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Volumn , Issue , 1999, Pages 77-105

Plant chitinases (PR-3, PR-4, PR-8, PR-11)

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Indexed keywords


EID: 85056330647     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1201/9781420049299     Document Type: Chapter
Times cited : (153)

References (122)
  • 1
    • 0025402915 scopus 로고
    • Structure of a tobacco endochitinase gene: Evidence that different chitinase genes can arise by transposition of sequences encoding a cysteine-rich domain
    • Shinshi, H., Neuhaus, J.-M., Ryals, J., and Meins, F., Jr., Structure of a tobacco endochitinase gene: evidence that different chitinase genes can arise by transposition of sequences encoding a cysteine-rich domain, Plant Mol. Biol., 14, 357, 1990.
    • (1990) Plant Mol. Biol , vol.14 , pp. 357
    • Shinshi, H.1    Neuhaus, J.-M.2    Ryals, J.3    Meins, F.4
  • 3
    • 0001480645 scopus 로고
    • Biological function of pathogenesis-related proteins: Four tobacco pathogenesis-related proteins are chitinases
    • Legrand, M. and Fritig, B., Biological function of pathogenesis-related proteins: four tobacco pathogenesis-related proteins are chitinases, Proc. Natl. Acad. Sci. U.S.A., 84, 6750, 1987.
    • (1987) Proc. Natl. Acad. Sci. U.S.A , vol.84 , pp. 6750
    • Legrand, M.1    Fritig, B.2
  • 5
    • 0026055308 scopus 로고
    • A classification of glycosyl hydrolases based on amino acid sequence similarities
    • Henrissat, B., A classification of glycosyl hydrolases based on amino acid sequence similarities, Biochemical J., 280, 309, 1991.
    • (1991) Biochemical J , vol.280 , pp. 309
    • Henrissat, B.1
  • 7
    • 0029071185 scopus 로고
    • The refined crystal structure of an endochitinase from Hordeum vulgare L. seeds at 1.8 angstrom resolution
    • Hart, P. J., Pfluger, H. D., Monzingo, A. F., Hollis, T., and Robertus, J. D., The refined crystal structure of an endochitinase from Hordeum vulgare L. seeds at 1.8 angstrom resolution, J. Mol. Biol., 248, 402, 1995.
    • (1995) J. Mol. Biol , vol.248 , pp. 402
    • Hart, P.J.1    Pfluger, H.D.2    Monzingo, A.F.3    Hollis, T.4    Robertus, J.D.5
  • 8
    • 0028268204 scopus 로고
    • Structural similarity of plant chitinase and lysozymes from animals and phage - an evolutionary connection
    • Holm, L. and Sander, C., Structural similarity of plant chitinase and lysozymes from animals and phage - an evolutionary connection, FEBS Lett., 340, 129, 1994.
    • (1994) FEBS Lett , vol.340 , pp. 129
    • Holm, L.1    Sander, C.2
  • 10
    • 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. and Meins, F., Jr., 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. U.S.A., 84, 89, 1987.
    • (1987) Proc. Natl. Acad. Sci. U.S.A , vol.84 , pp. 89
    • Shinshi, H.1    Meins, F.2
  • 11
    • 0025840612 scopus 로고
    • A short C-terminal sequence is necessary and sufficient for the targeting of chitinases to the plant vacuole
    • Neuhaus, J-M., Sticher, L., Meins, F., Jr., and Boller, T., A short C-terminal sequence is necessary and sufficient for the targeting of chitinases to the plant vacuole, Proc. Natl. Acad. Sci., 88, 10362, 1991.
    • (1991) Proc. Natl. Acad. Sci , vol.88 , pp. 10362
    • Neuhaus, J.-M.1    Sticher, L.2    Meins, F.3    Boller, T.4
  • 12
    • 0026688273 scopus 로고
    • Vacuolar chitinases of tobacco: A new class of hydroxyproline-containing proteins
    • Sticher, L., Hofsteenge, J., Milani, A., Neuhaus, J. M., and Meins, F., Jr., Vacuolar chitinases of tobacco: a new class of hydroxyproline-containing proteins, Science, 257, 655, 1992.
    • (1992) Science , vol.257 , pp. 655
    • Sticher, L.1    Hofsteenge, J.2    Milani, A.3    Neuhaus, J.M.4    Meins, F.5
  • 13
    • 0028086941 scopus 로고
    • Primary structure and expression of mRNAs encoding basic chitinase and 1,3-ß-glucanase in potato
    • Beerhues, L. and Kombrink, E., Primary structure and expression of mRNAs encoding basic chitinase and 1,3-ß-glucanase in potato, Plant Mol. Biol., 24, 353, 1994.
    • (1994) Plant Mol. Biol , vol.24 , pp. 353
    • Beerhues, L.1    Kombrink, E.2
  • 14
    • 0345111189 scopus 로고
    • Identification of a 28,000 Dalton endochitinase in barley endosperm
    • Leah, R., Mikkelsen, J. D., and Svendsen, I. B., Identification of a 28,000 Dalton endochitinase in barley endosperm, Carlsberg Res. Commun., 52, 31, 1987.
    • (1987) Carlsberg Res. Commun , vol.52 , pp. 31
    • Leah, R.1    Mikkelsen, J.D.2    Svendsen, I.B.3
  • 15
    • 0023643145 scopus 로고
    • In vitro synthesis and processing of a bean pathogenesis-related (PR4) protein
    • de Tapia, M., Dietrich, A., and Burkard, G., In vitro synthesis and processing of a bean pathogenesis-related (PR4) protein, Eur. J. Biochem., 166, 559, 1987.
    • (1987) Eur. J. Biochem , vol.166 , pp. 559
    • de Tapia, M.1    Dietrich, A.2    Burkard, G.3
  • 16
    • 0026668497 scopus 로고
    • The gene for stinging nettle lectin (Urtica dioica agglutinin) encodes both a lectin and a chitinase
    • Lerner, D. R. and Raikhel, N. V., The gene for stinging nettle lectin (Urtica dioica agglutinin) encodes both a lectin and a chitinase, J. Biol. Chem., 267, 11085, 1992.
    • (1992) J. Biol. Chem , vol.267 , pp. 11085
    • Lerner, D.R.1    Raikhel, N.V.2
  • 18
    • 0030175283 scopus 로고    scopus 로고
    • Cloning of a cDNA for a chitinase homologue which lacks chitin-binding sites and is downregulated by water stress and wounding
    • Chang, S. J., Puryear, J., Funkhouser, E. A., Newton, R. J., and Calmey, J., Cloning of a cDNA for a chitinase homologue which lacks chitin-binding sites and is downregulated by water stress and wounding, Plant Mol. Biol., 31, 693, 1996.
    • (1996) Plant Mol. Biol , vol.31 , pp. 693
    • Chang, S.J.1    Puryear, J.2    Funkhouser, E.A.3    Newton, R.J.4    Calmey, J.5
  • 19
    • 0026002418 scopus 로고
    • Chitinase is required for cell separation during growth of Saccharomyces cerevisiae
    • Kuranda, M. J. and Robbins, P. W., Chitinase is required for cell separation during growth of Saccharomyces cerevisiae, J. Biol. Chem., 266, 19758, 1991.
    • (1991) J. Biol. Chem , vol.266 , pp. 19758
    • Kuranda, M.J.1    Robbins, P.W.2
  • 21
    • 0000624077 scopus 로고
    • Purification and Nterminal amino-acid sequence of a basic lysozyme from Parthenocissus quinquifolia cultured in vitro
    • Bernasconi, P., Locher, R., Pilet, P. E., Jollés, J., and Jollés, P., Purification and Nterminal amino-acid sequence of a basic lysozyme from Parthenocissus quinquifolia cultured in vitro, Biochim. Biophys. Acta, 915, 254, 1987.
    • (1987) Biochim. Biophys. Acta , vol.915 , pp. 254
    • Bernasconi, P.1    Locher, R.2    Pilet, P.E.3    Jollés, J.4    Jollés, P.5
  • 23
    • 0025739769 scopus 로고
    • The primary structure of hevamine, an enzyme with lysozyme/chitinase activity from Hevea brasiliensis latex
    • Jekel, P. A., Hartmann, J. B. H., and Beintema, J. J., The primary structure of hevamine, an enzyme with lysozyme/chitinase activity from Hevea brasiliensis latex, Eur. J. Biochem., 200, 123, 1991.
    • (1991) Eur. J. Biochem , vol.200 , pp. 123
    • Jekel, P.A.1    Hartmann, J.B.H.2    Beintema, J.J.3
  • 24
    • 0028774705 scopus 로고
    • Crystal structures of hevamine, a plant defence protein with chitinase and lysozyme activity, and its complex with an inhibitor
    • Terwisscha van Scheltinga, A. C., Kalk, K. H., Beintema, J. J., and Dijkstra, B. S., Crystal structures of hevamine, a plant defence protein with chitinase and lysozyme activity, and its complex with an inhibitor, Structure, 2, 1181, 1994.
    • (1994) Structure , vol.2 , pp. 1181
    • Terwisscha van Scheltinga, A.C.1    Kalk, K.H.2    Beintema, J.J.3    Dijkstra, B.S.4
  • 26
    • 0001695171 scopus 로고
    • Isolation and characterization of the genes encoding basic and acidic chitinase in Arabidopsis thaliana
    • Samac, D. A. and Shah, D. M., Isolation and characterization of the genes encoding basic and acidic chitinase in Arabidopsis thaliana, Plant Physiol., 93, 907, 1990.
    • (1990) Plant Physiol , vol.93 , pp. 907
    • Samac, D.A.1    Shah, D.M.2
  • 27
    • 0028845991 scopus 로고
    • Crystal structure of concanavalin B at 1.65 Å resolution, an “inactived” chitinase from seeds of Canavalia ensiformis
    • Hennig, M., Jansonius, J. N., Terwisscha van Scheltinga, A. C., Dijkstra, B. S., and Schlesier, B., Crystal structure of concanavalin B at 1.65 Å resolution, an “inactived” chitinase from seeds of Canavalia ensiformis, J. Mol. Biol., 254, 237, 1995.
    • (1995) J. Mol. Biol , vol.254 , pp. 237
    • Hennig, M.1    Jansonius, J.N.2    Terwisscha van Scheltinga, A.C.3    Dijkstra, B.S.4    Schlesier, B.5
  • 28
    • 0028113585 scopus 로고
    • Molecular characterization of a novel tobacco pathogenesis-related (PR) protein: A new plant chitinase/lysozyme
    • Heitz, T., Segond, S., Kauffmann, S., Geoffroy, P., Prasad, V., Brunner, F., Fritig, B., and Legrand, M., Molecular characterization of a novel tobacco pathogenesis-related (PR) protein: a new plant chitinase/lysozyme, Mol. Gen. Genet., 245, 246, 1994.
    • (1994) Mol. Gen. Genet , vol.245 , pp. 246
    • Heitz, T.1    Segond, S.2    Kauffmann, S.3    Geoffroy, P.4    Prasad, V.5    Brunner, F.6    Fritig, B.7    Legrand, M.8
  • 30
    • 0001590948 scopus 로고
    • cDNA cloning of six mRNAs induced by TMV infection of tobacco and a characterization of their translation products
    • Hooft van Huijsduijnen, R. A. M., Van Loon, L. C., and Bol, J. F., cDNA cloning of six mRNAs induced by TMV infection of tobacco and a characterization of their translation products, EMBO J., 5, 2057, 1986.
    • (1986) EMBO J , vol.5 , pp. 2057
    • Hooft van Huijsduijnen, R.A.M.1    Van Loon, L.C.2    Bol, J.F.3
  • 31
    • 0028033747 scopus 로고
    • A proposed structure for “Family 18" chitinases - a possible function for narbonin
    • Coulson, A. F. W., A proposed structure for “Family 18" chitinases - a possible function for narbonin, FEBS Lett., 354, 41, 1994.
    • (1994) FEBS Lett , vol.354 , pp. 41
    • Coulson, A.F.W.1
  • 32
    • 34249919394 scopus 로고
    • Hevein: An antifungal protein from rubber-tree (Hevea brasiliensis) latex
    • van Parijs, J., Broekaert, W. F., and Peumans, W. J., Hevein: an antifungal protein from rubber-tree (Hevea brasiliensis) latex, Planta, 183, 258, 1991.
    • (1991) Planta , vol.183 , pp. 258
    • van Parijs, J.1    Broekaert, W.F.2    Peumans, W.J.3
  • 33
    • 0027510717 scopus 로고
    • Hevein: NMR assignment and assessment of solution-state folding for the agglutinin-toxin domain
    • Andersen, N. H., Cao, B., Rodriguez-Romero, A., and Arreguin, B., Hevein: NMR assignment and assessment of solution-state folding for the agglutinin-toxin domain, Biochem., 32, 1407, 1993.
    • (1993) Biochem , vol.32 , pp. 1407
    • Andersen, N.H.1    Cao, B.2    Rodriguez-Romero, A.3    Arreguin, B.4
  • 34
    • 0022892736 scopus 로고
    • Structural differences in the two major wheat germ agglutinin isolectins
    • Wright, C. S. and Olafsdottir, S., Structural differences in the two major wheat germ agglutinin isolectins, J. Biol. Chem., 261, 7191, 1986.
    • (1986) J. Biol. Chem , vol.261 , pp. 7191
    • Wright, C.S.1    Olafsdottir, S.2
  • 35
    • 0024572846 scopus 로고
    • Differential expression within a family of novel wound-induced genes in potato
    • Stanford, A., Bevan, M., and Northcote, D., Differential expression within a family of novel wound-induced genes in potato, Mol. Gen. Genet., 215, 200, 1989.
    • (1989) Mol. Gen. Genet , vol.215 , pp. 200
    • Stanford, A.1    Bevan, M.2    Northcote, D.3
  • 36
    • 0028925252 scopus 로고
    • Processed products of the hevein precursor in the latex of the rubber tree (Hevea brasiliensis)
    • Soedjanaatmadja, U. M. S., Subroto, T., and Beintema, J. J., Processed products of the hevein precursor in the latex of the rubber tree (Hevea brasiliensis), FEBS Lett., 363, 211, 1995.
    • (1995) FEBS Lett , vol.363 , pp. 211
    • Soedjanaatmadja, U.M.S.1    Subroto, T.2    Beintema, J.J.3
  • 39
    • 0025933319 scopus 로고
    • Pathogenesis-related protein-4 is structurally homologous to the carboxy-terminal domains of hevein Win-1 and Win-2
    • Friedrich, L., Moyer, M., Ward, E., and Ryals, J., Pathogenesis-related protein-4 is structurally homologous to the carboxy-terminal domains of hevein, Win-1 and Win-2, Mol. Gen. Genet., 230, 113, 1991.
    • (1991) Mol. Gen. Genet , vol.230 , pp. 113
    • Friedrich, L.1    Moyer, M.2    Ward, E.3    Ryals, J.4
  • 40
    • 0026666191 scopus 로고
    • Three-dimensional structure in solution of barwin, a protein from barley seed
    • Ludvigsen, S. and Poulsen, F. M., Three-dimensional structure in solution of barwin, a protein from barley seed, Biochemistry, 31, 8783, 1992.
    • (1992) Biochemistry , vol.31 , pp. 8783
    • Ludvigsen, S.1    Poulsen, F.M.2
  • 41
    • 0017610344 scopus 로고
    • A rapid and sensitive assay for chitinase using tritiated chitin
    • Molano, J., Duran, A., and Cabib, E., A rapid and sensitive assay for chitinase using tritiated chitin, Anal. Biochem., 83, 648, 1977.
    • (1977) Anal. Biochem , vol.83 , pp. 648
    • Molano, J.1    Duran, A.2    Cabib, E.3
  • 42
    • 0025604145 scopus 로고
    • Dye-labelled substrates for the assay and detection of chitinase and lysozyme activity
    • Wirth, S. J. and Wolf, G. A., Dye-labelled substrates for the assay and detection of chitinase and lysozyme activity, J. Microbiol. Meth., 12, 197, 1990.
    • (1990) J. Microbiol. Meth , vol.12 , pp. 197
    • Wirth, S.J.1    Wolf, G.A.2
  • 43
    • 0014475358 scopus 로고
    • The stereospecificity of human, hen, and papaya lysozymes
    • Dahlquist, F. W., Borders, C. L., Jacobson, G., and Raftery, M. A., The stereospecificity of human, hen, and papaya lysozymes, Biochem., 8, 694, 1969.
    • (1969) Biochem , vol.8 , pp. 694
    • Dahlquist, F.W.1    Borders, C.L.2    Jacobson, G.3    Raftery, M.A.4
  • 44
    • 0024669485 scopus 로고
    • Detection of chitinase activity after polyacrylamide gel electrophoresis
    • Trudel, J. and Asselin, A., Detection of chitinase activity after polyacrylamide gel electrophoresis, Anal. Biochem., 178, 362, 1989.
    • (1989) Anal. Biochem , vol.178 , pp. 362
    • Trudel, J.1    Asselin, A.2
  • 46
    • 0031567587 scopus 로고    scopus 로고
    • Hevamine, a chitinase from the rubber tree Hevea brasiliensis, cleaves peptidoglycan between the C-1 of N-acetylglucosamine and C-4 of N-acetylmuramic acid and therefore is not a lysozyme
    • Bokma, E., Van Koningsveld, G. A., Jeronimus-Stratingh, M., and Beintema, J. J., Hevamine, a chitinase from the rubber tree Hevea brasiliensis, cleaves peptidoglycan between the C-1 of N-acetylglucosamine and C-4 of N-acetylmuramic acid and therefore is not a lysozyme, FEBS Lett., 411, 161, 1997.
    • (1997) FEBS Lett , vol.411 , pp. 161
    • Bokma, E.1    Van Koningsveld, G.A.2    Jeronimus-Stratingh, M.3    Beintema, J.J.4
  • 47
  • 48
    • 0001616015 scopus 로고
    • Comparative biochemistry of chitinases - anomeric form of the reaction products
    • Fukamizo, T., Koga, D., and Goto, S., Comparative biochemistry of chitinases - anomeric form of the reaction products, Biosci. Biotechnol. Biochem., 59, 311, 1995.
    • (1995) Biosci. Biotechnol. Biochem , vol.59 , pp. 311
    • Fukamizo, T.1    Koga, D.2    Goto, S.3
  • 49
    • 0030904072 scopus 로고    scopus 로고
    • Heterologous expression and characterization of wild-type and mutant forms of a 26 kda endochitinase from barley (Hordeum vulgare L)
    • Andersen, M. D., Jensen, A., Robertus, J. D., Leah, R., and Skriver, J. K., Heterologous expression and characterization of wild-type and mutant forms of a 26 kda endochitinase from barley (Hordeum vulgare L), Biochemical J., 322 (Part 3) 815, 1997.
    • (1997) Biochemical J , vol.322 , pp. 815
    • Andersen, M.D.1    Jensen, A.2    Robertus, J.D.3    Leah, R.4    Skriver, J.K.5
  • 50
    • 0032507714 scopus 로고    scopus 로고
    • Mutation of either of two essential glutamates converts the catalytic domain of tobacco class I chitinase into a chitinbinding domain
    • Iseli-Gamboni, B., Boller, T., and Neuhaus, J-M., Mutation of either of two essential glutamates converts the catalytic domain of tobacco class I chitinase into a chitinbinding domain, Plant Sci., 134, 45, 1998.
    • (1998) Plant Sci , vol.134 , pp. 45
    • Iseli-Gamboni, B.1    Boller, T.2    Neuhaus, J.-M.3
  • 51
    • 0026672242 scopus 로고
    • Identification of an essential tyrosine residue in the catalytic site of a chitinase isolated from Zea mays that is selectively modified during inactivation with 1-ethyl-3-(3-dimethylaminopropyl)-carbodiimide
    • Verburg, J. G., Smith, C. E., Lisek, C. A., and Huynh, Q. K., Identification of an essential tyrosine residue in the catalytic site of a chitinase isolated from Zea mays that is selectively modified during inactivation with 1-ethyl-3-(3-dimethylaminopropyl)-carbodiimide, J. Biol. Chem., 267, 3886, 1992.
    • (1992) J. Biol. Chem , vol.267 , pp. 3886
    • Verburg, J.G.1    Smith, C.E.2    Lisek, C.A.3    Huynh, Q.K.4
  • 52
    • 0028815139 scopus 로고
    • Identification of the tryptophan residue located at the substrate-binding site of rye seed chitinase-C
    • Yamagami, T. and Funatsu, G., Identification of the tryptophan residue located at the substrate-binding site of rye seed chitinase-C, Biosci. Biotech. Biochem., 59, 1076, 1995.
    • (1995) Biosci. Biotech. Biochem , vol.59 , pp. 1076
    • Yamagami, T.1    Funatsu, G.2
  • 54
    • 0027666351 scopus 로고
    • The N-terminal cysteine-rich domain of tobacco class I chitinase is essential for chitin binding but not for catalytic or antifungal activity
    • Iseli, B., Boller, T., and Neuhaus, J-M., The N-terminal cysteine-rich domain of tobacco class I chitinase is essential for chitin binding but not for catalytic or antifungal activity, Plant Physiol., 103, 221, 1993.
    • (1993) Plant Physiol , vol.103 , pp. 221
    • Iseli, B.1    Boller, T.2    Neuhaus, J.-M.3
  • 55
    • 0028426944 scopus 로고
    • A hydroxyprolinecontaining class IV chitinase of sugar beet is glycosylated with xylose
    • Nielsen, K. K., Bojsen, K., Roepstorff, P., and Mikkelsen, J. D., A hydroxyprolinecontaining class IV chitinase of sugar beet is glycosylated with xylose, Plant Mol. Biol., 25, 241, 1994.
    • (1994) Plant Mol. Biol , vol.25 , pp. 241
    • Nielsen, K.K.1    Bojsen, K.2    Roepstorff, P.3    Mikkelsen, J.D.4
  • 57
    • 0030220995 scopus 로고    scopus 로고
    • Proteolytic processing of class IV chitinase in the compatible interaction of bean roots with Fusarium solani
    • Lange, J., Mohr, U., Wiemken, A., Boller, T., and Vögeli-Lange, R., Proteolytic processing of class IV chitinase in the compatible interaction of bean roots with Fusarium solani, Plant Physiol., 111, 1135, 1996.
    • (1996) Plant Physiol , vol.111 , pp. 1135
    • Lange, J.1    Mohr, U.2    Wiemken, A.3    Boller, T.4    Vögeli-Lange, R.5
  • 58
    • 0001008022 scopus 로고
    • Functional implications of the subcellular localization of ethylene-induced chitinase and ß-1,3-glucanase in bean leaves
    • Mauch, F. and Staehelin, L. A., Functional implications of the subcellular localization of ethylene-induced chitinase and ß-1,3-glucanase in bean leaves, Plant Cell, 1, 447, 1989.
    • (1989) Plant Cell , vol.1 , pp. 447
    • Mauch, F.1    Staehelin, L.A.2
  • 59
    • 0028002143 scopus 로고
    • Mutation analysis of the C-terminal vacuolar targeting peptide of tobacco chitinase: Low specificity of the sorting system, and gradual transition between intracellular retention and secretion into the extracellular space
    • Neuhaus, J.-M., Pietrzak, M., and Boller, T., Mutation analysis of the C-terminal vacuolar targeting peptide of tobacco chitinase: low specificity of the sorting system, and gradual transition between intracellular retention and secretion into the extracellular space, Plant J., 5, 45, 1994.
    • (1994) Plant J , vol.5 , pp. 45
    • Neuhaus, J.-M.1    Pietrzak, M.2    Boller, T.3
  • 60
    • 0001324013 scopus 로고
    • Local and systemic induction of chitinase in cucumber plants in response to viral, bacterial and fungal infections
    • Métraux, J. P. and Boller, T., Local and systemic induction of chitinase in cucumber plants in response to viral, bacterial and fungal infections, Physiol. Molec. Plant Pathol., 28, 161, 1986.
    • (1986) Physiol. Molec. Plant Pathol , vol.28 , pp. 161
    • Métraux, J.P.1    Boller, T.2
  • 61
    • 38249025994 scopus 로고
    • Biological function of bean pathogenesisrelated (PR3 and PR4) proteins
    • Awade, A., de Tapia, M., and Burkard, B., Biological function of bean pathogenesisrelated (PR3 and PR4) proteins, Plant Sci., 63, 121, 1989.
    • (1989) Plant Sci , vol.63 , pp. 121
    • Awade, A.1    de Tapia, M.2    Burkard, B.3
  • 62
    • 0001413068 scopus 로고
    • Developmental and pathogen-induced activation of the Arabidopsis acidic chitinase promoter
    • Samac, D. A. and Shah, D. M., Developmental and pathogen-induced activation of the Arabidopsis acidic chitinase promoter, Plant Cell, 3, 1063, 1991.
    • (1991) Plant Cell , vol.3 , pp. 1063
    • Samac, D.A.1    Shah, D.M.2
  • 63
    • 0003088848 scopus 로고
    • The latex of Hevea brasiliensis contains high levels of both chitinases and chitinases/lysozymes
    • Martin, M. N, The latex of Hevea brasiliensis contains high levels of both chitinases and chitinases/lysozymes, Plant Physiol., 95, 469, 1991.
    • (1991) Plant Physiol , vol.95 , pp. 469
    • Martin, M.N.1
  • 64
    • 0026901010 scopus 로고
    • Acidic and basic class III chitinase mRNA accumulation in response to TMV infection of tobacco
    • Lawton, K., Ward, E., Payne, G., Moyer, M., and Ryals, J., Acidic and basic class III chitinase mRNA accumulation in response to TMV infection of tobacco, Plant Mol Biol., 19, 735 1992.
    • (1992) Plant Mol Biol , vol.19 , pp. 735
    • Lawton, K.1    Ward, E.2    Payne, G.3    Moyer, M.4    Ryals, J.5
  • 65
    • 0027631006 scopus 로고
    • An acidic class-III chitinase in sugar beet - induction by Cercospora beticola, characterization, and expression in transgenic tobacco plants
    • Nielsen, K. K., Mikkelsen, J. D., Kragh, K. M., and Bojsen, K., An acidic class-III chitinase in sugar beet - induction by Cercospora beticola, characterization, and expression in transgenic tobacco plants, Mol. Plant-Microbe Interact., 6, 495, 1993.
    • (1993) Mol. Plant-Microbe Interact , vol.6 , pp. 495
    • Nielsen, K.K.1    Mikkelsen, J.D.2    Kragh, K.M.3    Bojsen, K.4
  • 66
    • 0027347474 scopus 로고
    • Cloning of a complementary DNA that encodes an acidic chitinase which is induced by ethylene and expression of the corresponding gene
    • Ishige, F., Mori, H., Yamazaki, K., and Imaseki, H., Cloning of a complementary DNA that encodes an acidic chitinase which is induced by ethylene and expression of the corresponding gene, Plant Cell Physiol., 34, 103, 1993.
    • (1993) Plant Cell Physiol , vol.34 , pp. 103
    • Ishige, F.1    Mori, H.2    Yamazaki, K.3    Imaseki, H.4
  • 67
    • 0027136629 scopus 로고
    • Tissue specificity and induction of class I, II and III chitinases in barley (Hordeum vulgare)
    • Kragh, K. M., Jacobsen, S., Mikkelsen, J. D., and Nielsen, K. A., Tissue specificity and induction of class I, II and III chitinases in barley (Hordeum vulgare), Physiol. Plant., 89, 490, 1993.
    • (1993) Physiol. Plant , vol.89 , pp. 490
    • Kragh, K.M.1    Jacobsen, S.2    Mikkelsen, J.D.3    Nielsen, K.A.4
  • 68
    • 0028384733 scopus 로고
    • Genes encoding acidic and basic class III ß-1,3-glucanases are expressed in tomato plants upon viroid infection
    • Domingo, C., Conejero, V., and Vera P., Genes encoding acidic and basic class III ß-1,3-glucanases are expressed in tomato plants upon viroid infection, Plant Mol. Biol., 24, 725, 1994.
    • (1994) Plant Mol. Biol , vol.24 , pp. 725
    • Domingo, C.1    Conejero, V.2    Vera, P.3
  • 70
    • 0028311863 scopus 로고
    • Characterization of a wheat class Ib chitinase gene differentially induced in isogenic lines by infection with Puccinia graminis
    • Liao, Y. C., Kreuzaler, F., Fischer, R., Reisener, H. J., and Tiburzy, R., Characterization of a wheat class Ib chitinase gene differentially induced in isogenic lines by infection with Puccinia graminis, Plant Sci., 103, 177, 1994.
    • (1994) Plant Sci , vol.103 , pp. 177
    • Liao, Y.C.1    Kreuzaler, F.2    Fischer, R.3    Reisener, H.J.4    Tiburzy, R.5
  • 71
    • 0031005186 scopus 로고    scopus 로고
    • Expression of ß-1,3-glucanase and chitinase in healthy, stem rust-affected and elicitortreated near-isogenic wheat lines showing Sr5 or Sr24-specified race-specific rust resistance
    • Münch-Garthoff, S., Neuhaus, J. -M., Boller, T., Kemmerling, B., and Kogel, K. H., Expression of ß-1,3-glucanase and chitinase in healthy, stem rust-affected and elicitortreated near-isogenic wheat lines showing Sr5 or Sr24-specified race-specific rust resistance, Planta, 201, 235, 1997.
    • (1997) Planta , vol.201 , pp. 235
    • Münch-Garthoff, S.1    Neuhaus, J.-M.2    Boller, T.3    Kemmerling, B.4    Kogel, K.H.5
  • 72
    • 0024978414 scopus 로고
    • Sequence analysis of a genomic clone encoding an endochitinase from Solanum tuberosum
    • Gaynorl, J. J. and Unkenholz, K. M., Sequence analysis of a genomic clone encoding an endochitinase from Solanum tuberosum, Nucl. Acid Res., 17, 5855, 1989.
    • (1989) Nucl. Acid Res , vol.17 , pp. 5855
    • Gaynorl, J.J.1    Unkenholz, K.M.2
  • 73
    • 0026507396 scopus 로고
    • The structure and regulation of homeologous tobacco endochitinase genes of Nicotiana sylvestris and N. tomentosiformis origin
    • van Buuren, M., Neuhaus J.-M., Shinshi, H., Ryals, J., and Meins, F., The structure and regulation of homeologous tobacco endochitinase genes of Nicotiana sylvestris and N. tomentosiformis origin, Mol. Gen. Genet., 232, 460, 1992.
    • (1992) Mol. Gen. Genet , vol.232 , pp. 460
    • van Buuren, M.1    Neuhaus, J.-M.2    Shinshi, H.3    Ryals, J.4    Meins, F.5
  • 74
    • 38249030841 scopus 로고
    • Induction of the defense-related glucanohydrolases, ß-1,3-glucanase and chitinase by tobacco mosaic virus infection of tobacco leaves
    • Vögeli-Lange, R., Hansen-Gehri, A., Boller, T., and Meins, F. J., Induction of the defense-related glucanohydrolases, ß-1,3-glucanase and chitinase by tobacco mosaic virus infection of tobacco leaves, Plant Sci., 54, 171, 1988.
    • (1988) Plant Sci , vol.54 , pp. 171
    • Vögeli-Lange, R.1    Hansen-Gehri, A.2    Boller, T.3    Meins, F.J.4
  • 75
    • 0002225242 scopus 로고
    • The effect of ethylene on the cell-type-specific and intracellular localization of ß-1,3-glucanase and chitinase in tobacco leaves
    • Keefe, D., Hinz, U., and Meins, F., Jr., The effect of ethylene on the cell-type-specific and intracellular localization of ß-1,3-glucanase and chitinase in tobacco leaves, Planta, 182, 43, 1990.
    • (1990) Planta , vol.182 , pp. 43
    • Keefe, D.1    Hinz, U.2    Meins, F.3
  • 76
    • 0038931437 scopus 로고
    • Virus-induced synthesis of mRNAs for precursors of pathogenesis-related proteins in tobacco
    • Hooft van Huijsduijnen, R. A. M., Cornelissen, B. J. C., and Bol, J. F., Virus-induced synthesis of mRNAs for precursors of pathogenesis-related proteins in tobacco, EMBO J., 4, 2167, 1985.
    • (1985) EMBO J , vol.4 , pp. 2167
    • Hooft van Huijsduijnen, R.A.M.1    Cornelissen, B.J.C.2    Bol, J.F.3
  • 77
    • 45249128738 scopus 로고
    • Localization of pathogenesis-related proteins in infected and non-infected leaves of Samsun NN tobacco during the hypersensitive reaction to tobacco mosaic virus
    • van Loon, L. C. and Gerritsen, Y. A. M., Localization of pathogenesis-related proteins in infected and non-infected leaves of Samsun NN tobacco during the hypersensitive reaction to tobacco mosaic virus, Plant Sci., 63, 131, 1989.
    • (1989) Plant Sci , vol.63 , pp. 131
    • van Loon, L.C.1    Gerritsen, Y.A.M.2
  • 78
    • 0024720664 scopus 로고
    • Pathogenesis-related proteins are developmentally regulated in tobacco flowers
    • Lotan, T., Ori, N., and Fluhr, R., Pathogenesis-related proteins are developmentally regulated in tobacco flowers, Plant Cell, 1, 881, 1989.
    • (1989) Plant Cell , vol.1 , pp. 881
    • Lotan, T.1    Ori, N.2    Fluhr, R.3
  • 80
    • 0028151832 scopus 로고
    • The most abundant soluble basic protein of the stylar transmitting tract in potato (Solanum tuberosum L.) is an endochitinase
    • Wemmer, T., Kaufmann, H., Kirch, H. H., Schneider, K., Lottspeich, F., and Thompson, R. D., The most abundant soluble basic protein of the stylar transmitting tract in potato (Solanum tuberosum L.) is an endochitinase, Planta, 194, 264, 1994.
    • (1994) Planta , vol.194 , pp. 264
    • Wemmer, T.1    Kaufmann, H.2    Kirch, H.H.3    Schneider, K.4    Lottspeich, F.5    Thompson, R.D.6
  • 81
    • 0012000983 scopus 로고
    • Endochitinases from Castanea crenata cotyledons
    • Collada, C., Casado, R., and Aragoncillo, C., Endochitinases from Castanea crenata cotyledons, J. Agr. Food Chem., 41, 1716, 1993.
    • (1993) J. Agr. Food Chem , vol.41 , pp. 1716
    • Collada, C.1    Casado, R.2    Aragoncillo, C.3
  • 82
    • 0026640655 scopus 로고
    • Antifungal proteins from plants - purification, molecular cloning, and antifungal properties of chitinases from maize seed
    • Huynh, Q. K., Hironaka, C. M,. Levine, E. B., Smith, C. E., Borgmeyer, J. R., and Shah, D. M., Antifungal proteins from plants - purification, molecular cloning, and antifungal properties of chitinases from maize seed, J. Biol. Chem., 267, 6635, 1992.
    • (1992) J. Biol. Chem , vol.267 , pp. 6635
    • Huynh, Q.K.1    Hironaka, C.M.2    Smith, C.E.3    Borgmeyer, J.R.4    Shah, D.M.5
  • 83
    • 44049124019 scopus 로고
    • Chitinases from seeds of Zea mays and Coix lachryma-jobi L. Purification and some properties
    • Lin, Z. F., Wu, D. Q., Luo, A. N., and Zhang, W. Q., Chitinases from seeds of Zea mays and Coix lachryma-jobi L. Purification and some properties, Process Biochem., 27, 83, 1992.
    • (1992) Process Biochem , vol.27 , pp. 83
    • Lin, Z.F.1    Wu, D.Q.2    Luo, A.N.3    Zhang, W.Q.4
  • 84
    • 0024785461 scopus 로고
    • Purification and characterization of an insect alpha-amylase inhibitor/endochitinase from seeds of Job’s Tears (Coix lachryma jobi)
    • Ary, M. B., Richardson, M., and Shewry, P. R., Purification and characterization of an insect alpha-amylase inhibitor/endochitinase from seeds of Job’s Tears (Coix lachryma jobi), Biochim. Biophys. Acta, 999, 260, 1989.
    • (1989) Biochim. Biophys. Acta , vol.999 , pp. 260
    • Ary, M.B.1    Richardson, M.2    Shewry, P.R.3
  • 85
    • 0001610671 scopus 로고
    • Properties of barley seed chitinases and release of embryo-associated isoforms during early stages of imbibition
    • Swegle, M., Kramer, K. J., and Muthukrishnan, S., Properties of barley seed chitinases and release of embryo-associated isoforms during early stages of imbibition, Plant Physiol., 99, 1009, 1992.
    • (1992) Plant Physiol , vol.99 , pp. 1009
    • Swegle, M.1    Kramer, K.J.2    Muthukrishnan, S.3
  • 86
    • 0027585164 scopus 로고
    • Purification and some properties of 3 chitinases from the seeds of rye (Secale cereale)
    • Yamagami, T. and Funatsu, G., Purification and some properties of 3 chitinases from the seeds of rye (Secale cereale), Biosci. Biotechnol. Biochem., 57, 643, 1993.
    • (1993) Biosci. Biotechnol. Biochem , vol.57 , pp. 643
    • Yamagami, T.1    Funatsu, G.2
  • 87
    • 0000177220 scopus 로고
    • Chitinase cDNA cloning and mRNA induction by fungal elicitor, wounding and infection
    • Hedrick, S. A., Boller, T., and Lamb, C.J., Chitinase cDNA cloning and mRNA induction by fungal elicitor, wounding and infection, Plant Physiol., 86, 182, 1988.
    • (1988) Plant Physiol , vol.86 , pp. 182
    • Hedrick, S.A.1    Boller, T.2    Lamb, C.J.3
  • 88
    • 0027134140 scopus 로고
    • Marked induction of basic chitinase in pumpkin in response to wounding
    • Esaka, M., Toyota, A., and Kitabayashi, M., Marked induction of basic chitinase in pumpkin in response to wounding, Phytochemistry, 34, 631, 1993.
    • (1993) Phytochemistry , vol.34 , pp. 631
    • Esaka, M.1    Toyota, A.2    Kitabayashi, M.3
  • 89
    • 0029133975 scopus 로고
    • Characterization of a class I chitinase gene and of wound-inducible, root and flower-specific chitinase expression in Brassica napus
    • Hamel, F. and Bellemare, G., Characterization of a class I chitinase gene and of wound-inducible, root and flower-specific chitinase expression in Brassica napus, Biochimica et Biophysica Acta, 1263, 212, 1995.
    • (1995) Biochimica et Biophysica Acta , vol.1263 , pp. 212
    • Hamel, F.1    Bellemare, G.2
  • 90
    • 0024743258 scopus 로고
    • Systemic accumulation of specific mRNAs in response to wounding in poplar
    • Parsons, T. J. and Gordon, M. P., Systemic accumulation of specific mRNAs in response to wounding in poplar, Proc. Natl. Acad. Sci. U.S.A., 86, 7895, 1989.
    • (1989) Proc. Natl. Acad. Sci. U.S.A , vol.86 , pp. 7895
    • Parsons, T.J.1    Gordon, M.P.2
  • 91
    • 0001197492 scopus 로고
    • Stress induction and developmental regulation of a rice chitinase promoter in transgenic tobacco
    • Zhu, Q., Doerner, P. W., and Lamb, C. J., Stress induction and developmental regulation of a rice chitinase promoter in transgenic tobacco, Plant J., 3, 203, 1993.
    • (1993) Plant J , vol.3 , pp. 203
    • Zhu, Q.1    Doerner, P.W.2    Lamb, C.J.3
  • 92
    • 0029257358 scopus 로고
    • Identification of an ethylene-responsive region in the promoter of a tobacco class I chitinase gene
    • Shinshi, H., Usami, S., and Ohme-Takagi, M., Identification of an ethylene-responsive region in the promoter of a tobacco class I chitinase gene, Plant Mol. Biol., 27, 923, 1995.
    • (1995) Plant Mol. Biol , vol.27 , pp. 923
    • Shinshi, H.1    Usami, S.2    Ohme-Takagi, M.3
  • 93
    • 0030087774 scopus 로고    scopus 로고
    • Regulation, expression and function of a new basic chitinase gene in rice (Oryza sativa L)
    • Xu, Y., Zhu, Q., Panbangred, W., Shirasu, K., and Lamb, C., Regulation, expression and function of a new basic chitinase gene in rice (Oryza sativa L), Plant Mol. Biol., 30, 387, 1996.
    • (1996) Plant Mol. Biol , vol.30 , pp. 387
    • Xu, Y.1    Zhu, Q.2    Panbangred, W.3    Shirasu, K.4    Lamb, C.5
  • 94
    • 0028369211 scopus 로고
    • Characterization of a novel cis-acting element that is responsive to a fungal elicitor in the promoter of a tobacco class I chitinase gene
    • Fukuda, Y. and Shinshi, H., Characterization of a novel cis-acting element that is responsive to a fungal elicitor in the promoter of a tobacco class I chitinase gene, Plant Mol. Biol., 24, 485, 1994.
    • (1994) Plant Mol. Biol , vol.24 , pp. 485
    • Fukuda, Y.1    Shinshi, H.2
  • 95
    • 0031149259 scopus 로고    scopus 로고
    • Interaction of tobacco nuclear protein with an elicitor-responsive element in the promotor of a basic class I chitinase gene
    • Fukuda, Y., Interaction of tobacco nuclear protein with an elicitor-responsive element in the promotor of a basic class I chitinase gene, Plant Mol. Biol., 34, 81, 1997.
    • (1997) Plant Mol. Biol , vol.34 , pp. 81
    • Fukuda, Y.1
  • 96
    • 0025037649 scopus 로고
    • Spatial and temporal patterns of transcription of a wound-induced gene in potato
    • Stanford, A. C., Northcote, D. H., and Bevan, M. W., Spatial and temporal patterns of transcription of a wound-induced gene in potato, EMBO J., 9, 593, 1990.
    • (1990) EMBO J , vol.9 , pp. 593
    • Stanford, A.C.1    Northcote, D.H.2    Bevan, M.W.3
  • 97
    • 0001519173 scopus 로고
    • Plant chitinases are potent inhibitors of fungal growth
    • Schlumbaum, A., Mauch, F., Vögeli, U., and Boller, T., Plant chitinases are potent inhibitors of fungal growth, Nature, 324, 365, 1986.
    • (1986) Nature , vol.324 , pp. 365
    • Schlumbaum, A.1    Mauch, F.2    Vögeli, U.3    Boller, T.4
  • 98
    • 0002215662 scopus 로고
    • Inhibition of fungal growth by plant chitinases and ß-1,3-glucanases - a morphological study
    • Arlorio, M., Ludwig, A., Boller, T., and Bonfante, P., Inhibition of fungal growth by plant chitinases and ß-1,3-glucanases - a morphological study, Protoplasma, 171, 34, 1992.
    • (1992) Protoplasma , vol.171 , pp. 34
    • Arlorio, M.1    Ludwig, A.2    Boller, T.3    Bonfante, P.4
  • 99
    • 0001324867 scopus 로고
    • Antifungal hydrolases in pea tissue. 2. Inhibition of fungal growth by combinations of chitinase and ß-1,3-glucanase
    • Mauch, F., Mauch-Mani, B., and Boller, T., Antifungal hydrolases in pea tissue. 2. Inhibition of fungal growth by combinations of chitinase and ß-1,3-glucanase, Plant Physiol., 88, 936, 1988.
    • (1988) Plant Physiol , vol.88 , pp. 936
    • Mauch, F.1    Mauch-Mani, B.2    Boller, T.3
  • 102
    • 0000431179 scopus 로고
    • A chitinbinding lectin from stinging nettle rhizomes with antifungal properties
    • Broekaert, W. F., van Parijs, J., Leyns F., Joos, H., and Peumans, W. J., A chitinbinding lectin from stinging nettle rhizomes with antifungal properties, Science, 245, 1100, 1989.
    • (1989) Science , vol.245 , pp. 1100
    • Broekaert, W.F.1    van Parijs, J.2    Leyns, F.3    Joos, H.4    Peumans, W.J.5
  • 103
    • 0030220499 scopus 로고    scopus 로고
    • Antimicrobial peptides from Mirabilis jalapa and Amaranthus caudatus - expression, processing, localization and biological activity in transgenic tobacco
    • de Bolle, M. F. C., Osborn, R. W., Goderis, I. J., Noe, L., Acland, D., Hart, C. A., Torrekens, S., van Leuven, F., and Broekaert, W. F., Antimicrobial peptides from Mirabilis jalapa and Amaranthus caudatus - expression, processing, localization and biological activity in transgenic tobacco, Plant Mol. Biol., 31, 993, 1996.
    • (1996) Plant Mol. Biol , vol.31 , pp. 993
    • de Bolle, M.F.C.1    Osborn, R.W.2    Goderis, I.J.3    Noe, L.4    Acland, D.5    Hart, C.A.6    Torrekens, S.7    van Leuven, F.8    Broekaert, W.F.9
  • 104
    • 0025718126 scopus 로고
    • Lectins, lectin genes, and their role in plant defense
    • Chrispeels, M. J. and Raikhel, N. V., Lectins, lectin genes, and their role in plant defense, Plant Cell, 3, 1, 1991.
    • (1991) Plant Cell , vol.3 , pp. 1
    • Chrispeels, M.J.1    Raikhel, N.V.2
  • 105
    • 0025935356 scopus 로고
    • High-level expression of a tobacco chitinase gene in Nicotiana sylvestris - susceptibility of transgenic plants to Cercospora nicotianae infection
    • Neuhaus, J.-M., Ahl-Goy, P., Hinz, U., Flores, S., and Meins, F., Jr., High-level expression of a tobacco chitinase gene in Nicotiana sylvestris - susceptibility of transgenic plants to Cercospora nicotianae infection, Plant Mol. Biol., 16, 141, 1991.
    • (1991) Plant Mol. Biol , vol.16 , pp. 141
    • Neuhaus, J.-M.1    Ahl-Goy, P.2    Hinz, U.3    Flores, S.4    Meins, F.5
  • 107
    • 0027215763 scopus 로고
    • Antifungal effect of bean endochitinase on Rhizoctonia solani - ultrastructural changes and cytochemical aspects of chitin breakdown
    • Benhamou, N., Broglie, K., Broglie, R., and Chet, I., Antifungal effect of bean endochitinase on Rhizoctonia solani - ultrastructural changes and cytochemical aspects of chitin breakdown, Can. J. Microbiol., 39, 318, 1993.
    • (1993) Can. J. Microbiol , vol.39 , pp. 318
    • Benhamou, N.1    Broglie, K.2    Broglie, R.3    Chet, I.4
  • 108
    • 0000137924 scopus 로고
    • Effect of chitinase overexpression on the colonization of roots by pathogenic and symbiotic fungi
    • Vierheilig, H., Alt, M., Neuhaus, J.-M., Boller, T., and Wiemken, A., Effect of chitinase overexpression on the colonization of roots by pathogenic and symbiotic fungi, Mol. Plant-Microbe Interact., 6, 261, 1993.
    • (1993) Mol. Plant-Microbe Interact , vol.6 , pp. 261
    • Vierheilig, H.1    Alt, M.2    Neuhaus, J.-M.3    Boller, T.4    Wiemken, A.5
  • 110
    • 0027519716 scopus 로고
    • Lipo-oligosaccharide nodulation factors: A new class of signaling molecules mediating recognition and morphogenesis
    • Dénarié, J. and Cullimore, J., Lipo-oligosaccharide nodulation factors: a new class of signaling molecules mediating recognition and morphogenesis, Cell, 74, 951, 1993.
    • (1993) Cell , vol.74 , pp. 951
    • Dénarié, J.1    Cullimore, J.2
  • 112
    • 0013408182 scopus 로고    scopus 로고
    • Molecular cloning of Vigna cDNAs encoding class I (Accession No. X88800) and class IV (Accession No. X88803)
    • Lan, V. T. T., Neuhaus, J.-M., Boller, T., Broughton, W. J., and Krause, A., Molecular cloning of Vigna cDNAs encoding class I (Accession No. X88800) and class IV (Accession No. X88803), Plant Physiol., 110, 335, 1996.
    • (1996) Plant Physiol , vol.110 , pp. 335
    • Lan, V.T.T.1    Neuhaus, J.-M.2    Boller, T.3    Broughton, W.J.4    Krause, A.5
  • 113
    • 0013479219 scopus 로고
    • The sulfate group on the reducing end protects Nod signals of R. meliloti against hydrolysis by Medicago chitinases
    • Palacios, R., Mora, J., and Newton, W. E., Eds., Kluwer, Dordrecht, the Netherlands
    • Schultze, M., Kondorosi, E., Kondorosi, A., Staehelin, C., Mellor, R. B., and Boller, T., The sulfate group on the reducing end protects Nod signals of R. meliloti against hydrolysis by Medicago chitinases, in New Horizons in Nitrogen Fixation, Palacios, R., Mora, J., and Newton, W. E., Eds., Kluwer, Dordrecht, the Netherlands: 1993, 159.
    • (1993) New Horizons in Nitrogen Fixation , pp. 159
    • Schultze, M.1    Kondorosi, E.2    Kondorosi, A.3    Staehelin, C.4    Mellor, R.B.5    Boller, T.6
  • 114
    • 0028001965 scopus 로고
    • Structural modifications in Rhizobium meliloti Nod factors influence their stability against hydrolysis by root chitinases
    • Staehelin, C., Schultze, M., Kondorosi, E., Mellor, R. B., Boller, T., and Kondorosi, A., Structural modifications in Rhizobium meliloti Nod factors influence their stability against hydrolysis by root chitinases, Plant J., 5, 319, 1994.
    • (1994) Plant J , vol.5 , pp. 319
    • Staehelin, C.1    Schultze, M.2    Kondorosi, E.3    Mellor, R.B.4    Boller, T.5    Kondorosi, A.6
  • 115
    • 0009589760 scopus 로고    scopus 로고
    • Characterization of CHRK1, a receptor-like kinase containing a chitinase-related domain in its N-terminus
    • Singapore
    • Kim, Y. S., Yoon, K., Liu, J. R., and Lee, H. S., Characterization of CHRK1, a receptor-like kinase containing a chitinase-related domain in its N-terminus, 5th International Congress of Plant Molecular Biology, Singapore, 1997, 789.
    • (1997) 5th International Congress of Plant Molecular Biology , pp. 789
    • Kim, Y.S.1    Yoon, K.2    Liu, J.R.3    Lee, H.S.4
  • 120
    • 0029411516 scopus 로고
    • Antifreeze proteins in winter rye are similar to pathogenesis-related proteins
    • Hon, W. C., Griffith, M., Mlynarz, A., Kwok, Y. C., and Yang, D. S. C., Antifreeze proteins in winter rye are similar to pathogenesis-related proteins, Plant Physiol., 109, 879, 1995.
    • (1995) Plant Physiol , vol.109 , pp. 879
    • Hon, W.C.1    Griffith, M.2    Mlynarz, A.3    Kwok, Y.C.4    Yang, D.S.C.5
  • 121
    • 0003125622 scopus 로고    scopus 로고
    • Nuisance proteins of wine are grape pathogenesis-related proteins
    • Waters, E. J., Shirley, N. J., and Williams, P. J., Nuisance proteins of wine are grape pathogenesis-related proteins, J. Agric. Food Chem., 44, 3, 1996.
    • (1996) J. Agric. Food Chem , vol.44 , pp. 3
    • Waters, E.J.1    Shirley, N.J.2    Williams, P.J.3
  • 122
    • 0031003510 scopus 로고    scopus 로고
    • Characterization and identification of latex allergens by two-dimensional electrophoresis and protein microsequencing
    • Posch, A., Chen, Z., Wheeler, C., Dunn, J., Faulf-Heimsoth, J., and Baur, X., Characterization and identification of latex allergens by two-dimensional electrophoresis and protein microsequencing, J. Allergy Clin. Immunol., 99, 385, 1997.
    • (1997) J. Allergy Clin. Immunol , vol.99 , pp. 385
    • Posch, A.1    Chen, Z.2    Wheeler, C.3    Dunn, J.4    Faulf-Heimsoth, J.5    Baur, X.6


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