 로고
    • Antioxidative defense system in an upland rice cultivar subjected to increasing intensity of water stress followed by recovery
    • Srivalli, B. Sharma, G and Khanna-Chopra, R. (2003) Antioxidative defense system in an upland rice cultivar subjected to increasing intensity of water stress followed by recovery. Physiol Plant, 119:503-512.
    • (2003) Physiol Plant , vol.119 , pp. 503-512
    • Srivalli, B.1    Sharma, G.2    Khanna-Chopra, R.3
  • 88
    • 85163503890 scopus 로고    scopus 로고
    • The effects of heat stress on cereals yield and quality
    • (Eds Basra, A. S.), Food products press, Binghamton, NY
    • Stone, P. (2001) The effects of heat stress on cereals yield and quality. In: Crop responses and adaptation to temperature stress, (Eds Basra, A. S.), Food products press, Binghamton, NY. pp 243-291.
    • (2001) Crop Responses and Adaptation to Temperature Stress , pp. 243-291
    • Stone, P.1
  • 89
    • 0021105282 scopus 로고
    • Superoxide anion permeability of phospholipid membranes and chloroplast thylakoids
    • Takahashi, M., and Asada K. (1983) Superoxide anion permeability of phospholipid membranes and chloroplast thylakoids. Arch.Biochem.Biophys. 226: 558-66.
    • (1983) Arch.Biochem.Biophys. , vol.226 , pp. 558-566
    • Takahashi, M.1    Asada, K.2
  • 90
    • 0001600620 scopus 로고
    • Cloning and nucleotide equence of a petunia gene encoding a chloroplast localized superoxide dismutase
    • Tepperman, J., Katayama, C. and Dunsmuir, P. (1988) Cloning and nucleotide equence of a petunia gene encoding a chloroplast localized superoxide dismutase. Plant Mol.Biol, 1: 871-872.
    • (1988) Plant Mol.Biol , vol.1 , pp. 871-872
    • Tepperman, J.1    Katayama, C.2    Dunsmuir, P.3
  • 91
    • 0026245748 scopus 로고
    • The tomato Cu/Zn superoxide dismutase genes and developmentally regulated and respond to light and stresss
    • Treves-Perl, R. and Galun, E (1991) The tomato Cu/Zn superoxide dismutase genes and developmentally regulated and respond to light and stresss. Plant Mol Biol, 17:745-760.
    • (1991) Plant Mol Biol , vol.17 , pp. 745-760
    • Treves-Perl, R.1    Galun, E.2
  • 92
    • 0142152464 scopus 로고    scopus 로고
    • Isolation of a Gene Encoding a Copper Chaperone for the Copper/Zinc Superoxide Dismutase and Characterization of Its Promoter in Potato
    • Trindade, L., Beatrix, M., Horvath, M., Marjan, J., Bergervoet, E., and Richard G.F. (2003) Isolation of a Gene Encoding a Copper Chaperone for the Copper/Zinc Superoxide Dismutase and Characterization of Its Promoter in Potato. Plant Physiol, 133: 618-629.
    • (2003) Plant Physiol , vol.133 , pp. 618-629
    • Trindade, L.1    Beatrix, M.2    Horvath, M.3    Marjan, J.4    Bergervoet, E.5    Richard, G.F.6
  • 94
    • 0033548190 scopus 로고    scopus 로고
    • Iron SOD from the archaeon, Sulfolobus Solfactaricus: Analysis of structure and thermostability
    • Ursby, T.B.S., Adinolfi, S., Al-Karadaghi, E., De Vendittis and Bocchini, V. (1999) Iron SOD from the archaeon, Sulfolobus Solfactaricus: analysis of structure and thermostability. J. Mol. Biol., 286: 189-205.
    • (1999) J Mol Biol , vol.286 , pp. 189-205
    • Ursby, T.B.S.1    Adinolfi, S.2    Al-Karadaghi, E.3    De Vendittis4    Bocchini, V.5
  • 95
    • 0030452648 scopus 로고    scopus 로고
    • Enhancement of oxidative stress tolerance in transgenic tobacco plants overexpressing Fe SOD in chloroplast
    • Van Camp, W., Capiaue, K., VanMontagu, M., Inze, D. and Slooten, S. (1996) Enhancement of oxidative stress tolerance in transgenic tobacco plants overexpressing Fe SOD in chloroplast. Plant Physiol, 112:1703-1714.
    • (1996) Plant Physiol , vol.112 , pp. 1703-1714
    • Van Camp, W.1    Capiaue, K.2    Vanmontagu, M.3    Inze, D.4    Slooten, S.5
  • 96
    • 0001204663 scopus 로고
    • Heat stability of superoxide dismutase in cabbage
    • Walker, J.L., McLennan, K.M. and Robinson, D. S. (1991) Heat stability of superoxide dismutase in cabbage. Food Chem, 23: 245-256.
    • (1991) Food Chem , vol.23 , pp. 245-256
    • Walker, J.L.1    McLennan, K.M.2    Robinson, D.S.3
  • 97
    • 0036669912 scopus 로고    scopus 로고
    • Plant copper chaperones
    • Wintz, H., Vulpe, C. (2002) Plant copper chaperones. Biochem Soc Trans, 30: 732-735.
    • (2002) Biochem Soc Trans , vol.30 , pp. 732-735
    • Wintz, H.1    Vulpe, C.2
  • 98
    • 0000249563 scopus 로고
    • Chilling enhanced photooxidation. Evidence for the role of singlet oxygen and superoxide in the breakdown of pigments and endogenous antioxidants
    • Wise, R. R and Naylor, A. W. (1987) Chilling enhanced photooxidation. Evidence for the role of singlet oxygen and superoxide in the breakdown of pigments and endogenous antioxidants; Plant Physiol, 83: 278-282.
    • (1987) Plant Physiol , vol.83 , pp. 278-282
    • Wise, R.R.1    Naylor, A.W.2
  • 99
    • 0033150269 scopus 로고    scopus 로고
    • Isolation, chromosomal localization, and differential expression of mitochondrial manganese superoxide dismutase and chloroplastic copper/zinc superoxide dismutase genes in wheat
    • Wu, G., Wilen, R. W., Robertson, A. J., and Gusta, L. V. (1999) Isolation, chromosomal localization, and differential expression of mitochondrial manganese superoxide dismutase and chloroplastic copper/zinc superoxide dismutase genes in wheat. Plant Physiol, 120: 513-520.
    • (1999) Plant Physiol , vol.120 , pp. 513-520
    • Wu, G.1    Wilen, R.W.2    Robertson, A.J.3    Gusta, L.V.4
  • 100
    • 0029851133 scopus 로고    scopus 로고
    • Flooding-induced membrane damage, lipid oxidation and activated oxygen generation in corn leaves
    • Yan, B., Dai, Q., Liu, X., Huang, S., and Wang, Z. (1996) Flooding-induced membrane damage, lipid oxidation and activated oxygen generation in corn leaves. Plant Soil, 179: 261-268.
    • (1996) Plant Soil , vol.179 , pp. 261-268
    • Yan, B.1    Dai, Q.2    Liu, X.3    Huang, S.4    Wang, Z.5
  • 102
    • 0027515397 scopus 로고
    • Maize mitochondrial manganese superoxide dismutases are encoded by a differentially expressed multigene family
    • USA
    • Zhu, D. and Scandalious, J.G. (1993) Maize mitochondrial manganese superoxide dismutases are encoded by a differentially expressed multigene family. Proc Natl Acad Sci. (USA), 90: 9310-9314.
    • (1993) Proc Natl Acad Sci , vol.90 , pp. 9310-9314
    • Zhu, D.1    Scandalious, J.G.2
  • 103
    • 0034624957 scopus 로고    scopus 로고
    • Cobalt (2+) binding to human and tomato copper chaperone for superoxide dismutase: Implications for the metal ion transfer mechanism
    • Zhu, H., Shipp, E., Sanchez, R.J., Liba, A., Stine, J.E., Hart, J., Gralla, E.B., Nersissian A.M., Valentine, J.S. (2000) Cobalt (2+) binding to human and tomato copper chaperone for superoxide dismutase: implications for the metal ion transfer mechanism. Biochemistry, 39: 5413-5421.
    • (2000) Biochemistry , vol.39 , pp. 5413-5421
    • Zhu, H.1    Shipp, E.2    Sanchez, R.J.3    Liba, A.4    Stine, J.E.5    Hart, J.6    Gralla, E.B.7    Nersissian, A.M.8    Valentine, J.S.9


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.