메뉴 건너뛰기




Volumn , Issue , 1999, Pages 1-19

Occurrence and properties of plant pathogenesis-related proteins

Author keywords

[No Author keywords available]

Indexed keywords


EID: 85056316333     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1201/9781420049299     Document Type: Chapter
Times cited : (140)

References (116)
  • 1
    • 0014736229 scopus 로고
    • Polyacrylamide disc electrophoresis of the soluble leaf proteins from Nicotiana tabacum var. “Samsun” and “Samsun NN” II. Changes in protein constitution after infection with tobacco mosaic virus
    • Van Loon, L. C. and Van Kammen, A., Polyacrylamide disc electrophoresis of the soluble leaf proteins from Nicotiana tabacum var. “Samsun” and “Samsun NN” II. Changes in protein constitution after infection with tobacco mosaic virus, Virology, 40, 199, 1970.
    • (1970) Virology , vol.40 , pp. 199
    • Van Loon, L.C.1    Van Kammen, A.2
  • 2
    • 0014941283 scopus 로고
    • Hypersensibilité aux virus, température et protéines solubles chez le Nicotiana Xanthi n.c. Apparition de nouvelles macromolécules lors de la répression de la synthèse virale
    • Gianinazzi, S., Martin, C., and Vallée, J.-C., Hypersensibilité aux virus, température et protéines solubles chez le Nicotiana Xanthi n.c. Apparition de nouvelles macromolécules lors de la répression de la synthèse virale, C.R. Acad. Sci. Paris, 270D, 2383, 1970.
    • (1970) C.R. Acad. Sci. Paris , vol.270 D , pp. 2383
    • Gianinazzi, S.1    Martin, C.2    Vallée, J.-C.3
  • 3
    • 78651163419 scopus 로고
    • Disc electrophoresis I. Background and theory
    • Ornstein, L., Disc electrophoresis I. Background and theory, Ann. N. Y. Acad. Sci., 121, 321, 1964.
    • (1964) Ann. N. Y. Acad. Sci , vol.121 , pp. 321
    • Ornstein, L.1
  • 4
    • 78651153791 scopus 로고
    • Disc electrophoresis II. Method and application to human serum proteins
    • Davis, B. J., Disc electrophoresis II. Method and application to human serum proteins, Ann. N. Y. Acad. Sci., 121, 404, 1964.
    • (1964) Ann. N. Y. Acad. Sci , vol.121 , pp. 404
    • Davis, B.J.1
  • 5
    • 0004734984 scopus 로고
    • Polyacrylamide disc electrophoresis of the soluble leaf proteins from Nicotiana tabacum var. “Samsun” and “Samsun NN” I
    • Van Loon, L. C. and Van Kammen, A., Polyacrylamide disc electrophoresis of the soluble leaf proteins from Nicotiana tabacum var. “Samsun” and “Samsun NN” I., Phytochemistry, 7, 1727, 1968.
    • (1968) Phytochemistry , vol.7 , pp. 1727
    • Van Loon, L.C.1    Van Kammen, A.2
  • 6
    • 0004759187 scopus 로고
    • Température et synthèse de matériel protéique viral chez le Nicotiana Xanthi n.c. infecté par le virus de la mosaïque du tabac
    • Gianinazzi, S. and Vallée, J.-C., Température et synthèse de matériel protéique viral chez le Nicotiana Xanthi n.c. infecté par le virus de la mosaïque du tabac, C.R. Acad. Sci. Paris, 269D, 593, 1969.
    • (1969) C.R. Acad. Sci. Paris , vol.269 D , pp. 593
    • Gianinazzi, S.1    Vallée, J.-C.2
  • 7
    • 0016160850 scopus 로고
    • A possible explanation of the resistance of virus-infected tobacco to second infection
    • Kassanis, B., Gianinazzi, S., and White, R. F., A possible explanation of the resistance of virus-infected tobacco to second infection, J. Gen. Virol., 23, 11, 1974.
    • (1974) J. Gen. Virol , vol.23 , pp. 11
    • Kassanis, B.1    Gianinazzi, S.2    White, R.F.3
  • 8
    • 0016828128 scopus 로고
    • Polyacrylamide disc electrophoresis of the soluble leaf proteins from Nicotiana tabacum var. “Samsun” and “Samsun NN” IV. Similarity of qualitative changes of specific proteins after infection with different viruses and their relationship to acquired resistance
    • Van Loon, L. C., Polyacrylamide disc electrophoresis of the soluble leaf proteins from Nicotiana tabacum var. “Samsun” and “Samsun NN” IV. Similarity of qualitative changes of specific proteins after infection with different viruses and their relationship to acquired resistance, Virology, 67, 566, 1975.
    • (1975) Virology , vol.67 , pp. 566
    • Van Loon, L.C.1
  • 9
    • 0039668294 scopus 로고
    • Polyacrylamide disk electrophoresis of the soluble leaf proteins from Nicotiana tabacum var. “Samsun” and “Samsun NN” III. Influence of temperature and virus strain on changes induced by tobacco mosaic virus
    • Van Loon, L. C., Polyacrylamide disk electrophoresis of the soluble leaf proteins from Nicotiana tabacum var. “Samsun” and “Samsun NN” III. Influence of temperature and virus strain on changes induced by tobacco mosaic virus, Physiol. Plant Pathol., 6, 289, 1975.
    • (1975) Physiol. Plant Pathol , vol.6 , pp. 289
    • Van Loon, L.C.1
  • 10
    • 0002501909 scopus 로고
    • Evidence for the occurrence of the “pathogenesis-related” proteins in leaves of healthy tobacco plants during flowering
    • Fraser, R. S. S., Evidence for the occurrence of the “pathogenesis-related” proteins in leaves of healthy tobacco plants during flowering, Physiol. Plant Pathol., 19, 69, 1981.
    • (1981) Physiol. Plant Pathol , vol.19 , pp. 69
    • Fraser, R.S.S.1
  • 11
    • 0018899012 scopus 로고
    • Comparison of three pathogenesis-related proteins from plants of two cultivars of tobacco infected with TMV
    • Antoniw, J. F., Ritter, C. E., Pierpoint, W. S., and Van Loon, L. C., Comparison of three pathogenesis-related proteins from plants of two cultivars of tobacco infected with TMV, J. Gen. Virol., 47, 79, 1980.
    • (1980) J. Gen. Virol , vol.47 , pp. 79
    • Antoniw, J.F.1    Ritter, C.E.2    Pierpoint, W.S.3    Van Loon, L.C.4
  • 12
    • 0017286205 scopus 로고
    • Specific soluble leaf proteins in virus-infected tobacco plants are not normal constituents
    • Van Loon, L. C., Specific soluble leaf proteins in virus-infected tobacco plants are not normal constituents, J. Gen. Virol., 30, 375, 1976.
    • (1976) J. Gen. Virol , vol.30 , pp. 375
    • Van Loon, L.C.1
  • 13
    • 0017358471 scopus 로고
    • Partial purification and preliminary characterization of soluble proteins specific to virus infected tobacco plants
    • Gianinazzi, S., Pratt, H. M., Shewry, P. R., and Miflin, B. J., Partial purification and preliminary characterization of soluble proteins specific to virus infected tobacco plants, J. Gen. Virol., 34, 345, 1977.
    • (1977) J. Gen. Virol , vol.34 , pp. 345
    • Gianinazzi, S.1    Pratt, H.M.2    Shewry, P.R.3    Miflin, B.J.4
  • 14
    • 0002930330 scopus 로고
    • Mechanisms of resistance in virus-infected plants
    • Bailey, J. A. and Deverall, B.J., Eds., Academic Press, North Ryde, NSW, Australia
    • Van Loon, L. C., Mechanisms of resistance in virus-infected plants, in The Dynamics of Host Defense, Bailey, J. A. and Deverall, B.J., Eds., Academic Press, North Ryde, NSW, Australia, 1983, 123.
    • (1983) The Dynamics of Host Defense , pp. 123
    • Van Loon, L.C.1
  • 15
    • 0001072380 scopus 로고
    • Detection of pathogenesis-related proteins (PR or b) and of other proteins in the intercellular fluid of hypersensitive plants infected with tobacco mosaic virus
    • Parent, J. G. and Asselin, A., Detection of pathogenesis-related proteins (PR or b) and of other proteins in the intercellular fluid of hypersensitive plants infected with tobacco mosaic virus, Can. J. Bot., 62, 564, 1984.
    • (1984) Can. J. Bot , vol.62 , pp. 564
    • Parent, J.G.1    Asselin, A.2
  • 16
    • 0006926771 scopus 로고
    • Occurrence of pathogenesis-related (b) and similar proteins in different plant species
    • Redolfi, P., Occurrence of pathogenesis-related (b) and similar proteins in different plant species, Neth. J. Plant Pathol., 89, 245, 1983.
    • (1983) Neth. J. Plant Pathol , vol.89 , pp. 245
    • Redolfi, P.1
  • 17
    • 0000625239 scopus 로고
    • Stress proteins in infected plants
    • Kosuge, T. and Nester, E. W., Eds., McGraw-Hill Book Co., New York
    • Van Loon, L. C., Stress proteins in infected plants, in Plant-Microbe Interactions, Molecular and Genetic Perspectives, Vol. 3, Kosuge, T. and Nester, E. W., Eds., McGraw-Hill Book Co., New York, 1989, 198.
    • (1989) Plant-Microbe Interactions, Molecular and Genetic Perspectives , vol.3 , pp. 198
    • Van Loon, L.C.1
  • 18
    • 0343373455 scopus 로고
    • The nomenclature of pathogenesis-related proteins
    • Van Loon, L. C., The nomenclature of pathogenesis-related proteins, Physiol. Mol. Plant Pathol., 37, 229, 1990.
    • (1990) Physiol. Mol. Plant Pathol , vol.37 , pp. 229
    • Van Loon, L.C.1
  • 20
    • 0018611493 scopus 로고
    • Acetylsalicylic acid (aspirin) induces resistance to tobacco mosaic virus in tobacco
    • White, R. F., Acetylsalicylic acid (aspirin) induces resistance to tobacco mosaic virus in tobacco, Virology, 99, 410, 1979.
    • (1979) Virology , vol.99 , pp. 410
    • White, R.F.1
  • 21
    • 0000576077 scopus 로고
    • Comparison of the effects of salicylic acid and ethephon with virus-induced hypersensitivity and acquired resistance in tobacco
    • Van Loon, L. C. and Antoniw, J. F., Comparison of the effects of salicylic acid and ethephon with virus-induced hypersensitivity and acquired resistance in tobacco, Neth. J. Plant Pathol., 88, 237, 1982.
    • (1982) Neth. J. Plant Pathol , vol.88 , pp. 237
    • Van Loon, L.C.1    Antoniw, J.F.2
  • 22
    • 0026200231 scopus 로고
    • Salicylic acid is a systemic signal and an inducer of pathogenesis-related proteins in virusinfected tobacco
    • Yalpani, N., Silverman, P., Wilson, T. M. A., Kleier, D. A., and Raskin, I., Salicylic acid is a systemic signal and an inducer of pathogenesis-related proteins in virusinfected tobacco, Plant Cell, 3, 809, 1991.
    • (1991) Plant Cell , vol.3 , pp. 809
    • Yalpani, N.1    Silverman, P.2    Wilson, T.M.A.3    Kleier, D.A.4    Raskin, I.5
  • 24
    • 0001068883 scopus 로고
    • Wound-induced proteinase inhibitor in plant leaves: A possible defense mechanism against insects
    • Green, T. R. and Ryan, C. A., Wound-induced proteinase inhibitor in plant leaves: a possible defense mechanism against insects, Science, 175, 776, 1972.
    • (1972) Science , vol.175 , pp. 776
    • Green, T.R.1    Ryan, C.A.2
  • 25
    • 0001713773 scopus 로고
    • b-Protein as a constitutive component in highly (TMV) resistant interspecific hybrids of Nicotiana glutinosa x Nicotiana debneyi
    • Ahl, P. and Gianinazzi, S., b-Protein as a constitutive component in highly (TMV) resistant interspecific hybrids of Nicotiana glutinosa x Nicotiana debneyi, Plant Sci. Lett., 26, 173, 1982.
    • (1982) Plant Sci. Lett , vol.26 , pp. 173
    • Ahl, P.1    Gianinazzi, S.2
  • 26
    • 0000431745 scopus 로고
    • Identification, purification, and characterization of pathogenesis-related proteins from virus-infected Samsun NN tobacco leaves
    • Van Loon, L. C., Gerritsen, Y. A. M., and Ritter, C. E., Identification, purification, and characterization of pathogenesis-related proteins from virus-infected Samsun NN tobacco leaves, Plant Mol. Biol., 9, 593, 1987.
    • (1987) Plant Mol. Biol , vol.9 , pp. 593
    • Van Loon, L.C.1    Gerritsen, Y.A.M.2    Ritter, C.E.3
  • 27
    • 33644535944 scopus 로고
    • Pathogenesis-related proteins of plants
    • Linthorst H. J. M., Pathogenesis-related proteins of plants, Crit. Rev. Plant Sci., 10, 123, 1991.
    • (1991) Crit. Rev. Plant Sci , vol.10 , pp. 123
    • Linthorst, H.J.M.1
  • 29
    • 0028094240 scopus 로고
    • The role of thionins in plant protection
    • Bohlmann, H., The role of thionins in plant protection, Crit. Rev. Plant Sci., 13, 1, 1994.
    • (1994) Crit. Rev. Plant Sci , vol.13 , pp. 1
    • Bohlmann, H.1
  • 30
    • 0029347190 scopus 로고
    • Plant defensins: Novel antimicrobial peptides as components of the host defense system
    • Broekaert, W. F., Terras, F. R. G., Cammue, B. P. A., and Osborn, R. W., Plant defensins: novel antimicrobial peptides as components of the host defense system, Plant Physiol., 108, 1353, 1995.
    • (1995) Plant Physiol , vol.108 , pp. 1353
    • Broekaert, W.F.1    Terras, F.R.G.2    Cammue, B.P.A.3    Osborn, R.W.4
  • 31
    • 0023966339 scopus 로고
    • A virus-inducible tobacco gene encoding a glycine-rich protein shares putative regulatory elements with the ribulose bisphosphate carboxylase small subunit gene
    • Van Kan, J. A. L., Cornelissen, B. J. C., and Bol, J. F., A virus-inducible tobacco gene encoding a glycine-rich protein shares putative regulatory elements with the ribulose bisphosphate carboxylase small subunit gene, Mol. Plant-Microbe Interact., 1, 107, 1988.
    • (1988) Mol. Plant-Microbe Interact , vol.1 , pp. 107
    • Van Kan, J.A.L.1    Cornelissen, B.J.C.2    Bol, J.F.3
  • 32
    • 0001581521 scopus 로고
    • Biological function of “pathogenesis-related” proteins: Four PR proteins of tobacco have 1,3-ß-glucanase activity
    • Kauffmann, S., Legrand, M., Geoffroy, P., and Fritig, B., Biological function of “pathogenesis-related” proteins: four PR proteins of tobacco have 1,3-ß-glucanase activity, EMBO J., 6, 3209, 1987.
    • (1987) EMBO J , vol.6 , pp. 3209
    • Kauffmann, S.1    Legrand, M.2    Geoffroy, P.3    Fritig, B.4
  • 33
    • 0001480645 scopus 로고
    • Biological function of pathogenesis-related proteins: Four tobacco pathogenesis-related proteins are chitinases
    • Legrand, M., Kauffmann, S., Geoffroy, P., 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    Kauffmann, S.2    Geoffroy, P.3    Fritig, B.4
  • 37
    • 0001068155 scopus 로고
    • A possible function for thaumatin and a TMV-induced protein suggested by homology to a maize inhibitor
    • Richardson, M., Valdez-Rodriguez, S., and Blanco-Labra, A., A possible function for thaumatin and a TMV-induced protein suggested by homology to a maize inhibitor, Nature, 327, 432, 1987.
    • (1987) Nature , vol.327 , pp. 432
    • Richardson, M.1    Valdez-Rodriguez, S.2    Blanco-Labra, A.3
  • 39
    • 0031417776 scopus 로고    scopus 로고
    • Induced resistance in plants and the role of pathogenesis-related proteins
    • Van Loon, L. C., Induced resistance in plants and the role of pathogenesis-related proteins, Eur. J. Plant Pathol., 103, 753, 1997.
    • (1997) Eur. J. Plant Pathol , vol.103 , pp. 753
    • Van Loon, L.C.1
  • 40
    • 6244270831 scopus 로고
    • Effect of polyacrylic acid and b proteins on TMV multiplication in tobacco protoplasts
    • Kassanis, B. and White, R. F., Effect of polyacrylic acid and b proteins on TMV multiplication in tobacco protoplasts, Phytopath. Z., 91, 269, 1978.
    • (1978) Phytopath. Z , vol.91 , pp. 269
    • Kassanis, B.1    White, R.F.2
  • 41
    • 0010495225 scopus 로고
    • Pathogenesis-related (b) proteins do not play a central role in TMV localization in Nicotiana rustica
    • Dumas, E. and Gianinazzi, S., Pathogenesis-related (b) proteins do not play a central role in TMV localization in Nicotiana rustica, Physiol. Mol. Plant Pathol., 28, 243, 1986.
    • (1986) Physiol. Mol. Plant Pathol , vol.28 , pp. 243
    • Dumas, E.1    Gianinazzi, S.2
  • 42
    • 0022551299 scopus 로고
    • Induction by salicylic acid of pathogenesis-related proteins and resistance to alfalfa mosaic virus infection in various plant species
    • Hooft van Huijsduijnen, R. A. M., Alblas, S. W., De Rijk, R. H., and Bol, J. F., Induction by salicylic acid of pathogenesis-related proteins and resistance to alfalfa mosaic virus infection in various plant species, J. Gen. Virol., 67, 2135, 1986.
    • (1986) J. Gen. Virol , vol.67 , pp. 2135
    • Hooft van Huijsduijnen, R.A.M.1    Alblas, S.W.2    De Rijk, R.H.3    Bol, J.F.4
  • 43
    • 0000660621 scopus 로고
    • Are “pathogenesis-related” proteins involved in acquired systemic resistance of tobacco plants to tobacco mosaic virus?
    • Fraser, R. S. S., Are “pathogenesis-related” proteins involved in acquired systemic resistance of tobacco plants to tobacco mosaic virus?, J. Gen. Virol., 58, 305, 1982.
    • (1982) J. Gen. Virol , vol.58 , pp. 305
    • Fraser, R.S.S.1
  • 44
    • 0024619654 scopus 로고
    • Constitutive expression of pathogenesis-related proteins PR-1, GRP, and PR-S in tobacco has no effect on virus infection
    • Linthorst, H. J. M., Meuwissen, R. L. J., Kauffmann, S., and Bol, J. F., Constitutive expression of pathogenesis-related proteins PR-1, GRP, and PR-S in tobacco has no effect on virus infection, Plant Cell, 1, 285, 1989.
    • (1989) Plant Cell , vol.1 , pp. 285
    • Linthorst, H.J.M.1    Meuwissen, R.L.J.2    Kauffmann, S.3    Bol, J.F.4
  • 47
    • 0030574262 scopus 로고    scopus 로고
    • Pathogenesis-related functions of plant ß-1,3-glucanases investigated by antisense transformation - a review
    • Beffa, R. S. and Meins, F., Pathogenesis-related functions of plant ß-1,3-glucanases investigated by antisense transformation - a review, Gene, 179, 97, 1996.
    • (1996) Gene , vol.179 , pp. 97
    • Beffa, R.S.1    Meins, F.2
  • 48
    • 33645680660 scopus 로고
    • Differential changes in soluble tomato leaf proteins after inoculation with virulent and avirulent races of Cladosporium fulvum (syn. Fulvia fulva)
    • De Wit, P. J. G. M. and Bakker, J., Differential changes in soluble tomato leaf proteins after inoculation with virulent and avirulent races of Cladosporium fulvum (syn. Fulvia fulva), Physiol. Plant Pathol., 17, 121, 1980.
    • (1980) Physiol. Plant Pathol , vol.17 , pp. 121
    • De Wit, P.J.G.M.1    Bakker, J.2
  • 49
    • 0029110165 scopus 로고
    • Induced systemic resistance in radish is not associated with accumulation of pathogenesis-related proteins
    • Hoffland, E., Pieterse, C. M. J., Bik, L., and Van Pelt, J. A., Induced systemic resistance in radish is not associated with accumulation of pathogenesis-related proteins, Physiol. Mol. Plant Pathol., 46, 309, 1995.
    • (1995) Physiol. Mol. Plant Pathol , vol.46 , pp. 309
    • Hoffland, E.1    Pieterse, C.M.J.2    Bik, L.3    Van Pelt, J.A.4
  • 50
    • 0030221453 scopus 로고    scopus 로고
    • Systemic resistance in Arabidopsis induced by biocontrol bacteria is independent of salicylic acid accumulation and pathogenesis-related gene expression
    • Pieterse, C. M. J., Van Wees, S. C. M., Hoffland, E., Van Pelt, J. A., and Van Loon, L. C., Systemic resistance in Arabidopsis induced by biocontrol bacteria is independent of salicylic acid accumulation and pathogenesis-related gene expression, Plant Cell, 8, 1225, 1996.
    • (1996) Plant Cell , vol.8 , pp. 1225
    • Pieterse, C.M.J.1    Van Wees, S.C.M.2    Hoffland, E.3    Van Pelt, J.A.4    Van Loon, L.C.5
  • 51
    • 0002488202 scopus 로고
    • Pathogenesis-related proteins of tomato. P-69 as an alkaline endoproteinase
    • Vera, P. and Conejero, V., Pathogenesis-related proteins of tomato. P-69 as an alkaline endoproteinase, Plant Physiol., 87, 58, 1988.
    • (1988) Plant Physiol , vol.87 , pp. 58
    • Vera, P.1    Conejero, V.2
  • 52
    • 0027490930 scopus 로고
    • Plant “pathogenesis-related” proteins and their role in defense against pathogens
    • Stintzi, A., Heitz, T., Prasad, V., Wiedemann-Merdinoglu, S., Kauffmann, S., Geoffroy, P., Legrand, M., and Fritig, B., Plant “pathogenesis-related” proteins and their role in defense against pathogens, Biochimie, 75, 687, 1993.
    • (1993) Biochimie , vol.75 , pp. 687
    • Stintzi, A.1    Heitz, T.2    Prasad, V.3    Kauffmann, S.4    Geoffroy, P.5    Legrand, M.6    Fritig, B.7
  • 53
    • 0000159821 scopus 로고
    • Rapid activation by fungal elicitor of genes encoding “pathogenesis-related” proteins in cultured parsley cells
    • Somssich, I. E., Schmelzer, E., Bollmann, J., and Hahlbrock, K., Rapid activation by fungal elicitor of genes encoding “pathogenesis-related” proteins in cultured parsley cells, Proc. Natl. Acad. Sci. U.S.A., 83, 2427, 1986.
    • (1986) Proc. Natl. Acad. Sci. U.S.A , vol.83 , pp. 2427
    • Somssich, I.E.1    Schmelzer, E.2    Bollmann, J.3    Hahlbrock, K.4
  • 54
    • 0027975651 scopus 로고
    • High sequence similarity between a ribonuclease from ginseng calluses and fungus-elicited proteins from parsley indicates that intracellular pathogenesis-related (IPR) proteins are ribonucleases
    • Moiseyev, G., Beintema, J. J., Fedoreyeva, L. I., and Yakovlev, G. I., High sequence similarity between a ribonuclease from ginseng calluses and fungus-elicited proteins from parsley indicates that intracellular pathogenesis-related (IPR) proteins are ribonucleases, Planta, 193, 470, 1994.
    • (1994) Planta , vol.193 , pp. 470
    • Moiseyev, G.1    Beintema, J.J.2    Fedoreyeva, L.I.3    Yakovlev, G.I.4
  • 55
    • 0001566766 scopus 로고
    • Developmental and hormonal regulation of ß-1,3-glucanase in tobacco
    • Felix, G. and Meins, F., Developmental and hormonal regulation of ß-1,3-glucanase in tobacco, Planta, 167, 206, 1986.
    • (1986) Planta , vol.167 , pp. 206
    • Felix, G.1    Meins, F.2
  • 56
    • 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., and Meins, F., 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    Mohnen, D.2    Meins, F.3
  • 57
    • 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
  • 58
    • 0025382823 scopus 로고
    • Tobacco genes encoding acidic and basic isoforms of pathogenesis-related proteins display different expression patterns
    • Memelink, J., Linthorst, H. J. M., Schilperoort, R. A., and Hoge, J. H. C., Tobacco genes encoding acidic and basic isoforms of pathogenesis-related proteins display different expression patterns, Plant Mol. Biol., 14, 119, 1990.
    • (1990) Plant Mol. Biol , vol.14 , pp. 119
    • Memelink, J.1    Linthorst, H.J.M.2    Schilperoort, R.A.3    Hoge, J.H.C.4
  • 59
    • 0026411035 scopus 로고
    • Differential induction of acquired resistance and PR gene expression in tobacco by virus infection, ethephon treatment, UV light and wounding
    • Brederode, F. T., Linthorst, H. J. M., and Bol, J. F., Differential induction of acquired resistance and PR gene expression in tobacco by virus infection, ethephon treatment, UV light and wounding, Plant Mol. Biol., 17, 1117, 1991.
    • (1991) Plant Mol. Biol , vol.17 , pp. 1117
    • Brederode, F.T.1    Linthorst, H.J.M.2    Bol, J.F.3
  • 60
    • 0000444688 scopus 로고
    • Regulation of ethylene biosynthesis in virus infected tobacco leaves. II. Time course of levels of intermediates and in vivo conversion rates
    • De Laat, A. M. M. and Van Loon, L. C., Regulation of ethylene biosynthesis in virus infected tobacco leaves. II. Time course of levels of intermediates and in vivo conversion rates, Plant Physiol., 69, 240, 1982.
    • (1982) Plant Physiol , vol.69 , pp. 240
    • De Laat, A.M.M.1    Van Loon, L.C.2
  • 61
    • 33646120953 scopus 로고
    • Ethylene in pathogenesis and disease resistance
    • Mattoo, A. K. and Suttle, J. C., Eds., CRC Press, Boca Raton, FL
    • Boller, T., Ethylene in pathogenesis and disease resistance, in The Plant Hormone Ethylene, Mattoo, A. K. and Suttle, J. C., Eds., CRC Press, Boca Raton, FL, 1991, 293.
    • (1991) The Plant Hormone Ethylene , pp. 293
    • Boller, T.1
  • 62
    • 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
  • 64
    • 0029294601 scopus 로고
    • Pathogenesis-related PR-1 proteins are antifungal; isolation and characterization of three 14-kilodalton proteins of tomato and of a basic PR-1 of tobacco with inhibitory activity against Phytophthora infestans
    • Niderman, T., Genetet, I., Bruyère, T., Gees, R., Stintzi, A., Legrand, M., Fritig, B., and Mösinger, E., Pathogenesis-related PR-1 proteins are antifungal; isolation and characterization of three 14-kilodalton proteins of tomato and of a basic PR-1 of tobacco with inhibitory activity against Phytophthora infestans, Plant Physiol., 108, 17, 1995.
    • (1995) Plant Physiol , vol.108 , pp. 17
    • Niderman, T.1    Genetet, I.2    Bruyère, T.3    Gees, R.4    Stintzi, A.5    Legrand, M.6    Fritig, B.7    Mösinger, E.8
  • 65
    • 0030041342 scopus 로고    scopus 로고
    • Analysis of late-blight disease resistance and freezing tolerance in transgenic potato plants expressing sense and antisense genes for an osmotin-like protein
    • Zhu, B. L., Chen, T. H. H., and Li, P. H., Analysis of late-blight disease resistance and freezing tolerance in transgenic potato plants expressing sense and antisense genes for an osmotin-like protein, Planta, 198, 70, 1996.
    • (1996) Planta , vol.198 , pp. 70
    • Zhu, B.L.1    Chen, T.H.H.2    Li, P.H.3
  • 67
    • 0028001451 scopus 로고
    • Enhanced protection against fungal attack by constitutive co-expression of chitinase and glucanase genes in transgenic tobacco
    • Zhu, Q., Maher, E. A., Masoud, S., Dixon, R. A., and Lamb, C. J., Enhanced protection against fungal attack by constitutive co-expression of chitinase and glucanase genes in transgenic tobacco, Biotechnology, 12, 807, 1994.
    • (1994) Biotechnology , vol.12 , pp. 807
    • Zhu, Q.1    Maher, E.A.2    Masoud, S.3    Dixon, R.A.4    Lamb, C.J.5
  • 68
    • 0029328434 scopus 로고
    • Enhanced quantitative resistance against fungal disease by combinatorial expression of different barley antifungal proteins in transgenic tobacco
    • Jach, G., Görnhardt, B., Mundy, J., Logemann, J., Pinsdorf, E., Leah, R., Schell, J., and Maas, C., Enhanced quantitative resistance against fungal disease by combinatorial expression of different barley antifungal proteins in transgenic tobacco, Plant J., 8, 97, 1995.
    • (1995) Plant J , vol.8 , pp. 97
    • Jach, G.1    Görnhardt, B.2    Mundy, J.3    Logemann, J.4    Pinsdorf, E.5    Leah, R.6    Schell, J.7    Maas, C.8
  • 69
    • 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
  • 70
    • 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. J., 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.J.5
  • 71
    • 0001194009 scopus 로고
    • Plant and bacterial chitinases differ in antifungal activity
    • Roberts, W. K. and Selitrennikoff, C. P., Plant and bacterial chitinases differ in antifungal activity, J. Gen. Microbiol., 134, 169, 1988.
    • (1988) J. Gen. Microbiol , vol.134 , pp. 169
    • Roberts, W.K.1    Selitrennikoff, C.P.2
  • 72
    • 0025864523 scopus 로고
    • Two antifungal thaumatin-like proteins from barley grain
    • Hejgaard, J., Jacobsen, S., and Svendsen, I., Two antifungal thaumatin-like proteins from barley grain, FEBS Lett., 291, 127, 1991.
    • (1991) FEBS Lett , vol.291 , pp. 127
    • Hejgaard, J.1    Jacobsen, S.2    Svendsen, I.3
  • 74
    • 0030887368 scopus 로고    scopus 로고
    • Fungal pathogens secrete an inhibitor protein that distinguishes isoforms of plant pathogenesis-related endo-ß-1,3-glucanases
    • Ham, K. S., Wu, S. C., Darvill, A. G., and Albersheim, P., Fungal pathogens secrete an inhibitor protein that distinguishes isoforms of plant pathogenesis-related endo-ß-1,3-glucanases, Plant J., 11, 169, 1997.
    • (1997) Plant J , vol.11 , pp. 169
    • Ham, K.S.1    Wu, S.C.2    Darvill, A.G.3    Albersheim, P.4
  • 75
    • 0022918330 scopus 로고
    • Molecular cloning of the cDNA for androgen-dependent sperm-coating glycoproteins secreted by the rat epididymis
    • Brooks, D. E., Means, A. R., Wright, E. J., Singh, S. P., and Tiver, K. K., Molecular cloning of the cDNA for androgen-dependent sperm-coating glycoproteins secreted by the rat epididymis, Eur. J. Biochem., 161, 13, 1986.
    • (1986) Eur. J. Biochem , vol.161 , pp. 13
    • Brooks, D.E.1    Means, A.R.2    Wright, E.J.3    Singh, S.P.4    Tiver, K.K.5
  • 76
    • 0023854882 scopus 로고
    • cDNA cloning and primary structure of a white-face hornet venom allergen, antigen 5
    • Fang, K. S. Y., Vitale, M., Fehlner, P., and King, T. P., cDNA cloning and primary structure of a white-face hornet venom allergen, antigen 5, Proc. Natl. Acad. Sci. U.S.A., 85, 895, 1988.
    • (1988) Proc. Natl. Acad. Sci. U.S.A , vol.85 , pp. 895
    • Fang, K.S.Y.1    Vitale, M.2    Fehlner, P.3    King, T.P.4
  • 77
    • 0027424323 scopus 로고
    • The Sc7/Sc14 gene family of Schizophyllum commune codes for extracellular proteins specifically expressed during fruit-body formation
    • Schuren, F. H. J., ásgeirsdóttir, S. A., Kothe, E. M., Scheer, J. M. J., and Wessels, J. G. H., The Sc7/Sc14 gene family of Schizophyllum commune codes for extracellular proteins specifically expressed during fruit-body formation, J. Gen. Microbiol., 139, 2083, 1993.
    • (1993) J. Gen. Microbiol , vol.139 , pp. 2083
    • Schuren, F.H.J.1    Ásgeirsdóttir, S.A.2    Kothe, E.M.3    Scheer, J.M.J.4    Wessels, J.G.H.5
  • 78
    • 0029848759 scopus 로고    scopus 로고
    • CRISP-3, a protein with homology to plant defense proteins, is expressed in mouse B cells under the control of Oct. 2
    • Pfisterer, P., König, H., Hess, J., Lipowsky, G., Haendler, B., Schleuning, W.-D., and Wirth, T., CRISP-3, a protein with homology to plant defense proteins, is expressed in mouse B cells under the control of Oct. 2, Mol. Cell. Biol., 16, 6160, 1996.
    • (1996) Mol. Cell. Biol , vol.16 , pp. 6160
    • Pfisterer, P.1    König, H.2    Hess, J.3    Lipowsky, G.4    Haendler, B.5    Schleuning, W.-D.6    Wirth, T.7
  • 79
    • 0017367018 scopus 로고
    • Induction by 2-chloroethylphosphonic acid of viral-like lesions, associated proteins, and systemic resistance in tobacco
    • Van Loon, L. C., Induction by 2-chloroethylphosphonic acid of viral-like lesions, associated proteins, and systemic resistance in tobacco, Virology, 80, 417, 1977.
    • (1977) Virology , vol.80 , pp. 417
    • Van Loon, L.C.1
  • 80
    • 0344292459 scopus 로고
    • Induction of “pathogenesis-related” proteins in tobacco leaves by physiological (non-pathogenic) disorders
    • Edreva, A. M., Induction of “pathogenesis-related” proteins in tobacco leaves by physiological (non-pathogenic) disorders, J. Exp. Bot., 41, 701, 1990.
    • (1990) J. Exp. Bot , vol.41 , pp. 701
    • Edreva, A.M.1
  • 81
    • 77649192978 scopus 로고
    • Comparison of virus-elicited and other stresses on the soluble protein fraction of cucumber cotyledons
    • Wagih, E. E. and Coutts, R. H. A., Comparison of virus-elicited and other stresses on the soluble protein fraction of cucumber cotyledons, Phytopath. Z., 104, 364, 1982.
    • (1982) Phytopath. Z , vol.104 , pp. 364
    • Wagih, E.E.1    Coutts, R.H.A.2
  • 82
    • 0022497214 scopus 로고
    • The chemical induction of PR (b) proteins and resistance to TMV infection in tobacco
    • White, R. F., Dumas, E., Shaw, P., and Antoniw, J. F., The chemical induction of PR (b) proteins and resistance to TMV infection in tobacco, Antiviral Res., 6, 177, 1986.
    • (1986) Antiviral Res , vol.6 , pp. 177
    • White, R.F.1    Dumas, E.2    Shaw, P.3    Antoniw, J.F.4
  • 83
    • 0345177287 scopus 로고
    • Alterations in the soluble protein patterns of tobacco and cowpea leaves following inoculation with tobacco necrosis virus
    • Coutts, R. H. A., Alterations in the soluble protein patterns of tobacco and cowpea leaves following inoculation with tobacco necrosis virus, Plant Sci. Lett., 12, 189, 1978.
    • (1978) Plant Sci. Lett , vol.12 , pp. 189
    • Coutts, R.H.A.1
  • 84
    • 79959307072 scopus 로고
    • Changes in the proteins of bean leaves infected with tobacco necrosis or alfalfa mosaic viruses
    • Szczepanski, M. and Redolfi, P., Changes in the proteins of bean leaves infected with tobacco necrosis or alfalfa mosaic viruses, Phytopath. Z., 113, 57, 1985.
    • (1985) Phytopath. Z , vol.113 , pp. 57
    • Szczepanski, M.1    Redolfi, P.2
  • 85
    • 84969792040 scopus 로고
    • Molecular cloning of osmotin and regulation of its expression by ABA and adaptation to low water potential
    • Singh, N. K., Nelson, D. E., Kuhn, D., Hasegawa, P. M., and Bressan, R. A., Molecular cloning of osmotin and regulation of its expression by ABA and adaptation to low water potential, Plant Physiol., 90, 1096, 1989.
    • (1989) Plant Physiol , vol.90 , pp. 1096
    • Singh, N.K.1    Nelson, D.E.2    Kuhn, D.3    Hasegawa, P.M.4    Bressan, R.A.5
  • 88
    • 0000599813 scopus 로고
    • Stress-induced proteins: Characterization and the regulation of their synthesis
    • Stumpf, P. K. and Conn, E. E., Eds.,: Molecular Biology, Marcus A., Ed., Academic Press, New York
    • Ho, T. H. D. and Sachs, M. M., Stress-induced proteins: characterization and the regulation of their synthesis, in The Biochemistry of Plants, A Comprehensive Treatise, Stumpf, P. K. and Conn, E. E., Eds., Vol. 15: Molecular Biology, Marcus A., Ed., Academic Press, New York, 1989, 347.
    • (1989) The Biochemistry of Plants, A Comprehensive Treatise , vol.15 , pp. 347
    • Ho, T.H.D.1    Sachs, M.M.2
  • 89
    • 0030766822 scopus 로고    scopus 로고
    • Jasmonate-signalled plant gene expression
    • Wasternack, C. and Parthier, B., Jasmonate-signalled plant gene expression, Trends Plant Sci., 2, 302, 1997.
    • (1997) Trends Plant Sci , vol.2 , pp. 302
    • Wasternack, C.1    Parthier, B.2
  • 90
    • 0026322998 scopus 로고
    • Uncoupling thermotolerance from the induction of heat shock proteins
    • Smith, B. J. and Yaffe, M. P., Uncoupling thermotolerance from the induction of heat shock proteins, Proc. Natl. Acad. Sci. U.S.A., 88, 11091, 1991.
    • (1991) Proc. Natl. Acad. Sci. U.S.A , vol.88 , pp. 11091
    • Smith, B.J.1    Yaffe, M.P.2
  • 93
    • 0026584271 scopus 로고
    • Protein folding in the cell
    • Gething, M. J. and Sambrook, J., Protein folding in the cell, Nature, 355, 33, 1992.
    • (1992) Nature , vol.355 , pp. 33
    • Gething, M.J.1    Sambrook, J.2
  • 94
    • 0007981095 scopus 로고
    • DNA sequence analysis of a PR-1a gene from tobacco: Molecular relationship of heat shock and pathogen responses in plants
    • Pfitzner, U. M., Pfitzner, A. J. P., and Goodman, H. M., DNA sequence analysis of a PR-1a gene from tobacco: molecular relationship of heat shock and pathogen responses in plants, Mol. Gen. Genet., 211, 290, 1988.
    • (1988) Mol. Gen. Genet , vol.211 , pp. 290
    • Pfitzner, U.M.1    Pfitzner, A.J.P.2    Goodman, H.M.3
  • 95
    • 0024052390 scopus 로고
    • Gene structure and in situ transcript localisation of pathogenesis-related protein 1 in parsley
    • Somssich, I. E., Schmelzer, E., Kawalleck, P., and Hahlbrock, K., Gene structure and in situ transcript localisation of pathogenesis-related protein 1 in parsley, Mol. Gen. Genet., 213, 93, 1988.
    • (1988) Mol. Gen. Genet , vol.213 , pp. 93
    • Somssich, I.E.1    Schmelzer, E.2    Kawalleck, P.3    Hahlbrock, K.4
  • 96
    • 0344843486 scopus 로고
    • Induction of pathogenesis-related proteins in tobacco leaves
    • Matsuoka, M. and Ohashi, Y., Induction of pathogenesis-related proteins in tobacco leaves, Plant Physiol., 80, 505, 1986.
    • (1986) Plant Physiol , vol.80 , pp. 505
    • Matsuoka, M.1    Ohashi, Y.2
  • 97
    • 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
  • 98
    • 0000354309 scopus 로고
    • Molecular cloning and ethylene induction of mRNA encoding a phytoalexin elicitorreleasing factor ß-1,3-endoglucanase, in soybean
    • Takeuchi, Y., Yoshikawa, M., Takeba, G., Tanaka, K., Shibata, D., and Horino, O., Molecular cloning and ethylene induction of mRNA encoding a phytoalexin elicitorreleasing factor, ß-1,3-endoglucanase, in soybean, Plant Physiol., 93, 673, 1990.
    • (1990) Plant Physiol , vol.93 , pp. 673
    • Takeuchi, Y.1    Yoshikawa, M.2    Takeba, G.3    Tanaka, K.4    Shibata, D.5    Horino, O.6
  • 99
    • 0001456880 scopus 로고
    • Host-pathogen interactions XXXIX. A soybean pathogenesis-related protein with ß-1,3-glucanase activity releases phytoalexin elicitor-active heat stable fragments from fungal cell walls
    • Ham, K. S., Kauffmann, S., Albersheim, P., and Darvill, A. G., Host-pathogen interactions XXXIX. A soybean pathogenesis-related protein with ß-1,3-glucanase activity releases phytoalexin elicitor-active heat stable fragments from fungal cell walls, Mol. Plant-Microbe Interact., 4, 545, 1991.
    • (1991) Mol. Plant-Microbe Interact , vol.4 , pp. 545
    • Ham, K.S.1    Kauffmann, S.2    Albersheim, P.3    Darvill, A.G.4
  • 100
    • 0001864819 scopus 로고
    • Tissue-specific expression of cell wall proteins in developing soybean tissues
    • Ye, Z. H. and Varner, J. E., Tissue-specific expression of cell wall proteins in developing soybean tissues, Plant Cell, 3, 23, 1991.
    • (1991) Plant Cell , vol.3 , pp. 23
    • Ye, Z.H.1    Varner, J.E.2
  • 102
    • 0001503966 scopus 로고
    • Phytoalexins and their elicitors - a defense against microbial infection in plants
    • Darvill, A. G. and Albersheim, P., Phytoalexins and their elicitors - a defense against microbial infection in plants, Annu. Rev. Plant Physiol., 35, 243, 1984.
    • (1984) Annu. Rev. Plant Physiol , vol.35 , pp. 243
    • Darvill, A.G.1    Albersheim, P.2
  • 103
    • 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
  • 104
    • 0002886806 scopus 로고
    • Chitinase in bean leaves: Induction by ethylene purification, properties and possible function
    • Boller, T., Gehri, A., Mauch, F., and Vögeli, U., Chitinase in bean leaves: induction by ethylene, purification, properties and possible function, Planta, 157, 22, 1983.
    • (1983) Planta , vol.157 , pp. 22
    • Boller, T.1    Gehri, A.2    Mauch, F.3    Vögeli, U.4
  • 105
    • 84981566094 scopus 로고
    • Translatable mRNA changes in ethylene induced abscission zones of Phaseolus vulgaris (Red Kidney)
    • Kelly, P., Trewavas, A. J., Lewis, L. N., Durbin, M. L., and Sexton, R., Translatable mRNA changes in ethylene induced abscission zones of Phaseolus vulgaris (Red Kidney), Plant Cell Environ., 10, 11, 1987.
    • (1987) Plant Cell Environ , vol.10 , pp. 11
    • Kelly, P.1    Trewavas, A.J.2    Lewis, L.N.3    Durbin, M.L.4    Sexton, R.5
  • 106
    • 0001040585 scopus 로고
    • Identification and kinetics of accumulation of proteins induced by ethylene in bean abscission zones
    • Del Campillo, E. and Lewis, L. N., Identification and kinetics of accumulation of proteins induced by ethylene in bean abscission zones, Plant Physiol., 98, 955, 1992.
    • (1992) Plant Physiol , vol.98 , pp. 955
    • Del Campillo, E.1    Lewis, L.N.2
  • 107
    • 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
  • 112
  • 113
    • 0025187049 scopus 로고
    • A major stylar matrix polypeptide (sp41) is a member of the pathogenesis-related proteins superclass
    • Ori, N., Sessa, G., Lotan, T., Himmelhoch, S., and Fluhr, R., A major stylar matrix polypeptide (sp41) is a member of the pathogenesis-related proteins superclass, EMBO J., 9, 3429, 1990.
    • (1990) EMBO J , vol.9 , pp. 3429
    • Ori, N.1    Sessa, G.2    Lotan, T.3    Himmelhoch, S.4    Fluhr, R.5
  • 114
    • 0026131071 scopus 로고
    • Pathogenesis-related acidic ß-1,3-glucanase genes of tobacco are regulated by both stress and developmental signals
    • Coté, F., Cutt, J. R., Asselin, A., and Klessig, D. F., Pathogenesis-related acidic ß-1,3-glucanase genes of tobacco are regulated by both stress and developmental signals, Mol. Plant-Microbe Interact., 4, 173, 1991.
    • (1991) Mol. Plant-Microbe Interact , vol.4 , pp. 173
    • Coté, F.1    Cutt, J.R.2    Asselin, A.3    Klessig, D.F.4
  • 115
    • 0008864672 scopus 로고
    • Immunological evidence of thaumatin-like proteins during tobacco floral differentiation
    • Richard, L., Arró, M., Hoebeke, J., Meeks-Wagner, D. R., and Van, K. T. T., Immunological evidence of thaumatin-like proteins during tobacco floral differentiation, Plant Physiol., 98, 337, 1992.
    • (1992) Plant Physiol , vol.98 , pp. 337
    • Richard, L.1    Arró, M.2    Hoebeke, J.3    Meeks-Wagner, D.R.4    Van, K.T.T.5
  • 116
    • 0001227910 scopus 로고
    • Involvement of plant chitinase in sexual reproduction of higher plants
    • Leung, D. W. M., Involvement of plant chitinase in sexual reproduction of higher plants, Phytochemistry, 31, 1899, 1992.
    • (1992) Phytochemistry , vol.31 , pp. 1899
    • Leung, D.W.M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.