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Volumn 34, Issue 3, 2003, Pages 327-338

Characterization of a tomato protein that inhibits a xyloglucan-specific endoglucanase

Author keywords

Endoglucanase; Fungi; Inhibitor; Pathogenesis; Plants; Xyloglucan

Indexed keywords

AMINO ACIDS; FUNGUS ATTACK; PROTEINS;

EID: 0038706377     PISSN: 09607412     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1365-313X.2003.01726.x     Document Type: Article
Times cited : (96)

References (72)
  • 1
    • 0015101709 scopus 로고
    • Host-pathogen interactions III. Proteins from plant cell walls inhibit polygalacturonases secreted by plant pathogens
    • Albersheim, P. and Anderson, A.J. (1971) Host-pathogen interactions III. Proteins from plant cell walls inhibit polygalacturonases secreted by plant pathogens. Proc. Natl. Acad. Sci. USA, 68, 1815-1819.
    • (1971) Proc. Natl. Acad. Sci. USA , vol.68 , pp. 1815-1819
    • Albersheim, P.1    Anderson, A.J.2
  • 2
    • 0033819692 scopus 로고    scopus 로고
    • Characterization of a basic chitinase which is secreted by cultured pumpkin cells
    • Arie, M., Hikichi, K., Takahashi, K. and Esaka, M. (2000) Characterization of a basic chitinase which is secreted by cultured pumpkin cells. Physiol. Plant. 110, 232-239.
    • (2000) Physiol. Plant. , vol.110 , pp. 232-239
    • Arie, M.1    Hikichi, K.2    Takahashi, K.3    Esaka, M.4
  • 3
    • 0025134781 scopus 로고
    • A glycoproteins inhibitor of pectin methylesterase in kiwi fruit (Actinidia chinensis)
    • Balestrieri, C., Castaldo, O., Giovane, A., Quagliuolo, L. and Servillo, L. (1990) A glycoproteins inhibitor of pectin methylesterase in kiwi fruit (Actinidia chinensis). Eur. J. Biochem. 193, 183-187.
    • (1990) Eur. J. Biochem. , vol.193 , pp. 183-187
    • Balestrieri, C.1    Castaldo, O.2    Giovane, A.3    Quagliuolo, L.4    Servillo, L.5
  • 4
    • 0002618659 scopus 로고
    • Isolation, purification and characterization of the seed globulins of Lupinus angustifolius
    • Blagrove, R.J. and Gillespie, J.M. (1975) Isolation, purification and characterization of the seed globulins of Lupinus angustifolius. Aust. J. Plant Physiol. 2, 13-27.
    • (1975) Aust. J. Plant Physiol. , vol.2 , pp. 13-27
    • Blagrove, R.J.1    Gillespie, J.M.2
  • 5
    • 0003103794 scopus 로고
    • Physicochemical studies of conglutin gamma, a storage globulin from seeds of Lupinus angustifolius
    • Blagrove, R.J., Gillespie, J.M., Lilley, G.G. and Woods, E.F. (1980) Physicochemical studies of conglutin gamma, a storage globulin from seeds of Lupinus angustifolius. Aust. J. Plant Physiol. 7, 1-13.
    • (1980) Aust. J. Plant Physiol. , vol.7 , pp. 1-13
    • Blagrove, R.J.1    Gillespie, J.M.2    Lilley, G.G.3    Woods, E.F.4
  • 6
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M.M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 7
    • 0001158491 scopus 로고
    • Differential expression of 2 peanut peroxidase cDNA clones in peanut plants and cells in suspension-culture in response to stress
    • Breda, C., Buffard, D., Vanhuystee, R.B. and Esnault, R. (1993) Differential expression of 2 peanut peroxidase cDNA clones in peanut plants and cells in suspension-culture in response to stress. Plant Cell Rep. 12, 268-272.
    • (1993) Plant Cell Rep. , vol.12 , pp. 268-272
    • Breda, C.1    Buffard, D.2    Vanhuystee, R.B.3    Esnault, R.4
  • 8
    • 0027349625 scopus 로고
    • Purification of extensin from cell walls of tomato (hybrid of Lycopersicon esculentum and Lycopersicon peruvianum) cells in suspension-culture
    • Brownleader, M.D. and Dey, P.M. (1993) Purification of extensin from cell walls of tomato (hybrid of Lycopersicon esculentum and Lycopersicon peruvianum) cells in suspension-culture. Planta, 191, 457-469.
    • (1993) Planta , vol.191 , pp. 457-469
    • Brownleader, M.D.1    Dey, P.M.2
  • 9
    • 0002625707 scopus 로고
    • A pectin lyase inhibitor protein from cell walls of sugar beet
    • Bugbee, W.M. (1993) A pectin lyase inhibitor protein from cell walls of sugar beet. Phytopathology, 83, 63-68.
    • (1993) Phytopathology , vol.83 , pp. 63-68
    • Bugbee, W.M.1
  • 10
    • 0012888474 scopus 로고    scopus 로고
    • Kiwi protein inhibitor of pectin methylesterase amino-acid sequence and structural importance of two disulfide bridges
    • Camardella, L., Carratore, V., Ciardiello, M.A., Servillo, L., Balestrieri, C. and Giovane, A. (2000) Kiwi protein inhibitor of pectin methylesterase amino-acid sequence and structural importance of two disulfide bridges. Eur. J. Biochem. 267, 4561-4565.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 4561-4565
    • Camardella, L.1    Carratore, V.2    Ciardiello, M.A.3    Servillo, L.4    Balestrieri, C.5    Giovane, A.6
  • 11
    • 0034144554 scopus 로고    scopus 로고
    • Auxin-regulated genes encoding cell wall-modifying proteins are expressed during early tomato fruit growth
    • Catalá, C., Rose, J.K.C. and Bennett, A.B. (2000) Auxin-regulated genes encoding cell wall-modifying proteins are expressed during early tomato fruit growth. Plant Physiol. 122, 527-534.
    • (2000) Plant Physiol. , vol.122 , pp. 527-534
    • Catalá, C.1    Rose, J.K.C.2    Bennett, A.B.3
  • 12
    • 0035202023 scopus 로고    scopus 로고
    • Characterization of a tomato xyloglucan endotransglycosylase gene that is down-regulated by auxin in etiolated hypocotyls
    • Catalá, C., Rose, J.K.C., York, W.S., Albersheim, P., Darvill, A.G. and Bennett, A.B. (2001) Characterization of a tomato xyloglucan endotransglycosylase gene that is down-regulated by auxin in etiolated hypocotyls. Plant Physiol. 127, 1180-1192.
    • (2001) Plant Physiol. , vol.127 , pp. 1180-1192
    • Catalá, C.1    Rose, J.K.C.2    York, W.S.3    Albersheim, P.4    Darvill, A.G.5    Bennett, A.B.6
  • 13
    • 0343742570 scopus 로고    scopus 로고
    • Purification and characterization of basic proteins with in vitro antifungal activity from seeds of cotton, Gossypium hirsutum
    • Chung, R.P.T., Neumann, G.M. and Polya, G.M. (1997) Purification and characterization of basic proteins with in vitro antifungal activity from seeds of cotton, Gossypium hirsutum. Plant Sci. 127, 1-16.
    • (1997) Plant Sci. , vol.127 , pp. 1-16
    • Chung, R.P.T.1    Neumann, G.M.2    Polya, G.M.3
  • 14
    • 0033180109 scopus 로고    scopus 로고
    • Fungal polygalacturonases exhibit different substrate degradation patterns and differ in their susceptibilities to polygalacturonase-inhibiting proteins
    • Cook, B.J., Clay, R.P., Bergmann, C.W., Albersheim, P. and Darvill, A.G. (1999) Fungal polygalacturonases exhibit different substrate degradation patterns and differ in their susceptibilities to polygalacturonase-inhibiting proteins. Mol. Plant Microbe Interact. 12, 703-711.
    • (1999) Mol. Plant Microbe Interact. , vol.12 , pp. 703-711
    • Cook, B.J.1    Clay, R.P.2    Bergmann, C.W.3    Albersheim, P.4    Darvill, A.G.5
  • 15
    • 0028721071 scopus 로고
    • Oligosaccharins: Structures and signal transduction
    • Côté, F. and Hahn, M.G. (1994) Oligosaccharins: structures and signal transduction. Plant Mol. Biol. 26, 1379-1411.
    • (1994) Plant Mol. Biol. , vol.26 , pp. 1379-1411
    • Côté, F.1    Hahn, M.G.2
  • 16
    • 0001973467 scopus 로고    scopus 로고
    • Carbohydrate-active enzymes: An integrated database approach
    • (Gilbert, H.J., Davies, G., Henrissat, B. and Svensson, B., eds). Cambridge: The Royal Society of Chemistry
    • Coutinho, P.M. and Henrissat, B. (1999) Carbohydrate-active enzymes: an integrated database approach. In Recent Advances in Carbohydrate Bioengineering (Gilbert, H.J., Davies, G., Henrissat, B. and Svensson, B., eds). Cambridge: The Royal Society of Chemistry, pp. 3-12.
    • (1999) Recent Advances in Carbohydrate Bioengineering , pp. 3-12
    • Coutinho, P.M.1    Henrissat, B.2
  • 17
    • 0034789069 scopus 로고    scopus 로고
    • The role of polygalacturonase-inhibiting proteins (PGIPS) in defense against pathogenic fungi
    • De Lorenzo, G., D'Ovidio, R. and Cervone, F. (2001) The role of polygalacturonase-inhibiting proteins (PGIPS) in defense against pathogenic fungi. Annu. Rev. Phytopathol. 39, 313-335.
    • (2001) Annu. Rev. Phytopathol. , vol.39 , pp. 313-335
    • De Lorenzo, G.1    D'Ovidio, R.2    Cervone, F.3
  • 18
    • 0002186110 scopus 로고    scopus 로고
    • Triticum aestivum xylanase inhibitor (TAXI), a new class of enzyme inhibitor affecting breadmaking performance
    • Debyser, W., Peumans, W.J., Van Damme, E.J.M. and Delcour, J.A. (1999) Triticum aestivum xylanase inhibitor (TAXI), a new class of enzyme inhibitor affecting breadmaking performance. J. Cereal Sci. 30, 39-43.
    • (1999) J. Cereal Sci. , vol.30 , pp. 39-43
    • Debyser, W.1    Peumans, W.J.2    Van Damme, E.J.M.3    Delcour, J.A.4
  • 19
    • 0001586670 scopus 로고
    • Inactivation of multiple virulence genes reduces the ability of Pseudomonas solanacearum to cause wilt symptoms
    • Denny, T.P., Carney, B.F. and Schell, M.A. (1990) Inactivation of multiple virulence genes reduces the ability of Pseudomonas solanacearum to cause wilt symptoms. Mol. Plant Microbe Interact. 3, 293-300.
    • (1990) Mol. Plant Microbe Interact. , vol.3 , pp. 293-300
    • Denny, T.P.1    Carney, B.F.2    Schell, M.A.3
  • 20
    • 0035845495 scopus 로고    scopus 로고
    • Plant gene expression response to Agrobacterium tumefaciens
    • Ditt, R.F., Nester, E.W. and Comai, L. (2001) Plant gene expression response to Agrobacterium tumefaciens. Proc. Natl. Acad. Sci. USA, 98, 10954-10959.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 10954-10959
    • Ditt, R.F.1    Nester, E.W.2    Comai, L.3
  • 22
    • 0028852399 scopus 로고
    • Lectin-like activity of lupin seed conglutin γ, a glycoprotein previously referred to as a storage protein
    • Duranti, M., Gius, C. and Scarafoni, A. (1995) Lectin-like activity of lupin seed conglutin γ, a glycoprotein previously referred to as a storage protein. J. Exp. Bot. 46, 725-728.
    • (1995) J. Exp. Bot. , vol.46 , pp. 725-728
    • Duranti, M.1    Gius, C.2    Scarafoni, A.3
  • 23
    • 0028232944 scopus 로고
    • Heat-induced synthesis and tunicamycin-sensitive secretion of the putative storage glycoprotein conglutin γ from mature lupin seeds
    • Duranti, M., Scarafoni, A., Gius, C., Negri, A. and Faoro, F. (1994) Heat-induced synthesis and tunicamycin-sensitive secretion of the putative storage glycoprotein conglutin γ from mature lupin seeds. Eur. J. Biochem. 222, 387-393.
    • (1994) Eur. J. Biochem. , vol.222 , pp. 387-393
    • Duranti, M.1    Scarafoni, A.2    Gius, C.3    Negri, A.4    Faoro, F.5
  • 24
    • 0017475566 scopus 로고
    • Amino acid sequence of smaller subunit of conglutin ã, a storage globulin of Lupinus angustifolius
    • Elleman, T.C. (1977) Amino acid sequence of smaller subunit of conglutin ã, a storage globulin of Lupinus angustifolius. Aust. J. Biol. Sci. 30, 33-45.
    • (1977) Aust. J. Biol. Sci. , vol.30 , pp. 33-45
    • Elleman, T.C.1
  • 25
    • 0037157113 scopus 로고    scopus 로고
    • Functional identification of the cDNA coding for a wheat endo-1,4-beta-D-xyla nase inhibitor
    • Elliott, G.O., Hughes, R.K., Juge, N., Kroon, P.A. and Williamson, G. (2002) Functional identification of the cDNA coding for a wheat endo-1,4-beta-D-xyla nase inhibitor. FEBS Lett. 519, 66-70.
    • (2002) FEBS Lett. , vol.519 , pp. 66-70
    • Elliott, G.O.1    Hughes, R.K.2    Juge, N.3    Kroon, P.A.4    Williamson, G.5
  • 26
    • 0000648333 scopus 로고
    • Specific and abundant secretion of a novel hydroxyproline-rich glycoprotein from salt-adapted winged bean cells
    • Esaka, M., Hayakawa, H., Hashimoto, M. and Matsubara, N. (1992) Specific and abundant secretion of a novel hydroxyproline-rich glycoprotein from salt-adapted winged bean cells. Plant Physiol. 100, 1339-1345.
    • (1992) Plant Physiol. , vol.100 , pp. 1339-1345
    • Esaka, M.1    Hayakawa, H.2    Hashimoto, M.3    Matsubara, N.4
  • 27
    • 0035863101 scopus 로고    scopus 로고
    • Triticum aestivum L. endoxylanase inhibitor (TAXI) consists of two inhibitors, TAXI I and TAXI II, with different specificities
    • Gebruers, K., Debyser, W., Goesaert, H., Proost, P., Van Damme, J. and Delcour, J.A. (2001) Triticum aestivum L. endoxylanase inhibitor (TAXI) consists of two inhibitors, TAXI I and TAXI II, with different specificities. Biochem. J. 353, 239-244.
    • (2001) Biochem. J. , vol.353 , pp. 239-244
    • Gebruers, K.1    Debyser, W.2    Goesaert, H.3    Proost, P.4    Van Damme, J.5    Delcour, J.A.6
  • 28
    • 0028808263 scopus 로고
    • A glycoprotein inhibitor of pectin methylesterase in kiwi fruit. Purification by affinity chromatography and evidence of a ripening-related precursor
    • Giovane, A., Balestrieri, C., Quagliuolo, L., Castaldo, D. and Servillo, L. (1995) A glycoprotein inhibitor of pectin methylesterase in kiwi fruit. Purification by affinity chromatography and evidence of a ripening-related precursor. Eur. J. Biochem. 233, 926-929.
    • (1995) Eur. J. Biochem. , vol.233 , pp. 926-929
    • Giovane, A.1    Balestrieri, C.2    Quagliuolo, L.3    Castaldo, D.4    Servillo, L.5
  • 30
    • 0030887368 scopus 로고    scopus 로고
    • Fungal pathogens secrete an inhibitor protein that distinguishes isoforms of plant pathogenesis-related endo-β-1,3-glucanases
    • Ham, K.-S., Wu, S.C., Darvill, A.G. and Albersheim, P. (1997) Fungal pathogens secrete an inhibitor protein that distinguishes isoforms of plant pathogenesis-related endo-β-1,3-glucanases. Plant J. 11, 169-179.
    • (1997) Plant J. , vol.11 , pp. 169-179
    • Ham, K.-S.1    Wu, S.C.2    Darvill, A.G.3    Albersheim, P.4
  • 31
    • 0029929874 scopus 로고    scopus 로고
    • Updating the sequence-based classification of glycosyl hydrolases
    • Henrissat, B. and Bairoch, A. (1996) Updating the sequence-based classification of glycosyl hydrolases. Biochem. J. 316, 695-696.
    • (1996) Biochem. J. , vol.316 , pp. 695-696
    • Henrissat, B.1    Bairoch, A.2
  • 32
    • 0030994829 scopus 로고    scopus 로고
    • Characterization of a tobacco extensin gene and regulation of its gene family in healthy plants and under various stress conditions
    • Hirsinger, C., Parmentier, Y., Durr, A., Fleck, J. and Jamet, E. (1997) Characterization of a tobacco extensin gene and regulation of its gene family in healthy plants and under various stress conditions. Plant Mol. Biol. 33, 279-289.
    • (1997) Plant Mol. Biol. , vol.33 , pp. 279-289
    • Hirsinger, C.1    Parmentier, Y.2    Durr, A.3    Fleck, J.4    Jamet, E.5
  • 33
    • 0003000268 scopus 로고    scopus 로고
    • Breaching the outer barriers - Cuticle and cell wall penetration
    • (Carroll, G.C. and Tudzynski, P., eds). Berlin: Springer-Verlag
    • Howard, R.J. (1997) Breaching the outer barriers - cuticle and cell wall penetration. In The Mycota. V. Plant Relationships, Part A (Carroll, G.C. and Tudzynski, P., eds). Berlin: Springer-Verlag, pp. 43-60.
    • (1997) The Mycota. V. Plant Relationships, Part A , pp. 43-60
    • Howard, R.J.1
  • 34
    • 0034045514 scopus 로고    scopus 로고
    • The endo-β-1,4-glucanase CelA of Clavibacter michiganensis subsp, michiganensis is a pathogenicity determinant required for induction of bacterial wilt of tomato
    • Jahr, H., Dreier, J., Meletzus, D., Bahro, R. and Eichenlaub, R. (2000) The endo-β-1,4-glucanase CelA of Clavibacter michiganensis subsp, michiganensis is a pathogenicity determinant required for induction of bacterial wilt of tomato. Mol. Plant Microbe Interact. 13, 703-714.
    • (2000) Mol. Plant Microbe Interact. , vol.13 , pp. 703-714
    • Jahr, H.1    Dreier, J.2    Meletzus, D.3    Bahro, R.4    Eichenlaub, R.5
  • 35
    • 79957949748 scopus 로고    scopus 로고
    • Sample preparation for MALDI mass analysis of peptides and proteins
    • (Coligan, J.E., ed.). Brooklyn, NY: Wiley
    • Jiménez, C.R., Huang, L., Qiu, Y. and Burlingame, A.L. (1998) Sample preparation for MALDI mass analysis of peptides and proteins. In Current Protocols in Protein Science (Coligan, J.E., ed.). Brooklyn, NY: Wiley, pp. 16.3.1-16.3.6.
    • (1998) Current Protocols in Protein Science , pp. 1631-1636
    • Jiménez, C.R.1    Huang, L.2    Qiu, Y.3    Burlingame, A.L.4
  • 36
    • 0024430203 scopus 로고
    • Sequence of a cDNA encoding soybean basic 7S globulin
    • Kagawa, H. and Hirano, H. (1989) Sequence of a cDNA encoding soybean basic 7S globulin. Nucl. Acids Res. 17, 8868.
    • (1989) Nucl. Acids Res. , vol.17 , pp. 8868
    • Kagawa, H.1    Hirano, H.2
  • 37
    • 38249034876 scopus 로고
    • Soybean Basic 7 S globulin represents a protein widely distributed in legume species
    • Kagawa, H., Yamauchi, F. and Hirano, H. (1987) Soybean Basic 7 S globulin represents a protein widely distributed in legume species. FEBS Lett. 226, 145-149.
    • (1987) FEBS Lett. , vol.226 , pp. 145-149
    • Kagawa, H.1    Yamauchi, F.2    Hirano, H.3
  • 38
    • 0028137399 scopus 로고
    • Dramatically reduced virulence of mutants of Pseudomonas solanacearum defective in export of extracellular proteins across the outer membrane
    • Kang, Y.W., Huang, J.Z., Mao, G.Z., He, L.Y. and Schell, M.A. (1994) Dramatically reduced virulence of mutants of Pseudomonas solanacearum defective in export of extracellular proteins across the outer membrane. Mol. Plant Microbe Interact. 7, 370-377.
    • (1994) Mol. Plant Microbe Interact. , vol.7 , pp. 370-377
    • Kang, Y.W.1    Huang, J.Z.2    Mao, G.Z.3    He, L.Y.4    Schell, M.A.5
  • 40
    • 0027350951 scopus 로고
    • Structure of the cDNA coding for conglutin γ, a sulfur-rich protein from Lupinus angustifolius
    • Kolivas, S. and Gayler, K.R. (1993) Structure of the cDNA coding for conglutin γ, a sulfur-rich protein from Lupinus angustifolius. Plant Mol. Biol. 21, 397-401.
    • (1993) Plant Mol. Biol. , vol.21 , pp. 397-401
    • Kolivas, S.1    Gayler, K.R.2
  • 41
    • 0026060468 scopus 로고
    • Plant basic 7S globulin-like proteins have insulin and insulin-like growth factor binding activity
    • Komatsu, S. and Hirano, H. (1991) Plant basic 7S globulin-like proteins have insulin and insulin-like growth factor binding activity. FEBS Lett. 294, 210-212.
    • (1991) FEBS Lett. , vol.294 , pp. 210-212
    • Komatsu, S.1    Hirano, H.2
  • 42
    • 0032080157 scopus 로고    scopus 로고
    • Evidence for secretion of vacuolar α-mannosidase, class I chitinase, and class I β-1,3-glucanase in suspension cultures of tobacco cells
    • Kunze, I., Kunze, G., Broker, M., Manteuffel, R., Meins, F., Jr and Muntz, K. (1998) Evidence for secretion of vacuolar α-mannosidase, class I chitinase, and class I β-1,3-glucanase in suspension cultures of tobacco cells. Planta, 205, 92-99.
    • (1998) Planta , vol.205 , pp. 92-99
    • Kunze, I.1    Kunze, G.2    Broker, M.3    Manteuffel, R.4    Meins F., Jr.5    Muntz, K.6
  • 43
    • 0034793521 scopus 로고    scopus 로고
    • Life behind cell walls: Paradigm lost, paradigm regained
    • Lamport, D.T.A. (2001) Life behind cell walls: paradigm lost, paradigm regained. Cell Mol. Life Sci. 58, 1363-1385.
    • (2001) Cell Mol. Life Sci. , vol.58 , pp. 1363-1385
    • Lamport, D.T.A.1
  • 44
    • 0001593842 scopus 로고
    • Hydroxyproline in primary cell walls of higher plants
    • Lamport, D.T.A. and Northcote, D.H. (1960) Hydroxyproline in primary cell walls of higher plants. Nature, 188, 665-666.
    • (1960) Nature , vol.188 , pp. 665-666
    • Lamport, D.T.A.1    Northcote, D.H.2
  • 45
    • 0024115579 scopus 로고
    • Characterization of β-fructosidase, an extracellular glycoprotein of carrot cells
    • Lauriere, C., Lauriere, M., Sturm, A., Faye, L. and Chrispeels, M.J. (1988) Characterization of β-fructosidase, an extracellular glycoprotein of carrot cells. Biochimie, 70, 1483-1491.
    • (1988) Biochimie , vol.70 , pp. 1483-1491
    • Lauriere, C.1    Lauriere, M.2    Sturm, A.3    Faye, L.4    Chrispeels, M.J.5
  • 46
    • 0015333650 scopus 로고
    • New reaction for colorimetric determination of carbohydrates
    • Lever, M. (1972) New reaction for colorimetric determination of carbohydrates. Anal. Biochem. 47, 273-279.
    • (1972) Anal. Biochem. , vol.47 , pp. 273-279
    • Lever, M.1
  • 47
    • 0028960275 scopus 로고
    • Structure and regulation of the Erwinia carotovora subspecies carotovora SCC3193 cellulase gene CelV1 and the role of cellulase in phytopathogenicity
    • Mae, A., Heikinheimo, R. and Palva, E.T. (1995) Structure and regulation of the Erwinia carotovora subspecies carotovora SCC3193 cellulase gene CelV1 and the role of cellulase in phytopathogenicity. Mol. Gen. Genet. 247, 17-26.
    • (1995) Mol. Gen. Genet. , vol.247 , pp. 17-26
    • Mae, A.1    Heikinheimo, R.2    Palva, E.T.3
  • 49
    • 0019321718 scopus 로고
    • Rapid isolation of high molecular weight plant DNA
    • Murray, M.G. and Thompson, W.F. (1980) Rapid isolation of high molecular weight plant DNA. Nucl. Acids Res. 8, 4321-4325.
    • (1980) Nucl. Acids Res. , vol.8 , pp. 4321-4325
    • Murray, M.G.1    Thompson, W.F.2
  • 50
    • 0032942942 scopus 로고    scopus 로고
    • A xyloglucan-specific endo-β-1,4-glucanase from Aspergillus aculeatus: Expression cloning in yeast, purification and characterization of the recombinant enzyme
    • Pauly, M., Andersen, L.N., Kauppinen, S., Kofod, L.V., York, W.S., Albersheim, P. and Darvill, A. (1999) A xyloglucan-specific endo-β-1,4-glucanase from Aspergillus aculeatus: expression cloning in yeast, purification and characterization of the recombinant enzyme. Glycobiology, 9, 93-100.
    • (1999) Glycobiology , vol.9 , pp. 93-100
    • Pauly, M.1    Andersen, L.N.2    Kauppinen, S.3    Kofod, L.V.4    York, W.S.5    Albersheim, P.6    Darvill, A.7
  • 51
    • 0035032504 scopus 로고    scopus 로고
    • Changes in the structure of xyloglucan during cell elongation
    • Pauly, M., Qin, Q., Greene, H., Albersheim, P., Darvill, A. and York, W.S. (2001) Changes in the structure of xyloglucan during cell elongation. Planta, 212, 842-850.
    • (2001) Planta , vol.212 , pp. 842-850
    • Pauly, M.1    Qin, Q.2    Greene, H.3    Albersheim, P.4    Darvill, A.5    York, W.S.6
  • 54
    • 0033965855 scopus 로고    scopus 로고
    • The TIGR gene indices: Reconstruction and representation of expressed gene sequences
    • Quackenbush, J., Liang, F., Holt, I., Pertea, G. and Upton, J. (2000) The TIGR gene indices: reconstruction and representation of expressed gene sequences. Nucl. Acids Res. 28, 141-145.
    • (2000) Nucl. Acids Res. , vol.28 , pp. 141-145
    • Quackenbush, J.1    Liang, F.2    Holt, I.3    Pertea, G.4    Upton, J.5
  • 55
    • 0023989865 scopus 로고
    • Cloning of the egl gene of Pseudomonas solanacearum and analysis of its role in phytopathogenicity
    • Roberts, D.P., Denny, T.P. and Schell, M.A. (1988) Cloning of the egl gene of Pseudomonas solanacearum and analysis of its role in phytopathogenicity. J. Bacteriol. 170, 1445-1451.
    • (1988) J. Bacteriol. , vol.170 , pp. 1445-1451
    • Roberts, D.P.1    Denny, T.P.2    Schell, M.A.3
  • 56
    • 0030087686 scopus 로고    scopus 로고
    • Two divergent xyloglucan endotransglycosylases exhibit mutually exclusive patterns of expression in Nasturtium
    • Rose, J.K.C., Brummell, D.A. and Bennett, A.B. (1996) Two divergent xyloglucan endotransglycosylases exhibit mutually exclusive patterns of expression in Nasturtium. Plant Physiol. 110, 493-499.
    • (1996) Plant Physiol. , vol.110 , pp. 493-499
    • Rose, J.K.C.1    Brummell, D.A.2    Bennett, A.B.3
  • 57
    • 0035983846 scopus 로고    scopus 로고
    • Molecular cloning and characterization of glucanase inhibitor proteins: Coevolution of a counterdefense mechanism by plant pathogens
    • Rose, J.K.C., Ham, K.-S., Darvill, A.G. and Albersheim, P. (2002) Molecular cloning and characterization of glucanase inhibitor proteins: coevolution of a counterdefense mechanism by plant pathogens. Plant Cell, 14, 1329-1345.
    • (2002) Plant Cell , vol.14 , pp. 1329-1345
    • Rose, J.K.C.1    Ham, K.-S.2    Darvill, A.G.3    Albersheim, P.4
  • 58
    • 0030995515 scopus 로고    scopus 로고
    • Expression of a divergent expansin gene is fruit-specific and ripening-regulated
    • Rose, J.K.C., Lee, H.H. and Bennett, A.B. (1997) Expression of a divergent expansin gene is fruit-specific and ripening-regulated. Proc. Natl. Acad. Sci. USA, 94, 5955-5960.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 5955-5960
    • Rose, J.K.C.1    Lee, H.H.2    Bennett, A.B.3
  • 59
    • 0002360454 scopus 로고    scopus 로고
    • Evidence for the presence of a pentosanase inhibitor in wheat flours
    • Rouau, X. and Surget, A. (1998) Evidence for the presence of a pentosanase inhibitor in wheat flours. J. Cereal Sci. 28, 63-70.
    • (1998) J. Cereal Sci. , vol.28 , pp. 63-70
    • Rouau, X.1    Surget, A.2
  • 60
    • 0030729924 scopus 로고    scopus 로고
    • Role of extracellular polysaccharide and endoglucanase in root invasion and colonization of tomato plants by Ralstonia solanacearum
    • Saile, E., McGarvey, J.A., Schell, M.A. and Denny, T.P. (1997) Role of extracellular polysaccharide and endoglucanase in root invasion and colonization of tomato plants by Ralstonia solanacearum. Phytopathology, 87, 1264-1271.
    • (1997) Phytopathology , vol.87 , pp. 1264-1271
    • Saile, E.1    McGarvey, J.A.2    Schell, M.A.3    Denny, T.P.4
  • 61
    • 0001603180 scopus 로고
    • Purification of GP57, and auxin-regulated extracellular glycoprotein of carrots, and its immunocytochemical localization in dermal tissues
    • Satoh, S. and Fujii, T. (1988) Purification of GP57, and auxin-regulated extracellular glycoprotein of carrots, and its immunocytochemical localization in dermal tissues. Planta, 175, 364-373.
    • (1988) Planta , vol.175 , pp. 364-373
    • Satoh, S.1    Fujii, T.2
  • 62
    • 0000368835 scopus 로고
    • cDNA cloning of an extracellular dermal glycoprotein of carrot and its expression in response to wounding
    • Satoh, S., Sturm, A., Fujii, T. and Chrispeels, M.J. (1992) cDNA cloning of an extracellular dermal glycoprotein of carrot and its expression in response to wounding. Planta, 188, 432-438.
    • (1992) Planta , vol.188 , pp. 432-438
    • Satoh, S.1    Sturm, A.2    Fujii, T.3    Chrispeels, M.J.4
  • 63
    • 0030131115 scopus 로고    scopus 로고
    • Isolation of pl 4.6 extensin peroxidase from tomato cell suspension cultures and identification of Val-Tyr-Lys as putative intermolecutar cross-link site
    • Schnabelrauch, L.S., Kieliszewski, M., Upham, B.L., Alizedeh, H. and Lamport, D.T.A. (1996) Isolation of pl 4.6 extensin peroxidase from tomato cell suspension cultures and identification of Val-Tyr-Lys as putative intermolecutar cross-link site. Plant J. 9, 477-489.
    • (1996) Plant J. , vol.9 , pp. 477-489
    • Schnabelrauch, L.S.1    Kieliszewski, M.2    Upham, B.L.3    Alizedeh, H.4    Lamport, D.T.A.5
  • 65
    • 0035675616 scopus 로고    scopus 로고
    • Oligosaccharide signaling for defence responses in plant
    • Shibuya, N. and Minami, E. (2001) Oligosaccharide signaling for defence responses in plant. Physiol. Mol. Plant Pathol. 59, 223-233.
    • (2001) Physiol. Mol. Plant Pathol. , vol.59 , pp. 223-233
    • Shibuya, N.1    Minami, E.2
  • 66
    • 0001513502 scopus 로고
    • Isolation of extensin precursors by direct elution of intact tomato cell suspension cultures
    • Smith, J.J., Muldoon, E.P. and Lamport, D.T.A. (1984) Isolation of extensin precursors by direct elution of intact tomato cell suspension cultures. Phytochemistry, 23, 1233-1239.
    • (1984) Phytochemistry , vol.23 , pp. 1233-1239
    • Smith, J.J.1    Muldoon, E.P.2    Lamport, D.T.A.3
  • 68
    • 0035199524 scopus 로고    scopus 로고
    • Aspergillus enzymes involved in degradation of plant cell wall polysaccharides
    • de Vries, R.P. and Visser, J. (2001) Aspergillus enzymes involved in degradation of plant cell wall polysaccharides. Microbiol. Mol. Biol. Rep. 65, 497-522.
    • (2001) Microbiol. Mol. Biol. Rep. , vol.65 , pp. 497-522
    • De Vries, R.P.1    Visser, J.2
  • 69
    • 0027966841 scopus 로고
    • The major secreted cellulase, CelV, of Erwinia carotovora ssp. carotovora is an important soft rot virulence factor
    • Walker, D.S., Reeves, P.J. and Salmond, G.P.C. (1994) The major secreted cellulase, CelV, of Erwinia carotovora ssp. carotovora is an important soft rot virulence factor. Mol. Plant Microbe Interact. 7, 425-431.
    • (1994) Mol. Plant Microbe Interact. , vol.7 , pp. 425-431
    • Walker, D.S.1    Reeves, P.J.2    Salmond, G.P.C.3
  • 70
    • 0028007674 scopus 로고
    • Deconstructing the cell wall
    • Walton, J.D. (1994) Deconstructing the cell wall. Plant Physiol. 104, 1113-1118.
    • (1994) Plant Physiol. , vol.104 , pp. 1113-1118
    • Walton, J.D.1
  • 71
    • 0031610745 scopus 로고    scopus 로고
    • Secretion of stress-related proteins by suspension-cultured Lupinus atbus cells
    • Wojtaszek, P., Pislewska, M., Bolwell, G.P. and Stobiecki, M. (1998) Secretion of stress-related proteins by suspension-cultured Lupinus atbus cells. Acta Biochim. Pol. 45, 281-285.
    • (1998) Acta Biochim. Pol. , vol.45 , pp. 281-285
    • Wojtaszek, P.1    Pislewska, M.2    Bolwell, G.P.3    Stobiecki, M.4
  • 72
    • 0034835925 scopus 로고    scopus 로고
    • A fungal endoglucanase with plant cell wall extension activity
    • Yuan, S., Wu, Y.J. and Cosgrove, D.J. (2001) A fungal endoglucanase with plant cell wall extension activity. Plant Physiol. 127, 324-333.
    • (2001) Plant Physiol. , vol.127 , pp. 324-333
    • Yuan, S.1    Wu, Y.J.2    Cosgrove, D.J.3


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