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Volumn 59, Issue 1, 1997, Pages 1-10

Involvement of catalase and superoxide dismutase in resistance of Botrytis cinerea to dicarboximide fungicide vinclozolin

Author keywords

[No Author keywords available]

Indexed keywords

BOTRYOTINIA FUCKELIANA; BOTRYTIS; BOTRYTIS CINEREA; FELIS CATUS;

EID: 0343778712     PISSN: 00483575     EISSN: None     Source Type: Journal    
DOI: 10.1006/pest.1997.2300     Document Type: Article
Times cited : (27)

References (42)
  • 1
    • 0001820824 scopus 로고
    • Antifungal activity of dicarboximides and aromatic hydrocarbons and resistance to these fungicides
    • Cambridge: Cambridge Univ. Press. p. 207-237
    • Leroux P., Fritz R. Antifungal activity of dicarboximides and aromatic hydrocarbons and resistance to these fungicides. "Mode of Action of Antifungal Agents" 1984;Cambridge Univ. Press, Cambridge. p. 207-237.
    • (1984) "mode of Action of Antifungal Agents"
    • Leroux, P.1    Fritz, R.2
  • 4
    • 84985437566 scopus 로고
    • Strains ofBotrytis cinerea
    • Beever R. E. Strains ofBotrytis cinerea. Plant Pathol. 38:1989;427.
    • (1989) Plant Pathol. , vol.38 , pp. 427
    • Beever, R.E.1
  • 5
    • 0003168177 scopus 로고
    • Responses to several fungicides ofBotrytis cinerea
    • Kim B. S., Choi G. J., Cho K. Y. Responses to several fungicides ofBotrytis cinerea. Korean J. Plant Pathol. 9:1993;98.
    • (1993) Korean J. Plant Pathol. , vol.9 , pp. 98
    • Kim, B.S.1    Choi, G.J.2    Cho, K.Y.3
  • 8
    • 0002102307 scopus 로고
    • The physiological basis of resistance to the dicarboximide fungicide iprodione inBotrytis cinerea
    • (tan)
    • Steel C. C., Nair N. G. (Tan). The physiological basis of resistance to the dicarboximide fungicide iprodione inBotrytis cinerea. Pestic. Biochem. Physiol. 47:1993;60.
    • (1993) Pestic. Biochem. Physiol. , vol.47 , pp. 60
    • Steel, C.C.1    Nair, N.G.2
  • 9
    • 0011294148 scopus 로고
    • Lipid peroxidation, a consequence of the mechanism of action of aromatic hydrocarbonand dicarboximide fungicides and a side effect in DMI fungicide
    • Lyr H., Edlich W. Lipid peroxidation, a consequence of the mechanism of action of aromatic hydrocarbonand dicarboximide fungicides and a side effect in DMI fungicide. Proc. Br. Crop Prot. Conf. Pests Dis. 1:1986;879.
    • (1986) Proc. Br. Crop Prot. Conf. Pests Dis. , vol.1 , pp. 879
    • Lyr, H.1    Edlich, W.2
  • 11
    • 38249027864 scopus 로고
    • Lipid peroxidation: A side effect of sterol demethylation inhibitor fungicides inMucor mucedoUstilago maydis
    • Lyr H. Lipid peroxidation: A side effect of sterol demethylation inhibitor fungicides inMucor mucedoUstilago maydis. Pestic. Biochem. Physiol. 32:1988;197.
    • (1988) Pestic. Biochem. Physiol. , vol.32 , pp. 197
    • Lyr, H.1
  • 12
    • 84992235357 scopus 로고
    • Target sites of fungicides with primary effects on lipid peroxidation
    • Köller W. Boca Raton: CRC Press
    • Edlich W., Lyr H. Target sites of fungicides with primary effects on lipid peroxidation. Köller W. "Target Sites of Fungicide Action" 1992;53-68 CRC Press, Boca Raton.
    • (1992) "target Sites of Fungicide Action" , pp. 53-68
    • Edlich, W.1    Lyr, H.2
  • 14
    • 0002778035 scopus 로고
    • An investigation into the role of lipid peroxidation in themode of action of aromatic hydrocarbon and dicarboximide fungicides
    • Orth A. B., Sfarra A., Pell E. J., Tien M. An investigation into the role of lipid peroxidation in themode of action of aromatic hydrocarbon and dicarboximide fungicides. Pestic. Biochem. Physiol. 44:1992;91.
    • (1992) Pestic. Biochem. Physiol. , vol.44 , pp. 91
    • Orth, A.B.1    Sfarra, A.2    Pell, E.J.3    Tien, M.4
  • 15
    • 0030136466 scopus 로고    scopus 로고
    • Lipid peroxidation and membrane disruption by vinclozolin indicarboximide-susceptible and -resistant isolates ofBotrytiscinerea
    • Choi G. J., Lee H. J., Cho K. Y. Lipid peroxidation and membrane disruption by vinclozolin indicarboximide-susceptible and -resistant isolates ofBotrytiscinerea. Pestic. Biochem. Physiol. 55:1996;29.
    • (1996) Pestic. Biochem. Physiol. , vol.55 , pp. 29
    • Choi, G.J.1    Lee, H.J.2    Cho, K.Y.3
  • 16
    • 0029975038 scopus 로고    scopus 로고
    • Catalase activity and sensitivity to the fungicides, iprodione and fludioxonil inBotrytis cinerea
    • Steel C. C. Catalase activity and sensitivity to the fungicides, iprodione and fludioxonil inBotrytis cinerea. Lett. Appl. Microbiol. 22:1996;335.
    • (1996) Lett. Appl. Microbiol. , vol.22 , pp. 335
    • Steel, C.C.1
  • 17
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizingthe principle of protein-dye binding
    • Bradford M. M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizingthe principle of protein-dye binding. Anal. Biochem. 72:1976;248.
    • (1976) Anal. Biochem. , vol.72 , pp. 248
    • Bradford, M.M.1
  • 18
    • 0019944971 scopus 로고
    • Comparative biochemistry of oxygen toxicity in lactic acid-forming aquatic fungi
    • Natvig D. O. Comparative biochemistry of oxygen toxicity in lactic acid-forming aquatic fungi. Arch. Microbiol. 132:1982;107.
    • (1982) Arch. Microbiol. , vol.132 , pp. 107
    • Natvig, D.O.1
  • 19
    • 0014810439 scopus 로고
    • Xanthine oxidase for calibration of the oxygen electrode apparatus
    • Billiar R. B., Knappenberger M., Little B. Xanthine oxidase for calibration of the oxygen electrode apparatus. Anal. Biochem. 36:1970;101.
    • (1970) Anal. Biochem. , vol.36 , pp. 101
    • Billiar, R.B.1    Knappenberger, M.2    Little, B.3
  • 20
    • 11944254277 scopus 로고
    • Superoxide dismutase, catalase, and α-tocopherol content of storedpotato tubers
    • Spychalla J. P., Desborough S. L. Superoxide dismutase, catalase, and α-tocopherol content of storedpotato tubers. Plant Physiol. 94:1990;1214.
    • (1990) Plant Physiol. , vol.94 , pp. 1214
    • Spychalla, J.P.1    Desborough, S.L.2
  • 22
    • 0029177962 scopus 로고
    • Changes in isozyme profiles of catalase, peroxidase,and glutathione reductase during acclimation to chilling in mesocotyls of maize seedlings
    • Anderson M. D., Prasad T. K., Steward C. R. Changes in isozyme profiles of catalase, peroxidase,and glutathione reductase during acclimation to chilling in mesocotyls of maize seedlings. Plant Physiol. 109:1995;1247.
    • (1995) Plant Physiol. , vol.109 , pp. 1247
    • Anderson, M.D.1    Prasad, T.K.2    Steward, C.R.3
  • 23
    • 0030023240 scopus 로고    scopus 로고
    • Ultraviolet-B- And ozone- induced biochemical changes in antioxidantenzymes ofArabidopsis thaliana
    • Rao M. V., Paliyath G., Ormrod D. P. Ultraviolet-B- and ozone- induced biochemical changes in antioxidantenzymes ofArabidopsis thaliana. Plant Physiol. 110:1996;125.
    • (1996) Plant Physiol. , vol.110 , pp. 125
    • Rao, M.V.1    Paliyath, G.2    Ormrod, D.P.3
  • 24
    • 0017859596 scopus 로고
    • Superoxide dismutase and oxygen metabolism inStreptococcusfaecalis
    • Britton L., Malinowski D. P., Fridovich I. Superoxide dismutase and oxygen metabolism inStreptococcusfaecalis. J. Bacteriol. 134:1978;229.
    • (1978) J. Bacteriol. , vol.134 , pp. 229
    • Britton, L.1    Malinowski, D.P.2    Fridovich, I.3
  • 25
    • 84985772794 scopus 로고
    • Developmental expression and intracellular localization of superoxidedismutase in maize
    • Baum J. A., Scandalios J. G. Developmental expression and intracellular localization of superoxidedismutase in maize. Differentiation. 13:1979;133.
    • (1979) Differentiation , vol.13 , pp. 133
    • Baum, J.A.1    Scandalios, J.G.2
  • 28
    • 0002696602 scopus 로고
    • Oxygen stress and superoxide dismutase
    • Scandalios J. G. Oxygen stress and superoxide dismutase. Plant Physiol. 101:1993;7.
    • (1993) Plant Physiol. , vol.101 , pp. 7
    • Scandalios, J.G.1
  • 30
    • 0015511160 scopus 로고
    • Interaction of hydrogen peroxide with superoxide dismutase fromerythrocytes
    • Simonyan M. A., Nalbandyan R. M. Interaction of hydrogen peroxide with superoxide dismutase fromerythrocytes. FEBS Lett. 28:1972;22.
    • (1972) FEBS Lett. , vol.28 , pp. 22
    • Simonyan, M.A.1    Nalbandyan, R.M.2
  • 33
    • 0344225582 scopus 로고
    • The role of active oxygen in fungicidal action
    • E.J. Pell, Steffen K.L. Rockville: Am. Soc. Plant Physiol.
    • Sisler H. D., Orth A. B. The role of active oxygen in fungicidal action. Pell E. J., Steffen K. L. "Active Oxygen/Oxidative Stress and Plant Metabolism" 1991;76-83 Am. Soc. Plant Physiol. Rockville.
    • (1991) "active Oxygen/Oxidative Stress and Plant Metabolism" , pp. 76-83
    • Sisler, H.D.1    Orth, A.B.2
  • 35
    • 0021318441 scopus 로고
    • Catalasein vitro
    • Aebi H. Catalasein vitro. Methods Enzymol. 105:1984;121.
    • (1984) Methods Enzymol. , vol.105 , pp. 121
    • Aebi, H.1
  • 36
    • 0024407187 scopus 로고
    • Biochemistry of oxygen toxicity
    • Cadenas E. Biochemistry of oxygen toxicity. Annu. Rev. Biochem. 58:1989;79.
    • (1989) Annu. Rev. Biochem. , vol.58 , pp. 79
    • Cadenas, E.1
  • 37
    • 0001414007 scopus 로고
    • Antioxidant mechanisms of enzymes and proteins
    • Ahmad S. London: Chapman & Hall
    • Ahmad S. Antioxidant mechanisms of enzymes and proteins. Ahmad S. "Oxidative Stress and Antioxidant Defenses in Biology" 1995;238-272 Chapman & Hall, London.
    • (1995) "oxidative Stress and Antioxidant Defenses in Biology" , pp. 238-272
    • Ahmad, S.1
  • 38
    • 0025126555 scopus 로고
    • Role of free radicals and catalytic metal ions in human disease: Anoverview
    • Halliwell B., Gutteridge M. J. C. Role of free radicals and catalytic metal ions in human disease: Anoverview. Methods Enzymol. 186:1990;1.
    • (1990) Methods Enzymol. , vol.186 , pp. 1
    • Halliwell, B.1    Gutteridge, M.J.C.2
  • 39
    • 0015501087 scopus 로고
    • The purification and properties of superoxide dismutase fromNeurospora crassa
    • Misra H. P., Fridovich I. The purification and properties of superoxide dismutase fromNeurospora crassa. J. Biol. Chem. 247:1972;3410.
    • (1972) J. Biol. Chem. , vol.247 , pp. 3410
    • Misra, H.P.1    Fridovich, I.2
  • 40
    • 0022426858 scopus 로고
    • Purification and characterization of an iron-containing superoxide dismutase froma eukaryote,Ginko biloba
    • Duke M. V., Salin M. L. Purification and characterization of an iron-containing superoxide dismutase froma eukaryote,Ginko biloba. Arch. Biochem. Biophys. 243:1985;305.
    • (1985) Arch. Biochem. Biophys. , vol.243 , pp. 305
    • Duke, M.V.1    Salin, M.L.2
  • 41
    • 0022504269 scopus 로고
    • Effect of the free radical-generating herbicide paraquat on the expressionof the superoxide dismutase (Sod
    • Matters G. L., Scandalios J. G. Effect of the free radical-generating herbicide paraquat on the expressionof the superoxide dismutase (Sod. Biochim. Biophys. Acta. 882:1986;29.
    • (1986) Biochim. Biophys. Acta , vol.882 , pp. 29
    • Matters, G.L.1    Scandalios, J.G.2
  • 42
    • 0025351115 scopus 로고
    • Mechanisms for regulating oxygen toxicity in phytophagous insects
    • Ahmad S., Pardini R. S. Mechanisms for regulating oxygen toxicity in phytophagous insects. Free Radical Biol. Med. 8:1990;401.
    • (1990) Free Radical Biol. Med. , vol.8 , pp. 401
    • Ahmad, S.1    Pardini, R.S.2


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