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Volumn 36, Issue 2, 2011, Pages 180-186

Periplaneta americana midgut proteases differentially expressed against dietary components from different plant seeds

Author keywords

Bioassay; Gel X ray film contact print method; Insensitive proteases; Periplaneta americana; Plant protease inhibitors

Indexed keywords

BIOASSAY; COCKROACH; CROP PEST; DIET; ENZYME ACTIVITY; INHIBITOR; SEED; SOYBEAN; SURVIVAL;

EID: 79955852338     PISSN: 03076962     EISSN: 13653032     Source Type: Journal    
DOI: 10.1111/j.1365-3032.2011.00784.x     Document Type: Article
Times cited : (11)

References (48)
  • 1
    • 77953323891 scopus 로고    scopus 로고
    • Detection of novel trypsin inhibitors in the cotyledons of Phaseolus vulgaris seeds.
    • Alves, M., Chaves, I., Carrilho, D. et al. (2010) Detection of novel trypsin inhibitors in the cotyledons of Phaseolus vulgaris seeds. Journal of Plant Physiology, 167, 848-854.
    • (2010) Journal of Plant Physiology , vol.167 , pp. 848-854
    • Alves, M.1    Chaves, I.2    Carrilho, D.3
  • 2
    • 0031177988 scopus 로고    scopus 로고
    • Differentially regulated inhibitor sensitive and insensitive protease genes from the phytophagous insect pest, Helicoverpa armigera, are members of complex multigene families.
    • Bown, D.P., Wilkinson, H.S. & Gatehouse, J.A. (1997) Differentially regulated inhibitor sensitive and insensitive protease genes from the phytophagous insect pest, Helicoverpa armigera, are members of complex multigene families. Insect Biochemistry and Molecular Biology, 27, 625-638.
    • (1997) Insect Biochemistry and Molecular Biology , vol.27 , pp. 625-638
    • Bown, D.P.1    Wilkinson, H.S.2    Gatehouse, J.A.3
  • 3
    • 35448998534 scopus 로고    scopus 로고
    • General up regulation of Spodoptera frugiperda trypsins and chymotrypsins allows its adaptation to soybean proteinase inhibitor.
    • Brioschi, D., Nadalini, L., Bengtson, M.H. et al. (2007) General up regulation of Spodoptera frugiperda trypsins and chymotrypsins allows its adaptation to soybean proteinase inhibitor. Insect Biochemistry and Molecular Biology, 37, 1283-1290.
    • (2007) Insect Biochemistry and Molecular Biology , vol.37 , pp. 1283-1290
    • Brioschi, D.1    Nadalini, L.2    Bengtson, M.H.3
  • 4
    • 0000668775 scopus 로고
    • Are insects resistant to plant proteinase inhibitors?
    • Broadway, R.M. (1995) Are insects resistant to plant proteinase inhibitors? Journal of Insect Physiology, 41, 107-116.
    • (1995) Journal of Insect Physiology , vol.41 , pp. 107-116
    • Broadway, R.M.1
  • 5
    • 0002338378 scopus 로고    scopus 로고
    • Dietary proteinase inhibitors alter complement of midgut proteases.
    • Broadway, R.M. (1996) Dietary proteinase inhibitors alter complement of midgut proteases. Archives of Insect Biochemistry and Physiology, 32, 39-53.
    • (1996) Archives of Insect Biochemistry and Physiology , vol.32 , pp. 39-53
    • Broadway, R.M.1
  • 6
    • 0001260377 scopus 로고
    • Plant proteinase inhibitors: mechanism of action and effect on the growth and digestive physiology of larval Heliothis zea and Spodoptera exigua.
    • Broadway, R.M. & Duffey, S.S. (1986) Plant proteinase inhibitors: mechanism of action and effect on the growth and digestive physiology of larval Heliothis zea and Spodoptera exigua. Journal of Insect Physiology, 32, 827-833.
    • (1986) Journal of Insect Physiology , vol.32 , pp. 827-833
    • Broadway, R.M.1    Duffey, S.S.2
  • 7
    • 0141839117 scopus 로고    scopus 로고
    • Differential inhibition of Helicoverpa armigera guts proteinases by proteinase inhibitors of pigeonpea (Cajanus cajan) and its wild relatives.
    • Chougule, N.P., Hivrale, V.K., Chhabda, P.J. et al. (2003) Differential inhibition of Helicoverpa armigera guts proteinases by proteinase inhibitors of pigeonpea (Cajanus cajan) and its wild relatives. Phytochemistry, 64, 681-687.
    • (2003) Phytochemistry , vol.64 , pp. 681-687
    • Chougule, N.P.1    Hivrale, V.K.2    Chhabda, P.J.3
  • 8
    • 0034201087 scopus 로고    scopus 로고
    • Adult Colorado potato beetles, Leptinotarsa decemlineata compensate for nutritional stress on oryzacystatin I-transgenic potato plants by hypertrophic behavior and over-production of insensitive proteases.
    • Cloutier, C., Jean, C., Fournier, M. et al. (2000) Adult Colorado potato beetles, Leptinotarsa decemlineata compensate for nutritional stress on oryzacystatin I-transgenic potato plants by hypertrophic behavior and over-production of insensitive proteases. Archives of Insect Biochemistry and Physiology, 44, 69-81.
    • (2000) Archives of Insect Biochemistry and Physiology , vol.44 , pp. 69-81
    • Cloutier, C.1    Jean, C.2    Fournier, M.3
  • 9
    • 0029670583 scopus 로고    scopus 로고
    • Transgenic rice plants harboring an introduced potato proteinase inhibitor II gene are insect resistant.
    • Duan, X., Xue, Q., Abo-El-Saad, M. et al. (1996) Transgenic rice plants harboring an introduced potato proteinase inhibitor II gene are insect resistant. Nature Biotechnology, 14, 444-498.
    • (1996) Nature Biotechnology , vol.14 , pp. 444-498
    • Duan, X.1    Xue, Q.2    Abo-El-Saad, M.3
  • 11
    • 77956988073 scopus 로고    scopus 로고
    • Coexpression of potato type I and II proteinase inhibitors gives cotton plants protection against insect damage in the field.
    • Dunse, K.M., Stevens, J.A., Lay, F.T. et al. (2010b) Coexpression of potato type I and II proteinase inhibitors gives cotton plants protection against insect damage in the field. Proceedings of the National Academy of Science of the United States of Amercia, 107, 15011-15015.
    • (2010) Proceedings of the National Academy of Science of the United States of Amercia , vol.107 , pp. 15011-15015
    • Dunse, K.M.1    Stevens, J.A.2    Lay, F.T.3
  • 12
    • 0031014713 scopus 로고
    • Activity staining of protein inhibitors of proteases on gelatin containing polyacrylamide gel electrophoresis.
    • Feliocioli, R., Garzelli, B., Vaccari, L. et al. (1970) Activity staining of protein inhibitors of proteases on gelatin containing polyacrylamide gel electrophoresis. Analytical Biochemistry, 244, 176-178.
    • (1970) Analytical Biochemistry , vol.244 , pp. 176-178
    • Feliocioli, R.1    Garzelli, B.2    Vaccari, L.3
  • 13
    • 0000551928 scopus 로고    scopus 로고
    • Nutritive quality of plant protein: sources of variation and insect herbivore response.
    • Felton, G.W. (1996) Nutritive quality of plant protein: sources of variation and insect herbivore response. Archives of Insect Biochemistry and Physiology, 32, 107-130.
    • (1996) Archives of Insect Biochemistry and Physiology , vol.32 , pp. 107-130
    • Felton, G.W.1
  • 15
    • 0344784409 scopus 로고    scopus 로고
    • Characterization of major midgut proteinases cDNAs from Helicoverpa armigera larvae and changes in gene expression in response to four proteinase inhibitors in the diet.
    • Gatehouse, L.N., Shannon, A.L., Burgess, E.P.J. & Christeller, J.T. (1997) Characterization of major midgut proteinases cDNAs from Helicoverpa armigera larvae and changes in gene expression in response to four proteinase inhibitors in the diet. Insect Biochemistry and Molecular Biology, 27, 929-944.
    • (1997) Insect Biochemistry and Molecular Biology , vol.27 , pp. 929-944
    • Gatehouse, L.N.1    Shannon, A.L.2    Burgess, E.P.J.3    Christeller, J.T.4
  • 16
    • 0032032037 scopus 로고    scopus 로고
    • Growth stimulation of beetle larvae reared on transgenic oilseed rape expressing a cysteine proteinase inhibitor.
    • Girard, C., Metayer, M., Zaccomer, B. et al. (1998) Growth stimulation of beetle larvae reared on transgenic oilseed rape expressing a cysteine proteinase inhibitor. Journal of Insect Physiology, 44, 263-270.
    • (1998) Journal of Insect Physiology , vol.44 , pp. 263-270
    • Girard, C.1    Metayer, M.2    Zaccomer, B.3
  • 17
    • 0031984542 scopus 로고    scopus 로고
    • Amylase inhibitors of pigeonpea (Cajanus cajan) seeds.
    • Giri, A.P. & Kachole, M.S. (1998) Amylase inhibitors of pigeonpea (Cajanus cajan) seeds. Phytochemistry, 47, 197-202.
    • (1998) Phytochemistry , vol.47 , pp. 197-202
    • Giri, A.P.1    Kachole, M.S.2
  • 18
    • 0031759565 scopus 로고    scopus 로고
    • Chickpea defensive proteinase inhibitors can be inactivated by pod-borer gut proteinases.
    • Giri, A.P., Harsulkar, A.M., Deshpande, V.V. et al. (1998) Chickpea defensive proteinase inhibitors can be inactivated by pod-borer gut proteinases. Plant Physiology, 116, 393-401.
    • (1998) Plant Physiology , vol.116 , pp. 393-401
    • Giri, A.P.1    Harsulkar, A.M.2    Deshpande, V.V.3
  • 19
    • 1542580602 scopus 로고    scopus 로고
    • Analysis of proteinaceous antinutritional compounds in soya oilseed products.
    • Hessing, M., Bleeker, H., Biert, R. et al. (1996) Analysis of proteinaceous antinutritional compounds in soya oilseed products. ACS Symposium Series, 621, 219-230.
    • (1996) ACS Symposium Series , vol.621 , pp. 219-230
    • Hessing, M.1    Bleeker, H.2    Biert, R.3
  • 20
    • 0023652138 scopus 로고
    • A novel mechanism of insect resistance engineered into tobacco.
    • Hilder, V.A., Gatehouse, A.M.R., Sheerman, S.E. et al. (1987) A novel mechanism of insect resistance engineered into tobacco. Nature, 330, 160-163.
    • (1987) Nature , vol.330 , pp. 160-163
    • Hilder, V.A.1    Gatehouse, A.M.R.2    Sheerman, S.E.3
  • 21
    • 20544464368 scopus 로고    scopus 로고
    • Unrevealing biochemical properties of coakroach (Periplaneta americana) proteinases with gel-X-ray film contact print method.
    • Hivrale, V.K., Chougule, N.P., Chhabda, P.J. et al. (2005) Unrevealing biochemical properties of coakroach (Periplaneta americana) proteinases with gel-X-ray film contact print method. Comparative Biochemistry and Physiology B, 141, 261-266.
    • (2005) Comparative Biochemistry and Physiology B , vol.141 , pp. 261-266
    • Hivrale, V.K.1    Chougule, N.P.2    Chhabda, P.J.3
  • 22
    • 0001669768 scopus 로고
    • The partial purification and characterization of serine protease activity in midgut of larval Helicoverpa armigera.
    • Johnston, K.A., Lee, M.J., Gatehouse, J.A. & Anstee, J.H. (1991) The partial purification and characterization of serine protease activity in midgut of larval Helicoverpa armigera. Insect Biochemistry, 21, 389-397.
    • (1991) Insect Biochemistry , vol.21 , pp. 389-397
    • Johnston, K.A.1    Lee, M.J.2    Gatehouse, J.A.3    Anstee, J.H.4
  • 23
    • 0029128219 scopus 로고
    • Adaptation of Spodoptera exigua larvae to plant protease inhibitors by induction of gut proteinase activity insensitive to inhibition.
    • Jongsma, M.A., Bakker, P.L., Peteres, J. et al. (1995) Adaptation of Spodoptera exigua larvae to plant protease inhibitors by induction of gut proteinase activity insensitive to inhibition. Proceedings of the National Academy of Science of the United States of Amercia, 92, 8041-8045.
    • (1995) Proceedings of the National Academy of Science of the United States of Amercia , vol.92 , pp. 8041-8045
    • Jongsma, M.A.1    Bakker, P.L.2    Peteres, J.3
  • 24
    • 0030057503 scopus 로고    scopus 로고
    • Characterization and partial purification of gut proteinases of Spodoptera exigua Hubner (Lepidoptera: Noctuidae).
    • Jongsma, M., Peters, J., Stiekema, W.J. & Bosch, D. (1996) Characterization and partial purification of gut proteinases of Spodoptera exigua Hubner (Lepidoptera: Noctuidae). Insect Biochemistry and Molecular Biology, 26, 185-193.
    • (1996) Insect Biochemistry and Molecular Biology , vol.26 , pp. 185-193
    • Jongsma, M.1    Peters, J.2    Stiekema, W.J.3    Bosch, D.4
  • 25
    • 0014949207 scopus 로고
    • Cleavage of structural protein during the assembly of the head of bacteriophage T4.
    • Laemmli, U.K. (1970) Cleavage of structural protein during the assembly of the head of bacteriophage T4. Nature, 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 26
    • 0010763149 scopus 로고    scopus 로고
    • Soybean Kunitz trypsin inhibitor (SKTI) confers resistance to the brown plant hopper (Nilaparvata lugens Stal) in transgenic rice.
    • Lee, S.I., Lee, S.H., Koo, J.C. et al. (1999) Soybean Kunitz trypsin inhibitor (SKTI) confers resistance to the brown plant hopper (Nilaparvata lugens Stal) in transgenic rice. Molecular Breeding, 5, 1-9.
    • (1999) Molecular Breeding , vol.5 , pp. 1-9
    • Lee, S.I.1    Lee, S.H.2    Koo, J.C.3
  • 27
    • 0003187258 scopus 로고    scopus 로고
    • Obtaining transgenic cotton plants with cowpea trypsin inhibitor.
    • Li, Y.E., Zhu, Z., Chen, Z.X. et al. (1998) Obtaining transgenic cotton plants with cowpea trypsin inhibitor. Acta Gossypii Sinica, 10, 237-243.
    • (1998) Acta Gossypii Sinica , vol.10 , pp. 237-243
    • Li, Y.E.1    Zhu, Z.2    Chen, Z.X.3
  • 29
    • 73449146028 scopus 로고    scopus 로고
    • Properties of a Kunitz-type trypsin inhibitor from Delonix regia seeds against digestive proteinases of Anagasta kuehniella (Z.) and Corcyra cephalonica (S.) (Lepidoptera: Pyralidae).
    • Macedo, M.L.R., Pando, S.C., Chevreuil, L.R. & Marangoni, S. (2009) Properties of a Kunitz-type trypsin inhibitor from Delonix regia seeds against digestive proteinases of Anagasta kuehniella (Z.) and Corcyra cephalonica (S.) (Lepidoptera: Pyralidae). Protein and Peptide Letters, 16, 1459-1465.
    • (2009) Protein and Peptide Letters , vol.16 , pp. 1459-1465
    • Macedo, M.L.R.1    Pando, S.C.2    Chevreuil, L.R.3    Marangoni, S.4
  • 30
    • 77953641530 scopus 로고    scopus 로고
    • Adenanthera pavonina trypsin inhibitor retard growth of Anagasta kuehniella (Lepidoptera: Pyralidae).
    • Macedo, M., Durigan, R., Silva, D. et al. (2010) Adenanthera pavonina trypsin inhibitor retard growth of Anagasta kuehniella (Lepidoptera: Pyralidae). Archives of Insect Biochemistry and Physiology, 73, 213-231.
    • (2010) Archives of Insect Biochemistry and Physiology , vol.73 , pp. 213-231
    • Macedo, M.1    Durigan, R.2    Silva, D.3
  • 31
    • 0031030737 scopus 로고    scopus 로고
    • Avoiding protease mediated resistance in herbivorous pests.
    • Michaud, D. (1997) Avoiding protease mediated resistance in herbivorous pests. Trends in Biotechnology, 15, 4-6.
    • (1997) Trends in Biotechnology , vol.15 , pp. 4-6
    • Michaud, D.1
  • 33
    • 73449118609 scopus 로고    scopus 로고
    • Two Kunitz-type inhibitors with activity against trypsin and papain from Pithecellobium dumosum seeds: purification, characterization, and activity towards pest insect digestive enzyme.
    • Oliveira, A.S., Migliolo, L., Aquino, R.O. et al. (2009) Two Kunitz-type inhibitors with activity against trypsin and papain from Pithecellobium dumosum seeds: purification, characterization, and activity towards pest insect digestive enzyme. Protein and Peptide Letters, 16, 1526-1532.
    • (2009) Protein and Peptide Letters , vol.16 , pp. 1526-1532
    • Oliveira, A.S.1    Migliolo, L.2    Aquino, R.O.3
  • 34
    • 15744367539 scopus 로고    scopus 로고
    • Compensatory proteolytic responses to dietary proteinase inhibitors in the red flour beetle, Tribolium castaneum (Coleoptera: Tenebrionidae).
    • Oppert, B.T., Morgana, T.D., Hartzerb, K. & Kramer, K.J. (2005) Compensatory proteolytic responses to dietary proteinase inhibitors in the red flour beetle, Tribolium castaneum (Coleoptera: Tenebrionidae). Comparative Biochemistry and Physiology C, 140, 53-58.
    • (2005) Comparative Biochemistry and Physiology C , vol.140 , pp. 53-58
    • Oppert, B.T.1    Morgana, T.D.2    Hartzerb, K.3    Kramer, K.J.4
  • 35
    • 0000259353 scopus 로고
    • Inhibition of Diabrotica larval growth by a multicystatin from potato tubers.
    • Orr, G.L., Strickland, J.A. & Walsh, T.A. (1994) Inhibition of Diabrotica larval growth by a multicystatin from potato tubers. Journal of Insect Physiology, 40, 893-900.
    • (1994) Journal of Insect Physiology , vol.40 , pp. 893-900
    • Orr, G.L.1    Strickland, J.A.2    Walsh, T.A.3
  • 36
    • 73649120985 scopus 로고    scopus 로고
    • Pyrosequencing the Manduca sexta larval midgut transcriptome: messages for digestion, detoxification and defence.
    • Pauchet, Y., Wilkinson, P., Vogel, H. et al. (2010) Pyrosequencing the Manduca sexta larval midgut transcriptome: messages for digestion, detoxification and defence. Insect Molecular Biology, 19, 61-75.
    • (2010) Insect Molecular Biology , vol.19 , pp. 61-75
    • Pauchet, Y.1    Wilkinson, P.2    Vogel, H.3
  • 37
    • 0028273981 scopus 로고
    • Detection of electrophoretically separated protease inhibitors using x-ray film.
    • Pichare, M.M. & Kachole, M.S. (1994) Detection of electrophoretically separated protease inhibitors using x-ray film. Journal of Biochemical and Biophysical Methods, 28, 215-224.
    • (1994) Journal of Biochemical and Biophysical Methods , vol.28 , pp. 215-224
    • Pichare, M.M.1    Kachole, M.S.2
  • 38
    • 76249093070 scopus 로고    scopus 로고
    • Purification and characterization of a Bowman-Birk proteinase inhibitor from the seeds of black gram (Vigna mungo).
    • Prasad, E.R., Dutta-Gupta, A. & Padmasree, K. (2010) Purification and characterization of a Bowman-Birk proteinase inhibitor from the seeds of black gram (Vigna mungo). Phytochemistry, 71, 363-372.
    • (2010) Phytochemistry , vol.71 , pp. 363-372
    • Prasad, E.R.1    Dutta-Gupta, A.2    Padmasree, K.3
  • 39
    • 0000180578 scopus 로고
    • Protease inhibitors in plants: genes for improving defenses against insect and pathogens.
    • Ryan, C.A. (1990) Protease inhibitors in plants: genes for improving defenses against insect and pathogens. Annual Reviews of Phytopathology, 28, 425-449.
    • (1990) Annual Reviews of Phytopathology , vol.28 , pp. 425-449
    • Ryan, C.A.1
  • 40
    • 71949093356 scopus 로고    scopus 로고
    • Genetically pyramiding protease-inhibitor genes for dual broad-spectrum resistance against insect and phytopathogens in transgenic tobacco.
    • Senthilkumar, R., Cheng, C. & Yeh, K. (2010) Genetically pyramiding protease-inhibitor genes for dual broad-spectrum resistance against insect and phytopathogens in transgenic tobacco. Plant Biotechnology Journal, 8, 65-75.
    • (2010) Plant Biotechnology Journal , vol.8 , pp. 65-75
    • Senthilkumar, R.1    Cheng, C.2    Yeh, K.3
  • 41
    • 27644529742 scopus 로고    scopus 로고
    • Podborer (Helicoverpa armigera Hubn.) does not show specific adaptations in gut proteinases to dietary Cicer arietinum Kunitz proteinase inhibitor.
    • Srinivasan, A., Chougule, N.P., Giri, A.P. et al. (2005) Podborer (Helicoverpa armigera Hubn.) does not show specific adaptations in gut proteinases to dietary Cicer arietinum Kunitz proteinase inhibitor. Journal of insect Physiology, 51, 1268-1276.
    • (2005) Journal of insect Physiology , vol.51 , pp. 1268-1276
    • Srinivasan, A.1    Chougule, N.P.2    Giri, A.P.3
  • 42
    • 0028944193 scopus 로고
    • Recombinant proregions from papain and papaya proteinase IV are selective high affinity inhibitors of the mature papaya enzymes.
    • Taylor, M.A.J., Baker, K.C., Briggs, G.S. et al. (1995) Recombinant proregions from papain and papaya proteinase IV are selective high affinity inhibitors of the mature papaya enzymes. Protein Engineering, 1, 59-62.
    • (1995) Protein Engineering , vol.1 , pp. 59-62
    • Taylor, M.A.J.1    Baker, K.C.2    Briggs, G.S.3
  • 43
    • 27744440981 scopus 로고    scopus 로고
    • Expression of the maize proteinase inhibitor (mpi) gene in rice plants enhances resistance against the striped stem borer (Chilo suppressalis): effects on larval growth and insect gut proteinases.
    • Vila, L., Quilis, J., Meynard, D. et al. (2005) Expression of the maize proteinase inhibitor (mpi) gene in rice plants enhances resistance against the striped stem borer (Chilo suppressalis): effects on larval growth and insect gut proteinases. Plant Biotechnol Journal, 3, 187-202.
    • (2005) Plant Biotechnol Journal , vol.3 , pp. 187-202
    • Vila, L.1    Quilis, J.2    Meynard, D.3
  • 44
    • 0000128089 scopus 로고
    • Diversity in digestive proteinase activity among insects.
    • Wolfson, J.L. & Murdock, L.L. (1990) Diversity in digestive proteinase activity among insects. Journal of Chemical Ecology, 16, 1089-1102.
    • (1990) Journal of Chemical Ecology , vol.16 , pp. 1089-1102
    • Wolfson, J.L.1    Murdock, L.L.2
  • 45
    • 0029473256 scopus 로고
    • Potential use of protease inhibitors for host plant resistance: a text cased.
    • Wolfson, J.L. & Murdock, L.L. (1995) Potential use of protease inhibitors for host plant resistance: a text cased. Environmental Entomology, 24, 52-57.
    • (1995) Environmental Entomology , vol.24 , pp. 52-57
    • Wolfson, J.L.1    Murdock, L.L.2
  • 46
    • 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.
    • Xu, D., Xue, Q., McElory, D. et al. (1996) Constitutive expression of a cowpea trypsin inhibitor gene, CpTi, in transgenic rice plants confers resistance to two major rice insect pests. Molecular Breeding, 2, 167-173.
    • (1996) Molecular Breeding , vol.2 , pp. 167-173
    • Xu, D.1    Xue, Q.2    McElory, D.3
  • 47
    • 0031418108 scopus 로고    scopus 로고
    • cDNAs for a chymotrypsinogen-like protein from two strains of Plodia interpunctella.
    • Zhu, Y.C., Oppert, B., Kramer, K.J. et al. (1997) cDNAs for a chymotrypsinogen-like protein from two strains of Plodia interpunctella. Insect Biochemistry and Molecular Biology, 27, 1027-1037.
    • (1997) Insect Biochemistry and Molecular Biology , vol.27 , pp. 1027-1037
    • Zhu, Y.C.1    Oppert, B.2    Kramer, K.J.3
  • 48
    • 0345146929 scopus 로고    scopus 로고
    • Cowpea bruchid Callosobruchus maculatus uses a three-component strategy to overcome a plant defensive cysteine protease inhibitor.
    • Zhu-Salzman, K., Koiwa, H., Salzman, R.A. et al. (2003) Cowpea bruchid Callosobruchus maculatus uses a three-component strategy to overcome a plant defensive cysteine protease inhibitor. Insect Molecular Biology, 12, 135-145.
    • (2003) Insect Molecular Biology , vol.12 , pp. 135-145
    • Zhu-Salzman, K.1    Koiwa, H.2    Salzman, R.A.3


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