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Volumn 505, Issue 2, 2012, Pages 309-317

Biochemical and molecular analyses of copper-zinc superoxide dismutase from a C 4 plant Pennisetum glaucum reveals an adaptive role in response to oxidative stress

Author keywords

Abiotic stress; Homology modeling; In gel activity; Methyl viologen; Thermostability; Transcript analysis

Indexed keywords

COPPER ZINC SUPEROXIDE DISMUTASE; PARAQUAT;

EID: 84864145862     PISSN: 03781119     EISSN: 18790038     Source Type: Journal    
DOI: 10.1016/j.gene.2012.06.001     Document Type: Article
Times cited : (24)

References (68)
  • 1
    • 74449091635 scopus 로고    scopus 로고
    • Superoxide dismutases - a review of the metal-associated mechanistic variations
    • Abreu I.S., Cabelli D.E. Superoxide dismutases - a review of the metal-associated mechanistic variations. Biochim. Biophys. Acta 2010, 1804:263-274.
    • (2010) Biochim. Biophys. Acta , vol.1804 , pp. 263-274
    • Abreu, I.S.1    Cabelli, D.E.2
  • 2
    • 0036001083 scopus 로고    scopus 로고
    • Role of superoxide dismutases SODs in controlling oxidative stress in plants
    • Alscher R.G., Erturk N., Heath L.S. Role of superoxide dismutases SODs in controlling oxidative stress in plants. J. Exp. Bot. 2002, 53:1331-1341.
    • (2002) J. Exp. Bot. , vol.53 , pp. 1331-1341
    • Alscher, R.G.1    Erturk, N.2    Heath, L.S.3
  • 3
    • 32144432437 scopus 로고    scopus 로고
    • The SWISS-MODEL workspace: a web based environment for protein structure homology modeling
    • Arnold K., Bordoli L., Kopp J., Schwede T. The SWISS-MODEL workspace: a web based environment for protein structure homology modeling. Bioinformatics 2006, 22:195-201.
    • (2006) Bioinformatics , vol.22 , pp. 195-201
    • Arnold, K.1    Bordoli, L.2    Kopp, J.3    Schwede, T.4
  • 4
    • 0033513358 scopus 로고    scopus 로고
    • The water-water cycle in chloroplasts: scavenging of active oxygens and dissipation of excess photons
    • Asada K. The water-water cycle in chloroplasts: scavenging of active oxygens and dissipation of excess photons. Annu. Rev. Plant Physiol. Plant Mol. Biol. 1999, 50:601-639.
    • (1999) Annu. Rev. Plant Physiol. Plant Mol. Biol. , vol.50 , pp. 601-639
    • Asada, K.1
  • 6
    • 33645219172 scopus 로고    scopus 로고
    • The hydrogen peroxide reactivity of peptidylglycine monooxygenase supports a Cu (II)-superoxo catalytic intermediate
    • Bauman A.T., Yukl E.T., Alkevich K., McCormack A.L., Blackburn N.J. The hydrogen peroxide reactivity of peptidylglycine monooxygenase supports a Cu (II)-superoxo catalytic intermediate. J. Biol. Chem. 2006, 281:4190-4198.
    • (2006) J. Biol. Chem. , vol.281 , pp. 4190-4198
    • Bauman, A.T.1    Yukl, E.T.2    Alkevich, K.3    McCormack, A.L.4    Blackburn, N.J.5
  • 7
    • 0020685136 scopus 로고
    • Purification and properties of a unique superoxide dismutase from Nocardia asteroides
    • Beaman B.L., Scates S.M., Moring S.E., Deem R., Misra H.P. Purification and properties of a unique superoxide dismutase from Nocardia asteroides. J. Biol. Chem. 1983, 258:91-96.
    • (1983) J. Biol. Chem. , vol.258 , pp. 91-96
    • Beaman, B.L.1    Scates, S.M.2    Moring, S.E.3    Deem, R.4    Misra, H.P.5
  • 8
    • 0015153416 scopus 로고
    • Superoxide dismutase: improved assays and an assay applicable to acrylamide gels
    • Beauchamp C., Fridovich I. Superoxide dismutase: improved assays and an assay applicable to acrylamide gels. Anal. Biochem. 1971, 44:276-287.
    • (1971) Anal. Biochem. , vol.44 , pp. 276-287
    • Beauchamp, C.1    Fridovich, I.2
  • 9
    • 0028228085 scopus 로고
    • Conserved patterns in the Cu-Zn superoxide dismutase family
    • Bordo D., Djinovic K., Bolognesi M. Conserved patterns in the Cu-Zn superoxide dismutase family. J. Mol. Biol. 1994, 238:366-386.
    • (1994) J. Mol. Biol. , vol.238 , pp. 366-386
    • Bordo, D.1    Djinovic, K.2    Bolognesi, M.3
  • 10
    • 33745655970 scopus 로고    scopus 로고
    • Reactive oxygen species in plant cell death
    • Breusegem F.V., Dat J.F. Reactive oxygen species in plant cell death. Plant Physiol. 2006, 141:384-390.
    • (2006) Plant Physiol. , vol.141 , pp. 384-390
    • Breusegem, F.V.1    Dat, J.F.2
  • 13
    • 70350464126 scopus 로고    scopus 로고
    • Heterologous oligonucleotide microarrays for transcriptomics in a non-model species; a proof-of-concept study of drought stress in Musa
    • Davey M.W., Graham N.S., Vanholme B., Swennen R., May S.T., Keulemans J. Heterologous oligonucleotide microarrays for transcriptomics in a non-model species; a proof-of-concept study of drought stress in Musa. BMC Genomics 2009, 10:436.
    • (2009) BMC Genomics , vol.10 , pp. 436
    • Davey, M.W.1    Graham, N.S.2    Vanholme, B.3    Swennen, R.4    May, S.T.5    Keulemans, J.6
  • 14
    • 79952705700 scopus 로고    scopus 로고
    • Molecular cloning and expression of two cytosolic copper-zinc superoxide dismutases genes from Nelumbo nucifera
    • Dong C., Zheng X., Li G., Zhu H., Zhou M., Hu Z. Molecular cloning and expression of two cytosolic copper-zinc superoxide dismutases genes from Nelumbo nucifera. Appl. Biochem. Biotechnol. 2011, 163:679-691.
    • (2011) Appl. Biochem. Biotechnol. , vol.163 , pp. 679-691
    • Dong, C.1    Zheng, X.2    Li, G.3    Zhu, H.4    Zhou, M.5    Hu, Z.6
  • 15
    • 84865746886 scopus 로고    scopus 로고
    • Modulation of tobacco bacterial disease resistance using cytosolic ascorbate peroxidase and Cu,Zn-superoxide
    • Faize M., et al. Modulation of tobacco bacterial disease resistance using cytosolic ascorbate peroxidase and Cu,Zn-superoxide. Plant Pathol. 2011, 10.1111/j.1365-3059.2011.02570.x.
    • (2011) Plant Pathol.
    • Faize, M.1
  • 16
    • 25844468618 scopus 로고    scopus 로고
    • Redox homeostasis and antioxidant signaling: a metabolic interface between stress perception and physiological responses
    • Foyer C.H., Noctor G. Redox homeostasis and antioxidant signaling: a metabolic interface between stress perception and physiological responses. Plant Cell 2005, 17:1866-1875.
    • (2005) Plant Cell , vol.17 , pp. 1866-1875
    • Foyer, C.H.1    Noctor, G.2
  • 17
    • 0002829382 scopus 로고
    • Superoxide dismutases
    • Fridovich I. Superoxide dismutases. Adv. Enzymol. 1986, 58:62-67.
    • (1986) Adv. Enzymol. , vol.58 , pp. 62-67
    • Fridovich, I.1
  • 18
    • 0024308039 scopus 로고
    • Superoxide dismutases
    • Fridovich I. Superoxide dismutases. J. Biol. Chem. 1989, 264:7761-7764.
    • (1989) J. Biol. Chem. , vol.264 , pp. 7761-7764
    • Fridovich, I.1
  • 19
    • 0029053451 scopus 로고
    • Superoxide radical and superoxide dismutases
    • Fridovich I. Superoxide radical and superoxide dismutases. Annu. Rev. Biochem. 1995, 64:97-112.
    • (1995) Annu. Rev. Biochem. , vol.64 , pp. 97-112
    • Fridovich, I.1
  • 20
    • 79958775004 scopus 로고    scopus 로고
    • Physiology and proteomics of drought stress acclimation in sunflower (Helianthus annuus L.)
    • Fulda S., Mikkat S., Stegmann H., Horn R. Physiology and proteomics of drought stress acclimation in sunflower (Helianthus annuus L.). Plant Biol. 2011, 13:632-642.
    • (2011) Plant Biol. , vol.13 , pp. 632-642
    • Fulda, S.1    Mikkat, S.2    Stegmann, H.3    Horn, R.4
  • 21
    • 83355177425 scopus 로고    scopus 로고
    • Over-expression of Potentilla superoxide dismutase improves salt stress tolerance during germination and growth in Arabidopsis thaliana
    • Gill T., Kumar S., Ahuja P.S., Sreenivasulu Y. Over-expression of Potentilla superoxide dismutase improves salt stress tolerance during germination and growth in Arabidopsis thaliana. J. Plant Genet. Transgenics 2010, 1:1-10.
    • (2010) J. Plant Genet. Transgenics , vol.1 , pp. 1-10
    • Gill, T.1    Kumar, S.2    Ahuja, P.S.3    Sreenivasulu, Y.4
  • 23
    • 33845489442 scopus 로고    scopus 로고
    • Differential responses of antioxidative system to chilling and drought in four rice cultivars differing in sensitivity
    • Guo Z., Ou W., Lu S., Zhong Q. Differential responses of antioxidative system to chilling and drought in four rice cultivars differing in sensitivity. Plant Physiol. Biochem. 2006, 44:828-836.
    • (2006) Plant Physiol. Biochem. , vol.44 , pp. 828-836
    • Guo, Z.1    Ou, W.2    Lu, S.3    Zhong, Q.4
  • 24
    • 0036736412 scopus 로고    scopus 로고
    • Cold and salt stress regulates the expression and activity of a chickpea cytosolic Cu/Zn superoxide dismutase
    • Hernández-Nistal J., Dopico B., Labrador E. Cold and salt stress regulates the expression and activity of a chickpea cytosolic Cu/Zn superoxide dismutase. Plant Sci. 2002, 163:507-514.
    • (2002) Plant Sci. , vol.163 , pp. 507-514
    • Hernández-Nistal, J.1    Dopico, B.2    Labrador, E.3
  • 25
    • 50649117912 scopus 로고    scopus 로고
    • Cellular defense against superoxide and hydrogen peroxide
    • Imlay J.A. Cellular defense against superoxide and hydrogen peroxide. Annu. Rev. Biochem. 2008, 77:755-776.
    • (2008) Annu. Rev. Biochem. , vol.77 , pp. 755-776
    • Imlay, J.A.1
  • 26
    • 0031787515 scopus 로고    scopus 로고
    • Oxidative damage in pea plants exposed to water deficit or paraquat
    • Iturbe-Ormaetxe P.R., Escuredo C., Arrese-Igor, Becana M. Oxidative damage in pea plants exposed to water deficit or paraquat. Plant Physiol. 1998, 116:173-181.
    • (1998) Plant Physiol. , vol.116 , pp. 173-181
    • Iturbe-Ormaetxe, P.R.1    Escuredo, C.2    Arrese-Igor3    Becana, M.4
  • 27
    • 0034520591 scopus 로고    scopus 로고
    • Human Cu/Zn superoxide dismutase (SOD1) overexpression in mice causes mitochondrial vacuolization, axonal degeneration, and premature motoneuron death and accelerates motorneuron disease in mice expressing a familial amyotrophic lateral sclerosis mutant SOD1
    • Jaarsma D., et al. Human Cu/Zn superoxide dismutase (SOD1) overexpression in mice causes mitochondrial vacuolization, axonal degeneration, and premature motoneuron death and accelerates motorneuron disease in mice expressing a familial amyotrophic lateral sclerosis mutant SOD1. Neurobiol. Dis. 2000, 7:623-643.
    • (2000) Neurobiol. Dis. , vol.7 , pp. 623-643
    • Jaarsma, D.1
  • 28
    • 61349171237 scopus 로고    scopus 로고
    • Biotic and abiotic stress down-regulate miR398 expression in Arabidopsis
    • Jagadeeswaran G., Saini A., Sunkar R. Biotic and abiotic stress down-regulate miR398 expression in Arabidopsis. Planta 2009, 229:1009-1014.
    • (2009) Planta , vol.229 , pp. 1009-1014
    • Jagadeeswaran, G.1    Saini, A.2    Sunkar, R.3
  • 29
    • 33746100259 scopus 로고    scopus 로고
    • Monitoring expression profiles of antioxidant genes to salinity, iron, oxidative, light and hyperosmotic stresses in the highly salt tolerant grey mangrove, Avicennia marina (Forsk.)Vierh. by mRNA analysis
    • Jithesh M.N., Prashanth S.R., Sivaprakash K.R., Parida A.K. Monitoring expression profiles of antioxidant genes to salinity, iron, oxidative, light and hyperosmotic stresses in the highly salt tolerant grey mangrove, Avicennia marina (Forsk.)Vierh. by mRNA analysis. Plant Cell Rep. 2006, 25:865-876.
    • (2006) Plant Cell Rep. , vol.25 , pp. 865-876
    • Jithesh, M.N.1    Prashanth, S.R.2    Sivaprakash, K.R.3    Parida, A.K.4
  • 30
    • 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. Characteristic amino acid sequences of chloroplast and cytosol isozymes of CuZn-superoxide dismutase in spinach, rice and horsetail. Plant Cell Physiol. 1990, 31:99-112.
    • (1990) Plant Cell Physiol. , vol.31 , pp. 99-112
    • Kanematsu, S.1    Asada, K.2
  • 31
    • 27244461647 scopus 로고    scopus 로고
    • Structural organization, regulation and enzyme expression of the chloroplastic superoxide dismutase Sod1 gene in maize
    • Kernodle S.P., Scandalios J.G. Structural organization, regulation and enzyme expression of the chloroplastic superoxide dismutase Sod1 gene in maize. Arch. Biochem. Biophys. 2001, 391:137-147.
    • (2001) Arch. Biochem. Biophys. , vol.391 , pp. 137-147
    • Kernodle, S.P.1    Scandalios, J.G.2
  • 32
    • 0029849183 scopus 로고    scopus 로고
    • Differential expression of superoxide dismutases containing Ni and Fe/Zn in Streptomyces coelicolor
    • Kim B.J., Kim H.P., Hah Y.C., Roe J.H. Differential expression of superoxide dismutases containing Ni and Fe/Zn in Streptomyces coelicolor. Eur. J. Biochem. 1996, 241:178-185.
    • (1996) Eur. J. Biochem. , vol.241 , pp. 178-185
    • Kim, B.J.1    Kim, H.P.2    Hah, Y.C.3    Roe, J.H.4
  • 33
    • 0033918167 scopus 로고    scopus 로고
    • Molecular cloning and expression of CuZn containing superoxide dismutase from Fasciola hepatica
    • Kim T.S., Jung Y., Na B.K., Kim K.S., Chung P.R. Molecular cloning and expression of CuZn containing superoxide dismutase from Fasciola hepatica. Infect. Immun. 2000, 68:3941-3948.
    • (2000) Infect. Immun. , vol.68 , pp. 3941-3948
    • Kim, T.S.1    Jung, Y.2    Na, B.K.3    Kim, K.S.4    Chung, P.R.5
  • 34
    • 0019834273 scopus 로고
    • Isolation and characterization of the iron containing superoxide dismutase of Methanobacterium bryantii
    • Kirby T.W., Lancaster J.R., Fridovich I. Isolation and characterization of the iron containing superoxide dismutase of Methanobacterium bryantii. Arch. Biochem. Biophys. 1981, 210:140-148.
    • (1981) Arch. Biochem. Biophys. , vol.210 , pp. 140-148
    • Kirby, T.W.1    Lancaster, J.R.2    Fridovich, I.3
  • 35
    • 45049084143 scopus 로고    scopus 로고
    • Identification and characterization of a super-stable CuZnSOD from leaves of turmeric (Curcuma longa L.)
    • Kochhar S., Kochhar V.K. Identification and characterization of a super-stable CuZnSOD from leaves of turmeric (Curcuma longa L.). Planta 2008, 288:307-318.
    • (2008) Planta , vol.288 , pp. 307-318
    • Kochhar, S.1    Kochhar, V.K.2
  • 36
    • 79954478501 scopus 로고    scopus 로고
    • Superoxide anion radicals generated by methyl viologen in photosystem I damage photosystem II
    • Krieger-Liszkay A., Kos P.B., Hideg E. Superoxide anion radicals generated by methyl viologen in photosystem I damage photosystem II. Physiol. Plant. 2011, 142:17-25.
    • (2011) Physiol. Plant. , vol.142 , pp. 17-25
    • Krieger-Liszkay, A.1    Kos, P.B.2    Hideg, E.3
  • 38
    • 34247557623 scopus 로고    scopus 로고
    • Enhanced tolerance to oxidative stress in transgenic tobacco plants expressing three antioxidant enzymes in chloroplasts
    • Lee J.P., Kim S.H., Bang J.W., Lee H.S., Kwak S.S., Kwon S.Y. Enhanced tolerance to oxidative stress in transgenic tobacco plants expressing three antioxidant enzymes in chloroplasts. Plant Cell Rep. 2007, 26:591-598.
    • (2007) Plant Cell Rep. , vol.26 , pp. 591-598
    • Lee, J.P.1    Kim, S.H.2    Bang, J.W.3    Lee, H.S.4    Kwak, S.S.5    Kwon, S.Y.6
  • 39
    • 44449173081 scopus 로고    scopus 로고
    • Molecular characterization of Arabidopsis and Brassica juncea Cu/Zn superoxide dismutases reveals their regulation of shoot regeneration
    • Lim T.S., Chitra T.R., Tay B.H., Pua E.C., Yu H. Molecular characterization of Arabidopsis and Brassica juncea Cu/Zn superoxide dismutases reveals their regulation of shoot regeneration. J. Plant Growth Regul. 2008, 27:99-109.
    • (2008) J. Plant Growth Regul. , vol.27 , pp. 99-109
    • Lim, T.S.1    Chitra, T.R.2    Tay, B.H.3    Pua, E.C.4    Yu, H.5
  • 40
    • 77956128048 scopus 로고    scopus 로고
    • Identification of differentially expressed genes under drought stress in perennial grass
    • Liu S., Jiang Y. Identification of differentially expressed genes under drought stress in perennial grass. Physiol. Plant. 2010, 139:375-387.
    • (2010) Physiol. Plant. , vol.139 , pp. 375-387
    • Liu, S.1    Jiang, Y.2
  • 41
    • 77956587485 scopus 로고    scopus 로고
    • The salt and drought inducible poplar GRAS protein SCL7 confers salt and drought tolerance in Arabidopsis thaliana
    • Ma H.S., Liang D., Shuai P., Xia X.L., Yin W.L. The salt and drought inducible poplar GRAS protein SCL7 confers salt and drought tolerance in Arabidopsis thaliana. J. Exp. Bot. 2010, 61:4011-4019.
    • (2010) J. Exp. Bot. , vol.61 , pp. 4011-4019
    • Ma, H.S.1    Liang, D.2    Shuai, P.3    Xia, X.L.4    Yin, W.L.5
  • 42
    • 0029144863 scopus 로고
    • Modeling the three-dimensional structure and the electrostatic potential field of two Cu, Zn superoxide dismutase variants from tomato leaves
    • Marino M., Galvano M., Cambria A., Polticelli F., Desideri A. Modeling the three-dimensional structure and the electrostatic potential field of two Cu, Zn superoxide dismutase variants from tomato leaves. Protein Eng. 1995, 8:551-556.
    • (1995) Protein Eng. , vol.8 , pp. 551-556
    • Marino, M.1    Galvano, M.2    Cambria, A.3    Polticelli, F.4    Desideri, A.5
  • 43
    • 77951013891 scopus 로고    scopus 로고
    • Reactive oxygen species homeostasis and signaling during drought and salinity stresses
    • Miller G., Suzuki N., Ciftci-Yilmaz S., Mittler R. Reactive oxygen species homeostasis and signaling during drought and salinity stresses. Plant Cell Environ. 2010, 33:453-467.
    • (2010) Plant Cell Environ. , vol.33 , pp. 453-467
    • Miller, G.1    Suzuki, N.2    Ciftci-Yilmaz, S.3    Mittler, R.4
  • 44
    • 27644434274 scopus 로고    scopus 로고
    • A modified cDNA subtraction to identify differentially expressed genes from plants with universal application to other eukaryotes
    • Mishra R.N., Ramesha A., Kaul T., Nair S., Sopory S.K., Reddy M.K. A modified cDNA subtraction to identify differentially expressed genes from plants with universal application to other eukaryotes. Anal. Biochem. 2005, 345:149-157.
    • (2005) Anal. Biochem. , vol.345 , pp. 149-157
    • Mishra, R.N.1    Ramesha, A.2    Kaul, T.3    Nair, S.4    Sopory, S.K.5    Reddy, M.K.6
  • 45
    • 0036728244 scopus 로고    scopus 로고
    • Oxidative stress, antioxidants and stress tolerance
    • Mittler R. Oxidative stress, antioxidants and stress tolerance. Trends Plant Sci. 2002, 7:405-410.
    • (2002) Trends Plant Sci. , vol.7 , pp. 405-410
    • Mittler, R.1
  • 46
    • 34547773214 scopus 로고    scopus 로고
    • Responses of photosynthesis, chlorophyll fluorescence and ROS-scavenging systems to salt stress during seedling and reproductive stages in rice
    • Moradi F., Ismail A.M. Responses of photosynthesis, chlorophyll fluorescence and ROS-scavenging systems to salt stress during seedling and reproductive stages in rice. Ann. Bot. 2007, 99:1161-1173.
    • (2007) Ann. Bot. , vol.99 , pp. 1161-1173
    • Moradi, F.1    Ismail, A.M.2
  • 47
    • 43149090878 scopus 로고    scopus 로고
    • Mechanisms of salinity tolerance
    • Munns R., Tester M. Mechanisms of salinity tolerance. Annu. Rev. Plant Biol. 2008, 59:651-681.
    • (2008) Annu. Rev. Plant Biol. , vol.59 , pp. 651-681
    • Munns, R.1    Tester, M.2
  • 48
    • 0023265273 scopus 로고
    • Human copper-zinc superoxide dismutase complements superoxide dismutase deficient Escherichia coli mutants
    • Natvig D.O., Imlay K., Touati D., Hallewell R.A. Human copper-zinc superoxide dismutase complements superoxide dismutase deficient Escherichia coli mutants. J. Biol. Chem. 1987, 262:14697-14701.
    • (1987) J. Biol. Chem. , vol.262 , pp. 14697-14701
    • Natvig, D.O.1    Imlay, K.2    Touati, D.3    Hallewell, R.A.4
  • 50
    • 77954758267 scopus 로고    scopus 로고
    • Structural analysis of peroxide-soaked MnSOD crystals reveals side-on binding of peroxide to active site manganese
    • Porta J., Vahedi-Faridi A., Borgstahl E.O. Structural analysis of peroxide-soaked MnSOD crystals reveals side-on binding of peroxide to active site manganese. J. Mol. Biol. 2010, 399:377-384.
    • (2010) J. Mol. Biol. , vol.399 , pp. 377-384
    • Porta, J.1    Vahedi-Faridi, A.2    Borgstahl, E.O.3
  • 51
    • 41049090626 scopus 로고    scopus 로고
    • Overexpression of cytosolic copper/zinc superoxide dismutase from a mangrove plant Avicennia marina in indica rice var Pusa Basmati-1 confers abiotic stress tolerance
    • Prashanth S.R., Sadhasivam V., Parida A. Overexpression of cytosolic copper/zinc superoxide dismutase from a mangrove plant Avicennia marina in indica rice var Pusa Basmati-1 confers abiotic stress tolerance. Transgenic Res. 2007, 17:281-291.
    • (2007) Transgenic Res. , vol.17 , pp. 281-291
    • Prashanth, S.R.1    Sadhasivam, V.2    Parida, A.3
  • 52
    • 78650971246 scopus 로고    scopus 로고
    • Differential expression of copper-zinc superoxide dismutase gene of Polygonum sibricum leaves, stems and underground stems, subjected to high-salt stress
    • Qu C.P., et al. Differential expression of copper-zinc superoxide dismutase gene of Polygonum sibricum leaves, stems and underground stems, subjected to high-salt stress. Int. J. Mol. Sci. 2010, 11:5234-5245.
    • (2010) Int. J. Mol. Sci. , vol.11 , pp. 5234-5245
    • Qu, C.P.1
  • 53
    • 0036853024 scopus 로고    scopus 로고
    • The combined effect of drought stress and heat shock on gene expression in tobacco
    • Rizhsky L., Liang H., Mittler R. The combined effect of drought stress and heat shock on gene expression in tobacco. Plant Physiol. 2002, 130:1143-1151.
    • (2002) Plant Physiol. , vol.130 , pp. 1143-1151
    • Rizhsky, L.1    Liang, H.2    Mittler, R.3
  • 54
    • 57449112526 scopus 로고    scopus 로고
    • Possible involvement of an extracellular superoxide dismutase (SodA) as a radical scavenger in poly (cis-1.4-isoprene) degradation
    • Schulte C., Arenskotter M., Berekaa M.M., Arenskotter Q., Priefert H., Steinbuchel A. Possible involvement of an extracellular superoxide dismutase (SodA) as a radical scavenger in poly (cis-1.4-isoprene) degradation. Appl. Environ. Microbiol. 2008, 74:7643-7653.
    • (2008) Appl. Environ. Microbiol. , vol.74 , pp. 7643-7653
    • Schulte, C.1    Arenskotter, M.2    Berekaa, M.M.3    Arenskotter, Q.4    Priefert, H.5    Steinbuchel, A.6
  • 55
    • 0026633193 scopus 로고
    • A comparison of evolutionary rates of the two major kinds of superoxide dismutases
    • Smith M.W., Doolittle R.F. A comparison of evolutionary rates of the two major kinds of superoxide dismutases. J. Mol. Evol. 1992, 34:175-184.
    • (1992) J. Mol. Evol. , vol.34 , pp. 175-184
    • Smith, M.W.1    Doolittle, R.F.2
  • 57
    • 33747505089 scopus 로고    scopus 로고
    • Posttranscriptional induction of two Cu/Zn superoxide dismutase genes in Arabidopsis is mediated by down regulation of miR398 and important for oxidative stress tolerance
    • Sunkar R., Kapoor A., Zhu J.K. Posttranscriptional induction of two Cu/Zn superoxide dismutase genes in Arabidopsis is mediated by down regulation of miR398 and important for oxidative stress tolerance. Plant Cell 2006, 18:2051-2065.
    • (2006) Plant Cell , vol.18 , pp. 2051-2065
    • Sunkar, R.1    Kapoor, A.2    Zhu, J.K.3
  • 58
    • 0021105282 scopus 로고
    • Superoxide anion permeability of phospholipid membranes and chloroplast thylakoids
    • Takahashi M.A., Asada K. Superoxide anion permeability of phospholipid membranes and chloroplast thylakoids. Arch. Biochem. Biophys. 1983, 226:558-566.
    • (1983) Arch. Biochem. Biophys. , vol.226 , pp. 558-566
    • Takahashi, M.A.1    Asada, K.2
  • 59
    • 12144266372 scopus 로고    scopus 로고
    • Overexpression of mutated CuZnSOD in neuroblastoma cells results in cytoskeletal change
    • Takamiya R., et al. Overexpression of mutated CuZnSOD in neuroblastoma cells results in cytoskeletal change. Am. J. Physiol. Cell Physiol. 2005, 288:C253-C259.
    • (2005) Am. J. Physiol. Cell Physiol. , vol.288
    • Takamiya, R.1
  • 62
    • 84861742503 scopus 로고    scopus 로고
    • Purification and Characterization of CuZn-superoxide Dismutase from Black Soybean
    • Wang S., Shao B., Liu S., Ye X., Rao P. Purification and Characterization of CuZn-superoxide Dismutase from Black Soybean. Food Res. Int. 2011, (http://dx.doi.org/10.1016/j.foodres.2011.10.023).
    • (2011) Food Res. Int.
    • Wang, S.1    Shao, B.2    Liu, S.3    Ye, X.4    Rao, P.5
  • 63
    • 78751704275 scopus 로고    scopus 로고
    • Characterization of copper/zinc and manganese superoxide dismutase In green bamboo (Bambusa oldhamii): cloning, expression and regulation
    • Wu T.H., Liao M.H., Kuo W., Huang C.H., Hiseh H.L., Jinn T.L. Characterization of copper/zinc and manganese superoxide dismutase In green bamboo (Bambusa oldhamii): cloning, expression and regulation. Plant Physiol. Biochem. 2011, 49:195-200.
    • (2011) Plant Physiol. Biochem. , vol.49 , pp. 195-200
    • Wu, T.H.1    Liao, M.H.2    Kuo, W.3    Huang, C.H.4    Hiseh, H.L.5    Jinn, T.L.6
  • 64
    • 65149101011 scopus 로고    scopus 로고
    • Molecular cloning and expression of a Cu/Zn containing superoxide dismutase from Thellungiella halophile
    • Xiaojing X. Molecular cloning and expression of a Cu/Zn containing superoxide dismutase from Thellungiella halophile. Mol. Cells 2009, 27:423-428.
    • (2009) Mol. Cells , vol.27 , pp. 423-428
    • Xiaojing, X.1
  • 65
    • 77956881011 scopus 로고    scopus 로고
    • Drought response of pearl millet landrace-based populations and their crosses with elite composites
    • Yadav O.P. Drought response of pearl millet landrace-based populations and their crosses with elite composites. Field Crops Res. 2010, 118:51-56.
    • (2010) Field Crops Res. , vol.118 , pp. 51-56
    • Yadav, O.P.1
  • 66
    • 34447623057 scopus 로고    scopus 로고
    • SAD phasing of a structure based on co-crystallized iodides using an in-house Cu Kalpha X-ray source: effects of data redundancy and completeness on structure solution
    • Yogavel M., Gill J., Mishra P.C., Sharma A. SAD phasing of a structure based on co-crystallized iodides using an in-house Cu Kalpha X-ray source: effects of data redundancy and completeness on structure solution. Acta Crystallogr. 2007, 63:931-934.
    • (2007) Acta Crystallogr. , vol.63 , pp. 931-934
    • Yogavel, M.1    Gill, J.2    Mishra, P.C.3    Sharma, A.4
  • 67
    • 47749102927 scopus 로고    scopus 로고
    • Structure of a superoxide dismutase and implications for copper-ion chelation
    • Yogavel M., et al. Structure of a superoxide dismutase and implications for copper-ion chelation. Acta Crystallogr. 2008, 64:892-901.
    • (2008) Acta Crystallogr. , vol.64 , pp. 892-901
    • Yogavel, M.1
  • 68
    • 44449110652 scopus 로고    scopus 로고
    • Cloning, characterization and expression analysis of two superoxide dismutase (SOD) genes in wheat (Triticum aestivum L.)
    • Zhang H., Guo C., Li C., Xiao K. Cloning, characterization and expression analysis of two superoxide dismutase (SOD) genes in wheat (Triticum aestivum L.). Front. Agric. China 2008, 2:141-149.
    • (2008) Front. Agric. China , vol.2 , pp. 141-149
    • Zhang, H.1    Guo, C.2    Li, C.3    Xiao, K.4


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