메뉴 건너뛰기




Volumn 69, Issue 3, 2008, Pages 715-728

Proteomic analysis of rice defense response induced by probenazole

Author keywords

Defense; Disease resistance; Graminaceae; Oryza sativa; Probenazole; Proteomics; Rice

Indexed keywords

CAFFEATE O METHYLTRANSFERASE; CAFFEATE O-METHYLTRANSFERASE; GLUTATHIONE TRANSFERASE; MESSENGER RNA; METHYLTRANSFERASE; PHENYLALANINE AMMONIA LYASE; PROBENAZOLE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE (UBIQUINONE); THIAZOLE DERIVATIVE; UNCLASSIFIED DRUG; VEGETABLE PROTEIN;

EID: 38349098770     PISSN: 00319422     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.phytochem.2007.09.005     Document Type: Article
Times cited : (30)

References (69)
  • 1
    • 0036892782 scopus 로고    scopus 로고
    • A pathogen-induced novel rice (Oryza sativa L.) gene encodes a putative protein homologous to type II glutathione S-transferases
    • Agrawal G., Jwa N., and Rakwal R. A pathogen-induced novel rice (Oryza sativa L.) gene encodes a putative protein homologous to type II glutathione S-transferases. Plant Sci. 163 (2002) 1153-1160
    • (2002) Plant Sci. , vol.163 , pp. 1153-1160
    • Agrawal, G.1    Jwa, N.2    Rakwal, R.3
  • 2
    • 0036668513 scopus 로고    scopus 로고
    • Proteome analysis of differentially displayed proteins as a tool for investigating ozone stress in rice (Oryza sativa L.) seedlings
    • Agrawal G.K., Rakwal R., Yonekura M., Kubo A., and Saji H. Proteome analysis of differentially displayed proteins as a tool for investigating ozone stress in rice (Oryza sativa L.) seedlings. Proteomics 2 (2002) 947-959
    • (2002) Proteomics , vol.2 , pp. 947-959
    • Agrawal, G.K.1    Rakwal, R.2    Yonekura, M.3    Kubo, A.4    Saji, H.5
  • 3
    • 33644848361 scopus 로고    scopus 로고
    • Rice proteomics: a cornerstone for cereal food crop proteomes
    • Agrawal G.K., and Rakwal R. Rice proteomics: a cornerstone for cereal food crop proteomes. Mass Spectrom. Rev. 25 (2006) 1-53
    • (2006) Mass Spectrom. Rev. , vol.25 , pp. 1-53
    • Agrawal, G.K.1    Rakwal, R.2
  • 4
    • 0032811334 scopus 로고    scopus 로고
    • Phosphorylation of phenylalanine ammonia-lyase: evidence for a novel protein kinase and identification of the phosphorylated residue
    • Allwood E.G., Davies D.R., Gerrish C., Ellis B.E., and Bolwell G.P. Phosphorylation of phenylalanine ammonia-lyase: evidence for a novel protein kinase and identification of the phosphorylated residue. FEBS Lett. 457 (1999) 47-52
    • (1999) FEBS Lett. , vol.457 , pp. 47-52
    • Allwood, E.G.1    Davies, D.R.2    Gerrish, C.3    Ellis, B.E.4    Bolwell, G.P.5
  • 5
    • 0035983890 scopus 로고    scopus 로고
    • Regulation of CDPKs, including identification of PAL kinase, in biotically stressed cells of French bean
    • Allwood E.G., Davies D.R., Gerrish C., and Bolwell G.P. Regulation of CDPKs, including identification of PAL kinase, in biotically stressed cells of French bean. Plant Mol. Biol. 49 (2002) 533-544
    • (2002) Plant Mol. Biol. , vol.49 , pp. 533-544
    • Allwood, E.G.1    Davies, D.R.2    Gerrish, C.3    Bolwell, G.P.4
  • 6
    • 0028799894 scopus 로고
    • Arabidopsis thaliana NADPH oxidoreductase homologs confer tolerance of yeasts toward the thiol-oxidizing drug diamide
    • Babiychuk E., Kushnir S., Belles-Boix E., Van Montagu M., and Inze D. Arabidopsis thaliana NADPH oxidoreductase homologs confer tolerance of yeasts toward the thiol-oxidizing drug diamide. J. Biol. Chem. 270 (1995) 26224-26231
    • (1995) J. Biol. Chem. , vol.270 , pp. 26224-26231
    • Babiychuk, E.1    Kushnir, S.2    Belles-Boix, E.3    Van Montagu, M.4    Inze, D.5
  • 8
    • 0023277545 scopus 로고
    • Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction
    • Chomczynski P., and Sacchi N. Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Anal. Biochem. 162 (1987) 156-159
    • (1987) Anal. Biochem. , vol.162 , pp. 156-159
    • Chomczynski, P.1    Sacchi, N.2
  • 9
    • 0036202462 scopus 로고    scopus 로고
    • Plant glutathione transferases
    • (Reviews3004)
    • Dixon D.P., Lapthorn A., and Ewards R. Plant glutathione transferases. Genome Biol. 3 (2002) 1-10 (Reviews3004)
    • (2002) Genome Biol. , vol.3 , pp. 1-10
    • Dixon, D.P.1    Lapthorn, A.2    Ewards, R.3
  • 10
    • 0035859039 scopus 로고    scopus 로고
    • Natural products and plant disease resistance
    • Dixon R.A. Natural products and plant disease resistance. Nature 411 (2001) 843-847
    • (2001) Nature , vol.411 , pp. 843-847
    • Dixon, R.A.1
  • 11
    • 0029109382 scopus 로고
    • Tissue-specific expression of germin-like oxalate oxidase during development and fungal Infection of barley seedlings
    • Dumas B., Freyssinet G., and Pallett K.E. Tissue-specific expression of germin-like oxalate oxidase during development and fungal Infection of barley seedlings. Plant Physiol. 107 (1995) 1091-1096
    • (1995) Plant Physiol. , vol.107 , pp. 1091-1096
    • Dumas, B.1    Freyssinet, G.2    Pallett, K.E.3
  • 12
    • 0034192572 scopus 로고    scopus 로고
    • Plant glutathione S-transferases: enzymes with multiple functions in sickness and in health
    • Edwards R., Dixon D.P., and Walbot V. Plant glutathione S-transferases: enzymes with multiple functions in sickness and in health. Trends Plant Sci. 5 (2000) 193-198
    • (2000) Trends Plant Sci. , vol.5 , pp. 193-198
    • Edwards, R.1    Dixon, D.P.2    Walbot, V.3
  • 13
    • 30144437159 scopus 로고    scopus 로고
    • Plant glutathione transferases
    • Edwards R., and Dixon D.P. Plant glutathione transferases. Meth. Enzymol. 401 (2005) 169-186
    • (2005) Meth. Enzymol. , vol.401 , pp. 169-186
    • Edwards, R.1    Dixon, D.P.2
  • 14
    • 0033016717 scopus 로고    scopus 로고
    • Correlation between protein and mRNA abundance in yeast
    • Gygi S.P., Rochon Y., Franza B.R., and Aebersold R. Correlation between protein and mRNA abundance in yeast. Mol. Cell Biol. 19 (1999) 1720-1730
    • (1999) Mol. Cell Biol. , vol.19 , pp. 1720-1730
    • Gygi, S.P.1    Rochon, Y.2    Franza, B.R.3    Aebersold, R.4
  • 15
    • 0034858234 scopus 로고    scopus 로고
    • High-resolution two-dimensional electrophoresis separation of proteins from metal-stressed rice (Oryza sativa L.) leaves: drastic reductions/fragmentation of ribulose-1,5-bisphosphate carboxylase/oxygenase and induction of stress-related proteins
    • Hajduch M., Rakwal R., Agrawal G.K., Yonekura M., and Pretova A. High-resolution two-dimensional electrophoresis separation of proteins from metal-stressed rice (Oryza sativa L.) leaves: drastic reductions/fragmentation of ribulose-1,5-bisphosphate carboxylase/oxygenase and induction of stress-related proteins. Electrophoresis 22 (2001) 2824-2831
    • (2001) Electrophoresis , vol.22 , pp. 2824-2831
    • Hajduch, M.1    Rakwal, R.2    Agrawal, G.K.3    Yonekura, M.4    Pretova, A.5
  • 16
    • 0026918137 scopus 로고
    • General roles of abscisic and jasmonic acids in gene activation as a result of mechanical wounding
    • Hildmann T., Ebneth M., Pena-Cortes H., Sanchez-Serrano J.J., Willmitzer L., and Prat S. General roles of abscisic and jasmonic acids in gene activation as a result of mechanical wounding. Plant Cell 4 (1992) 1157-1170
    • (1992) Plant Cell , vol.4 , pp. 1157-1170
    • Hildmann, T.1    Ebneth, M.2    Pena-Cortes, H.3    Sanchez-Serrano, J.J.4    Willmitzer, L.5    Prat, S.6
  • 17
    • 0030468571 scopus 로고    scopus 로고
    • Overexpression of l-phenylalanine ammonia-lyase in transgenic tobacco plants reveals control points for flux into phenylpropanoid biosynthesis
    • Howles P.A., Sewalt V., Paiva N.L., Elkind Y., Bate N.J., Lamb C., and Dixon R.A. Overexpression of l-phenylalanine ammonia-lyase in transgenic tobacco plants reveals control points for flux into phenylpropanoid biosynthesis. Plant Physiol. 112 (1996) 1617-1624
    • (1996) Plant Physiol. , vol.112 , pp. 1617-1624
    • Howles, P.A.1    Sewalt, V.2    Paiva, N.L.3    Elkind, Y.4    Bate, N.J.5    Lamb, C.6    Dixon, R.A.7
  • 19
    • 84907150192 scopus 로고    scopus 로고
    • International Rice Genome Sequencing Project. 2005. The map-based sequence of the rice genome. Nature 436, 793-800.
  • 20
    • 0034884982 scopus 로고    scopus 로고
    • A deficiency of coproporphyrinogen III oxidase causes lesion formation in Arabidopsis
    • Ishikawa A., Okamoto H., Iwasaki Y., and Asahi T. A deficiency of coproporphyrinogen III oxidase causes lesion formation in Arabidopsis. Plant J. 27 (2001) 89-99
    • (2001) Plant J. , vol.27 , pp. 89-99
    • Ishikawa, A.1    Okamoto, H.2    Iwasaki, Y.3    Asahi, T.4
  • 21
    • 0001453908 scopus 로고
    • Effect of probenazole on the activities of enzymes related to the resistant reaction in rice plant
    • Iwata M., Suzuki Y., Watanabe T., Mase S., and Sekizawa Y. Effect of probenazole on the activities of enzymes related to the resistant reaction in rice plant. Ann. Phytopathol. Soc. Jpn. 46 (1980) 297-306
    • (1980) Ann. Phytopathol. Soc. Jpn. , vol.46 , pp. 297-306
    • Iwata, M.1    Suzuki, Y.2    Watanabe, T.3    Mase, S.4    Sekizawa, Y.5
  • 22
    • 3242743833 scopus 로고    scopus 로고
    • Specific changes in the Arabidopsis proteome in response to bacterial challenge: differentiating basal and R-gene mediated resistance
    • Jones A.M., Thomas V., Truman B., Lilley K., Mansfield J., and Grant M. Specific changes in the Arabidopsis proteome in response to bacterial challenge: differentiating basal and R-gene mediated resistance. Phytochemistry 65 (2004) 1805-1816
    • (2004) Phytochemistry , vol.65 , pp. 1805-1816
    • Jones, A.M.1    Thomas, V.2    Truman, B.3    Lilley, K.4    Mansfield, J.5    Grant, M.6
  • 23
    • 0014804502 scopus 로고
    • Selective media for isolation of Agrobacterium, Corynebacterium, Erwinia, Pseudomonas, and Xanthomonas
    • Kado C.I., and Heskett M.G. Selective media for isolation of Agrobacterium, Corynebacterium, Erwinia, Pseudomonas, and Xanthomonas. Phytopathology 60 (1970) 969-976
    • (1970) Phytopathology , vol.60 , pp. 969-976
    • Kado, C.I.1    Heskett, M.G.2
  • 24
    • 0000663168 scopus 로고
    • An improved technique for evaluation of resistance of rice varieties to Xanthomonas oryzae
    • Kauffman H.E., Reddy A.P.K., Hsieh S.P.V., and Marca S.D. An improved technique for evaluation of resistance of rice varieties to Xanthomonas oryzae. Plant Dis. Rep. 57 (1973) 537-541
    • (1973) Plant Dis. Rep. , vol.57 , pp. 537-541
    • Kauffman, H.E.1    Reddy, A.P.K.2    Hsieh, S.P.V.3    Marca, S.D.4
  • 25
    • 0034663640 scopus 로고    scopus 로고
    • Diversity and origin of alternative NADH:ubiquinone oxidoreductases
    • Kerscher S.J. Diversity and origin of alternative NADH:ubiquinone oxidoreductases. Biochim. Biophys. Acta 1459 (2000) 274-283
    • (2000) Biochim. Biophys. Acta , vol.1459 , pp. 274-283
    • Kerscher, S.J.1
  • 26
    • 0346256836 scopus 로고    scopus 로고
    • Proteomic analysis of differentially expressed proteins induced by rice blast fungus and elicitor in suspension-cultured rice cells
    • Kim S.T., Cho K.S., Yu S., Kim S.G., Hong J.C., Han C.D., Bae D.W., Nam M.H., and Kang K.Y. Proteomic analysis of differentially expressed proteins induced by rice blast fungus and elicitor in suspension-cultured rice cells. Proteomics 3 (2003) 2368-2378
    • (2003) Proteomics , vol.3 , pp. 2368-2378
    • Kim, S.T.1    Cho, K.S.2    Yu, S.3    Kim, S.G.4    Hong, J.C.5    Han, C.D.6    Bae, D.W.7    Nam, M.H.8    Kang, K.Y.9
  • 27
    • 8744262736 scopus 로고    scopus 로고
    • Proteomic analysis of pathogen-responsive proteins from rice leaves induced by rice blast fungus, Magnaporthe grisea
    • Kim S.T., Kim S.G., Hwang du H., Kang S.Y., Kim H.J., Lee B.H., Lee J.J., and Kang K.Y. Proteomic analysis of pathogen-responsive proteins from rice leaves induced by rice blast fungus, Magnaporthe grisea. Proteomics 4 (2004) 3569-3578
    • (2004) Proteomics , vol.4 , pp. 3569-3578
    • Kim, S.T.1    Kim, S.G.2    Hwang du, H.3    Kang, S.Y.4    Kim, H.J.5    Lee, B.H.6    Lee, J.J.7    Kang, K.Y.8
  • 29
    • 0141560827 scopus 로고    scopus 로고
    • Rice proteomics: a step toward functional analysis of the rice genome
    • Komatsu S., Konishi H., Shen S., and Yang G. Rice proteomics: a step toward functional analysis of the rice genome. Mol. Cell. Proteomics 2 (2003) 2-10
    • (2003) Mol. Cell. Proteomics , vol.2 , pp. 2-10
    • Komatsu, S.1    Konishi, H.2    Shen, S.3    Yang, G.4
  • 30
    • 85047683665 scopus 로고    scopus 로고
    • A proteomics approach towards understanding blast fungus infection of rice grown under different levels of nitrogen fertilization
    • Konishi H., Ishiguro K., and Komatsu S. A proteomics approach towards understanding blast fungus infection of rice grown under different levels of nitrogen fertilization. Proteomics 1 (2001) 1162-1171
    • (2001) Proteomics , vol.1 , pp. 1162-1171
    • Konishi, H.1    Ishiguro, K.2    Komatsu, S.3
  • 31
    • 3142781659 scopus 로고    scopus 로고
    • Proteomic screening and identification of differentially distributed membrane proteins in Escherichia coli
    • Lai E.M., Nair U., Phadke N.D., and Maddock J.R. Proteomic screening and identification of differentially distributed membrane proteins in Escherichia coli. Mol. Microbiol. 52 (2004) 1029-1044
    • (2004) Mol. Microbiol. , vol.52 , pp. 1029-1044
    • Lai, E.M.1    Nair, U.2    Phadke, N.D.3    Maddock, J.R.4
  • 32
    • 0025719084 scopus 로고
    • Cellular desiccation and hydration: developmentally regulated proteins, and the maturation and germination of seed embryos
    • Lane B.G. Cellular desiccation and hydration: developmentally regulated proteins, and the maturation and germination of seed embryos. FASEB J. 5 (1991) 2893-2901
    • (1991) FASEB J. , vol.5 , pp. 2893-2901
    • Lane, B.G.1
  • 33
    • 0346887175 scopus 로고    scopus 로고
    • Strategic shotgun proteomics approach for efficient construction of an expression map of targeted protein families in hepatoma cell lines
    • Lee C.L., Hsiao H.H., Lin C.W., Wu S.P., Huang S.Y., Wu C.Y., Wang A.H., and Khoo K.H. Strategic shotgun proteomics approach for efficient construction of an expression map of targeted protein families in hepatoma cell lines. Proteomics 3 (2003) 2472-2486
    • (2003) Proteomics , vol.3 , pp. 2472-2486
    • Lee, C.L.1    Hsiao, H.H.2    Lin, C.W.3    Wu, S.P.4    Huang, S.Y.5    Wu, C.Y.6    Wang, A.H.7    Khoo, K.H.8
  • 34
    • 33748337522 scopus 로고    scopus 로고
    • Proteomic and genetic approaches to identifying defence-related proteins in rice challenged with the fungal pathogen Rhizoctonia solani
    • Lee O., Bricker T.M., Lefevre M., Pinson S.R.M., and Oard J.H. Proteomic and genetic approaches to identifying defence-related proteins in rice challenged with the fungal pathogen Rhizoctonia solani. Mol. Plant Pathol. 7 (2006) 177-189
    • (2006) Mol. Plant Pathol. , vol.7 , pp. 177-189
    • Lee, O.1    Bricker, T.M.2    Lefevre, M.3    Pinson, S.R.M.4    Oard, J.H.5
  • 35
    • 0031172678 scopus 로고    scopus 로고
    • Vacuolar uptake of the phytoalexin medicarpin by the glutathione conjugate pump
    • Li Z.S., Alfenito M., Rea P.A., Walbot V., and Dixon R.A. Vacuolar uptake of the phytoalexin medicarpin by the glutathione conjugate pump. Phytochemistry 45 (1997) 689-693
    • (1997) Phytochemistry , vol.45 , pp. 689-693
    • Li, Z.S.1    Alfenito, M.2    Rea, P.A.3    Walbot, V.4    Dixon, R.A.5
  • 36
    • 27944490899 scopus 로고    scopus 로고
    • OsWRKY03, a rice transcriptional activator that functions in defense signaling pathway upstream of OsNPR1
    • Liu X.Q., Bai X.Q., Qian Q., Wang X.J., Chen M.S., and Chu C.C. OsWRKY03, a rice transcriptional activator that functions in defense signaling pathway upstream of OsNPR1. Cell Res. 15 (2005) 593-603
    • (2005) Cell Res. , vol.15 , pp. 593-603
    • Liu, X.Q.1    Bai, X.Q.2    Qian, Q.3    Wang, X.J.4    Chen, M.S.5    Chu, C.C.6
  • 37
    • 0027994499 scopus 로고
    • Increased disease susceptibility of transgenic tobacco plants with suppressed levels of preformed phenylpropanoid products
    • Maher E.A., Bate N.J., Ni W., Elkind Y., Dixon R.A., and Lamb C.J. Increased disease susceptibility of transgenic tobacco plants with suppressed levels of preformed phenylpropanoid products. Proc. Natl. Acad. Sci. USA 91 (1994) 7802-7806
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 7802-7806
    • Maher, E.A.1    Bate, N.J.2    Ni, W.3    Elkind, Y.4    Dixon, R.A.5    Lamb, C.J.6
  • 38
    • 33845195949 scopus 로고    scopus 로고
    • Proteomic analysis of bacterial-blight defense-responsive proteins in rice leaf blades
    • Mahmood T., Jan A., Kakishima M., and Komatsu S. Proteomic analysis of bacterial-blight defense-responsive proteins in rice leaf blades. Proteomics 6 (2006) 6053-6065
    • (2006) Proteomics , vol.6 , pp. 6053-6065
    • Mahmood, T.1    Jan, A.2    Kakishima, M.3    Komatsu, S.4
  • 39
    • 1242316937 scopus 로고    scopus 로고
    • Proteomic analysis of the effect of heat stress on hexaploid wheat grain: characterization of heat-responsive proteins from non-prolamins fraction
    • Majoul T., Bancel E., Triboi E., Ben Hamida J., and Branlard G. Proteomic analysis of the effect of heat stress on hexaploid wheat grain: characterization of heat-responsive proteins from non-prolamins fraction. Proteomics 4 (2004) 505-513
    • (2004) Proteomics , vol.4 , pp. 505-513
    • Majoul, T.1    Bancel, E.2    Triboi, E.3    Ben Hamida, J.4    Branlard, G.5
  • 40
    • 0000677401 scopus 로고    scopus 로고
    • The functions and regulation of glutathione S-transferases in plants
    • Marrs K.A. The functions and regulation of glutathione S-transferases in plants. Annu. Rev. Plant Physiol. Plant Mol. Biol. 47 (1996) 127-158
    • (1996) Annu. Rev. Plant Physiol. Plant Mol. Biol. , vol.47 , pp. 127-158
    • Marrs, K.A.1
  • 41
    • 0036674222 scopus 로고    scopus 로고
    • Recent breakthroughs in the study of salicylic acid biosynthesis
    • Metraux J.P. Recent breakthroughs in the study of salicylic acid biosynthesis. Trends Plant Sci. 7 (2002) 332-334
    • (2002) Trends Plant Sci. , vol.7 , pp. 332-334
    • Metraux, J.P.1
  • 42
    • 0030065342 scopus 로고    scopus 로고
    • Cloning and characterization of a probenazole-inducible gene for an intracellular pathogenesis-related protein in rice
    • Midoh N., and Iwata M. Cloning and characterization of a probenazole-inducible gene for an intracellular pathogenesis-related protein in rice. Plant Cell Physiol. 37 (1996) 9-18
    • (1996) Plant Cell Physiol. , vol.37 , pp. 9-18
    • Midoh, N.1    Iwata, M.2
  • 43
    • 0142200326 scopus 로고    scopus 로고
    • Osgstu3 and osgtu4, encoding tau class glutathione S-transferases, are heavy metal- and hypoxic stress-induced and differentially salt stress-responsive in rice roots
    • Moons A. Osgstu3 and osgtu4, encoding tau class glutathione S-transferases, are heavy metal- and hypoxic stress-induced and differentially salt stress-responsive in rice roots. FEBS Lett. 553 (2003) 427-432
    • (2003) FEBS Lett. , vol.553 , pp. 427-432
    • Moons, A.1
  • 48
    • 1642464018 scopus 로고    scopus 로고
    • A proteomic approach to identify early molecular targets of oxidative stress in human epithelial lens cells
    • Paron I., D'Elia A., D'Ambrosio C., Scaloni A., D'Aurizio F., Prescott A., Damante G., and Tell G. A proteomic approach to identify early molecular targets of oxidative stress in human epithelial lens cells. Biochem. J. 378 (2004) 929-937
    • (2004) Biochem. J. , vol.378 , pp. 929-937
    • Paron, I.1    D'Elia, A.2    D'Ambrosio, C.3    Scaloni, A.4    D'Aurizio, F.5    Prescott, A.6    Damante, G.7    Tell, G.8
  • 49
    • 0035109146 scopus 로고    scopus 로고
    • Germins and germin like proteins: an overview
    • Patnaik D., and Khurana P. Germins and germin like proteins: an overview. Indian J. Exp. Biol. 39 (2001) 191-200
    • (2001) Indian J. Exp. Biol. , vol.39 , pp. 191-200
    • Patnaik, D.1    Khurana, P.2
  • 50
    • 0027490705 scopus 로고
    • Leucine aminopeptidase: an inducible component of the defense response in Lycopersicon esculentum (tomato)
    • Pautot V., Holzer F.M., Reisch B., and Walling L.L. Leucine aminopeptidase: an inducible component of the defense response in Lycopersicon esculentum (tomato). Proc. Natl. Acad. Sci. USA 90 (1993) 9906-9910
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 9906-9910
    • Pautot, V.1    Holzer, F.M.2    Reisch, B.3    Walling, L.L.4
  • 51
    • 63249119658 scopus 로고    scopus 로고
    • The proteome of maize leaves: use of gene sequences and expressed sequence tag data for identification of proteins with peptide mass fingerprints
    • Porubleva L., Vander Velden K., Kothari S., Oliver D.J., and Chitnis P.R. The proteome of maize leaves: use of gene sequences and expressed sequence tag data for identification of proteins with peptide mass fingerprints. Electrophoresis 22 (2001) 1724-1738
    • (2001) Electrophoresis , vol.22 , pp. 1724-1738
    • Porubleva, L.1    Vander Velden, K.2    Kothari, S.3    Oliver, D.J.4    Chitnis, P.R.5
  • 52
    • 0032714679 scopus 로고    scopus 로고
    • Separation of proteins from stressed rice (Oryza sativa L.) leaf tissues by two-dimensional polyacrylamide gel electrophoresis: induction of pathogenesis-related and cellular protectant proteins by jasmonic acid, UV irradiation and copper chloride
    • Rakwal R., Agrawal G.K., and Yonekura M. Separation of proteins from stressed rice (Oryza sativa L.) leaf tissues by two-dimensional polyacrylamide gel electrophoresis: induction of pathogenesis-related and cellular protectant proteins by jasmonic acid, UV irradiation and copper chloride. Electrophoresis 20 (1999) 3472-3478
    • (1999) Electrophoresis , vol.20 , pp. 3472-3478
    • Rakwal, R.1    Agrawal, G.K.2    Yonekura, M.3
  • 53
    • 0034729787 scopus 로고    scopus 로고
    • Naringenin 7-O-methyltransferase involved in the biosynthesis of the flavanone phytoalexin sakuranetin from rice (Oryza sativa L.)
    • Rakwal R., Agrawal G.K., Yonekura M., and Kodama O. Naringenin 7-O-methyltransferase involved in the biosynthesis of the flavanone phytoalexin sakuranetin from rice (Oryza sativa L.). Plant Sci. 155 (2000) 213-221
    • (2000) Plant Sci. , vol.155 , pp. 213-221
    • Rakwal, R.1    Agrawal, G.K.2    Yonekura, M.3    Kodama, O.4
  • 54
    • 0033167213 scopus 로고    scopus 로고
    • Chemical induction of disease resistance in rice is correlated with the expression of a gene encoding a nucleotide binding site and leucine-rich repeats
    • Sakamoto K., Tada Y., Yokozeki Y., Akagi H., Hayashi N., Fujimura T., and Ichikawa N. Chemical induction of disease resistance in rice is correlated with the expression of a gene encoding a nucleotide binding site and leucine-rich repeats. Plant Mol. Biol. 40 (1999) 847-855
    • (1999) Plant Mol. Biol. , vol.40 , pp. 847-855
    • Sakamoto, K.1    Tada, Y.2    Yokozeki, Y.3    Akagi, H.4    Hayashi, N.5    Fujimura, T.6    Ichikawa, N.7
  • 55
    • 0028853096 scopus 로고
    • Primary metabolism in plant defense (regulation of a bean malic enzyme gene promoter in transgenic tobacco by developmental and environmental cues)
    • Schaaf J., Walter M.H., and Hess D. Primary metabolism in plant defense (regulation of a bean malic enzyme gene promoter in transgenic tobacco by developmental and environmental cues). Plant Physiol. 108 (1995) 949-960
    • (1995) Plant Physiol. , vol.108 , pp. 949-960
    • Schaaf, J.1    Walter, M.H.2    Hess, D.3
  • 56
    • 0033807105 scopus 로고    scopus 로고
    • Characterization of RCI-1, a chloroplastic rice lipoxygenase whose synthesis is induced by chemical plant resistance activators
    • Schaffrath U., Zabbai F., and Dudler R. Characterization of RCI-1, a chloroplastic rice lipoxygenase whose synthesis is induced by chemical plant resistance activators. Eur. J. Biochem. 267 (2000) 5935-5942
    • (2000) Eur. J. Biochem. , vol.267 , pp. 5935-5942
    • Schaffrath, U.1    Zabbai, F.2    Dudler, R.3
  • 57
    • 0000375725 scopus 로고
    • Dynamic behavior of superoxide generation in rice leaf tissue infected with blast fungus and its regulation by some substances
    • Sekizawa Y., Haga M., Hirabayashi E., Takeuchi N., and Takino Y. Dynamic behavior of superoxide generation in rice leaf tissue infected with blast fungus and its regulation by some substances. Agric. Biol. Chem. 51 (1987) 763-770
    • (1987) Agric. Biol. Chem. , vol.51 , pp. 763-770
    • Sekizawa, Y.1    Haga, M.2    Hirabayashi, E.3    Takeuchi, N.4    Takino, Y.5
  • 58
    • 0041320812 scopus 로고    scopus 로고
    • Phenylpropanoid compounds and disease resistance in transgenic tobacco with altered expression of l-phenylalanine ammonia-lyase
    • Shadle G.L., Wesley S.V., Korth K.L., Chen F., Lamb C., and Dixon R.A. Phenylpropanoid compounds and disease resistance in transgenic tobacco with altered expression of l-phenylalanine ammonia-lyase. Phytochemistry 64 (2003) 153-161
    • (2003) Phytochemistry , vol.64 , pp. 153-161
    • Shadle, G.L.1    Wesley, S.V.2    Korth, K.L.3    Chen, F.4    Lamb, C.5    Dixon, R.A.6
  • 60
    • 0036944850 scopus 로고    scopus 로고
    • OsBIMK1, a rice MAP kinase gene involved in disease resistance responses
    • Song F., and Goodman R.M. OsBIMK1, a rice MAP kinase gene involved in disease resistance responses. Planta 215 (2002) 997-1005
    • (2002) Planta , vol.215 , pp. 997-1005
    • Song, F.1    Goodman, R.M.2
  • 61
    • 3142677326 scopus 로고    scopus 로고
    • Organisation and structural evolution of the rice glutathione S-transferase gene family
    • Soranzo N., Sari Gorla M., Mizzi L., De Toma G., and Frova C. Organisation and structural evolution of the rice glutathione S-transferase gene family. Mol. Genet. Genomics 271 (2004) 511-521
    • (2004) Mol. Genet. Genomics , vol.271 , pp. 511-521
    • Soranzo, N.1    Sari Gorla, M.2    Mizzi, L.3    De Toma, G.4    Frova, C.5
  • 63
    • 11144272581 scopus 로고    scopus 로고
    • Proteome analysis of programmed cell death and defense signaling using the rice lesion mimic mutant cdr2
    • Tsunezuka H., Fujiwara M., Kawasaki T., and Shimamoto K. Proteome analysis of programmed cell death and defense signaling using the rice lesion mimic mutant cdr2. Mol. Plant Microbe. Interact. 18 (2005) 52-59
    • (2005) Mol. Plant Microbe. Interact. , vol.18 , pp. 52-59
    • Tsunezuka, H.1    Fujiwara, M.2    Kawasaki, T.3    Shimamoto, K.4
  • 64
    • 0037072486 scopus 로고    scopus 로고
    • Transcription factors controlling plant secondary metabolism: what regulates the regulators?
    • Vom Endt D., Kijne J.W., and Memelink J. Transcription factors controlling plant secondary metabolism: what regulates the regulators?. Phytochemistry 61 (2002) 107-114
    • (2002) Phytochemistry , vol.61 , pp. 107-114
    • Vom Endt, D.1    Kijne, J.W.2    Memelink, J.3
  • 65
    • 0024060924 scopus 로고
    • Cinnamyl-alcohol dehydrogenase, a molecular marker specific for lignin synthesis: cDNA cloning and mRNA induction by fungal elicitor
    • Walter M.H., Grima-Pettenati J., Grand C., Boudet A.M., and Lamb C.J. Cinnamyl-alcohol dehydrogenase, a molecular marker specific for lignin synthesis: cDNA cloning and mRNA induction by fungal elicitor. Proc. Natl. Acad. Sci. USA 85 (1988) 5546-5550
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 5546-5550
    • Walter, M.H.1    Grima-Pettenati, J.2    Grand, C.3    Boudet, A.M.4    Lamb, C.J.5
  • 68
    • 0035140298 scopus 로고    scopus 로고
    • Probenazole induces systemic acquired resistance in Arabidopsis with a novel type of action
    • Yoshioka K., Nakashita H., Klessig D.F., and Yamaguchi I. Probenazole induces systemic acquired resistance in Arabidopsis with a novel type of action. Plant J. 25 (2001) 149-157
    • (2001) Plant J. , vol.25 , pp. 149-157
    • Yoshioka, K.1    Nakashita, H.2    Klessig, D.F.3    Yamaguchi, I.4
  • 69
    • 0029410802 scopus 로고
    • Cloning and properties of a rice gene encoding phenylalanine ammonia-lyase
    • Zhu Q., Dabi T., Beeche A., Yamamoto R., Lawton M.A., and Lamb C. Cloning and properties of a rice gene encoding phenylalanine ammonia-lyase. Plant Mol. Biol. 29 (1995) 535-550
    • (1995) Plant Mol. Biol. , vol.29 , pp. 535-550
    • Zhu, Q.1    Dabi, T.2    Beeche, A.3    Yamamoto, R.4    Lawton, M.A.5    Lamb, C.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.