메뉴 건너뛰기




Volumn 114, Issue 3, 1997, Pages 957-968

Differential effect of purified spruce chitinases and β-1,3-glucanases on the activity of elicitors from ectomycorrhizal fungi

Author keywords

[No Author keywords available]

Indexed keywords

1,3 BETA GLUCANASE; CHITINASE; ELICITOR; ENZYME ACTIVITY; SPRUCE; SYMBIOSIS;

EID: 0031177743     PISSN: 00320889     EISSN: None     Source Type: Journal    
DOI: 10.1104/pp.114.3.957     Document Type: Article
Times cited : (48)

References (63)
  • 1
    • 0027947217 scopus 로고
    • Chitinase activities are induced in Eucalyptus globulus roots by ectomycorrhizal or pathogenic fungi during early colonization
    • Albrecht C, Asselin A, Piché Y, Lapeyrie F (1994a) Chitinase activities are induced in Eucalyptus globulus roots by ectomycorrhizal or pathogenic fungi during early colonization. Physiol Plant 91: 104-110
    • (1994) Physiol Plant , vol.91 , pp. 104-110
    • Albrecht, C.1    Asselin, A.2    Piché, Y.3    Lapeyrie, F.4
  • 2
    • 0028042178 scopus 로고
    • Chitinase and peroxidase activities are induced in eucalyptus roots according to aggressiveness of Australian ectomycorrhizal strains of Pisolithus sp
    • Albrecht C, Burgess T, Dell B, Lapeyrie F (1994b) Chitinase and peroxidase activities are induced in eucalyptus roots according to aggressiveness of Australian ectomycorrhizal strains of Pisolithus sp. New Phytol 127: 217-222
    • (1994) New Phytol , vol.127 , pp. 217-222
    • Albrecht, C.1    Burgess, T.2    Dell, B.3    Lapeyrie, F.4
  • 3
    • 0022067755 scopus 로고
    • Fast and sensitive detection of protein and DNA bands by treatment with potassium permanganate
    • Ansorge W (1985) Fast and sensitive detection of protein and DNA bands by treatment with potassium permanganate. J Biochem Biophys Methods 11: 13-20
    • (1985) J Biochem Biophys Methods , vol.11 , pp. 13-20
    • Ansorge, W.1
  • 4
    • 0002215662 scopus 로고
    • Inhibition of fungal growth by plant chitinases and β-1,3-glucanases
    • Arlorio M, Ludwig A, Boller T, Bonfante P (1992) Inhibition of fungal growth by plant chitinases and β-1,3-glucanases. Protoplasma 171: 34-43
    • (1992) Protoplasma , vol.171 , pp. 34-43
    • Arlorio, M.1    Ludwig, A.2    Boller, T.3    Bonfante, P.4
  • 5
    • 0007654234 scopus 로고
    • Effects of chitinase and β-1,3-glucanase from pea on the growth of saprophytic, pathogenic and mycorrhizal fungi
    • Arlorio M, Ludwig A, Boller T, Mischiati P, Bonfante P (1991) Effects of chitinase and β-1,3-glucanase from pea on the growth of saprophytic, pathogenic and mycorrhizal fungi. Giornale Botanico Italiano 125: 956-959
    • (1991) Giornale Botanico Italiano , vol.125 , pp. 956-959
    • Arlorio, M.1    Ludwig, A.2    Boller, T.3    Mischiati, P.4    Bonfante, P.5
  • 7
    • 0029861785 scopus 로고    scopus 로고
    • + efflux, and extracellular alkalinization in soybean cells carrying the disease-resistance gene Rpg4
    • + efflux, and extracellular alkalinization 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
  • 8
    • 0001770740 scopus 로고
    • Chitin oligosaccharides elicit lignification in wounded wheat leaves
    • Barber MS, Bertram RE, Ride JP (1989) Chitin oligosaccharides elicit lignification in wounded wheat leaves. Physiol Mol Plant Pathol 34: 3-12
    • (1989) Physiol Mol Plant Pathol , vol.34 , pp. 3-12
    • Barber, M.S.1    Bertram, R.E.2    Ride, J.P.3
  • 9
    • 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, 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
  • 10
    • 0028890620 scopus 로고
    • Ultrastructural and cytochemical characterization of elicitor-induced structural responses in tomato root tissues infected by Fusarium oxysporum f.sp. radicislycopcrsici
    • Benhamou N, Lafontaine PJ (1995) Ultrastructural and cytochemical characterization of elicitor-induced structural responses in tomato root tissues infected by Fusarium oxysporum f.sp. radicislycopcrsici. Planta 197: 89-102
    • (1995) Planta , vol.197 , pp. 89-102
    • Benhamou, N.1    Lafontaine, P.J.2
  • 11
    • 11944249594 scopus 로고
    • Woundinduced accumulation of mRNA containing a hevein sequence in lactifers of rubber tree (Hevea brasiliensis)
    • Broekaert W, Lee H, Kush A, Chua NH, Raikhel N (1990) Woundinduced accumulation of mRNA containing a hevein sequence in lactifers of rubber tree (Hevea brasiliensis). Proc Natl Acad Sci USA 87: 7633-7637
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 7633-7637
    • Broekaert, W.1    Lee, H.2    Kush, A.3    Chua, N.H.4    Raikhel, N.5
  • 14
    • 0025967962 scopus 로고
    • + release, and increases coumarin synthesis in parsley cells
    • + release, and increases coumarin synthesis in parsley cells. FEBS Lett 279: 141-144
    • (1991) FEBS Lett , vol.279 , pp. 141-144
    • Conrath, U.1    Jeblick, W.2    Kauss, H.3
  • 15
    • 0029803282 scopus 로고    scopus 로고
    • Highaffinity binding of fungal β-glucan elicitors to cell membranes of species of the plant family Fabaceae
    • Cosio EG, Feger M, Miller CJ, Antelo L, Ebel J (1996) Highaffinity binding of fungal β-glucan elicitors to cell membranes of species of the plant family Fabaceae. Planta 200: 92-99
    • (1996) Planta , vol.200 , pp. 92-99
    • Cosio, E.G.1    Feger, M.2    Miller, C.J.3    Antelo, L.4    Ebel, J.5
  • 16
  • 17
    • 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, 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
  • 18
    • 0027141602 scopus 로고
    • Induction of chitinase and β-1,3glucanase in Parthenocissus quinquefolia cells cultured in vitro
    • Flach J, Jolles P, Pilet PE (1993) Induction of chitinase and β-1,3glucanase in Parthenocissus quinquefolia cells cultured in vitro. Physiol Plant 89: 399-403
    • (1993) Physiol Plant , vol.89 , pp. 399-403
    • Flach, J.1    Jolles, P.2    Pilet, P.E.3
  • 19
    • 0000791611 scopus 로고
    • Cellular and eenetical aspects of interactions between hosts and fungal symbionts in mycorrhizae
    • Gianinazzi-Pearson Y, Gianinazzi S (1989) Cellular and eenetical aspects of interactions between hosts and fungal symbionts in mycorrhizae. Genome 31: 336-341
    • (1989) Genome , vol.31 , pp. 336-341
    • Gianinazzi-Pearson, Y.1    Gianinazzi, S.2
  • 20
    • 0001666145 scopus 로고
    • Cellular localization and cytochemical probing of resistance reactions to arbuscular mycorrhizal fungi in a "locus a" myc mutant of Pisum sativum L
    • Gollotte A, Gianinazzi-Pearson V, Giovanetti M, Sbrana C, Avio L, Gianinazzi S (1993) Cellular localization and cytochemical probing of resistance reactions to arbuscular mycorrhizal fungi in a "locus a" myc mutant of Pisum sativum L. Planta 191: 112-122
    • (1993) Planta , vol.191 , pp. 112-122
    • Gollotte, A.1    Gianinazzi-Pearson, V.2    Giovanetti, M.3    Sbrana, C.4    Avio, L.5    Gianinazzi, S.6
  • 21
    • 0028190813 scopus 로고
    • Studies on vacuole regeneration in eyacuolated tobacco mesophyll protoplasts: Protein analysis by One- And two-dimensional microgel-electrophoresis
    • Hoffmann EM, Hampp R (1994) Studies on vacuole regeneration in eyacuolated tobacco mesophyll protoplasts: protein analysis by One- and two-dimensional microgel-electrophoresis. Physiol Plant 92: 563-570
    • (1994) Physiol Plant , vol.92 , pp. 563-570
    • Hoffmann, E.M.1    Hampp, R.2
  • 23
    • 0028796219 scopus 로고
    • Effect of exogenous glucose on mycorrhizal colonisation in vitro by early-stage and late-stage ectomycorrhizal fungi
    • Hutchinson LJ, Piché Y (1995) Effect of exogenous glucose on mycorrhizal colonisation in vitro by early-stage and late-stage ectomycorrhizal fungi. Can J Bot 73: 898-904
    • (1995) Can J Bot , vol.73 , pp. 898-904
    • Hutchinson, L.J.1    Piché, Y.2
  • 24
    • 0001177601 scopus 로고
    • Induction of chitinases in rice callus treated with chitin derivatives
    • Inui H, Kosaki H, Uno Y, Tabata K, Hirano S (1991) Induction of chitinases in rice callus treated with chitin derivatives. Agric Biol Chem 55: 3107-3109
    • (1991) Agric Biol Chem , vol.55 , pp. 3107-3109
    • Inui, H.1    Kosaki, H.2    Uno, Y.3    Tabata, K.4    Hirano, S.5
  • 25
    • 0027666351 scopus 로고
    • The N-terminal cystein-rich domain of tobacco class I chitinase is essential for chitin binding but not for catalytic or antifungal activity
    • Iseli B, Boiler T, Neuhaus JM (1993) The N-terminal cystein-rich domain of tobacco class I chitinase is essential for chitin binding but not for catalytic or antifungal activity. Plant Physiol 103: 221-226
    • (1993) Plant Physiol , vol.103 , pp. 221-226
    • Iseli, B.1    Boiler, T.2    Neuhaus, J.M.3
  • 26
    • 0039640145 scopus 로고
    • Characterization of two antifungal endochitinases from barley grain
    • Jacobsen S, Mikkelsen JD, Hejgaard J (1990) Characterization of two antifungal endochitinases from barley grain. Physiol Plant 79: 554-562
    • (1990) Physiol Plant , vol.79 , pp. 554-562
    • Jacobsen, S.1    Mikkelsen, J.D.2    Hejgaard, J.3
  • 27
    • 0027450563 scopus 로고
    • Purification and characterization of extracellular, acidic chitinase isoenzymes from elicitor-stimulated parsley cells
    • Kirsch C, Hahlbrock K, Kombrink E (1993) Purification and characterization of extracellular, acidic chitinase isoenzymes from elicitor-stimulated parsley cells. Eur J Biochem 213: 419-425
    • (1993) Eur J Biochem , vol.213 , pp. 419-425
    • Kirsch, C.1    Hahlbrock, K.2    Kombrink, E.3
  • 28
    • 0001256291 scopus 로고
    • Induction pattern of chitinases in yam callus by inoculation with autoclaved Fusarium oxysporum, ethylene, and chitin and chitosan oligosaccharides
    • Koga D, Hirata T, Sueshige N, Tanaka S, Ide A (1992) Induction pattern of chitinases in yam callus by inoculation with autoclaved Fusarium oxysporum, ethylene, and chitin and chitosan oligosaccharides. Biosci Biotechnol Biochem 56: 280-285
    • (1992) Biosci Biotechnol Biochem , vol.56 , pp. 280-285
    • Koga, D.1    Hirata, T.2    Sueshige, N.3    Tanaka, S.4    Ide, A.5
  • 29
    • 2642641822 scopus 로고    scopus 로고
    • Structural approach to function in ectomycorrhizas
    • H Rennenberg, W Eschrich, H Ziegler, eds, SPB Academic Publishing, The Hague, The Netherlands (in press)
    • Kottke I, Münzenberger B, Oberwinkler F (1997), Structural approach to function in ectomycorrhizas. In H Rennenberg, W Eschrich, H Ziegler, eds, Trees-Contributions to Modern Tree Physiology. SPB Academic Publishing, The Hague, The Netherlands (in press)
    • (1997) Trees-Contributions to Modern Tree Physiology
    • Kottke, I.1    Münzenberger, B.2    Oberwinkler, F.3
  • 30
    • 0002945277 scopus 로고
    • Induction, purification and characterization of barley leaf chitinase
    • Kragh KM, Jacobsen IS, Mikkelsen JD (1990) Induction, purification and characterization of barley leaf chitinase. Plant Sci 71: 55-68
    • (1990) Plant Sci , vol.71 , pp. 55-68
    • Kragh, K.M.1    Jacobsen, I.S.2    Mikkelsen, J.D.3
  • 31
    • 0001599349 scopus 로고
    • Chitinase isoenzymes induced in carrot cell culture by treatment with ethylene
    • Kurosaki F, Tashiro N, Gamou R, Nishi A (1989) Chitinase isoenzymes induced in carrot cell culture by treatment with ethylene. Phytochemistry 28: 2989-2992
    • (1989) Phytochemistry , vol.28 , pp. 2989-2992
    • Kurosaki, F.1    Tashiro, N.2    Gamou, R.3    Nishi, A.4
  • 32
    • 0001854246 scopus 로고
    • Role of chitinase and chitin oligosaccharides in lignification response of cultured carrot cells treated with mycelial cell walls
    • Kurosaki F, Tashiro N, Nishi A (1988) Role of chitinase and chitin oligosaccharides in lignification response of cultured carrot cells treated with mycelial cell walls. Plant Cell Physiol 29: 527-531
    • (1988) Plant Cell Physiol , vol.29 , pp. 527-531
    • Kurosaki, F.1    Tashiro, N.2    Nishi, A.3
  • 33
    • 33644535944 scopus 로고
    • Pathogenesis-related proteins of plants
    • Linthorst HJM (1991) Pathogenesis-related proteins of plants. Crit Rev Plant Sci 10: 123-150
    • (1991) Crit Rev Plant Sci , vol.10 , pp. 123-150
    • Linthorst, H.J.M.1
  • 34
    • 0001932557 scopus 로고
    • Diversity of cucumber chitinase isoforms and characterization of one seed basic chitinase with lysozyme activity
    • Majeau N, Trudel J, Asselin A (1990) Diversity of cucumber chitinase isoforms and characterization of one seed basic chitinase with lysozyme activity. Plant Sci 68: 9-16
    • (1990) Plant Sci , vol.68 , pp. 9-16
    • Majeau, N.1    Trudel, J.2    Asselin, A.3
  • 35
    • 0001324867 scopus 로고
    • Antifungal hydrolases in pea tissue. II. Inhibition of fungal growth by combinations of chitinase and β-1,3-glucanase
    • Mauch F, Mauch-Mani B, Boller T (1988) Antifungal hydrolases in pea tissue. II. Inhibition of fungal growth by combinations of chitinase and β-1,3-glucanase. Plant Physiol 88: 936-942
    • (1988) Plant Physiol , vol.88 , pp. 936-942
    • Mauch, F.1    Mauch-Mani, B.2    Boller, T.3
  • 36
    • 0001818585 scopus 로고
    • The primary structure of plant pathogenesis related glucanohydrolases and their genes
    • T Boller, F Meins Jr, eds. Springer, Vienna
    • Meins F Jr, Neuhaus JM, Sperisen C, Ryals J (1992) The primary structure of plant pathogenesis related glucanohydrolases and their genes. In T Boller, F Meins Jr, eds, Genes Involved in Plant Defense. Springer, Vienna, pp 245-282
    • (1992) Genes Involved in Plant Defense , pp. 245-282
    • Meins Jr., F.1    Neuhaus, J.M.2    Sperisen, C.3    Ryals, J.4
  • 37
    • 0017610344 scopus 로고
    • A rapid and sensitive assay for chitinase using tritiated chitin
    • Molano J, Duran A, Cabib E (1977) A rapid and sensitive assay for chitinase using tritiated chitin. Anal Biochem 83: 648-656
    • (1977) Anal Biochem , vol.83 , pp. 648-656
    • Molano, J.1    Duran, A.2    Cabib, E.3
  • 38
    • 0018786852 scopus 로고
    • An endochitinase from wheat germ. Activity on nascent and preformed chitin
    • Molano J, Polacheck I, Duran A, Cabib E (1979) An endochitinase from wheat germ. Activity on nascent and preformed chitin. J Biol Chem 254: 4901-4907
    • (1979) J Biol Chem , vol.254 , pp. 4901-4907
    • Molano, J.1    Polacheck, I.2    Duran, A.3    Cabib, E.4
  • 39
    • 0022262821 scopus 로고
    • Clear background and highly sensitive protein staining with Coomassie blue dyes in polyacrylamide gels: A systematic analysis
    • Neuhoff V, Stamm R, Eibl H (1985) Clear background and highly sensitive protein staining with Coomassie blue dyes in polyacrylamide gels: a systematic analysis. Electrophoresis 6: 427-448
    • (1985) Electrophoresis , vol.6 , pp. 427-448
    • Neuhoff, V.1    Stamm, R.2    Eibl, H.3
  • 40
    • 0016711037 scopus 로고
    • High resolution two-dimensional electrophoresis of proteins
    • O'Farrell PH (1975) High resolution two-dimensional electrophoresis of proteins. J Biol Chem 250: 4007-4021
    • (1975) J Biol Chem , vol.250 , pp. 4007-4021
    • O'Farrell, P.H.1
  • 41
    • 0029411317 scopus 로고
    • A structural model for the mechanism of elicitor release from fungal cell walls by plant β-1,3-endoglucanase
    • Okinaka Y, Mimori K, Takeo K, Kitamura S, Takeuchi Y, Yamaoka N, Yoshikawa M (1995) A structural model for the mechanism of elicitor release from fungal cell walls by plant β-1,3-endoglucanase. Plant Physiol 109: 839-845
    • (1995) Plant Physiol , vol.109 , pp. 839-845
    • Okinaka, Y.1    Mimori, K.2    Takeo, K.3    Kitamura, S.4    Takeuchi, Y.5    Yamaoka, N.6    Yoshikawa, M.7
  • 42
    • 0000859095 scopus 로고
    • A technique for simultaneous detection of chitinase, beta-1,3-glucanase and protein patterns after polyacrylamide gel electrophoresis or isoelectrofocusing
    • Pan SQ, Ye XS, Kuc JA (1991) A technique for simultaneous detection of chitinase, beta-1,3-glucanase and protein patterns after polyacrylamide gel electrophoresis or isoelectrofocusing. Phytopathology 81: 970-974
    • (1991) Phytopathology , vol.81 , pp. 970-974
    • Pan, S.Q.1    Ye, X.S.2    Kuc, J.A.3
  • 44
    • 0030065247 scopus 로고    scopus 로고
    • Study of the intercellular fluid of healthy Lupinus albus organs. Presence of a chitinase and a thaumatin-like protein
    • Regalado AP, Ricardo CPP (1996) Study of the intercellular fluid of healthy Lupinus albus organs. Presence of a chitinase and a thaumatin-like protein. Plant Physiol 110: 227-232
    • (1996) Plant Physiol , vol.110 , pp. 227-232
    • Regalado, A.P.1    Ricardo, C.P.P.2
  • 45
    • 0001488348 scopus 로고
    • Purification and characterization of multiple forms of endochitinase from wheat leaves
    • Ride JP, Barber MS (1990) Purification and characterization of multiple forms of endochitinase from wheat leaves. Plant Sci 71: 185-197
    • (1990) Plant Sci , vol.71 , pp. 185-197
    • Ride, J.P.1    Barber, M.S.2
  • 46
    • 0030063723 scopus 로고    scopus 로고
    • Rapid reactions of spruce cells to elicitors released from the ectomycorrhizal fungus Hebeloma crustulini- Forme, and inactivation of these elicitors by extracellular spruce cell enzymes
    • Salzer P, Hebe G, Reith A, Zitterell-Haid B, Stransky H, Gaschler K, Hager A (1996) Rapid reactions of spruce cells to elicitors released from the ectomycorrhizal fungus Hebeloma crustulini- forme, and inactivation of these elicitors by extracellular spruce cell enzymes. Planta 198: 118-126
    • (1996) Planta , vol.198 , pp. 118-126
    • Salzer, P.1    Hebe, G.2    Reith, A.3    Zitterell-Haid, B.4    Stransky, H.5    Gaschler, K.6    Hager, A.7
  • 47
    • 2642678136 scopus 로고    scopus 로고
    • Signaling in ectomycorrhizal fungus-root interactions
    • H Rennenberg, W Eschrich, H Zieeler, eds, SPB Publishing, The Hague, The Netherlands (in press)
    • Salzer P, Münzenberger B, Schwacke R, Kottke I, Hager A (1997), Signaling in ectomycorrhizal fungus-root interactions, In H Rennenberg, W Eschrich, H Zieeler, eds, Trees-Contributions to Modern Tree Physiology. SPB Publishing, The Hague, The Netherlands (in press)
    • (1997) Trees-Contributions to Modern Tree Physiology
    • Salzer, P.1    Münzenberger, B.2    Schwacke, R.3    Kottke, I.4    Hager, A.5
  • 48
    • 0003092821 scopus 로고
    • The mycbrrhizal fungus Amanita muscaria induces chitinase activity in roots and in suspensioncultured cells of its host Picea abies
    • Sauter M, Hager A (1989) The mycbrrhizal fungus Amanita muscaria induces chitinase activity in roots and in suspensioncultured cells of its host Picea abies. Planta 179: 61-66
    • (1989) Planta , vol.179 , pp. 61-66
    • Sauter, M.1    Hager, A.2
  • 49
    • 0001519173 scopus 로고
    • Plant chitinases are potent inhibitors of fungal growth
    • Schlumbaum A, Mauch F, Vögeli U, Boller T (1986) Plant chitinases are potent inhibitors of fungal growth. Nature 324: 365-367
    • (1986) Nature , vol.324 , pp. 365-367
    • Schlumbaum, A.1    Mauch, F.2    Vögeli, U.3    Boller, T.4
  • 50
    • 0021770876 scopus 로고
    • The primary structures of one elicitor-active and seven elicitor-inactive hexa(β-Dglucopyranosyl)-D-glucitols isolated from the mycelial walls of Phytophthora megasperma f.sp. glycinea
    • Sharp JK, McNeil M, Albersheim P (1984) The primary structures of one elicitor-active and seven elicitor-inactive hexa(β-Dglucopyranosyl)-D-glucitols isolated from the mycelial walls of Phytophthora megasperma f.sp. glycinea. J Biol Chem 259: 11321-11336
    • (1984) J Biol Chem , vol.259 , pp. 11321-11336
    • Sharp, J.K.1    McNeil, M.2    Albersheim, P.3
  • 51
    • 0023130821 scopus 로고
    • Regulation of a plant pathogenesis-related enzyme: Inhibition of chitinase and chitinase mRNA accumulation in cultured tobacco tissues by auxin and cytokinin
    • Shinshi H, Mohnen D, Meins F (1987) Regulation of a plant pathogenesis-related enzyme: inhibition of chitinase and chitinase mRNA accumulation in cultured tobacco tissues by auxin and cytokinin. Proc Natl Acad Sci USA 84: 89-93
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 89-93
    • Shinshi, H.1    Mohnen, D.2    Meins, F.3
  • 52
    • 0029141601 scopus 로고
    • Induction of mycorrhizalike structures and defence reactions in dual cultures of spruce callus and ectomycorrhizal fungi
    • Sirrenberg A, Salzer P, Hager A (1995) Induction of mycorrhizalike structures and defence reactions in dual cultures of spruce callus and ectomycorrhizal fungi. New Phytol 130: 149-156
    • (1995) New Phytol , vol.130 , pp. 149-156
    • Sirrenberg, A.1    Salzer, P.2    Hager, A.3
  • 53
    • 0004754714 scopus 로고
    • A genomic clone (GenBank U30324) from Theobroma cacao L. with high similarity to plant class I endochitinase sequences (PGR 95-056)
    • Snyder-Leiby ET, Furtek DB (1995) A genomic clone (GenBank U30324) from Theobroma cacao L. with high similarity to plant class I endochitinase sequences (PGR 95-056). Plant Physiol 109: 338
    • (1995) Plant Physiol , vol.109 , pp. 338
    • Snyder-Leiby, E.T.1    Furtek, D.B.2
  • 55
    • 0024669485 scopus 로고
    • Detection of chitinase activity after polyacrylamide gel electrophoresis
    • Trudel J, Asselin A (1989) Detection of chitinase activity after polyacrylamide gel electrophoresis. Anal Biochem 178: 362-366
    • (1989) Anal Biochem , vol.178 , pp. 362-366
    • Trudel, J.1    Asselin, A.2
  • 56
    • 0002665314 scopus 로고
    • Induction, purification and characterization of chitinase isolated from pea leaves inoculated with Ascochyta pisi
    • Vad K, Mikkelsen JD, Collinge DB (1991) Induction, purification and characterization of chitinase isolated from pea leaves inoculated with Ascochyta pisi. Planta 184: 24-29
    • (1991) Planta , vol.184 , pp. 24-29
    • Vad, K.1    Mikkelsen, J.D.2    Collinge, D.B.3
  • 57
    • 0028080552 scopus 로고
    • Protein phosphorylation is induced in tobacco cells by the elicitor cryptogein
    • Viard MP, Martin F, Pugin A, Ricci P, Blein JP (1994) Protein phosphorylation is induced in tobacco cells by the elicitor cryptogein. Plant Physiol 104: 1245-1249
    • (1994) Plant Physiol , vol.104 , pp. 1245-1249
    • Viard, M.P.1    Martin, F.2    Pugin, A.3    Ricci, P.4    Blein, J.P.5
  • 58
    • 0000137924 scopus 로고
    • Colonization of transgenic Nicotiana sylvestris plants, expressing different forms of Nicotiana tabacum chitinase, by the root pathogen Rhizoctonia solani and by the mycorrhizal symbiont Glomus mosseae
    • Vierheilig H, Alt M, Neuhaus JM, Boller T, Wiemken A (1993) Colonization of transgenic Nicotiana sylvestris plants, expressing different forms of Nicotiana tabacum chitinase, by the root pathogen Rhizoctonia solani and by the mycorrhizal symbiont Glomus mosseae. Mol Plant Microbe Interact 6: 261-264
    • (1993) Mol Plant Microbe Interact , vol.6 , pp. 261-264
    • Vierheilig, H.1    Alt, M.2    Neuhaus, J.M.3    Boller, T.4    Wiemken, A.5
  • 59
    • 0027350252 scopus 로고
    • Purification, characterization and differential hormonal regulation of a β-1,3-glucanase and two chitinases from chickpea (Cicer arietinum L.)
    • Vogelsang R, Barz W (1993) Purification, characterization and differential hormonal regulation of a β-1,3-glucanase and two chitinases from chickpea (Cicer arietinum L.). Planta 189: 60-69
    • (1993) Planta , vol.189 , pp. 60-69
    • Vogelsang, R.1    Barz, W.2
  • 60
    • 84987049301 scopus 로고
    • Transley review No 45. Wall growth, protein excretion and morphogenesis in fungi
    • Wessels JGH (1993) Transley review No 45. Wall growth, protein excretion and morphogenesis in fungi. New Phytol 123: 397-413
    • (1993) New Phytol , vol.123 , pp. 397-413
    • Wessels, J.G.H.1
  • 62
    • 0027134948 scopus 로고
    • A specific binding site on soybean membranes for a phytoalexin elicitor released from fungal cell walls by β-1,3-endoglucanase
    • Yoshikawa M, Sugimoto K (1993) A specific binding site on soybean membranes for a phytoalexin elicitor released from fungal cell walls by β-1,3-endoglucanase. Plant Cell Physiol 34: 1229-1237
    • (1993) Plant Cell Physiol , vol.34 , pp. 1229-1237
    • Yoshikawa, M.1    Sugimoto, K.2
  • 63
    • 0028011331 scopus 로고
    • Induction and characterization of chitinase isoforms in cucumber (Cucumis sativus L.): Effect of elicitors, wounding and pathogen inoculation
    • Zhang YY, Punja ZK (1994) Induction and characterization of chitinase isoforms in cucumber (Cucumis sativus L.): effect of elicitors, wounding and pathogen inoculation. Plant Sci 99: 141-150
    • (1994) Plant Sci , vol.99 , pp. 141-150
    • Zhang, Y.Y.1    Punja, Z.K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.