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Volumn 11, Issue 12, 1998, Pages 1167-1174

Gene activation by cytoplasmic acidification in suspension-cultured rice cells in response to the potent elicitor, N-acetylchitoheptaose

Author keywords

Protein phosphorylation

Indexed keywords

1,3 BETA GLUCANASE; CHITINASE; DISEASE RESISTANCE; GENE ACTIVATION; N ACETYLCHITOHEPTAOSE; PATHOGENESIS; PHENYLALANINE AMMONIA LYASE;

EID: 0031736222     PISSN: 08940282     EISSN: None     Source Type: Journal    
DOI: 10.1094/MPMI.1998.11.12.1167     Document Type: Article
Times cited : (61)

References (52)
  • 1
    • 0029861785 scopus 로고    scopus 로고
    • + efflux, and extracellular alkalization in soybean cells carrying the disease-resistance gene Rpg4
    • + efflux, and extracellular alkalization in soybean cells carrying the disease-resistance gene Rpg4. Plant Physiol. 112:297-302.
    • (1996) Plant Physiol. , vol.112 , pp. 297-302
    • Atkinson, M.M.1    Midland, S.L.2    Sims, J.J.3    Keen, N.T.4
  • 2
    • 0029197672 scopus 로고
    • Reactive oxygen in plant pathogenesis
    • Baker, C. J., and Orlandi, E. W. 1995. Reactive oxygen in plant pathogenesis. Annu. Rev. Phytopathol. 33:299-321.
    • (1995) Annu. Rev. Phytopathol. , vol.33 , pp. 299-321
    • Baker, C.J.1    Orlandi, E.W.2
  • 3
    • 0027197331 scopus 로고
    • High affinity binding of glycopeptide elicitor to tomato cells and microsomal membranes and displacement by specific glucan suppressers
    • Basse, C. W., Fath, A., and Boller, T. 1993. High affinity binding of glycopeptide elicitor to tomato cells and microsomal membranes and displacement by specific glucan suppressers. J. Biol. Chem. 268: 14724-14731.
    • (1993) J. Biol. Chem. , vol.268 , pp. 14724-14731
    • Basse, C.W.1    Fath, A.2    Boller, T.3
  • 4
    • 0028364086 scopus 로고
    • Specific, high affinity binding of chitin fragments to tomato cells and membranes. Competitive inhibition of binding by derivatives of chitooligosaccharides and a Nod factor of Rhizobium
    • Baureithel, K., Felix, G., and Boller, T. 1994. Specific, high affinity binding of chitin fragments to tomato cells and membranes. Competitive inhibition of binding by derivatives of chitooligosaccharides and a Nod factor of Rhizobium. J. Biol. Chem. 269:17931-17938.
    • (1994) J. Biol. Chem. , vol.269 , pp. 17931-17938
    • Baureithel, K.1    Felix, G.2    Boller, T.3
  • 5
    • 0028797143 scopus 로고
    • Chemoperception of microbial signals in plant cells
    • Boller, T. 1995. Chemoperception of microbial signals in plant cells. Annu. Rev. Plant Physiol. Plant Mol. Biol. 46:189-214.
    • (1995) Annu. Rev. Plant Physiol. Plant Mol. Biol. , vol.46 , pp. 189-214
    • Boller, T.1
  • 6
    • 0026102624 scopus 로고
    • A specific, high-affinity binding site for the hepta-β-glucoside elicitor exists in soybean membranes
    • Cheong, J.-J., and Hahn, M. G. 1991. A specific, high-affinity binding site for the hepta-β-glucoside elicitor exists in soybean membranes. Plant Cell 3:137-147.
    • (1991) Plant Cell , vol.3 , pp. 137-147
    • Cheong, J.-J.1    Hahn, M.G.2
  • 7
    • 0028721071 scopus 로고
    • Oligosaccharins: Structures and signal transduction
    • Cote, F., and Hahn, M.G. 1994. Oligosaccharins: Structures and signal transduction. Plant Mol. Biol. 26:1379-1411.
    • (1994) Plant Mol. Biol. , vol.26 , pp. 1379-1411
    • Cote, F.1    Hahn, M.G.2
  • 8
    • 0025248871 scopus 로고
    • Fungal elicitor triggers rapid, transient, and specific protein phosphorylation in parsley cell suspension cultures
    • Dietrich, A., Mayers, J. E., and Hahlbrock, K. 1990. Fungal elicitor triggers rapid, transient, and specific protein phosphorylation in parsley cell suspension cultures. J. Biol. Chem. 265:6360-6368.
    • (1990) J. Biol. Chem. , vol.265 , pp. 6360-6368
    • Dietrich, A.1    Mayers, J.E.2    Hahlbrock, K.3
  • 9
    • 0025070571 scopus 로고
    • Activation, structure, and organization of genes involved in microbial defense in plants
    • Dixon, R. A., and Harrison, M. J. 1990. Activation, structure, and organization of genes involved in microbial defense in plants. Adv. Genet. 28:165-234.
    • (1990) Adv. Genet. , vol.28 , pp. 165-234
    • Dixon, R.A.1    Harrison, M.J.2
  • 10
    • 0028078429 scopus 로고
    • Early events in the activation of plant defense responses
    • Dixon, R. A., Harrison, M. J., and Lamb, C. J. 1994. Early events in the activation of plant defense responses. Annu. Rev. Phytopathol. 32: 479-501.
    • (1994) Annu. Rev. Phytopathol. , vol.32 , pp. 479-501
    • Dixon, R.A.1    Harrison, M.J.2    Lamb, C.J.3
  • 11
    • 0028354159 scopus 로고
    • Elicitors of plant defense responses
    • Ebel, J., and Cosio, E. G. 1994. Elicitors of plant defense responses. Int. Rev. Cytol. 148:1-36.
    • (1994) Int. Rev. Cytol. , vol.148 , pp. 1-36
    • Ebel, J.1    Cosio, E.G.2
  • 12
    • 0025759024 scopus 로고
    • Oligosaccharide signaling in plants. Specificity of oligouronide-enhanced plasma membrane protein phosphorylation
    • Farmer, E. E., Moloshok, T. D., Sacton, M. J., and Ryan, C. A. 1991. Oligosaccharide signaling in plants. Specificity of oligouronide-enhanced plasma membrane protein phosphorylation. J. Biol. Chem. 266:3140-3145.
    • (1991) J. Biol. Chem. , vol.266 , pp. 3140-3145
    • Farmer, E.E.1    Moloshok, T.D.2    Sacton, M.J.3    Ryan, C.A.4
  • 13
    • 0026076198 scopus 로고
    • Rapid changes of protein phosphorylation are involved in transduction of the elicitor signal in plant cells
    • Felix, G., Grosskopf, D. G., Regenass, M., and Boller, T. 1991. Rapid changes of protein phosphorylation are involved in transduction of the elicitor signal in plant cells. Proc. Natl. Acad. Sci. USA 88:8831-8834.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 8831-8834
    • Felix, G.1    Grosskopf, D.G.2    Regenass, M.3    Boller, T.4
  • 14
    • 0000538103 scopus 로고
    • Specific perception of subnanomolar concentrations of chitin fragments by tomato cells: Induction of extracellular alkalinization, changes in protein phosphorylation, and establishment of a refractory state
    • Felix, G., Regenass, M., and Boller, T. 1993. Specific perception of subnanomolar concentrations of chitin fragments by tomato cells: Induction of extracellular alkalinization, changes in protein phosphorylation, and establishment of a refractory state. Plant J. 4:307-316.
    • (1993) Plant J. , vol.4 , pp. 307-316
    • Felix, G.1    Regenass, M.2    Boller, T.3
  • 16
    • 0025008452 scopus 로고
    • K-252a inhibits the response of tomato cells to fungal elicitors in vivo and their microsomal protein kinase in vitro
    • Grosskopf, D. G., Felix, G., and Boller, T. 1990. K-252a inhibits the response of tomato cells to fungal elicitors in vivo and their microsomal protein kinase in vitro. FEBS Lett. 275:177-180.
    • (1990) FEBS Lett. , vol.275 , pp. 177-180
    • Grosskopf, D.G.1    Felix, G.2    Boller, T.3
  • 18
    • 0000568861 scopus 로고
    • Plant cells counteract cytoplasmic pH changes but likely use these pH changes as secondary messages in signal perception
    • Guern, J., Mathieu, Y., Thomine, S., Jouanneau, J.-P., and Beloeil, J.-C. 1992. Plant cells counteract cytoplasmic pH changes but likely use these pH changes as secondary messages in signal perception. Curr. Top. Plant Biochem. Physiol. 11:249-269.
    • (1992) Curr. Top. Plant Biochem. Physiol. , vol.11 , pp. 249-269
    • Guern, J.1    Mathieu, Y.2    Thomine, S.3    Jouanneau, J.-P.4    Beloeil, J.-C.5
  • 19
    • 0000335377 scopus 로고
    • Effect of elicitors on the plasmamembrane of Petunia hybrida cell suspensions - Role of ΔpH in signal transduction
    • Hagendoorn, M. J. M., Poortinga, A. M., Sang, H. W. W. F., van der Plas, L. H. W., and van Walraven, H. S. 1990a. Effect of elicitors on the plasmamembrane of Petunia hybrida cell suspensions - Role of ΔpH in signal transduction. Plant Physiol. 96:1261-1267.
    • (1990) Plant Physiol. , vol.96 , pp. 1261-1267
    • Hagendoorn, M.J.M.1    Poortinga, A.M.2    Sang, H.W.W.F.3    Van Der Plas, L.H.W.4    Van Walraven, H.S.5
  • 20
    • 0002126608 scopus 로고
    • Orthovanadate induced lignin production, in batch and continuous cultures of Petunia hybrida
    • Hagendoorn, M. J. M., Traas, T. P., Boon, J. J., and van der Plas, L. H. W. 1990b. Orthovanadate induced lignin production, in batch and continuous cultures of Petunia hybrida. J. Plant Physiol. 137:72-80.
    • (1990) J. Plant Physiol. , vol.137 , pp. 72-80
    • Hagendoorn, M.J.M.1    Traas, T.P.2    Boon, J.J.3    Van Der Plas, L.H.W.4
  • 21
    • 0001758546 scopus 로고
    • Induction of phenylalanine ammonia-lyase activation and isoflavone glucoside accumulation in suspension-cultured cells of red bean, Vigna angularis, by phytoalexin elicitors, vanadate, and elevation of medium pH
    • Hattori, T., and Ohta, Y. 1985. Induction of phenylalanine ammonia-lyase activation and isoflavone glucoside accumulation in suspension-cultured cells of red bean, Vigna angularis, by phytoalexin elicitors, vanadate, and elevation of medium pH. Plant Cell Physiol. 26:1101-1110.
    • (1985) Plant Cell Physiol. , vol.26 , pp. 1101-1110
    • Hattori, T.1    Ohta, Y.2
  • 22
    • 0001672150 scopus 로고
    • Effect of elicitation and changes in extracellular pH on the cytoplasmic and vacuolar pH of suspension-cultured soybean cells
    • Horn, M. A., Meadows, R. P., Apostol, I., Jones, C. R., Gorenstein, D. G., Heinstein, P. F., and Low, P. S. 1992. Effect of elicitation and changes in extracellular pH on the cytoplasmic and vacuolar pH of suspension-cultured soybean cells. Plant Physiol. 98:680-686.
    • (1992) Plant Physiol. , vol.98 , pp. 680-686
    • Horn, M.A.1    Meadows, R.P.2    Apostol, I.3    Jones, C.R.4    Gorenstein, D.G.5    Heinstein, P.F.6    Low, P.S.7
  • 23
    • 0027479225 scopus 로고
    • Induction of protein phosphorylation, protein synthesis, immediate-early-gene expression and cellular proliferation by intracellular pH modulation
    • Isfort, R. J., Cody, D. B., Asquith, T. N., Ridder, G. M., Stuard, S. B., and Leboeuf, R. A. 1993. Induction of protein phosphorylation, protein synthesis, immediate-early-gene expression and cellular proliferation by intracellular pH modulation. Eur. J. Biochem. 213:349-357.
    • (1993) Eur. J. Biochem. , vol.213 , pp. 349-357
    • Isfort, R.J.1    Cody, D.B.2    Asquith, T.N.3    Ridder, G.M.4    Stuard, S.B.5    Leboeuf, R.A.6
  • 24
    • 0031213917 scopus 로고    scopus 로고
    • Identification of a high-affinity binding protein for N-acetylchitooligosaccharide elicitor in the plasma membrane of suspension-cultured rice cells by affinity labeling
    • Ito, Y., Kaku, H., and Shibuya, N. 1997. Identification of a high-affinity binding protein for N-acetylchitooligosaccharide elicitor in the plasma membrane of suspension-cultured rice cells by affinity labeling. Plant J. 12:347-356.
    • (1997) Plant J. , vol.12 , pp. 347-356
    • Ito, Y.1    Kaku, H.2    Shibuya, N.3
  • 25
    • 0030865049 scopus 로고    scopus 로고
    • Membrane depolarization induced by N-acetylchitooligosaccharide elicitor in suspension-cultured rice cells
    • Kikuyama, M., Kuchitsu, K., and Shibuya, N. 1997. Membrane depolarization induced by N-acetylchitooligosaccharide elicitor in suspension-cultured rice cells. Plant Cell Physiol. 38:902-909.
    • (1997) Plant Cell Physiol. , vol.38 , pp. 902-909
    • Kikuyama, M.1    Kuchitsu, K.2    Shibuya, N.3
  • 26
    • 0002498976 scopus 로고
    • N-acetylchitooligosaccharides, biotic elicitor for phytoalexin production, induce transient membrane depolarization is suspension-cultured rice cells
    • Kuchitsu, K., Kikuyama, M., and Shibuya, N. 1993. N-acetylchitooligosaccharides, biotic elicitor for phytoalexin production, induce transient membrane depolarization is suspension-cultured rice cells. Protoplasma 174:79-81.
    • (1993) Protoplasma , vol.174 , pp. 79-81
    • Kuchitsu, K.1    Kikuyama, M.2    Shibuya, N.3
  • 27
    • 0028854442 scopus 로고
    • EPR evidence for generation of hydroxyl radical triggered by N-acetylchitooligosaccharide elicitor and a protein phosphatase inhibitor in suspension-cultured rice cells
    • Kuchitsu, K., Kosaka, H., Shiga, T., and Shibuya, N. 1995. EPR evidence for generation of hydroxyl radical triggered by N-acetylchitooligosaccharide elicitor and a protein phosphatase inhibitor in suspension-cultured rice cells. Protoplasma 188:138-142.
    • (1995) Protoplasma , vol.188 , pp. 138-142
    • Kuchitsu, K.1    Kosaka, H.2    Shiga, T.3    Shibuya, N.4
  • 28
    • 0002501498 scopus 로고
    • N-acetylchitooligosaccharides, specific fungal elicitor for defense responses, induce transient generation of reactive oxygen species in suspension-cultured rice cells
    • K. Asada and T. Yoshikawa, eds. Elsevier Science, Amsterdam
    • Kuchitsu, K., and Shibuya, N. 1994. N-acetylchitooligosaccharides, specific fungal elicitor for defense responses, induce transient generation of reactive oxygen species in suspension-cultured rice cells. Pages 255-256 in: Frontiers of Reactive Oxygen Species in Biology and Medicine K. Asada and T. Yoshikawa, eds. Elsevier Science, Amsterdam.
    • (1994) Frontiers of Reactive Oxygen Species in Biology and Medicine , pp. 255-256
    • Kuchitsu, K.1    Shibuya, N.2
  • 29
    • 0030765880 scopus 로고    scopus 로고
    • Transient cytoplasmic pH change and ion fluxes through the plasma membrane triggered by N-acetylchitooligosaccharide elicitor in suspension-cultured rice cells
    • Kuchitsu, K., Yazaki, Y., Sakano, K., and Shibuya, N. 1997. Transient cytoplasmic pH change and ion fluxes through the plasma membrane triggered by N-acetylchitooligosaccharide elicitor in suspension-cultured rice cells. Plant Cell Physiol. 38:1012-1018.
    • (1997) Plant Cell Physiol. , vol.38 , pp. 1012-1018
    • Kuchitsu, K.1    Yazaki, Y.2    Sakano, K.3    Shibuya, N.4
  • 30
    • 0028056888 scopus 로고
    • Acquired resistance signal transduction in Arabidopsis is ethylene independent
    • Lawton, K.A., Potter, S. L., Ukens, S., and Ryals, J. 1994. Acquired resistance signal transduction in Arabidopsis is ethylene independent. Plant Cell 6:581-588.
    • (1994) Plant Cell , vol.6 , pp. 581-588
    • Lawton, K.A.1    Potter, S.L.2    Ukens, S.3    Ryals, J.4
  • 31
    • 0028171293 scopus 로고
    • 2 from the oxidative burst orchestrated the plant hypersensitive disease resistance response
    • 2 from the oxidative burst orchestrated the plant hypersensitive disease resistance response. Cell 79:583-593.
    • (1994) Cell , vol.79 , pp. 583-593
    • Levine, A.1    Tenhaken, R.2    Dixon, R.3    Lamb, C.4
  • 32
    • 0028065895 scopus 로고
    • Protein phosphatase inhibitors activate anti-fungal defense responses of soybean cotyledons and cell cultures
    • MacIntosh, C., Lyon, G. D., and MacIntosh, R. W. 1994. Protein phosphatase inhibitors activate anti-fungal defense responses of soybean cotyledons and cell cultures. Plant J. 5:137-147.
    • (1994) Plant J. , vol.5 , pp. 137-147
    • MacIntosh, C.1    Lyon, G.D.2    MacIntosh, R.W.3
  • 34
    • 0029795667 scopus 로고    scopus 로고
    • Cytoplasmic acidification as an early phosphorylation-dependent response of tobacco cells to elicitors
    • Mathieu, Y., Lapous, D., Thomine, S., Lauriere, C., and Guern, J. 1996. Cytoplasmic acidification as an early phosphorylation-dependent response of tobacco cells to elicitors. Planta 199:416-424.
    • (1996) Planta , vol.199 , pp. 416-424
    • Mathieu, Y.1    Lapous, D.2    Thomine, S.3    Lauriere, C.4    Guern, J.5
  • 35
    • 0003906732 scopus 로고
    • An elicitor from Phytophthora megasperma f. sp. glycinea influences the membrane potential of soybean cotyledonary cells
    • Mayer, M. G., and Ziegler, E. 1988. An elicitor from Phytophthora megasperma f. sp. glycinea influences the membrane potential of soybean cotyledonary cells. Physiol. Mol. Plant Pathol. 33:397-407.
    • (1988) Physiol. Mol. Plant Pathol. , vol.33 , pp. 397-407
    • Mayer, M.G.1    Ziegler, E.2
  • 36
    • 0030174994 scopus 로고    scopus 로고
    • Two novel genes rapidly and transiently activated in suspension-cultured rice cells by treatment with N-acetylchitoheptaose, a biotic elicitor for phytoalexin production
    • Minami, E., Kuchitsu, K., He, D.-Y., Kouchi, H., Midoh, N., Ohtsuki, Y., and Shibuya, N. 1996. Two novel genes rapidly and transiently activated in suspension-cultured rice cells by treatment with N-acetylchitoheptaose, a biotic elicitor for phytoalexin production. Plant Cell Physiol. 37:563-567.
    • (1996) Plant Cell Physiol. , vol.37 , pp. 563-567
    • Minami, E.1    Kuchitsu, K.2    He, D.-Y.3    Kouchi, H.4    Midoh, N.5    Ohtsuki, Y.6    Shibuya, N.7
  • 37
    • 0024975177 scopus 로고
    • Structure and some characterization of the gene for phenylalanine ammonia-lyase from rice plants
    • Minami, E., Ozeki, Y., Matsuoka, M., Koizuka, N., and Tanaka, Y. 1989. Structure and some characterization of the gene for phenylalanine ammonia-lyase from rice plants. Eur. J. Biochem. 185:19-25.
    • (1989) Eur. J. Biochem. , vol.185 , pp. 19-25
    • Minami, E.1    Ozeki, Y.2    Matsuoka, M.3    Koizuka, N.4    Tanaka, Y.5
  • 38
    • 0000117228 scopus 로고
    • Rice chitinase gene: cDNA cloning and stress-induced expression
    • Nishizawa, Y., and Hibi, T. 1991. Rice chitinase gene: cDNA cloning and stress-induced expression. Plant Sci. 76:211-218.
    • (1991) Plant Sci. , vol.76 , pp. 211-218
    • Nishizawa, Y.1    Hibi, T.2
  • 39
    • 0027967403 scopus 로고
    • High-affinity binding of a fungal oligopeptide elicitor to parsley plasma membranes triggers multiple defense responses
    • Nürnberger, T., Nennstiel, D., Jabs, D., Sacks, W. R., Hahlbrock, K., and Sheel, D. 1994. High-affinity binding of a fungal oligopeptide elicitor to parsley plasma membranes triggers multiple defense responses. Cell 78:449-460.
    • (1994) Cell , vol.78 , pp. 449-460
    • Nürnberger, T.1    Nennstiel, D.2    Jabs, D.3    Sacks, W.R.4    Hahlbrock, K.5    Sheel, D.6
  • 40
    • 0000466840 scopus 로고
    • 31P NMR study of elicitor treated Phaseolus vulgaris cell suspension cultures
    • 31P NMR study of elicitor treated Phaseolus vulgaris cell suspension cultures. Plant Physiol. 85:716-719.
    • (1987) Plant Physiol. , vol.85 , pp. 716-719
    • Ojalvo, I.1    Rokem, S.2    Navon, G.3    Goldberg, I.4
  • 42
    • 0029853904 scopus 로고    scopus 로고
    • Interaction of elicitor-induced DNA-binding proteins with elicitor response elements in the promoters of parsley PR1 genes
    • Rushton, P. J., Torres, J. T., Parniske, M., Wernert, P., Hahlbrock, K., and Sommsich, I. 1996. Interaction of elicitor-induced DNA-binding proteins with elicitor response elements in the promoters of parsley PR1 genes. EMBO J. 15:5690-5700.
    • (1996) EMBO J. , vol.15 , pp. 5690-5700
    • Rushton, P.J.1    Torres, J.T.2    Parniske, M.3    Wernert, P.4    Hahlbrock, K.5    Sommsich, I.6
  • 44
    • 34249839473 scopus 로고
    • 2+ and protein-kinase activity
    • 2+ and protein-kinase activity. Planta 187:136-141.
    • (1992) Planta , vol.187 , pp. 136-141
    • Schwacke, R.1    Hager, R.2
  • 45
    • 0344370303 scopus 로고    scopus 로고
    • Protein complexes binding to cis elements of the plant histone gene promoters: Multiplicity, phosphorylation and cell cycle alteration
    • Shen, W. H., and Gigot, C. 1997. Protein complexes binding to cis elements of the plant histone gene promoters: multiplicity, phosphorylation and cell cycle alteration. Plant Mol. Biol. 33:367-379.
    • (1997) Plant Mol. Biol. , vol.33 , pp. 367-379
    • Shen, W.H.1    Gigot, C.2
  • 46
    • 0029807346 scopus 로고    scopus 로고
    • Localization and binding characteristics of a high-affinity binding site for N-acetylchitooligosaccharide elicitor in the plasma membrane from suspension-cultured rice cells suggest a role as a receptor for the elicitor signal at the cell surface
    • Shibuya, N., Ebisu, N., Kamada, Y., Kaku, H., Cohn, J., and Ito, Y. 1996. Localization and binding characteristics of a high-affinity binding site for N-acetylchitooligosaccharide elicitor in the plasma membrane from suspension-cultured rice cells suggest a role as a receptor for the elicitor signal at the cell surface. Plant Cell Physiol. 37:894-898.
    • (1996) Plant Cell Physiol. , vol.37 , pp. 894-898
    • Shibuya, N.1    Ebisu, N.2    Kamada, Y.3    Kaku, H.4    Cohn, J.5    Ito, Y.6
  • 47
    • 0027326649 scopus 로고
    • Identification of a novel high-affinity binding site for N-acetylchitooligosaccharide elicitor in the membrane fraction from suspension-cultured rice cells
    • Shibuya, N., Kaku, H., Kuchitsu, K., and Maliarik, M. J. 1993. Identification of a novel high-affinity binding site for N-acetylchitooligosaccharide elicitor in the membrane fraction from suspension-cultured rice cells. FEBS Lett. 329:75-78.
    • (1993) FEBS Lett. , vol.329 , pp. 75-78
    • Shibuya, N.1    Kaku, H.2    Kuchitsu, K.3    Maliarik, M.J.4
  • 48
    • 0000326768 scopus 로고
    • Vanadate mimics effects of fungal cell wall in eliciting gene activation in plant cell cultures
    • Steffens, M., Ettl, F., Kranz, D., and Kindl, H. 1989. Vanadate mimics effects of fungal cell wall in eliciting gene activation in plant cell cultures. Planta 177:160-168.
    • (1989) Planta , vol.177 , pp. 160-168
    • Steffens, M.1    Ettl, F.2    Kranz, D.3    Kindl, H.4
  • 49
    • 0345139564 scopus 로고
    • Nucleotide sequence and genomic organisation of a wheat histone H3 gene
    • Tabata, T., Fukasawa, M., and Iwabuchi, M. 1984. Nucleotide sequence and genomic organisation of a wheat histone H3 gene. Mol. Gen. Genet. 196:397-400.
    • (1984) Mol. Gen. Genet. , vol.196 , pp. 397-400
    • Tabata, T.1    Fukasawa, M.2    Iwabuchi, M.3
  • 50
    • 0021760552 scopus 로고
    • The complete nucleotide sequence of a rice 17S rRNA gene
    • Takaiwa, F., Oono, K., and Sugiura, M. 1984. The complete nucleotide sequence of a rice 17S rRNA gene. Nucleic Acids Res. 12:5441-5448.
    • (1984) Nucleic Acids Res. , vol.12 , pp. 5441-5448
    • Takaiwa, F.1    Oono, K.2    Sugiura, M.3
  • 51
    • 0020930611 scopus 로고
    • Hybridization of denatured RNA transferred or dotted to nitrocellulose paper
    • Thomas, P. S. 1983. Hybridization of denatured RNA transferred or dotted to nitrocellulose paper. Methods Enzymol. 100:255-256.
    • (1983) Methods Enzymol. , vol.100 , pp. 255-256
    • Thomas, P.S.1
  • 52
    • 0000956263 scopus 로고
    • Induction of phytoalexin formation in suspension-cultured rice cells by N-acetylchitooligosaccharides
    • Yamada, A., Shibuya, N., Kodama, O., and Akatsuka, T. 1993. Induction of phytoalexin formation in suspension-cultured rice cells by N-acetylchitooligosaccharides. Biosci. Biotech. Biochem. 57:405-409.
    • (1993) Biosci. Biotech. Biochem. , vol.57 , pp. 405-409
    • Yamada, A.1    Shibuya, N.2    Kodama, O.3    Akatsuka, T.4


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