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Volumn 168, Issue 5, 2005, Pages 1211-1220

Expression of the soybean (Kunitz) trypsin inhibitor in leaves of white clover (Trifolium repens L.)

Author keywords

Insect pest resistance; Soybean (Kunitz) trypsin inhibitor; Transgenic white clover; Trifolium repens L.

Indexed keywords

COLUMN CHROMATOGRAPHY; DNA; ELECTROPHORESIS; ENZYME INHIBITION; FRUITS; GENES; MONOCLONAL ANTIBODIES; TISSUE;

EID: 15744385503     PISSN: 01689452     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.plantsci.2004.12.020     Document Type: Article
Times cited : (16)

References (60)
  • 2
    • 0027950625 scopus 로고
    • Accumulation of a chymotrypsin inhibitor in transgenic tobacco can affect the growth of insect pests
    • M.T. McManus, D.W.R. White, and P.G. McGregor Accumulation of a chymotrypsin inhibitor in transgenic tobacco can affect the growth of insect pests Trans. Res. 3 1994 50 58
    • (1994) Trans. Res. , vol.3 , pp. 50-58
    • McManus, M.T.1    White, D.W.R.2    McGregor, P.G.3
  • 3
    • 0029670583 scopus 로고
    • Transgenic rice plants harboring an introduced potato proteinase inhibitor II gene are insect resistant
    • X. Duan, X. Li, Q. Xue, M. Abo-El-Saad, D. Xu, and R. Wu Transgenic rice plants harboring an introduced potato proteinase inhibitor II gene are insect resistant Nat. Biotechnol. 14 1995 494 498
    • (1995) Nat. Biotechnol. , vol.14 , pp. 494-498
    • Duan, X.1    Li, X.2    Xue, Q.3    Abo-El-Saad, M.4    Xu, D.5    Wu, R.6
  • 4
    • 0001552465 scopus 로고    scopus 로고
    • Constitutive expression of a cowpea trypsin inhibitor gene, CpTi, in transgenic rice plants confers resistance to two major rice insect pests
    • D. Xu, Q. Xue, D. McElroy, Y. Mawal, V.A. Hilder, and R. Wu Constitutive expression of a cowpea trypsin inhibitor gene, CpTi, in transgenic rice plants confers resistance to two major rice insect pests Mol. Breed. 2 1996 167 173
    • (1996) Mol. Breed. , vol.2 , pp. 167-173
    • Xu, D.1    Xue, Q.2    McElroy, D.3    Mawal, Y.4    Hilder, V.A.5    Wu, R.6
  • 7
    • 0000051893 scopus 로고    scopus 로고
    • Opposite effects on Spodoptera littoralis larvae of high expression level of a trypsin proteinase inhibitor in transgenic plants
    • F. De Leo, M.A. Bonade-Bottino, L.R. Cecil, R. Gallerani, and L. Jouanin Opposite effects on Spodoptera littoralis larvae of high expression level of a trypsin proteinase inhibitor in transgenic plants Plant Physiol. 118 1998 997 1004
    • (1998) Plant Physiol. , vol.118 , pp. 997-1004
    • De Leo, F.1    Bonade-Bottino, M.A.2    Cecil, L.R.3    Gallerani, R.4    Jouanin, L.5
  • 8
    • 0032840597 scopus 로고    scopus 로고
    • Transgenic tobacco and peas expressing a proteinase inhibitor from Nicotiana alata have increased insect resistance
    • J.A. Charity, M.A. Anderson, D.J. Bittisnich, M. Whitecross, and T.J.V. Higgins Transgenic tobacco and peas expressing a proteinase inhibitor from Nicotiana alata have increased insect resistance Mol. Breed. 5 1999 357 365
    • (1999) Mol. Breed. , vol.5 , pp. 357-365
    • Charity, J.A.1    Anderson, M.A.2    Bittisnich, D.J.3    Whitecross, M.4    Higgins, T.J.V.5
  • 9
    • 0010763149 scopus 로고    scopus 로고
    • Soybean Kunitz trypsin inhibitor (SKTI) confers resistance to the brown planthopper (Nilaparvata lugens Stål) in transgenic rice
    • S.I. Lee, S.-H. Lee, J.C. Koo, H.J. Chun, C.O. Lim, J.H. Mun, Y.H. Song, and M.J. Cho Soybean Kunitz trypsin inhibitor (SKTI) confers resistance to the brown planthopper (Nilaparvata lugens Stål) in transgenic rice Mol. Breed. 5 1999 1 9
    • (1999) Mol. Breed. , vol.5 , pp. 1-9
    • Lee, S.I.1    Lee, S.-H.2    Koo, J.C.3    Chun, H.J.4    Lim, C.O.5    Mun, J.H.6    Song, Y.H.7    Cho, M.J.8
  • 10
    • 0033796758 scopus 로고    scopus 로고
    • Soybean Kunitz, C-II and PI-IV inhibitor genes confer different levels of insect resistance to tobacco and potato transgenic plants
    • S. Marchetti, M. Delledonne, C. Fogher, C. Chiaba, F. Chiesa, F. Savazzini, and A. Giordano Soybean Kunitz, C-II and PI-IV inhibitor genes confer different levels of insect resistance to tobacco and potato transgenic plants Theor. Appl. Genet. 101 2000 510 526
    • (2000) Theor. Appl. Genet. , vol.101 , pp. 510-526
    • Marchetti, S.1    Delledonne, M.2    Fogher, C.3    Chiaba, C.4    Chiesa, F.5    Savazzini, F.6    Giordano, A.7
  • 13
    • 0038398775 scopus 로고    scopus 로고
    • Transgenic expression of trypsin inhibitor Cme from barley in indica and japonica rice, confers resistance to the rice weevil Sitophilus oryzae
    • J. Alfonso-Rubi, F. Ortego, P. Castanera, P. Carbonero, and I. Diaz Transgenic expression of trypsin inhibitor Cme from barley in indica and japonica rice, confers resistance to the rice weevil Sitophilus oryzae Trans. Res. 12 2003 23 31
    • (2003) Trans. Res. , vol.12 , pp. 23-31
    • Alfonso-Rubi, J.1    Ortego, F.2    Castanera, P.3    Carbonero, P.4    Diaz, I.5
  • 14
    • 0042567521 scopus 로고    scopus 로고
    • Expression of soybean proteinase inhibitors in transgenic sugarcane plants: Effects on natural defence against Diatraea saccharalis
    • M.C. Falco, and M.C. Silva-Filho Expression of soybean proteinase inhibitors in transgenic sugarcane plants: effects on natural defence against Diatraea saccharalis Plant Physiol. Biochem. 41 2003 761 766
    • (2003) Plant Physiol. Biochem. , vol.41 , pp. 761-766
    • Falco, M.C.1    Silva-Filho, M.C.2
  • 15
    • 0036244341 scopus 로고    scopus 로고
    • Ultrastructural changes to the midgets of the black field cricket (Teleogryllus commodus) following ingestion of potato protease inhibitor II
    • P.W. Sutherland, E.P.J. Burgess, B.A. Philip, M.T. McManus, L. Watson, and J.T. Christeller Ultrastructural changes to the midgets of the black field cricket (Teleogryllus commodus) following ingestion of potato protease inhibitor II J. Insect Physiol. 48 2002 327 336
    • (2002) J. Insect Physiol. , vol.48 , pp. 327-336
    • Sutherland, P.W.1    Burgess, E.P.J.2    Philip, B.A.3    McManus, M.T.4    Watson, L.5    Christeller, J.T.6
  • 16
    • 0029128219 scopus 로고
    • Adaptation of Spodoptera exigua larvae to plant proteinase inhibitors by induction of gut proteinase activity insensitive to inhibition
    • M.A. Jongsma, P.L. Bakker, J. Peters, D. Bosch, and W.J. Stiekema Adaptation of Spodoptera exigua larvae to plant proteinase inhibitors by induction of gut proteinase activity insensitive to inhibition Proc. Natl. Acad. Sci. U.S.A. 92 1995 8041 8045
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 8041-8045
    • Jongsma, M.A.1    Bakker, P.L.2    Peters, J.3    Bosch, D.4    Stiekema, W.J.5
  • 17
    • 0001285211 scopus 로고    scopus 로고
    • Adaptation of Heliocoverpa armigera (Lepidoptera: Noctuidae) to a proteinase inhibitor expressed in transgenic tobacco
    • Y. Wu, D. Llewellyn, A. Mathews, and E.S. Dennis Adaptation of Heliocoverpa armigera (Lepidoptera: Noctuidae) to a proteinase inhibitor expressed in transgenic tobacco Mol. Breed. 3 1997 371 380
    • (1997) Mol. Breed. , vol.3 , pp. 371-380
    • Wu, Y.1    Llewellyn, D.2    Mathews, A.3    Dennis, E.S.4
  • 18
    • 0031981483 scopus 로고    scopus 로고
    • Regeneration of Populus nigra transgenic plants expressing a Kunitz proteinase inhibitor (Kti3) gene
    • M. Confalonieri, G. Allegro, A. Balestrazzi, C. Fogher, and M. Delledonne Regeneration of Populus nigra transgenic plants expressing a Kunitz proteinase inhibitor (Kti3) gene Mol. Breed. 4 1998 137 145
    • (1998) Mol. Breed. , vol.4 , pp. 137-145
    • Confalonieri, M.1    Allegro, G.2    Balestrazzi, A.3    Fogher, C.4    Delledonne, M.5
  • 19
    • 0033016160 scopus 로고    scopus 로고
    • Digestive proteolytic activity in larvae of tomato moth, Lacanobiao oleracea: Effects of plant protease inhibitors in vitro and in vivo
    • A.M.R. Gatehouse, E. Norton, G.M. Davison, S.M. Babbe, C.A. Newell, and J.A. Gatehouse Digestive proteolytic activity in larvae of tomato moth, Lacanobiao oleracea: effects of plant protease inhibitors in vitro and in vivo J. Insect Physiol. 45 1999 545 558
    • (1999) J. Insect Physiol. , vol.45 , pp. 545-558
    • Gatehouse, A.M.R.1    Norton, E.2    Davison, G.M.3    Babbe, S.M.4    Newell, C.A.5    Gatehouse, J.A.6
  • 20
    • 0033796274 scopus 로고    scopus 로고
    • Adaptation of Spodoptera exigua (Lepidoptera: Noctuidae) to barley trypsin inhibitor BTI-CMe expressed in transgenic tobacco
    • P. Lara, F. Ortego, E. Gonzalez-Hidalgo, P. Castanera, P. Carbonera, and I. Diaz Adaptation of Spodoptera exigua (Lepidoptera: Noctuidae) to barley trypsin inhibitor BTI-CMe expressed in transgenic tobacco Trans. Res. 9 2000 169 178
    • (2000) Trans. Res. , vol.9 , pp. 169-178
    • Lara, P.1    Ortego, F.2    Gonzalez-Hidalgo, E.3    Castanera, P.4    Carbonera, P.5    Diaz, I.6
  • 22
    • 0032126825 scopus 로고    scopus 로고
    • Two strains of cabbage seed weevil (Coleoptera: Curculionidae) exhibit differential susceptibility to a transgenic oilseed rape expressing oryzacystatin I
    • C. Girard, M. Bonade-Bottino, M.-H. Pham-Delegue, and L. Jouanin Two strains of cabbage seed weevil (Coleoptera: Curculionidae) exhibit differential susceptibility to a transgenic oilseed rape expressing oryzacystatin I J. Insect Physiol. 44 1998 569 577
    • (1998) J. Insect Physiol. , vol.44 , pp. 569-577
    • Girard, C.1    Bonade-Bottino, M.2    Pham-Delegue, M.-H.3    Jouanin, L.4
  • 23
    • 0033380120 scopus 로고    scopus 로고
    • Expression of the soybean (Kunitz) trypsin inhibitor in transgenic tobacco: Effects on larval development of Spodoptera litura
    • M.T. McManus, E.P.J. Burgess, B. Philip, L.M. Watson, W.A. Laing, C.R. Voisey, and D.W.R. White Expression of the soybean (Kunitz) trypsin inhibitor in transgenic tobacco: effects on larval development of Spodoptera litura Trans. Res. 8 1999 383 395
    • (1999) Trans. Res. , vol.8 , pp. 383-395
    • McManus, M.T.1    Burgess, E.P.J.2    Philip, B.3    Watson, L.M.4    Laing, W.A.5    Voisey, C.R.6    White, D.W.R.7
  • 24
    • 0036009743 scopus 로고    scopus 로고
    • The mustard trypsin inhibitor 2 affects the fertility of Spodoptera littoralis larvae fed on transgenic plants
    • F. De Leo, and R. Gallerani The mustard trypsin inhibitor 2 affects the fertility of Spodoptera littoralis larvae fed on transgenic plants Insect Biochem. Mol. Biol. 32 2002 489 496
    • (2002) Insect Biochem. Mol. Biol. , vol.32 , pp. 489-496
    • De Leo, F.1    Gallerani, R.2
  • 25
    • 0024755662 scopus 로고
    • Kunitz trypsin inhibitor genes are differentially expressed during the soybean life cycle and in transformed tobacco plants
    • K.D. Jofuku, and R.B. Goldberg Kunitz trypsin inhibitor genes are differentially expressed during the soybean life cycle and in transformed tobacco plants Plant Cell 1 1989 1079 1093
    • (1989) Plant Cell , vol.1 , pp. 1079-1093
    • Jofuku, K.D.1    Goldberg, R.B.2
  • 27
    • 0001071906 scopus 로고
    • Effects of protease inhibitor concentration and combinations on the survival, growth and gut enzyme activities of the black field cricket, Teleogryllus commodus
    • E.P.J. Burgess, C.A. Main, P.S. Stevens, J.T. Christeller, A.M.R. Gatehouse, and W.A. Laing Effects of protease inhibitor concentration and combinations on the survival, growth and gut enzyme activities of the black field cricket, Teleogryllus commodus J. Insect Physiol. 40 1994 803 811
    • (1994) J. Insect Physiol. , vol.40 , pp. 803-811
    • Burgess, E.P.J.1    Main, C.A.2    Stevens, P.S.3    Christeller, J.T.4    Gatehouse, A.M.R.5    Laing, W.A.6
  • 28
    • 46549092233 scopus 로고
    • Proteolysis of Kunitz soybean trypsin inhibitor during germination
    • P.M. Hartl, A.L. Tan-Wilson, and K.A. Wilson Proteolysis of Kunitz soybean trypsin inhibitor during germination Phytochemistry 25 1986 23 26
    • (1986) Phytochemistry , vol.25 , pp. 23-26
    • Hartl, P.M.1    Tan-Wilson, A.L.2    Wilson, K.A.3
  • 29
    • 0034762019 scopus 로고    scopus 로고
    • Physiological response of Colarado potato beetle and beet armyworm larvae to depletion of wound-inducible proteinase inhibitors in trangenic potato plants
    • F. Ortego, C. Novillo, J.J. Sanchez-Serrano, and P. Castanera Physiological response of Colarado potato beetle and beet armyworm larvae to depletion of wound-inducible proteinase inhibitors in trangenic potato plants J. Insect Physiol. 47 2001 1291 1300
    • (2001) J. Insect Physiol. , vol.47 , pp. 1291-1300
    • Ortego, F.1    Novillo, C.2    Sanchez-Serrano, J.J.3    Castanera, P.4
  • 30
    • 0027093631 scopus 로고
    • Modified binary plant transformation vectors with wild-type gene encoding NPTII
    • R.S.S. Datla, J.K. Hammerlindl, B. Panchuk, L.E. Pelcher, and W. Keller Modified binary plant transformation vectors with wild-type gene encoding NPTII Gene 211 1992 383 384
    • (1992) Gene , vol.211 , pp. 383-384
    • Datla, R.S.S.1    Hammerlindl, J.K.2    Panchuk, B.3    Pelcher, L.E.4    Keller, W.5
  • 31
    • 1842349188 scopus 로고
    • Broad host range DNA cloning system for Gram-negative bacteria: Construction of a gene bank of Rhizobium meliloti
    • G. Ditta, S. Stanfield, D. Corbins, and D.R. Helinski Broad host range DNA cloning system for Gram-negative bacteria: construction of a gene bank of Rhizobium meliloti Proc. Natl. Acad. Sci. U.S.A. 77 1980 7347 7351
    • (1980) Proc. Natl. Acad. Sci. U.S.A. , vol.77 , pp. 7347-7351
    • Ditta, G.1    Stanfield, S.2    Corbins, D.3    Helinski, D.R.4
  • 34
    • 0025019244 scopus 로고
    • A simple and rapid method for the preparation of total plant DNA
    • H. Junghans, and M. Metzlaff A simple and rapid method for the preparation of total plant DNA Biotechniques 8 1990 176
    • (1990) Biotechniques , vol.8 , pp. 176
    • Junghans, H.1    Metzlaff, M.2
  • 35
    • 0026516892 scopus 로고
    • One hour downward alkaline capillary transfer for blotting of DNA and RNA
    • P. Chomczynski One hour downward alkaline capillary transfer for blotting of DNA and RNA Anal. Biochem. 201 1992 134 139
    • (1992) Anal. Biochem. , vol.201 , pp. 134-139
    • Chomczynski, P.1
  • 37
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilising the principle of protein dye binding
    • M.M. Bradford A rapid and sensitive method for the quantitation of microgram quantities of protein utilising the principle of protein dye binding Anal. Biochem. 72 1976 248 254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 38
    • 0000749791 scopus 로고
    • Effects of the soybean (Kunitz) trypsin inhibitor on growth and digestive proteases of larvae of Spodoptera litura
    • M.T. McManus, and E.P.J. Burgess Effects of the soybean (Kunitz) trypsin inhibitor on growth and digestive proteases of larvae of Spodoptera litura J. Insect Physiol. 41 1995 731 738
    • (1995) J. Insect Physiol. , vol.41 , pp. 731-738
    • McManus, M.T.1    Burgess, E.P.J.2
  • 39
    • 0000524481 scopus 로고    scopus 로고
    • Overproduction of digestive enzymes compensates for inhibitory effects of protease and α-amylase inhibitors fed to three species of leafrollers (Lepidoptera: Tortricidae)
    • N.P. Markwick, W.A. Laing, J.T. Christeller, J.Z. McHenry, and M.R. Newton Overproduction of digestive enzymes compensates for inhibitory effects of protease and α-amylase inhibitors fed to three species of leafrollers (Lepidoptera: Tortricidae) J. Econ. Entomol. 91 1998 1265 1276
    • (1998) J. Econ. Entomol. , vol.91 , pp. 1265-1276
    • Markwick, N.P.1    Laing, W.A.2    Christeller, J.T.3    McHenry, J.Z.4    Newton, M.R.5
  • 40
    • 0001701325 scopus 로고
    • Midgut protease activities in 12 phytophagous lepidopteran larvae: Dietary and proteinase inhibitor interactions
    • J.T. Christeller, W.A. Laing, N.P. Markwick, and E.P.J. Burgess Midgut protease activities in 12 phytophagous lepidopteran larvae: dietary and proteinase inhibitor interactions Insect Biochem. Mol. Biol. 22 1992 735 746
    • (1992) Insect Biochem. Mol. Biol. , vol.22 , pp. 735-746
    • Christeller, J.T.1    Laing, W.A.2    Markwick, N.P.3    Burgess, E.P.J.4
  • 41
    • 0032190445 scopus 로고    scopus 로고
    • A cysteine proteinase inhibitor purified from apple fruit
    • S.N. Ryan, W.A. Laing, and M.T. McManus A cysteine proteinase inhibitor purified from apple fruit Phytochemistry 49 1998 957 963
    • (1998) Phytochemistry , vol.49 , pp. 957-963
    • Ryan, S.N.1    Laing, W.A.2    McManus, M.T.3
  • 42
    • 0028519077 scopus 로고
    • Posttranslational modification of an isoinhibitor from the potato proteinase inhibitor II gene family in transgenic tobacco yields a peptide with homology to potato chymotrypsin inhibitor I
    • M.T. McManus, W.A. Laing, J.T. Christeller, and D.W.R. White Posttranslational modification of an isoinhibitor from the potato proteinase inhibitor II gene family in transgenic tobacco yields a peptide with homology to potato chymotrypsin inhibitor I Plant Physiol. 106 1994 771 777
    • (1994) Plant Physiol. , vol.106 , pp. 771-777
    • McManus, M.T.1    Laing, W.A.2    Christeller, J.T.3    White, D.W.R.4
  • 44
    • 0001435171 scopus 로고
    • Proteins arising during the late stages of embryogenesis in Pisum sativum L.
    • D.H.P. Barratt, and J.A. Clark Proteins arising during the late stages of embryogenesis in Pisum sativum L. Planta 184 1991 14 23
    • (1991) Planta , vol.184 , pp. 14-23
    • Barratt, D.H.P.1    Clark, J.A.2
  • 45
    • 0029170674 scopus 로고
    • The gene for the major cuticular wax-associated protein and three homologous genes from broccoli (Brassica oleracea) and their expression patterns
    • J. Pyee, and P.E. Kolattujudy The gene for the major cuticular wax-associated protein and three homologous genes from broccoli (Brassica oleracea) and their expression patterns Plant J. 7 1995 49 59
    • (1995) Plant J. , vol.7 , pp. 49-59
    • Pyee, J.1    Kolattujudy, P.E.2
  • 46
    • 0028851069 scopus 로고
    • Characterization of monoclonal antibodies that recognise the soybean (Kunitz) trypsin inhibitor: Binding to the inhibitor interrupts the formation of the trypsin:inhibitor complex
    • M.T. McManus, R. Corner, and I. Garthwaite Characterization of monoclonal antibodies that recognise the soybean (Kunitz) trypsin inhibitor: binding to the inhibitor interrupts the formation of the trypsin:inhibitor complex J. Plant Physiol. 146 1995 243 248
    • (1995) J. Plant Physiol. , vol.146 , pp. 243-248
    • McManus, M.T.1    Corner, R.2    Garthwaite, I.3
  • 48
    • 0041772039 scopus 로고    scopus 로고
    • Proteinase inhibitors
    • M.T. McManus W.A. Laing A.C. Allan Protein-Protein Interactions in Plant Biology Sheffield Academic Press UK
    • W.A. Laing, and M.T. McManus Proteinase inhibitors M.T. McManus W.A. Laing A.C. Allan Protein-Protein Interactions in Plant Biology Annual Plant Reviews vol. 7 2002 Sheffield Academic Press UK 77 119
    • (2002) Annual Plant Reviews , vol.7 , pp. 77-119
    • Laing, W.A.1    McManus, M.T.2
  • 49
    • 0031081348 scopus 로고    scopus 로고
    • Lipid-transfer proteins: A puzzling family of plant proteins
    • J.-C. Kader Lipid-transfer proteins: a puzzling family of plant proteins Trends Plant Sci. 2 1997 66 70
    • (1997) Trends Plant Sci. , vol.2 , pp. 66-70
    • Kader, J.-C.1
  • 50
    • 0036290222 scopus 로고    scopus 로고
    • Purification and characterization of a novel 7-kDa non-specific lipid transfer protein-2 from rice (Oryza sativa)
    • Y.-J. Liu, D. Samuel, C.-H. Lin, and P.-C. Lyu Purification and characterization of a novel 7-kDa non-specific lipid transfer protein-2 from rice (Oryza sativa) Biochem. Biophys. Res. Commun. 294 2002 535 540
    • (2002) Biochem. Biophys. Res. Commun. , vol.294 , pp. 535-540
    • Liu, Y.-J.1    Samuel, D.2    Lin, C.-H.3    Lyu, P.-C.4
  • 52
    • 0035129434 scopus 로고    scopus 로고
    • Inhibition of proteosome activity by the TED4 protein in extracellular space: A novel mechanism for protection of living cells from injury caused by dying cells
    • S. Endo, T. Demura, and H. Fukuda Inhibition of proteosome activity by the TED4 protein in extracellular space: a novel mechanism for protection of living cells from injury caused by dying cells Plant Cell Physiol. 42 2001 9 19
    • (2001) Plant Cell Physiol. , vol.42 , pp. 9-19
    • Endo, S.1    Demura, T.2    Fukuda, H.3
  • 53
    • 0033996898 scopus 로고    scopus 로고
    • Purification and partial characterization of a second cysteine proteinase inhibitor from ungerminated barley (Hordeum vulgare L.)
    • B.L. Jones, and L.A. Marinac Purification and partial characterization of a second cysteine proteinase inhibitor from ungerminated barley (Hordeum vulgare L.) J. Agric. Food Chem. 48 2000 257 264
    • (2000) J. Agric. Food Chem. , vol.48 , pp. 257-264
    • Jones, B.L.1    Marinac, L.A.2
  • 54
    • 0041318971 scopus 로고    scopus 로고
    • Identification and characterisation of proteinase inhibitors and their genes from seeds of apple (Malus domestica)
    • S. Ryan, M.T. McManus, and W.A. Laing Identification and characterisation of proteinase inhibitors and their genes from seeds of apple (Malus domestica) J. Biochem. 134 2003 31 42
    • (2003) J. Biochem. , vol.134 , pp. 31-42
    • Ryan, S.1    McManus, M.T.2    Laing, W.A.3
  • 55
    • 0000668775 scopus 로고
    • Are insects resistant to plant proteinase inhibitors
    • R.M. Broadway Are insects resistant to plant proteinase inhibitors J. Insect Physiol. 41 1995 107 116
    • (1995) J. Insect Physiol. , vol.41 , pp. 107-116
    • Broadway, R.M.1
  • 57
    • 0344784409 scopus 로고    scopus 로고
    • Characterization of major midgut proteinase cDNAs from Helicoverpa armigera larvae and changes in gene expression in response to four proteinase inhibitors in the diet
    • L.N. Gatehouse, A.L. Shannon, E.P.J. Burgess, and J.T. Christeller Characterization of major midgut proteinase cDNAs from Helicoverpa armigera larvae and changes in gene expression in response to four proteinase inhibitors in the diet Insect Biochem. Mol. Biol. 27 1998 929 944
    • (1998) Insect Biochem. Mol. Biol. , vol.27 , pp. 929-944
    • Gatehouse, L.N.1    Shannon, A.L.2    Burgess, E.P.J.3    Christeller, J.T.4
  • 58
    • 0028978963 scopus 로고
    • Does host range influence susceptibility of herbivorous insects to non-host proteinase inhibitors
    • R.M. Broadway, and M.G. Villani Does host range influence susceptibility of herbivorous insects to non-host proteinase inhibitors Entomol. Exp. Appl. 76 1995 303 312
    • (1995) Entomol. Exp. Appl. , vol.76 , pp. 303-312
    • Broadway, R.M.1    Villani, M.G.2
  • 59
    • 0344026311 scopus 로고    scopus 로고
    • Physiological adaptation explains the insensitivity of Baris coerulescens to transgenic oilseed rape expressing oryzacystatin I
    • M. Bonade-Bottino, J. Lerin, B. Zaccomer, and L. Jouanin Physiological adaptation explains the insensitivity of Baris coerulescens to transgenic oilseed rape expressing oryzacystatin I Insect Biochem. Mol. Biol. 29 1999 131 138
    • (1999) Insect Biochem. Mol. Biol. , vol.29 , pp. 131-138
    • Bonade-Bottino, M.1    Lerin, J.2    Zaccomer, B.3    Jouanin, L.4


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