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Volumn 68, Issue , 2006, Pages 427-457

Virus-Derived Genes for Insect-Resistant Transgenic Plants

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; CARRIER PROTEIN; CATHEPSIN; CHITIN BINDING PROTEIN 21, SERRATIA MARCESCENS; CHITIN-BINDING PROTEIN 21, SERRATIA MARCESCENS; CHITINASE; LECTIN; MATRIX METALLOPROTEINASE;

EID: 33748755873     PISSN: 00653527     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0065-3527(06)68012-3     Document Type: Review
Times cited : (19)

References (157)
  • 2
    • 0028835344 scopus 로고
    • Recent advances in the molecular biology of entomopoxviruses
    • Arif B. Recent advances in the molecular biology of entomopoxviruses. J. Gen. Virol. 76 1 (1995) 1-13
    • (1995) J. Gen. Virol. , vol.76 , Issue.1 , pp. 1-13
    • Arif, B.1
  • 3
    • 0028086144 scopus 로고
    • The complete DNA sequence of Autographa californica nuclear polyhedrosis virus
    • Ayres M.D., Howar S.C., Kuzio J., Lopez-Ferber M., and Possee R.D. The complete DNA sequence of Autographa californica nuclear polyhedrosis virus. Virology 202 (1994) 586-605
    • (1994) Virology , vol.202 , pp. 586-605
    • Ayres, M.D.1    Howar, S.C.2    Kuzio, J.3    Lopez-Ferber, M.4    Possee, R.D.5
  • 5
    • 0035123342 scopus 로고    scopus 로고
    • Transgenic GNA expressing potato plants augment the beneficial biocontrol of Lacanobia oleracea (Lepidoptera; Noctuidae) by the parasitoid Eulophus pennicornis (Hymenoptera; Eulophidae)
    • Bell H.A., Fitches E.C., Marris G.C., Bell J., Edwards J.P., Gatehouse J.A., and Gatehouse A.M.R. Transgenic GNA expressing potato plants augment the beneficial biocontrol of Lacanobia oleracea (Lepidoptera; Noctuidae) by the parasitoid Eulophus pennicornis (Hymenoptera; Eulophidae). Transgenic Res. 10 (2001) 35-42
    • (2001) Transgenic Res. , vol.10 , pp. 35-42
    • Bell, H.A.1    Fitches, E.C.2    Marris, G.C.3    Bell, J.4    Edwards, J.P.5    Gatehouse, J.A.6    Gatehouse, A.M.R.7
  • 6
    • 0029150795 scopus 로고
    • Proteolytic remodeling of extracellular matrix
    • Birkedal-Hansen H. Proteolytic remodeling of extracellular matrix. Curr. Opin. Cell Biol. 7 (1995) 728-735
    • (1995) Curr. Opin. Cell Biol. , vol.7 , pp. 728-735
    • Birkedal-Hansen, H.1
  • 7
    • 0030874019 scopus 로고    scopus 로고
    • Molecular analysis of an enhancin gene in the Lymantria dispar nuclear polyhedrosis virus
    • Bischoff D.S., and Slavicek J.M. Molecular analysis of an enhancin gene in the Lymantria dispar nuclear polyhedrosis virus. J. Virol. 71 (1997) 8133-8140
    • (1997) J. Virol. , vol.71 , pp. 8133-8140
    • Bischoff, D.S.1    Slavicek, J.M.2
  • 9
    • 33748740884 scopus 로고    scopus 로고
    • Insect immune defense system, part II: The recognition of nonself
    • Kluwer Academic Publishers, Boston
    • Boucias D.G., and Pendland J.C. Insect immune defense system, part II: The recognition of nonself. "Principles of Insect Pathology," (1998), Kluwer Academic Publishers, Boston 469-497
    • (1998) "Principles of Insect Pathology," , pp. 469-497
    • Boucias, D.G.1    Pendland, J.C.2
  • 10
    • 33748747934 scopus 로고    scopus 로고
    • Insect immune defense system, part III: Prophenoloxidase cascade and post-attachment processes of phagocytosis
    • Kluwer Academic Publishers, Boston
    • Boucias D.G., and Pendland J.C. Insect immune defense system, part III: Prophenoloxidase cascade and post-attachment processes of phagocytosis. "Principles of Insect Pathology," (1998), Kluwer Academic Publishers, Boston 499-537
    • (1998) "Principles of Insect Pathology," , pp. 499-537
    • Boucias, D.G.1    Pendland, J.C.2
  • 12
    • 0036929158 scopus 로고    scopus 로고
    • Transgenic tobacco plants carrying a baculovirus enhancin gene slows the development and increase the mortality of Trichoplusia ni larvae
    • Cao J., Ibrahim H., Garcia J.J., Mason H., Granados R.R., and Earle E.D. Transgenic tobacco plants carrying a baculovirus enhancin gene slows the development and increase the mortality of Trichoplusia ni larvae. Plant Cell Rep. 21 (2002) 244-250
    • (2002) Plant Cell Rep. , vol.21 , pp. 244-250
    • Cao, J.1    Ibrahim, H.2    Garcia, J.J.3    Mason, H.4    Granados, R.R.5    Earle, E.D.6
  • 13
    • 0030991499 scopus 로고    scopus 로고
    • Drosophila cellular immunity against parasitoids
    • Carton Y., and Nappi A.J. Drosophila cellular immunity against parasitoids. Parasitol. Today 13 6 (1997) 218-227
    • (1997) Parasitol. Today , vol.13 , Issue.6 , pp. 218-227
    • Carton, Y.1    Nappi, A.J.2
  • 14
    • 0033532165 scopus 로고    scopus 로고
    • Mosquito cathepsin B-like protease involved in embryonic degradation of vitellin in produced as a latent extraovarian precursor
    • Cho W.L., Tsao S.M., Hays A.R., Walter R., Chen J.S., Snigirevskaya E.S., and Raikhel A.S. Mosquito cathepsin B-like protease involved in embryonic degradation of vitellin in produced as a latent extraovarian precursor. J. Biol. Chem. 274 (1999) 13311-13321
    • (1999) J. Biol. Chem. , vol.274 , pp. 13311-13321
    • Cho, W.L.1    Tsao, S.M.2    Hays, A.R.3    Walter, R.4    Chen, J.S.5    Snigirevskaya, E.S.6    Raikhel, A.S.7
  • 15
    • 0031866632 scopus 로고    scopus 로고
    • The molecular biology of chitin digestion
    • Cohen-Kupiec R., and Chet I. The molecular biology of chitin digestion. Curr. Opin. Biotech. 9 (1998) 270-277
    • (1998) Curr. Opin. Biotech. , vol.9 , pp. 270-277
    • Cohen-Kupiec, R.1    Chet, I.2
  • 17
    • 23844481908 scopus 로고    scopus 로고
    • The cathepsin L-like proteinases from the midgut of Tenebrio molitor larvae: Sequence, properties, immunocytochemical localization and function
    • Cristofoletti P.T., Ribeiro A.F., and Terra W.R. The cathepsin L-like proteinases from the midgut of Tenebrio molitor larvae: Sequence, properties, immunocytochemical localization and function. Insect Biochem. Mol. Biol. 35 (2005) 883-901
    • (2005) Insect Biochem. Mol. Biol. , vol.35 , pp. 883-901
    • Cristofoletti, P.T.1    Ribeiro, A.F.2    Terra, W.R.3
  • 18
    • 0027291247 scopus 로고
    • A gene encoding a highly expressed spindle body protein of Heliothis armigera entomopoxvirus
    • Dall D., Sriskantha A., Vera A., Lai-Fook J., and Symonds T. A gene encoding a highly expressed spindle body protein of Heliothis armigera entomopoxvirus. J. Gen. Virol. 74 (1993) 1811-1818
    • (1993) J. Gen. Virol. , vol.74 , pp. 1811-1818
    • Dall, D.1    Sriskantha, A.2    Vera, A.3    Lai-Fook, J.4    Symonds, T.5
  • 19
    • 0035140792 scopus 로고    scopus 로고
    • Insect-virus relationships: Sifting by informatics
    • Dall D., Luque T., and O'Reilly D. Insect-virus relationships: Sifting by informatics. Bioessays 23 2 (2001) 184-193
    • (2001) Bioessays , vol.23 , Issue.2 , pp. 184-193
    • Dall, D.1    Luque, T.2    O'Reilly, D.3
  • 21
    • 0024110425 scopus 로고
    • Alteration of a lepidopteran peritrophic membrane by baculoviruses and enhancement of viral infectivity
    • Derksen A.C.G. Alteration of a lepidopteran peritrophic membrane by baculoviruses and enhancement of viral infectivity. Virology 167 (1988) 242-250
    • (1988) Virology , vol.167 , pp. 242-250
    • Derksen, A.C.G.1
  • 22
    • 18844433606 scopus 로고    scopus 로고
    • Stimulation of cell motility by a viral fibroblast growth factor homolog: Proposal for a role in viral pathogenesis
    • Detvisitsakun C., Berretta M.F., Lehiy C., and Passarelli A.L. Stimulation of cell motility by a viral fibroblast growth factor homolog: Proposal for a role in viral pathogenesis. Virology 336 2 (2005) 308-317
    • (2005) Virology , vol.336 , Issue.2 , pp. 308-317
    • Detvisitsakun, C.1    Berretta, M.F.2    Lehiy, C.3    Passarelli, A.L.4
  • 23
    • 17444401719 scopus 로고    scopus 로고
    • Storage and secretion of Ag-Aper14, a novel peritrophic matrix protein, and Ag-Muc1 from the mosquito Anopheles gambiae
    • Devenport M.F.H., Donnelly-Doman M., Shen Z., and Jacobs-Lorena M. Storage and secretion of Ag-Aper14, a novel peritrophic matrix protein, and Ag-Muc1 from the mosquito Anopheles gambiae. Cell Tissue Res. 320 (2005) 175-185
    • (2005) Cell Tissue Res. , vol.320 , pp. 175-185
    • Devenport, M.F.H.1    Donnelly-Doman, M.2    Shen, Z.3    Jacobs-Lorena, M.4
  • 25
    • 0030285860 scopus 로고    scopus 로고
    • Snowdrop lectin inhibits development and decreases fecundity of the glasshouse potato aphid (Aulacorthum solani) when administered in vitro and via transgenic plants both in laboratory and glasshouse trials
    • Down R.E., Gatehouse A.M.R., Davison G.M., Newell C.A., Merryweather A., Hamilton W.D.O., Burgess E.P.J., Gilbert R.J.C., and Gatehouse J.A. Snowdrop lectin inhibits development and decreases fecundity of the glasshouse potato aphid (Aulacorthum solani) when administered in vitro and via transgenic plants both in laboratory and glasshouse trials. J. Insect Physiol. 42 (1996) 1035-1045
    • (1996) J. Insect Physiol. , vol.42 , pp. 1035-1045
    • Down, R.E.1    Gatehouse, A.M.R.2    Davison, G.M.3    Newell, C.A.4    Merryweather, A.5    Hamilton, W.D.O.6    Burgess, E.P.J.7    Gilbert, R.J.C.8    Gatehouse, J.A.9
  • 26
    • 32044468332 scopus 로고    scopus 로고
    • Insecticidal spider venom toxin fused to snowdrop lectin is toxic to the peach-potato aphid, Myzus persicae (Hemiptera: Aphididae) and the rice brown planthopper, Nilaparvata lugens (Hemiptera: Delphacidae)
    • Down R.E., Fitches E.C., Wiles D.P., Corti P., Bell H.A., Gatehouse J.A., and Edwards J.P. Insecticidal spider venom toxin fused to snowdrop lectin is toxic to the peach-potato aphid, Myzus persicae (Hemiptera: Aphididae) and the rice brown planthopper, Nilaparvata lugens (Hemiptera: Delphacidae). Pest Manag. Sci. 62 (2006) 77-85
    • (2006) Pest Manag. Sci. , vol.62 , pp. 77-85
    • Down, R.E.1    Fitches, E.C.2    Wiles, D.P.3    Corti, P.4    Bell, H.A.5    Gatehouse, J.A.6    Edwards, J.P.7
  • 27
    • 0002394868 scopus 로고    scopus 로고
    • Use of transgenes to increase host plant resistance to insects: Opportunities and challenges
    • Carozzi N., and Koziel M. (Eds), Taylor & Francis, London
    • Duck N., and Evola S. Use of transgenes to increase host plant resistance to insects: Opportunities and challenges. In: Carozzi N., and Koziel M. (Eds). "Advances in Insect Control: The Role of Transgenic Plants" (1997), Taylor & Francis, London 1-20
    • (1997) "Advances in Insect Control: The Role of Transgenic Plants" , pp. 1-20
    • Duck, N.1    Evola, S.2
  • 29
    • 0029945647 scopus 로고    scopus 로고
    • Characterization of a major peritrophic membrane protein, peritrophin-44, from the larvae of Lucilia cuprina: cDNA and deduced amino acid sequences
    • Elvin C.M., Vuocolo T., Pearson R.D., East I.J., Riding G.A., Eisemann C.H., and Tellam R.L. Characterization of a major peritrophic membrane protein, peritrophin-44, from the larvae of Lucilia cuprina: cDNA and deduced amino acid sequences. J. Biol. Chem. 271 (1996) 8925-8935
    • (1996) J. Biol. Chem. , vol.271 , pp. 8925-8935
    • Elvin, C.M.1    Vuocolo, T.2    Pearson, R.D.3    East, I.J.4    Riding, G.A.5    Eisemann, C.H.6    Tellam, R.L.7
  • 30
    • 0028208258 scopus 로고
    • The insect tracheal system: A conduit for the systemic spread of Autographa californica M nuclear polyhedrosis virus
    • Engelhard E.K., Kam-Morgan L.N.W., Washburn J.O., and Volkman L.E. The insect tracheal system: A conduit for the systemic spread of Autographa californica M nuclear polyhedrosis virus. Proc. Natl. Acad. Sci. USA 91 (1994) 3224-3227
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 3224-3227
    • Engelhard, E.K.1    Kam-Morgan, L.N.W.2    Washburn, J.O.3    Volkman, L.E.4
  • 31
    • 0001939930 scopus 로고    scopus 로고
    • Chapter 3: Baculovirus pathogenesis
    • Miller L.K. (Ed), Plenum Press, New York
    • Federici B.A. Chapter 3: Baculovirus pathogenesis. In: Miller L.K. (Ed). "The Baculoviruses" (1997), Plenum Press, New York 33-60
    • (1997) "The Baculoviruses" , pp. 33-60
    • Federici, B.A.1
  • 32
    • 0036891358 scopus 로고    scopus 로고
    • Fusion proteins containing neuropeptides as novel insect control agents: Snowdrop lectin delivers fused allatostatin to insect haemolymph following oral ingestion
    • Fitches E., Audsley N., Gatehouse J.A., and Edwards J.P. Fusion proteins containing neuropeptides as novel insect control agents: Snowdrop lectin delivers fused allatostatin to insect haemolymph following oral ingestion. Insect Biochem. Mol. Biol. 32 (2002) 1653-1661
    • (2002) Insect Biochem. Mol. Biol. , vol.32 , pp. 1653-1661
    • Fitches, E.1    Audsley, N.2    Gatehouse, J.A.3    Edwards, J.P.4
  • 33
    • 0035161663 scopus 로고    scopus 로고
    • The effects of Phaseolus vulgaris erythro- and leucoagglutinating isolectins (PHA-E and PHA-L) delivered via artificial diet and transgenic plants on the growth and development of tomato moth (Lacanobia oleracea) larvae; lectin binding to gut glycoproteins in vitro and in vivo
    • Fitches E., Ilett C., Gatehouse A.M., Gatehouse L.N., Greene R., Edwards J.P., and Gatehouse J.A. The effects of Phaseolus vulgaris erythro- and leucoagglutinating isolectins (PHA-E and PHA-L) delivered via artificial diet and transgenic plants on the growth and development of tomato moth (Lacanobia oleracea) larvae; lectin binding to gut glycoproteins in vitro and in vivo. J. Insect Physiol. 47 (2001) 1389-1398
    • (2001) J. Insect Physiol. , vol.47 , pp. 1389-1398
    • Fitches, E.1    Ilett, C.2    Gatehouse, A.M.3    Gatehouse, L.N.4    Greene, R.5    Edwards, J.P.6    Gatehouse, J.A.7
  • 34
    • 0035013453 scopus 로고    scopus 로고
    • In vitro and in vivo binding of snowdrop (Galanthus nivalis agglutinin; GNA) and jackbean (Canavalia ensiformis; Con A) lectins within tomato moth (Lacanobia oleracea) larvae; mechanisms of insecticidal action
    • Fitches E., Woodhouse S.D., Edwards J.P., and Gatehouse J.A. In vitro and in vivo binding of snowdrop (Galanthus nivalis agglutinin; GNA) and jackbean (Canavalia ensiformis; Con A) lectins within tomato moth (Lacanobia oleracea) larvae; mechanisms of insecticidal action. J. Insect Physiol. 47 (2001) 777-787
    • (2001) J. Insect Physiol. , vol.47 , pp. 777-787
    • Fitches, E.1    Woodhouse, S.D.2    Edwards, J.P.3    Gatehouse, J.A.4
  • 35
    • 1642568734 scopus 로고    scopus 로고
    • Fusion proteins containing insect-specific toxins as pest control agents: Snowdrop lectin delivers fused insecticidal spider venom toxin to insect haemolymph following oral ingestion
    • Fitches E., Edwards M.G., Mee C., Grishin E., Gatehouse A.M.R., Edwards J.P., and Gatehouse J.A. Fusion proteins containing insect-specific toxins as pest control agents: Snowdrop lectin delivers fused insecticidal spider venom toxin to insect haemolymph following oral ingestion. J. Insect Physiol. 50 (2004) 61-71
    • (2004) J. Insect Physiol. , vol.50 , pp. 61-71
    • Fitches, E.1    Edwards, M.G.2    Mee, C.3    Grishin, E.4    Gatehouse, A.M.R.5    Edwards, J.P.6    Gatehouse, J.A.7
  • 36
    • 0028898165 scopus 로고
    • Passage of Autographa californica nuclear polyhedrosis virus through the midgut epithelium of Spodoptera exigua larvae
    • Flipsen J.T.M., Martens J.W.M., Oers M.M.V., Vlak J.M., and Lent J.W.M.V. Passage of Autographa californica nuclear polyhedrosis virus through the midgut epithelium of Spodoptera exigua larvae. Virology 208 (1995) 328-335
    • (1995) Virology , vol.208 , pp. 328-335
    • Flipsen, J.T.M.1    Martens, J.W.M.2    Oers, M.M.V.3    Vlak, J.M.4    Lent, J.W.M.V.5
  • 37
    • 0033814168 scopus 로고    scopus 로고
    • Hydrolysis and synthesis of substrate proteins for cathepsin L in the brain basement membranes of Sarcophaga during metamorphosis
    • Fujii-Taira I., Tanaka Y., Homma K.J., and Natori S. Hydrolysis and synthesis of substrate proteins for cathepsin L in the brain basement membranes of Sarcophaga during metamorphosis. J. Biochem. (Tokyo) 128 3 (2000) 539-542
    • (2000) J. Biochem. (Tokyo) , vol.128 , Issue.3 , pp. 539-542
    • Fujii-Taira, I.1    Tanaka, Y.2    Homma, K.J.3    Natori, S.4
  • 38
    • 0034236249 scopus 로고    scopus 로고
    • Chitinolytic enzymes: Catalysis, substrate binding, and their application
    • Fukamizo T. Chitinolytic enzymes: Catalysis, substrate binding, and their application. Curr. Protein Pept. Sci. 1 (2000) 105-124
    • (2000) Curr. Protein Pept. Sci. , vol.1 , pp. 105-124
    • Fukamizo, T.1
  • 39
    • 0035140749 scopus 로고    scopus 로고
    • Peroral infectivity of non-occluded viruses of Bombyx mori nucleopolyhedrovirus and polyhedrin-negative recombinant baculoviruses to silkworm larvae is drastically enhanced when administered with Anomala cuprea entomopoxvirus spindles
    • Furuta Y., Mitsuhashi W., Kobayashi J., Hayasaka S., Imanishi S., Chinzei Y., and Sato M. Peroral infectivity of non-occluded viruses of Bombyx mori nucleopolyhedrovirus and polyhedrin-negative recombinant baculoviruses to silkworm larvae is drastically enhanced when administered with Anomala cuprea entomopoxvirus spindles. J. Gen. Virol. 82 (2001) 307-312
    • (2001) J. Gen. Virol. , vol.82 , pp. 307-312
    • Furuta, Y.1    Mitsuhashi, W.2    Kobayashi, J.3    Hayasaka, S.4    Imanishi, S.5    Chinzei, Y.6    Sato, M.7
  • 40
    • 27144485212 scopus 로고    scopus 로고
    • Comparison of the bacterial enhancin-like proteins from Yersinia and Bacillus spp. with a baculovirus enhancin
    • Galloway C.S., Wang P., Winstanley D., and Jones I.M. Comparison of the bacterial enhancin-like proteins from Yersinia and Bacillus spp. with a baculovirus enhancin. J. Invertebr. Pathol. 90 (2005) 134-137
    • (2005) J. Invertebr. Pathol. , vol.90 , pp. 134-137
    • Galloway, C.S.1    Wang, P.2    Winstanley, D.3    Jones, I.M.4
  • 42
    • 0029107764 scopus 로고
    • Baculovirus-mediated expression of a Manduca sexta chitinase gene: Properties of the recombinant protein
    • Gopalakrishnan B., Muthukrishnan S., and Kramer K.J. Baculovirus-mediated expression of a Manduca sexta chitinase gene: Properties of the recombinant protein. Insect Biochem. Mol. Biol. 25 2 (1995) 255-265
    • (1995) Insect Biochem. Mol. Biol. , vol.25 , Issue.2 , pp. 255-265
    • Gopalakrishnan, B.1    Muthukrishnan, S.2    Kramer, K.J.3
  • 43
    • 0019382221 scopus 로고
    • In vivo pathway of Autographa californica baculovirus invasion and infection
    • Granados R.R., and Lawler K.A. In vivo pathway of Autographa californica baculovirus invasion and infection. Virology 108 (1981) 297-308
    • (1981) Virology , vol.108 , pp. 297-308
    • Granados, R.R.1    Lawler, K.A.2
  • 44
    • 0027452622 scopus 로고
    • A 37-kilodalton glycoprotein from a baculovirus of Orgyia pseudotsugata is localized to cytoplasmic inclusion bodies
    • Gross C.H., Wolgamot G.M., Russell R.L., Pearson M.N., and Rohrmann G.F. A 37-kilodalton glycoprotein from a baculovirus of Orgyia pseudotsugata is localized to cytoplasmic inclusion bodies. J. Virol. 67 1 (1993) 469-475
    • (1993) J. Virol. , vol.67 , Issue.1 , pp. 469-475
    • Gross, C.H.1    Wolgamot, G.M.2    Russell, R.L.3    Pearson, M.N.4    Rohrmann, G.F.5
  • 45
    • 26244457216 scopus 로고    scopus 로고
    • A novel chitin-binding protein identified from the peritrophic membrane of the cabbage looper, Trichoplusia ni
    • Guo W.L.G., Pang Y., and Wang P. A novel chitin-binding protein identified from the peritrophic membrane of the cabbage looper, Trichoplusia ni. Insect Biochem. Mol. Biol. 35 (2005) 1224-1234
    • (2005) Insect Biochem. Mol. Biol. , vol.35 , pp. 1224-1234
    • Guo, W.L.G.1    Pang, Y.2    Wang, P.3
  • 47
    • 0000113162 scopus 로고
    • Chitinolytic enzymes of Trichoderma harzianum purification of chitobiosidase and endochitinase
    • Harman G.E., Hayes C.K., Lorito M., Broadway R.M., Pietro A.D., and Tronsmo A. Chitinolytic enzymes of Trichoderma harzianum purification of chitobiosidase and endochitinase. Phytopathology 83 (1993) 313-318
    • (1993) Phytopathology , vol.83 , pp. 313-318
    • Harman, G.E.1    Hayes, C.K.2    Lorito, M.3    Broadway, R.M.4    Pietro, A.D.5    Tronsmo, A.6
  • 48
    • 0035074167 scopus 로고    scopus 로고
    • Use of proteases to improve the insecticidal activity of baculoviruses
    • Harrison R.L., and Bonning B.C. Use of proteases to improve the insecticidal activity of baculoviruses. Biol. Control 20 (2001) 199-209
    • (2001) Biol. Control , vol.20 , pp. 199-209
    • Harrison, R.L.1    Bonning, B.C.2
  • 49
    • 0025997341 scopus 로고
    • Location and nucleotide sequence of the gene encoding the viral enhancing factor of the Trichoplusia ni granulosis virus
    • Hashimoto Y., Corsaro B.G., and Granados R.R. Location and nucleotide sequence of the gene encoding the viral enhancing factor of the Trichoplusia ni granulosis virus. J. Gen. Virol. 72 (1991) 2645-2651
    • (1991) J. Gen. Virol. , vol.72 , pp. 2645-2651
    • Hashimoto, Y.1    Corsaro, B.G.2    Granados, R.R.3
  • 52
    • 0031585572 scopus 로고    scopus 로고
    • Liquefaction of Autographa californica nucleopolyhedrovirus-infected insects is dependent on the integrity of virus-encoded chitinase and cathepsin genes
    • Hawtin R.E., Zarkowska T., Arnold K., Thomas C.J., Gooday G.W., King L.A., Kuzio J.A., and Possee R.D. Liquefaction of Autographa californica nucleopolyhedrovirus-infected insects is dependent on the integrity of virus-encoded chitinase and cathepsin genes. Virology 238 (1997) 243-253
    • (1997) Virology , vol.238 , pp. 243-253
    • Hawtin, R.E.1    Zarkowska, T.2    Arnold, K.3    Thomas, C.J.4    Gooday, G.W.5    King, L.A.6    Kuzio, J.A.7    Possee, R.D.8
  • 53
    • 0030600450 scopus 로고    scopus 로고
    • Cloning and sequencing of the gene for an enhancing factor from Pseudoletia separata entomopoxvirus
    • Hayakawa T., Xu J., and Hukuhara T. Cloning and sequencing of the gene for an enhancing factor from Pseudoletia separata entomopoxvirus. Gene 177 1-2 (1996) 269-270
    • (1996) Gene , vol.177 , Issue.1-2 , pp. 269-270
    • Hayakawa, T.1    Xu, J.2    Hukuhara, T.3
  • 54
    • 0033619202 scopus 로고    scopus 로고
    • Sequence analysis of the Xestia c-nigrum granulovirus genome
    • Hayakawa T., Ko R., Okano K., Seong S., Goto C., and Maeda S. Sequence analysis of the Xestia c-nigrum granulovirus genome. Virology 262 (1999) 277-297
    • (1999) Virology , vol.262 , pp. 277-297
    • Hayakawa, T.1    Ko, R.2    Okano, K.3    Seong, S.4    Goto, C.5    Maeda, S.6
  • 55
    • 1842473792 scopus 로고    scopus 로고
    • Transgenic tobacco transformed with the Trichoplusia ni granulovirus enhancin gene affects insect development
    • Hayakawa T., Hashimoto Y., Mori M., Kaido M., Shimojo E., Furusawa I., and Granados R.R. Transgenic tobacco transformed with the Trichoplusia ni granulovirus enhancin gene affects insect development. Biocontrol Sci. Technol. 14 2 (2004) 211-214
    • (2004) Biocontrol Sci. Technol. , vol.14 , Issue.2 , pp. 211-214
    • Hayakawa, T.1    Hashimoto, Y.2    Mori, M.3    Kaido, M.4    Shimojo, E.5    Furusawa, I.6    Granados, R.R.7
  • 57
    • 38249033254 scopus 로고
    • Temporal events in the invasion of the codling moth, Cydia pomonella, by a granulosis virus
    • Hess R.T., and Falcon L.A. Temporal events in the invasion of the codling moth, Cydia pomonella, by a granulosis virus. J. Invertebr. Pathol. 50 (1987) 85-105
    • (1987) J. Invertebr. Pathol. , vol.50 , pp. 85-105
    • Hess, R.T.1    Falcon, L.A.2
  • 59
    • 0034634333 scopus 로고    scopus 로고
    • Autographa californica M nucleopolyhedrovirus chiA is required for processing of V-CATH
    • Hom L.G., and Volkman L.E. Autographa californica M nucleopolyhedrovirus chiA is required for processing of V-CATH. Virology 277 (2000) 178-183
    • (2000) Virology , vol.277 , pp. 178-183
    • Hom, L.G.1    Volkman, L.E.2
  • 60
    • 0029830056 scopus 로고    scopus 로고
    • Identification of substrate proteins for cathepsin L that are selectively hydrolyzed during the differentiation of imaginal discs of Sarcophaga peregrina
    • Homma K., and Natori S. Identification of substrate proteins for cathepsin L that are selectively hydrolyzed during the differentiation of imaginal discs of Sarcophaga peregrina. Eur. J. Biochem. 240 (1996) 443-447
    • (1996) Eur. J. Biochem. , vol.240 , pp. 443-447
    • Homma, K.1    Natori, S.2
  • 61
    • 0028243651 scopus 로고
    • Purification, characterization, and cDNA cloning of procathepsin L from the culture medium of NIH-Sape-4, an embryonic cell line of Sarcophaga peregrina (flesh fly), and its involvement in the differentiation of imaginal discs
    • Homma K., Jurata S., and Natori S. Purification, characterization, and cDNA cloning of procathepsin L from the culture medium of NIH-Sape-4, an embryonic cell line of Sarcophaga peregrina (flesh fly), and its involvement in the differentiation of imaginal discs. J. Biol. Chem. 269 (1994) 15258-15264
    • (1994) J. Biol. Chem. , vol.269 , pp. 15258-15264
    • Homma, K.1    Jurata, S.2    Natori, S.3
  • 62
    • 0035380995 scopus 로고    scopus 로고
    • Agrobacterium tumefaciens-mediated transformation of rice with the spider insecticidal gene conferring resistance to leaffolder and striped stem borer
    • Huang J.Q., Wel Z.M., An H.L., and Zhu Y.X. Agrobacterium tumefaciens-mediated transformation of rice with the spider insecticidal gene conferring resistance to leaffolder and striped stem borer. Cell Res. 11 2 (2001) 149-155
    • (2001) Cell Res. , vol.11 , Issue.2 , pp. 149-155
    • Huang, J.Q.1    Wel, Z.M.2    An, H.L.3    Zhu, Y.X.4
  • 63
    • 0034762189 scopus 로고    scopus 로고
    • Enhanced fusion of a nucleopolyhedrovirus with cultured cells by a virus enhacing factor from an entomopoxvirus
    • Hukuhara T., and Wijonarko A. Enhanced fusion of a nucleopolyhedrovirus with cultured cells by a virus enhacing factor from an entomopoxvirus. J. Invertebr. Pathol. 77 (2001) 62-67
    • (2001) J. Invertebr. Pathol. , vol.77 , pp. 62-67
    • Hukuhara, T.1    Wijonarko, A.2
  • 64
    • 85008269152 scopus 로고
    • Synergistic factor shows specificity in enhancing nuclear polyhedrosis virus infections
    • Hukuhara T., Tamura K., Zhu Y., Abe H., and Tanada Y. Synergistic factor shows specificity in enhancing nuclear polyhedrosis virus infections. Appl. Entomol. Zool. 22 (1987) 235-236
    • (1987) Appl. Entomol. Zool. , vol.22 , pp. 235-236
    • Hukuhara, T.1    Tamura, K.2    Zhu, Y.3    Abe, H.4    Tanada, Y.5
  • 65
    • 0032716837 scopus 로고    scopus 로고
    • Increased baculovirus susceptibility of armyworm larvae feeding on trangenic rice plants expressing an entomopoxvirus gene
    • Hukuhara T., Hayakawa T., and Wijonarko A. Increased baculovirus susceptibility of armyworm larvae feeding on trangenic rice plants expressing an entomopoxvirus gene. Nat. Biotechnol. 17 (1999) 1122-1124
    • (1999) Nat. Biotechnol. , vol.17 , pp. 1122-1124
    • Hukuhara, T.1    Hayakawa, T.2    Wijonarko, A.3
  • 66
    • 0034861385 scopus 로고    scopus 로고
    • A bacterially produced virus enhancing factor from an entomopoxvirus enhances nucleopolyhedrovirus infection in armyworm larvae
    • Hukuhara T., Hayakawa T., and Wijonarko A. A bacterially produced virus enhancing factor from an entomopoxvirus enhances nucleopolyhedrovirus infection in armyworm larvae. J. Invertebr. Pathol. 78 1 (2001) 25-30
    • (2001) J. Invertebr. Pathol. , vol.78 , Issue.1 , pp. 25-30
    • Hukuhara, T.1    Hayakawa, T.2    Wijonarko, A.3
  • 67
    • 0034468246 scopus 로고    scopus 로고
    • Structural and functional analysis of the Xestia c-nigrum granulovirus matrix metalloproteinase
    • Ko R., Okano K., and Maeda S. Structural and functional analysis of the Xestia c-nigrum granulovirus matrix metalloproteinase. J. Virol. 74 (2000) 11240-11246
    • (2000) J. Virol. , vol.74 , pp. 11240-11246
    • Ko, R.1    Okano, K.2    Maeda, S.3
  • 68
    • 1042290220 scopus 로고    scopus 로고
    • Papain protects papaya trees from herbivorous insects: Role of cysteine proteases in latex
    • Konno K., Hirayama C., Nakamura M., Tateishi K., Tamura Y., Hattori M., and Kohno K. Papain protects papaya trees from herbivorous insects: Role of cysteine proteases in latex. Plant J. 37 (2004) 370-378
    • (2004) Plant J. , vol.37 , pp. 370-378
    • Konno, K.1    Hirayama, C.2    Nakamura, M.3    Tateishi, K.4    Tamura, Y.5    Hattori, M.6    Kohno, K.7
  • 69
    • 0000913849 scopus 로고
    • Applications of solids NMR to the analysis of insect sclerotized structures
    • Kramer K.J., Hopkins T.L., and Schaefer J. Applications of solids NMR to the analysis of insect sclerotized structures. Insect Biochem. Mol. Biol. 25 (1995) 1067-1080
    • (1995) Insect Biochem. Mol. Biol. , vol.25 , pp. 1067-1080
    • Kramer, K.J.1    Hopkins, T.L.2    Schaefer, J.3
  • 70
    • 0025730806 scopus 로고
    • Participation of a 200-kDa hemocyte membrane protein in the dissociation of the fat body at the metamorphosis of Sarcophaga
    • Kurata S., Kobayashi H., and Natori S. Participation of a 200-kDa hemocyte membrane protein in the dissociation of the fat body at the metamorphosis of Sarcophaga. Dev. Biol. 146 (1991) 179-185
    • (1991) Dev. Biol. , vol.146 , pp. 179-185
    • Kurata, S.1    Kobayashi, H.2    Natori, S.3
  • 71
    • 0026663222 scopus 로고
    • The 29-kDa hemocyte proteinase dissociates fat body at metamorphosis of Sarcophaga
    • Kurata S., Saito H., and Natori S. The 29-kDa hemocyte proteinase dissociates fat body at metamorphosis of Sarcophaga. Dev. Biol. 153 (1992) 115-121
    • (1992) Dev. Biol. , vol.153 , pp. 115-121
    • Kurata, S.1    Saito, H.2    Natori, S.3
  • 73
    • 0030891189 scopus 로고    scopus 로고
    • Peritrophic matrix structure and function
    • Lehane M.J. Peritrophic matrix structure and function. Annu. Rev. Entomol. 42 (1997) 525-550
    • (1997) Annu. Rev. Entomol. , vol.42 , pp. 525-550
    • Lehane, M.J.1
  • 74
    • 0030236551 scopus 로고    scopus 로고
    • Enhancin, the granulosis virus protein that facilitates nucleopolyhedrovirus (NPV) infections is a metalloprotease
    • Lepore L.S., Roelvink P.R., and Granados R.R. Enhancin, the granulosis virus protein that facilitates nucleopolyhedrovirus (NPV) infections is a metalloprotease. J. Invert. Pathol. 68 (1996) 131-140
    • (1996) J. Invert. Pathol. , vol.68 , pp. 131-140
    • Lepore, L.S.1    Roelvink, P.R.2    Granados, R.R.3
  • 75
    • 16244394834 scopus 로고    scopus 로고
    • Insect resistance to Nilaparvata lugens and Cnaphalocrocis medinalis in transgenic indica rice and the inheritance of gna + sbti transgenes
    • Li G., Xu X., Xing H., Zhu H., and Fan Q. Insect resistance to Nilaparvata lugens and Cnaphalocrocis medinalis in transgenic indica rice and the inheritance of gna + sbti transgenes. Pest Manag. Sci. 61 (2005) 390-396
    • (2005) Pest Manag. Sci. , vol.61 , pp. 390-396
    • Li, G.1    Xu, X.2    Xing, H.3    Zhu, H.4    Fan, Q.5
  • 76
    • 0036308465 scopus 로고    scopus 로고
    • Identification and genomic analysis of a second species of nucleopolyhedrovirus isolated from Mamestra configurata
    • Li L., Donly C., Li Q., Willis L.G., Keddie B.A., Erlandson M.A., and Theilmann D.A. Identification and genomic analysis of a second species of nucleopolyhedrovirus isolated from Mamestra configurata. Virology 297 (2002) 226-244
    • (2002) Virology , vol.297 , pp. 226-244
    • Li, L.1    Donly, C.2    Li, Q.3    Willis, L.G.4    Keddie, B.A.5    Erlandson, M.A.6    Theilmann, D.A.7
  • 77
    • 0037234666 scopus 로고    scopus 로고
    • Characterization of Mamestra configurata nucleopolyhedrovirus enhancin and its functional analysis via expression in an Autographa californica M nucleopolyhedrovirus recombinant
    • Li Q., Li L., Moore K., Donly C., Theilmann D.A., and Erlandson M. Characterization of Mamestra configurata nucleopolyhedrovirus enhancin and its functional analysis via expression in an Autographa californica M nucleopolyhedrovirus recombinant. J. Gen. Virol. 84 (2003) 123-132
    • (2003) J. Gen. Virol. , vol.84 , pp. 123-132
    • Li, Q.1    Li, L.2    Moore, K.3    Donly, C.4    Theilmann, D.A.5    Erlandson, M.6
  • 78
    • 0034094295 scopus 로고    scopus 로고
    • Characterization of an overexpressed spindle protein during a baculovirus infection
    • Li X., Barrett J., Pang A., Klose R.J., Krell P.J., and Arif B.M. Characterization of an overexpressed spindle protein during a baculovirus infection. Virology 268 (2000) 56-67
    • (2000) Virology , vol.268 , pp. 56-67
    • Li, X.1    Barrett, J.2    Pang, A.3    Klose, R.J.4    Krell, P.J.5    Arif, B.M.6
  • 79
    • 0142123458 scopus 로고    scopus 로고
    • Characterization of a chitin-binding protein GP37 of Spodoptera litura multicapsid nucleopolyhedrovirus
    • Li Z., Li C., Yang K., Wang L., Yin C., Gong Y., and Pang Y. Characterization of a chitin-binding protein GP37 of Spodoptera litura multicapsid nucleopolyhedrovirus. Virus Res. 96 1-2 (2003) 113-122
    • (2003) Virus Res. , vol.96 , Issue.1-2 , pp. 113-122
    • Li, Z.1    Li, C.2    Yang, K.3    Wang, L.4    Yin, C.5    Gong, Y.6    Pang, Y.7
  • 80
    • 0027547387 scopus 로고
    • Circadian expression and induction by wounding of tobacco genes for cysteine proteinase
    • Linthorst H.J.M., Oers C.V.D., Brederode F.T., and Bol J.F. Circadian expression and induction by wounding of tobacco genes for cysteine proteinase. Plant Mol. Biol. 21 (1993) 685-694
    • (1993) Plant Mol. Biol. , vol.21 , pp. 685-694
    • Linthorst, H.J.M.1    Oers, C.V.D.2    Brederode, F.T.3    Bol, J.F.4
  • 81
    • 0030587448 scopus 로고    scopus 로고
    • Identification, molecular cloning, and transcription analysis of the Choristoneura fumiferana nuclear polyhedrosis virus spindle-like protein gene
    • Liu J.J., and Carstens E.B. Identification, molecular cloning, and transcription analysis of the Choristoneura fumiferana nuclear polyhedrosis virus spindle-like protein gene. Virology 223 2 (1996) 396
    • (1996) Virology , vol.223 , Issue.2 , pp. 396
    • Liu, J.J.1    Carstens, E.B.2
  • 82
    • 0037189532 scopus 로고    scopus 로고
    • Structural and enzymatic characterization of Drosophila Dm2-MMP, a membrane-bound matrix metalloproteinase with tissue-specific expression
    • Llano E., Adam G., Pendas A.M., Quesada V., Sanchez L.M., Santamaria I., Noselli S., and Lopez-Otin C. Structural and enzymatic characterization of Drosophila Dm2-MMP, a membrane-bound matrix metalloproteinase with tissue-specific expression. J. Biol. Chem. 277 (2002) 23321-23329
    • (2002) J. Biol. Chem. , vol.277 , pp. 23321-23329
    • Llano, E.1    Adam, G.2    Pendas, A.M.3    Quesada, V.4    Sanchez, L.M.5    Santamaria, I.6    Noselli, S.7    Lopez-Otin, C.8
  • 83
    • 0035029037 scopus 로고    scopus 로고
    • Metalloproteinase activity in growth plate chondrocyte cultures is regulated by 1,25-(OH)2D3 and 24,25-(OH)2D3 and mediated through protein kinase C
    • Maeda S., Dean D.D., Sylvia V.L., Boyan B.D., and Schwartz Z. Metalloproteinase activity in growth plate chondrocyte cultures is regulated by 1,25-(OH)2D3 and 24,25-(OH)2D3 and mediated through protein kinase C. Matrix Biol. 20 (2001) 87-97
    • (2001) Matrix Biol. , vol.20 , pp. 87-97
    • Maeda, S.1    Dean, D.D.2    Sylvia, V.L.3    Boyan, B.D.4    Schwartz, Z.5
  • 84
    • 0141519063 scopus 로고    scopus 로고
    • Antibiosis-type resistance in transgenic plants expressing a teratocyte secretory peptide (TSP) gene from a hymenopteran endoparasite (Microplitis croceipes)
    • Maiti I.B., O., N., Dahlman D.L., and Webb B.A. Antibiosis-type resistance in transgenic plants expressing a teratocyte secretory peptide (TSP) gene from a hymenopteran endoparasite (Microplitis croceipes). Plant Biotech. J. 1 (2003) 209-219
    • (2003) Plant Biotech. J. , vol.1 , pp. 209-219
    • Maiti I.B., O.,, N.1    Dahlman, D.L.2    Webb, B.A.3
  • 85
    • 0029686049 scopus 로고    scopus 로고
    • Immune responses in insects: The role of phenoloxidase in defense reactions in relation to melanization and sclerotization
    • Marmaras V.J., Charalambidis N.D., and Zervas C.G. Immune responses in insects: The role of phenoloxidase in defense reactions in relation to melanization and sclerotization. Arch. Insect Biochem. Physiol. 31 (1996) 119-133
    • (1996) Arch. Insect Biochem. Physiol. , vol.31 , pp. 119-133
    • Marmaras, V.J.1    Charalambidis, N.D.2    Zervas, C.G.3
  • 86
    • 0141747755 scopus 로고    scopus 로고
    • Pea lectin expressed transgenically in oilseed rape reduces growth rate of pollen beetle larvae
    • Melander M., Ahman I., Kamnert I., and Stromdahl A.C. Pea lectin expressed transgenically in oilseed rape reduces growth rate of pollen beetle larvae. Transgenic Res. 12 (2003) 555-567
    • (2003) Transgenic Res. , vol.12 , pp. 555-567
    • Melander, M.1    Ahman, I.2    Kamnert, I.3    Stromdahl, A.C.4
  • 87
    • 0346399742 scopus 로고    scopus 로고
    • Chitin metabolism in insects: Structure, function and regulation of chitin synthases and chitinases
    • Merzendorfer H., and Zimoch L. Chitin metabolism in insects: Structure, function and regulation of chitin synthases and chitinases. J. Exp. Biol. 206 (2003) 4393-4412
    • (2003) J. Exp. Biol. , vol.206 , pp. 4393-4412
    • Merzendorfer, H.1    Zimoch, L.2
  • 89
    • 0037253464 scopus 로고    scopus 로고
    • Disintegration of the peritrophic membrane of silkworm larvae due to spindles of an entomopoxvirus
    • Mitsuhashi W., and Miyamoto K. Disintegration of the peritrophic membrane of silkworm larvae due to spindles of an entomopoxvirus. J. Invertebr. Pathol. 82 (2003) 34-40
    • (2003) J. Invertebr. Pathol. , vol.82 , pp. 34-40
    • Mitsuhashi, W.1    Miyamoto, K.2
  • 90
    • 0000536049 scopus 로고    scopus 로고
    • The spindles of an entomopoxvirus of Coleoptera (Anomala cuprea) strongly enhance the infectivity of a nucleopolyhedrovirus in Lepidoptera (Bombyx mori)
    • Mitsuhashi W., Furuta Y., and Sato M. The spindles of an entomopoxvirus of Coleoptera (Anomala cuprea) strongly enhance the infectivity of a nucleopolyhedrovirus in Lepidoptera (Bombyx mori). J. Invertebr. Pathol. 71 (1998) 186-188
    • (1998) J. Invertebr. Pathol. , vol.71 , pp. 186-188
    • Mitsuhashi, W.1    Furuta, Y.2    Sato, M.3
  • 91
    • 11244271521 scopus 로고    scopus 로고
    • Transgenic rice plants expressing the snowdrop lectin gene (gna) exhibit high-level resistance to the whitebacked planthopper (Sogatella furcifera)
    • Nagadhara D., Ramesh S., Pasalu I.C., Rao Y.K., Sarma N.P., Reddy V.D., and Rao K.V. Transgenic rice plants expressing the snowdrop lectin gene (gna) exhibit high-level resistance to the whitebacked planthopper (Sogatella furcifera). Theor. Appl. Genet. 109 (2004) 1399-1405
    • (2004) Theor. Appl. Genet. , vol.109 , pp. 1399-1405
    • Nagadhara, D.1    Ramesh, S.2    Pasalu, I.C.3    Rao, Y.K.4    Sarma, N.P.5    Reddy, V.D.6    Rao, K.V.7
  • 92
    • 15944404330 scopus 로고    scopus 로고
    • Melanogenesis and associated cytotoxic reactions: Applications to insect innate immunity
    • Nappi A.J., and Christensen B.M. Melanogenesis and associated cytotoxic reactions: Applications to insect innate immunity. Insect Biochem. Mol. Biol. 35 (2005) 443-459
    • (2005) Insect Biochem. Mol. Biol. , vol.35 , pp. 443-459
    • Nappi, A.J.1    Christensen, B.M.2
  • 93
    • 0034898420 scopus 로고    scopus 로고
    • The extracellular matrix protein lacunin is expressed by a subset of hemocytes involved in basal lamina morphogenesis
    • Nardi J.B., Gao C., and Kanost M.R. The extracellular matrix protein lacunin is expressed by a subset of hemocytes involved in basal lamina morphogenesis. J. Insect Physiol. 47 (2001) 997-1006
    • (2001) J. Insect Physiol. , vol.47 , pp. 997-1006
    • Nardi, J.B.1    Gao, C.2    Kanost, M.R.3
  • 94
    • 12744277891 scopus 로고    scopus 로고
    • Effects of plants genetically modified for insect resistance on nontarget organisms
    • O'Callaghan M., Glare T.R., Burgess E.P.J., and Malone L.A. Effects of plants genetically modified for insect resistance on nontarget organisms. Annu. Rev. Entomol. 50 (2005) 251-292
    • (2005) Annu. Rev. Entomol. , vol.50 , pp. 251-292
    • O'Callaghan, M.1    Glare, T.R.2    Burgess, E.P.J.3    Malone, L.A.4
  • 95
    • 0028021961 scopus 로고
    • A cysteine protease encoded by the baculovirus Bombyx mori nuclear polyhedrosis virus
    • Ohkawa T., Majima K., and Maeda S. A cysteine protease encoded by the baculovirus Bombyx mori nuclear polyhedrosis virus. J. Virol. 68 (1994) 6619-6625
    • (1994) J. Virol. , vol.68 , pp. 6619-6625
    • Ohkawa, T.1    Majima, K.2    Maeda, S.3
  • 96
    • 0037239819 scopus 로고    scopus 로고
    • Drosophila matrix metalloproteinases are required for tissue remodeling, but not embryonic development
    • Page-McCaw A., Serano J., Sante J.M., and Rubin G.M. Drosophila matrix metalloproteinases are required for tissue remodeling, but not embryonic development. Dev. Cell 4 (2003) 95-106
    • (2003) Dev. Cell , vol.4 , pp. 95-106
    • Page-McCaw, A.1    Serano, J.2    Sante, J.M.3    Rubin, G.M.4
  • 97
    • 0025959668 scopus 로고
    • Mutational analysis of the transin (rat stromelysin) autoinhibitor region demonstrates a role for residues surrounding the "cysteine switch."
    • Park A.J., Matrisian L.M., Kells A.F., Pearson R., Yuan Z., and Navre M. Mutational analysis of the transin (rat stromelysin) autoinhibitor region demonstrates a role for residues surrounding the "cysteine switch.". J. Biol. Chem. 266 (1991) 1584-1590
    • (1991) J. Biol. Chem. , vol.266 , pp. 1584-1590
    • Park, A.J.1    Matrisian, L.M.2    Kells, A.F.3    Pearson, R.4    Yuan, Z.5    Navre, M.6
  • 98
    • 0028831616 scopus 로고
    • Effects of basement membranes on the behavior of hemocytes from Pseudoplusia includens (Lepidoptera: Noctuidae): Development of an in vitro encapsulation assay
    • Pech L.L., Trudeau D., and Strand M.R. Effects of basement membranes on the behavior of hemocytes from Pseudoplusia includens (Lepidoptera: Noctuidae): Development of an in vitro encapsulation assay. J. Insect Physiol. 41 9 (1995) 801
    • (1995) J. Insect Physiol. , vol.41 , Issue.9 , pp. 801
    • Pech, L.L.1    Trudeau, D.2    Strand, M.R.3
  • 99
    • 0033868878 scopus 로고    scopus 로고
    • A unique 33-kD cysteine protease accumulates in response to larval feeding in maize genotypes resistant to fall armyworm and other Lepidoptera
    • Pechan T., Ye L., Chang Y., Mitra A., Lin L., Davis F.M., Williams W.P., and Luthe D.S. A unique 33-kD cysteine protease accumulates in response to larval feeding in maize genotypes resistant to fall armyworm and other Lepidoptera. Plant Cell 12 (2000) 1031-1040
    • (2000) Plant Cell , vol.12 , pp. 1031-1040
    • Pechan, T.1    Ye, L.2    Chang, Y.3    Mitra, A.4    Lin, L.5    Davis, F.M.6    Williams, W.P.7    Luthe, D.S.8
  • 100
    • 44949274418 scopus 로고
    • Structure and composition of basement membranes and other basal matrix systems in selected invertebrates
    • Pedersen K.J. Structure and composition of basement membranes and other basal matrix systems in selected invertebrates. Acta Zool. 72 4 (1991) 181-201
    • (1991) Acta Zool. , vol.72 , Issue.4 , pp. 181-201
    • Pedersen, K.J.1
  • 101
    • 0031883673 scopus 로고    scopus 로고
    • Characterization of monoclonal antibodies against cell wall epitopes of the insect pathogenic fungus, Nomuraea rileyi: Differential binding to fungal surfaces and cross-reactivity with host hemocytes and basement membrane components
    • Pendland J.C., and Boucias D.G. Characterization of monoclonal antibodies against cell wall epitopes of the insect pathogenic fungus, Nomuraea rileyi: Differential binding to fungal surfaces and cross-reactivity with host hemocytes and basement membrane components. Eur. J. Cell Biol. 75 (1998) 118-127
    • (1998) Eur. J. Cell Biol. , vol.75 , pp. 118-127
    • Pendland, J.C.1    Boucias, D.G.2
  • 102
    • 0034108574 scopus 로고    scopus 로고
    • Comparative analysis of the binding of antibodies prepared against the insect Spodoptera exigua and against the mycopathogen Nomuraea rileyi
    • Pendland J.C., and Boucias D.G. Comparative analysis of the binding of antibodies prepared against the insect Spodoptera exigua and against the mycopathogen Nomuraea rileyi. J. Inverteb. Pathol. 75 (2000) 107-116
    • (2000) J. Inverteb. Pathol. , vol.75 , pp. 107-116
    • Pendland, J.C.1    Boucias, D.G.2
  • 103
    • 0032895628 scopus 로고    scopus 로고
    • A baculovirus enhancin alters the permeability of a mucosal midgut peritrophic matrix from lepidopteran larvae
    • Peng J., Zhong J., and Granados R.R. A baculovirus enhancin alters the permeability of a mucosal midgut peritrophic matrix from lepidopteran larvae. J. Insect Physiol. 45 (1999) 159-166
    • (1999) J. Insect Physiol. , vol.45 , pp. 159-166
    • Peng, J.1    Zhong, J.2    Granados, R.R.3
  • 105
    • 0034881152 scopus 로고    scopus 로고
    • Both Lymantria dispar nucleopolyhedrovirus enhancin genes contribute to viral potency
    • Popham H.J.R., Bischoff D.S., and Slavicek J.M. Both Lymantria dispar nucleopolyhedrovirus enhancin genes contribute to viral potency. J. Virol. 75 18 (2001) 8639-8648
    • (2001) J. Virol. , vol.75 , Issue.18 , pp. 8639-8648
    • Popham, H.J.R.1    Bischoff, D.S.2    Slavicek, J.M.3
  • 107
    • 0034029972 scopus 로고    scopus 로고
    • A new entomopoxvirus from a cockroach: Light and electron microscopy
    • Radek R., and Fabel P. A new entomopoxvirus from a cockroach: Light and electron microscopy. J. Invertebr. Pathol. 75 1 (2000) 19-27
    • (2000) J. Invertebr. Pathol. , vol.75 , Issue.1 , pp. 19-27
    • Radek, R.1    Fabel, P.2
  • 109
    • 0028814176 scopus 로고
    • Toxicity of lectins and processing of ingested in the pea aphid Acyrthosiphon pisum
    • Rahbe Y., Sauvion N., Febvay G., Peumans W.J., and Gatehouse A.M.R. Toxicity of lectins and processing of ingested in the pea aphid Acyrthosiphon pisum. Entomol. Exp. Appl. 76 (1995) 143-155
    • (1995) Entomol. Exp. Appl. , vol.76 , pp. 143-155
    • Rahbe, Y.1    Sauvion, N.2    Febvay, G.3    Peumans, W.J.4    Gatehouse, A.M.R.5
  • 112
    • 0027032145 scopus 로고
    • The baculovirus Autographa californica nuclear polyhedrosis virus genome includes a papain-like sequence
    • Rawlings N.D., Pearl L.H., and Buttle J. The baculovirus Autographa californica nuclear polyhedrosis virus genome includes a papain-like sequence. Biol. Chem. Hoppe Seyler 373 (1992) 1211-1215
    • (1992) Biol. Chem. Hoppe Seyler , vol.373 , pp. 1211-1215
    • Rawlings, N.D.1    Pearl, L.H.2    Buttle, J.3
  • 113
    • 0001554723 scopus 로고
    • The size limited penetration of gold particles through insect basal laminae
    • Reddy J.T., and Locke M. The size limited penetration of gold particles through insect basal laminae. J. Insect Physiol. 36 (1990) 397-407
    • (1990) J. Insect Physiol. , vol.36 , pp. 397-407
    • Reddy, J.T.1    Locke, M.2
  • 114
    • 0016237017 scopus 로고
    • Basement membrane abnormalities in melanotic tumor formation of Drosophila
    • Rizki R.M., and Rizki T.M. Basement membrane abnormalities in melanotic tumor formation of Drosophila. Experientia 30 5 (1974) 543-546
    • (1974) Experientia , vol.30 , Issue.5 , pp. 543-546
    • Rizki, R.M.1    Rizki, T.M.2
  • 115
    • 0001788246 scopus 로고
    • Hemocyte responses to implanted tissues in Drosophila melanogaster larvae
    • Rizki R.M., and Rizki T.M. Hemocyte responses to implanted tissues in Drosophila melanogaster larvae. Roux's Arch. Dev. Biol. 189 (1980) 207-213
    • (1980) Roux's Arch. Dev. Biol. , vol.189 , pp. 207-213
    • Rizki, R.M.1    Rizki, T.M.2
  • 116
    • 0028847068 scopus 로고
    • Characterization of the Helicoverpa armigera and Pseudaletia unipuncta granulovirus enhancin genes
    • Roelvink P.W., Corsaro B.G., and Granados R.R. Characterization of the Helicoverpa armigera and Pseudaletia unipuncta granulovirus enhancin genes. J. Gen. Virol. 76 (1995) 2693-2705
    • (1995) J. Gen. Virol. , vol.76 , pp. 2693-2705
    • Roelvink, P.W.1    Corsaro, B.G.2    Granados, R.R.3
  • 118
    • 0002113011 scopus 로고    scopus 로고
    • Basal laminae
    • Harrison F.W., and Locke M. (Eds), Wiley-Liss, Inc., New York
    • Ryerse J.S. Basal laminae. In: Harrison F.W., and Locke M. (Eds). "Insecta" Vol. 11A (1998), Wiley-Liss, Inc., New York 3-16
    • (1998) "Insecta" , vol.11 A , pp. 3-16
    • Ryerse, J.S.1
  • 120
    • 0027297246 scopus 로고
    • Chitinases of fungi and plants: Their involvement in morphogenesis and host parasite interaction
    • Sahai A.S., and Manocha M.S. Chitinases of fungi and plants: Their involvement in morphogenesis and host parasite interaction. FEMS Microbiol. Rev. 11 (1993) 317-338
    • (1993) FEMS Microbiol. Rev. , vol.11 , pp. 317-338
    • Sahai, A.S.1    Manocha, M.S.2
  • 121
    • 0029660198 scopus 로고    scopus 로고
    • Effects of GNA and other binding lectins on development and fecundity of the peach-potato aphid Myzus persicae
    • Sauvion N., Rahbe Y., Peumans W.J., Damme E.J.V., Gatehouse J.A., and Gatehouse A.M.R. Effects of GNA and other binding lectins on development and fecundity of the peach-potato aphid Myzus persicae. Entomol. Exp. Appl. 79 (1996) 285-293
    • (1996) Entomol. Exp. Appl. , vol.79 , pp. 285-293
    • Sauvion, N.1    Rahbe, Y.2    Peumans, W.J.3    Damme, E.J.V.4    Gatehouse, J.A.5    Gatehouse, A.M.R.6
  • 122
    • 0036547407 scopus 로고    scopus 로고
    • Evaluation of lectin-expressing transgenic sugarcane against stalkborers (Lepidoptera: Pyralidae): Effects on life history parameters
    • Setamou M., Bernal J.S., Legaspi J.C., Mirkov T.E., and B.C.L. Jr. Evaluation of lectin-expressing transgenic sugarcane against stalkborers (Lepidoptera: Pyralidae): Effects on life history parameters. J. Econ. Entomol. 95 (2002) 469-477
    • (2002) J. Econ. Entomol. , vol.95 , pp. 469-477
    • Setamou, M.1    Bernal, J.S.2    Legaspi, J.C.3    Mirkov, T.E.4    B.C.L., Jr.5
  • 123
    • 33748755336 scopus 로고    scopus 로고
    • Identification and characterization of a novel peritrophic matrix protein, Ae-Aper50, and the microvillar membrane protein, AEG12, from the mosquito, Aedes aegypti
    • Shao L., Devenport M., Fujioka H., Ghosh A., and Jacobs-Lorena M. Identification and characterization of a novel peritrophic matrix protein, Ae-Aper50, and the microvillar membrane protein, AEG12, from the mosquito, Aedes aegypti. Insect Biochem. Mol. Biol. 273 (2005) 17665-17670
    • (2005) Insect Biochem. Mol. Biol. , vol.273 , pp. 17665-17670
    • Shao, L.1    Devenport, M.2    Fujioka, H.3    Ghosh, A.4    Jacobs-Lorena, M.5
  • 124
    • 0032504233 scopus 로고    scopus 로고
    • A type I peritrophic matrix protein from the malaria vector Anopheles gambiae binds to chitin. Cloning, expression and characterization
    • Shen Z., and Jacobs-Lorena M. A type I peritrophic matrix protein from the malaria vector Anopheles gambiae binds to chitin. Cloning, expression and characterization. J. Biol. Chem. 273 28 (1998) 17665-17670
    • (1998) J. Biol. Chem. , vol.273 , Issue.28 , pp. 17665-17670
    • Shen, Z.1    Jacobs-Lorena, M.2
  • 125
    • 0029028116 scopus 로고
    • Characterization of v-cath, a cathepsin-L-like proteinase expressed by the baculovirus Autographa californica multiple nuclear polyhedrosis virus
    • Slack J.M., Kuzio J., and Faulkner P. Characterization of v-cath, a cathepsin-L-like proteinase expressed by the baculovirus Autographa californica multiple nuclear polyhedrosis virus. J. Gen. Virol. 76 (1995) 1091-1098
    • (1995) J. Gen. Virol. , vol.76 , pp. 1091-1098
    • Slack, J.M.1    Kuzio, J.2    Faulkner, P.3
  • 126
    • 23244437257 scopus 로고    scopus 로고
    • The Lymantria dispar nucleopolyhedrovirus enhancins are components of occlusion-derived virus
    • Slavicek J.M., and Popham H.J. The Lymantria dispar nucleopolyhedrovirus enhancins are components of occlusion-derived virus. J. Virol. 79 (2005) 10578-10588
    • (2005) J. Virol. , vol.79 , pp. 10578-10588
    • Slavicek, J.M.1    Popham, H.J.2
  • 127
    • 0022636080 scopus 로고
    • Infection of silkmoth follicular cells with Bombyx mori nuclear polyhedrosis virus
    • Smith-Johannsen H., Witkiewicz H., and Iatrou K. Infection of silkmoth follicular cells with Bombyx mori nuclear polyhedrosis virus. J. Inverteb. Pathol. 48 (1986) 74-84
    • (1986) J. Inverteb. Pathol. , vol.48 , pp. 74-84
    • Smith-Johannsen, H.1    Witkiewicz, H.2    Iatrou, K.3
  • 128
    • 0032987871 scopus 로고    scopus 로고
    • Expression of the insecticidal lectin from snowdrop (Galanthus nivalis aggluitin; GNA) in transgenic wheat plants: Effects on predation by the grain aphid Sitobion avenae
    • Stoger E., Williams S., Christou P., Down R.E., and Gatehouse J.A. Expression of the insecticidal lectin from snowdrop (Galanthus nivalis aggluitin; GNA) in transgenic wheat plants: Effects on predation by the grain aphid Sitobion avenae. Mol. Breeding 5 (1998) 65-73
    • (1998) Mol. Breeding , vol.5 , pp. 65-73
    • Stoger, E.1    Williams, S.2    Christou, P.3    Down, R.E.4    Gatehouse, J.A.5
  • 130
    • 0027493068 scopus 로고
    • Molecular cloning of cDNA for the 29 kDa proteinase participating in decomposition of the larval fat body, during metamorphosis of Sarcophaga peregrine (flesh fly)
    • Takahashi N., Kurata S., and Natori S. Molecular cloning of cDNA for the 29 kDa proteinase participating in decomposition of the larval fat body, during metamorphosis of Sarcophaga peregrine (flesh fly). FEBS. Lett. 334 (1993) 153-157
    • (1993) FEBS. Lett. , vol.334 , pp. 153-157
    • Takahashi, N.1    Kurata, S.2    Natori, S.3
  • 131
    • 0000890918 scopus 로고
    • Synergism between two viruses of the armyworm, Pseudaletia unipuncta (Haworth) (Lepidoptera, Noctuidae)
    • Tanada Y. Synergism between two viruses of the armyworm, Pseudaletia unipuncta (Haworth) (Lepidoptera, Noctuidae). J. Insect. Pathol. 1 (1959) 215-231
    • (1959) J. Insect. Pathol. , vol.1 , pp. 215-231
    • Tanada, Y.1
  • 132
    • 0015536782 scopus 로고
    • Isolation of a factor, from the capsule of a granulosis virus, synergistic for a nuclear-polyhedrosis virus of the armworm
    • Tanada Y., Himeno M., and Omi E.M. Isolation of a factor, from the capsule of a granulosis virus, synergistic for a nuclear-polyhedrosis virus of the armworm. J. Invertebr. Pathol. 21 (1973) 81-90
    • (1973) J. Invertebr. Pathol. , vol.21 , pp. 81-90
    • Tanada, Y.1    Himeno, M.2    Omi, E.M.3
  • 134
    • 0035378362 scopus 로고    scopus 로고
    • The origin and functions of the insect peritrophic membrane and peritrophic gel
    • Terra W.R. The origin and functions of the insect peritrophic membrane and peritrophic gel. Arch. Insect Biochem. Physiol. 47 (2001) 47-61
    • (2001) Arch. Insect Biochem. Physiol. , vol.47 , pp. 47-61
    • Terra, W.R.1
  • 135
    • 0027999854 scopus 로고
    • Insect digestive enzymes-properties, compartmentalization and function
    • Terra W.R., and Ferreira C. Insect digestive enzymes-properties, compartmentalization and function. Comp. Biochem. Physiol. B. 109 (1994) 1-62
    • (1994) Comp. Biochem. Physiol. B. , vol.109 , pp. 1-62
    • Terra, W.R.1    Ferreira, C.2
  • 136
    • 0034283015 scopus 로고    scopus 로고
    • Matrilysin-2, a new matrix metalloproteinase expressed in human tumors and showing the minimal domain organization required for secretion, latency, and activity
    • Uria J.A., and Lopez-Otin C. Matrilysin-2, a new matrix metalloproteinase expressed in human tumors and showing the minimal domain organization required for secretion, latency, and activity. Cancer Res. 60 (2000) 4745-4751
    • (2000) Cancer Res. , vol.60 , pp. 4745-4751
    • Uria, J.A.1    Lopez-Otin, C.2
  • 137
    • 23344446196 scopus 로고    scopus 로고
    • The non-catalytic chitin-binding protein CBP21 from Serratia marcescens is essential for chitin degradation
    • Vaaje-Kolstad G., Horn S.J., Aalten D.M.V., Synstad B., and Eijsink V.G. The non-catalytic chitin-binding protein CBP21 from Serratia marcescens is essential for chitin degradation. J. Biol. Chem. 280 (2005) 28492-28497
    • (2005) J. Biol. Chem. , vol.280 , pp. 28492-28497
    • Vaaje-Kolstad, G.1    Horn, S.J.2    Aalten, D.M.V.3    Synstad, B.4    Eijsink, V.G.5
  • 138
    • 0036921508 scopus 로고    scopus 로고
    • Insect inhibitors of metalloproteinases
    • Vilcinskas A., and Wedde M. Insect inhibitors of metalloproteinases. IUBMB Life 54 (2002) 339-343
    • (2002) IUBMB Life , vol.54 , pp. 339-343
    • Vilcinskas, A.1    Wedde, M.2
  • 139
    • 0030632479 scopus 로고    scopus 로고
    • Nucleopolyhedrovirus interactions with their insect hosts
    • Volkman L.E. Nucleopolyhedrovirus interactions with their insect hosts. Adv. Virus Res. 48 (1997) 313-348
    • (1997) Adv. Virus Res. , vol.48 , pp. 313-348
    • Volkman, L.E.1
  • 140
    • 1442348816 scopus 로고    scopus 로고
    • Characterization and phylogenetic analysis of the chitinase gene from the Helicoverpa armigera single nucleocapsid nucleopolyhedrovirus
    • Wang H., Wu D., Deng F., Peng H., Chen X., Lauzon H., Arif B.M., Jehle J.A., and Hu Z. Characterization and phylogenetic analysis of the chitinase gene from the Helicoverpa armigera single nucleocapsid nucleopolyhedrovirus. Virus Res. 100 (2004) 179-189
    • (2004) Virus Res. , vol.100 , pp. 179-189
    • Wang, H.1    Wu, D.2    Deng, F.3    Peng, H.4    Chen, X.5    Lauzon, H.6    Arif, B.M.7    Jehle, J.A.8    Hu, Z.9
  • 141
    • 27444433441 scopus 로고    scopus 로고
    • Novel insect resistance in Brassica napus developed by transformation of chitinase and scorpion toxin genes
    • Wang J., Chen Z., Du J., Sun Y., and Liang A. Novel insect resistance in Brassica napus developed by transformation of chitinase and scorpion toxin genes. Plant Cell Rep. 24 (2005) 549-555
    • (2005) Plant Cell Rep. , vol.24 , pp. 549-555
    • Wang, J.1    Chen, Z.2    Du, J.3    Sun, Y.4    Liang, A.5
  • 142
    • 0030990106 scopus 로고    scopus 로고
    • An intestinal mucin is the target substrate for a baculovirus enhancin
    • Wang P., and Granados R.R. An intestinal mucin is the target substrate for a baculovirus enhancin. Proc. Natl. Acad. Sci. USA 94 (1997) 6977-6982
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 6977-6982
    • Wang, P.1    Granados, R.R.2
  • 143
    • 0030985902 scopus 로고    scopus 로고
    • Molecular cloning and sequencing of a novel invertebrate intestinal mucin cDNA
    • Wang P., and Granados R.R. Molecular cloning and sequencing of a novel invertebrate intestinal mucin cDNA. J. Biol. Chem. 272 26 (1997) 16663-16669
    • (1997) J. Biol. Chem. , vol.272 , Issue.26 , pp. 16663-16669
    • Wang, P.1    Granados, R.R.2
  • 144
    • 0033975247 scopus 로고    scopus 로고
    • Calcofluor disrupts the midgut defense system of insects
    • Wang P., and Granados R.R. Calcofluor disrupts the midgut defense system of insects. Insect Biochem. Mol. Biol. 30 (2000) 135-143
    • (2000) Insect Biochem. Mol. Biol. , vol.30 , pp. 135-143
    • Wang, P.1    Granados, R.R.2
  • 145
    • 0035377371 scopus 로고    scopus 로고
    • Molecular structure of the peritrophic membrane (PM): Identification of potential PM target sites for insect control
    • Wang P., and Granados R.R. Molecular structure of the peritrophic membrane (PM): Identification of potential PM target sites for insect control. Arch. Insect Biochem. Physiol. 47 2 (2001) 110-118
    • (2001) Arch. Insect Biochem. Physiol. , vol.47 , Issue.2 , pp. 110-118
    • Wang, P.1    Granados, R.R.2
  • 146
    • 0027989844 scopus 로고
    • Interaction of Trichoplusia ni granulosis virus-encoded enhancin with the midgut epithelium and peritrophic membrane of four lepidopteran insects
    • Wang P., Hammer D.A., and Granados R.R. Interaction of Trichoplusia ni granulosis virus-encoded enhancin with the midgut epithelium and peritrophic membrane of four lepidopteran insects. J. Gen. Virol. 75 (1994) 1961-1967
    • (1994) J. Gen. Virol. , vol.75 , pp. 1961-1967
    • Wang, P.1    Hammer, D.A.2    Granados, R.R.3
  • 147
    • 1242322069 scopus 로고    scopus 로고
    • Identification of two new peritrophic membrane proteins from larval Trichoplusia ni: Structural characteristics and their functions in the protease rich insect gut
    • Wang P., Li G., and Granados R.R. Identification of two new peritrophic membrane proteins from larval Trichoplusia ni: Structural characteristics and their functions in the protease rich insect gut. Insect Biochem. Mol. Biol. 34 3 (2004) 215-227
    • (2004) Insect Biochem. Mol. Biol. , vol.34 , Issue.3 , pp. 215-227
    • Wang, P.1    Li, G.2    Granados, R.R.3
  • 148
    • 0032110330 scopus 로고    scopus 로고
    • Detection of a virus enhancing factor in the spheroid, spindle, and virion of an entomopoxvirus
    • Wijonarko A., and Hukuhara T. Detection of a virus enhancing factor in the spheroid, spindle, and virion of an entomopoxvirus. J. Invertebr. Pathol. 72 1 (1998) 82
    • (1998) J. Invertebr. Pathol. , vol.72 , Issue.1 , pp. 82
    • Wijonarko, A.1    Hukuhara, T.2
  • 150
    • 0000391222 scopus 로고
    • Enhanced infection of a nuclear polyhedrosis virus in larvae of the armyworm, Pseudoletia separata, by a factor in the spheroids of an entomopoxvirus
    • Xu J., and Hukuhara T. Enhanced infection of a nuclear polyhedrosis virus in larvae of the armyworm, Pseudoletia separata, by a factor in the spheroids of an entomopoxvirus. J. Invertebr. Pathol. 60 (1992) 259-264
    • (1992) J. Invertebr. Pathol. , vol.60 , pp. 259-264
    • Xu, J.1    Hukuhara, T.2
  • 151
    • 0028154297 scopus 로고
    • Biochemical properties of an enhancing factor of an entomopoxvirus
    • Xu J., and Hukuhara T. Biochemical properties of an enhancing factor of an entomopoxvirus. J. Invertebr. Pathol. 63 (1994) 14-18
    • (1994) J. Invertebr. Pathol. , vol.63 , pp. 14-18
    • Xu, J.1    Hukuhara, T.2
  • 152
    • 0030333563 scopus 로고    scopus 로고
    • Insect-resistant tobacco plants expressing insect-specific neurotoxin AaIT
    • Yao B., Fan Y., Zheng Q., and Zhao R. Insect-resistant tobacco plants expressing insect-specific neurotoxin AaIT. Chin. J. Biotechnol. 12 2 (1996) 67-72
    • (1996) Chin. J. Biotechnol. , vol.12 , Issue.2 , pp. 67-72
    • Yao, B.1    Fan, Y.2    Zheng, Q.3    Zhao, R.4
  • 153
    • 28044451541 scopus 로고    scopus 로고
    • Characterization of an exochitinase from Epiphyas postvittana nucleopolyhedrovirus (family Baculoviridae)
    • Young V.L., Simpson R.M., and Ward V.K. Characterization of an exochitinase from Epiphyas postvittana nucleopolyhedrovirus (family Baculoviridae). J. Gen. Virol. 86 (2005) 3253-3261
    • (2005) J. Gen. Virol. , vol.86 , pp. 3253-3261
    • Young, V.L.1    Simpson, R.M.2    Ward, V.K.3
  • 154
    • 0002517253 scopus 로고
    • Supramolecular organization of basement membranes
    • Rohrbach D.H., and Timpl R. (Eds), Academic Press, New York
    • Yurchenco P.D., and O'Rear J. Supramolecular organization of basement membranes. In: Rohrbach D.H., and Timpl R. (Eds). "Molecular and Cellular Aspects of Basement Membranes" (1993), Academic Press, New York 19-47
    • (1993) "Molecular and Cellular Aspects of Basement Membranes" , pp. 19-47
    • Yurchenco, P.D.1    O'Rear, J.2
  • 156
    • 0032052228 scopus 로고    scopus 로고
    • Purification and characterization of a cysteine proteinase from eggs of the cotton boll worm, Helicoverpa armigera
    • Zhao X.F., Wang J.X., and Wang Y.C. Purification and characterization of a cysteine proteinase from eggs of the cotton boll worm, Helicoverpa armigera. Insect Biochem. Mol. Biol. 28 (1998) 259-264
    • (1998) Insect Biochem. Mol. Biol. , vol.28 , pp. 259-264
    • Zhao, X.F.1    Wang, J.X.2    Wang, Y.C.3
  • 157
    • 0031609630 scopus 로고    scopus 로고
    • Inhibition effect of transgenic tobacco plants expressing snowdrop lectin on the population development of Myzus persicae
    • Zhou Y.T., Wu B., and Mang K. Inhibition effect of transgenic tobacco plants expressing snowdrop lectin on the population development of Myzus persicae. Chin. J. Biotechnol. 14 (1998) 9-16
    • (1998) Chin. J. Biotechnol. , vol.14 , pp. 9-16
    • Zhou, Y.T.1    Wu, B.2    Mang, K.3


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