메뉴 건너뛰기




Volumn 6, Issue 3, 2011, Pages

Reduced levels of membrane-bound alkaline phosphatase are common to lepidopteran strains resistant to Cry toxins from Bacillus thuringiensis

Author keywords

[No Author keywords available]

Indexed keywords

ALKALINE PHOSPHATASE; BACTERIAL TOXIN; BIOLOGICAL MARKER; CRY1AC TOXIN; CRY1FA PROTEIN; UNCLASSIFIED DRUG; BACTERIAL PROTEIN; ENDOTOXIN; HEMOLYSIN; INSECTICIDAL CRYSTAL PROTEIN, BACILLUS THURINGIENSIS; MESSENGER RNA;

EID: 79952295293     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0017606     Document Type: Article
Times cited : (142)

References (70)
  • 1
    • 28444491225 scopus 로고    scopus 로고
    • Global status of commercialized Biotech/GM crops: 2009
    • ISAAA briefs No 41 ISAAA, Ithaca, NY
    • James C, (2009) Global status of commercialized Biotech/GM crops: 2009. ISAAA briefs No 41 ISAAA, Ithaca, NY.
    • (2009)
    • James, C.1
  • 3
    • 77955312533 scopus 로고    scopus 로고
    • Discovery and characterization of field resistance to Bt maize: Spodoptera frugiperda (Lepidoptera: Noctuidae) in Puerto Rico
    • Storer NP, Babcock JM, Schlenz M, Meade T, Thompson GD, et al. (2010) Discovery and characterization of field resistance to Bt maize: Spodoptera frugiperda (Lepidoptera: Noctuidae) in Puerto Rico. J Econ Entomol 103: 1031-1038.
    • (2010) J Econ Entomol , vol.103 , pp. 1031-1038
    • Storer, N.P.1    Babcock, J.M.2    Schlenz, M.3    Meade, T.4    Thompson, G.D.5
  • 4
    • 35649020475 scopus 로고    scopus 로고
    • First report of field resistance by stem borer, Busseola fusca (Fuller) to Bt-transgenic maize
    • Van Rensburg JBJ, (2007) First report of field resistance by stem borer, Busseola fusca (Fuller) to Bt-transgenic maize. S African J Plant Soil 24: 147-151.
    • (2007) S African J Plant Soil , vol.24 , pp. 147-151
    • van Rensburg, J.B.J.1
  • 5
    • 0036006844 scopus 로고    scopus 로고
    • Biochemistry and genetics of insect resistance to Bacillus thuringiensis
    • Ferre J, Van Rie J, (2002) Biochemistry and genetics of insect resistance to Bacillus thuringiensis. Annu Rev Entomol 47: 501-533.
    • (2002) Annu Rev Entomol , vol.47 , pp. 501-533
    • Ferre, J.1    van Rie, J.2
  • 8
    • 67349236660 scopus 로고    scopus 로고
    • Signaling versus punching hole: How do Bacillus thuringiensis toxins kill insect midgut cells?
    • Soberon M, Gill SS, Bravo A, (2009) Signaling versus punching hole: How do Bacillus thuringiensis toxins kill insect midgut cells? Cell Mol Life Sci 66: 1337-1349.
    • (2009) Cell Mol Life Sci , vol.66 , pp. 1337-1349
    • Soberon, M.1    Gill, S.S.2    Bravo, A.3
  • 9
    • 77951246496 scopus 로고    scopus 로고
    • Role of alkaline phosphatase from Manduca sexta in the mechanism of action of Bacillus thuringiensis Cry1Ab toxin
    • Arenas I, Bravo A, Soberon M, Gomez I, (2010) Role of alkaline phosphatase from Manduca sexta in the mechanism of action of Bacillus thuringiensis Cry1Ab toxin. J Biol chem 285: 12497-12503.
    • (2010) J Biol Chem , vol.285 , pp. 12497-12503
    • Arenas, I.1    Bravo, A.2    Soberon, M.3    Gomez, I.4
  • 10
    • 7744222624 scopus 로고    scopus 로고
    • Oligomerization triggers binding of a Bacillus thuringiensis Cry1Ab pore-forming toxin to aminopeptidase N receptor leading to insertion into membrane microdomains
    • Bravo A, Gomez I, Conde J, Munoz-Garay C, Sanchez J, et al. (2004) Oligomerization triggers binding of a Bacillus thuringiensis Cry1Ab pore-forming toxin to aminopeptidase N receptor leading to insertion into membrane microdomains. Biochim Biophys Acta 1667: 38-46.
    • (2004) Biochim Biophys Acta , vol.1667 , pp. 38-46
    • Bravo, A.1    Gomez, I.2    Conde, J.3    Munoz-Garay, C.4    Sanchez, J.5
  • 11
    • 33748663289 scopus 로고    scopus 로고
    • Structural changes of the Cry1Ac oligomeric pre-pore from Bacillus thuringiensis induced by N-acetylgalactosamine facilitates toxin membrane insertion
    • Pardo-Lopez L, Gomez I, Rausell C, Sanchez J, Soberon M, et al. (2006) Structural changes of the Cry1Ac oligomeric pre-pore from Bacillus thuringiensis induced by N-acetylgalactosamine facilitates toxin membrane insertion. Biochemistry 45: 10329-10336.
    • (2006) Biochemistry , vol.45 , pp. 10329-10336
    • Pardo-Lopez, L.1    Gomez, I.2    Rausell, C.3    Sanchez, J.4    Soberon, M.5
  • 12
    • 0037134485 scopus 로고    scopus 로고
    • Heliothis virescens and Manduca sexta lipid rafts are involved in Cry1A toxin binding to the midgut epithelium and subsequent pore formation
    • Zhuang M, Oltean DI, Gomez I, Pullikuth AK, Soberon M, et al. (2002) Heliothis virescens and Manduca sexta lipid rafts are involved in Cry1A toxin binding to the midgut epithelium and subsequent pore formation. J Biol Chem 277: 13863-13872.
    • (2002) J Biol Chem , vol.277 , pp. 13863-13872
    • Zhuang, M.1    Oltean, D.I.2    Gomez, I.3    Pullikuth, A.K.4    Soberon, M.5
  • 13
    • 33745597608 scopus 로고    scopus 로고
    • A mechanism of cell death involving an adenylyl cyclase/PKA signaling pathway is induced by the Cry1Ab toxin of Bacillus thuringiensis
    • Zhang X, Candas M, Griko NB, Taussig R, Bulla LA Jr, (2006) A mechanism of cell death involving an adenylyl cyclase/PKA signaling pathway is induced by the Cry1Ab toxin of Bacillus thuringiensis. Proc Natl Acad Sci USA 103: 9897-9902.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 9897-9902
    • Zhang, X.1    Candas, M.2    Griko, N.B.3    Taussig, R.4    Bulla Jr., L.A.5
  • 14
    • 0035800472 scopus 로고    scopus 로고
    • Identification of a gene associated with Bt resistance in Heliothis virescens
    • Gahan LJ, Gould F, Heckel DG, (2001) Identification of a gene associated with Bt resistance in Heliothis virescens. Science 293: 857-860.
    • (2001) Science , vol.293 , pp. 857-860
    • Gahan, L.J.1    Gould, F.2    Heckel, D.G.3
  • 15
    • 13544258662 scopus 로고    scopus 로고
    • Disruption of a cadherin gene associated with resistance to Cry1Ac δ-endotoxin of Bacillus thuringiensis in Helicoverpa armigera
    • Xu X, Yu L, Wu Y, (2005) Disruption of a cadherin gene associated with resistance to Cry1Ac δ-endotoxin of Bacillus thuringiensis in Helicoverpa armigera. Appl Environ Microbiol 71: 948-954.
    • (2005) Appl Environ Microbiol , vol.71 , pp. 948-954
    • Xu, X.1    Yu, L.2    Wu, Y.3
  • 16
    • 0037628699 scopus 로고    scopus 로고
    • Three cadherin alleles associated with resistance to Bacillus thuringiensis in pink bollworm
    • Morin S, Biggs RW, Sisterson MS, Shriver L, Ellers-Kirk C, et al. (2003) Three cadherin alleles associated with resistance to Bacillus thuringiensis in pink bollworm. Proc Natl Acad Sci USA 100: 5004-5009.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 5004-5009
    • Morin, S.1    Biggs, R.W.2    Sisterson, M.S.3    Shriver, L.4    Ellers-Kirk, C.5
  • 18
    • 33947198680 scopus 로고    scopus 로고
    • A polymerase chain reaction screen of field populations of Heliothis virescens for a retrotransposon insertion conferring resistance to Bacillus thuringiensis toxin
    • Gahan LJ, Gould F, Lopez JD Jr, Micinski S, Heckel DG, (2007) A polymerase chain reaction screen of field populations of Heliothis virescens for a retrotransposon insertion conferring resistance to Bacillus thuringiensis toxin. J Econ Entomol 100: 187-194.
    • (2007) J Econ Entomol , vol.100 , pp. 187-194
    • Gahan, L.J.1    Gould, F.2    Lopez Jr., J.D.3    Micinski, S.4    Heckel, D.G.5
  • 19
    • 23844468163 scopus 로고    scopus 로고
    • Genetic basis of resistance to Cry1Ac and Cry2Aa in Heliothis virescens (Lepidoptera: Noctuidae)
    • Gahan LJ, Ma YT, Coble ML, Gould F, Moar WJ, et al. (2005) Genetic basis of resistance to Cry1Ac and Cry2Aa in Heliothis virescens (Lepidoptera: Noctuidae). J Econ Entomol 98: 1357-1368.
    • (2005) J Econ Entomol , vol.98 , pp. 1357-1368
    • Gahan, L.J.1    Ma, Y.T.2    Coble, M.L.3    Gould, F.4    Moar, W.J.5
  • 20
    • 20444422567 scopus 로고    scopus 로고
    • Novel genetic basis of field-evolved resistance to Bt toxins in Plutella xylostella
    • Baxter SW, Zhao JZ, Gahan LJ, Shelton AM, Tabashnik BE, et al. (2005) Novel genetic basis of field-evolved resistance to Bt toxins in Plutella xylostella. Insect Molec Biol 14: 327-334.
    • (2005) Insect Molec Biol , vol.14 , pp. 327-334
    • Baxter, S.W.1    Zhao, J.Z.2    Gahan, L.J.3    Shelton, A.M.4    Tabashnik, B.E.5
  • 21
    • 8344247837 scopus 로고    scopus 로고
    • The HevCaLP protein mediates binding specificity of the Cry1A class of Bacillus thuringiensis toxins in Heliothis virescens
    • Jurat-Fuentes JL, Gahan LJ, Gould FL, Heckel DG, Adang MJ, (2004) The HevCaLP protein mediates binding specificity of the Cry1A class of Bacillus thuringiensis toxins in Heliothis virescens. Biochemistry 43: 14299-14305.
    • (2004) Biochemistry , vol.43 , pp. 14299-14305
    • Jurat-Fuentes, J.L.1    Gahan, L.J.2    Gould, F.L.3    Heckel, D.G.4    Adang, M.J.5
  • 22
    • 0142104427 scopus 로고    scopus 로고
    • Dual resistance to Bacillus thuringiensis Cry1Ac and Cry2Aa toxins in Heliothis virescens suggests multiple mechanisms of resistance
    • Jurat-Fuentes JL, Gould FL, Adang MJ, (2003) Dual resistance to Bacillus thuringiensis Cry1Ac and Cry2Aa toxins in Heliothis virescens suggests multiple mechanisms of resistance. Appl Environ Microbiol 69: 5898-5906.
    • (2003) Appl Environ Microbiol , vol.69 , pp. 5898-5906
    • Jurat-Fuentes, J.L.1    Gould, F.L.2    Adang, M.J.3
  • 23
    • 0029174733 scopus 로고
    • Selection and genetic analysis of a Heliothis virescens (Lepidoptera: noctuidae) strain with high levels of resistance to Bacillus thuringiensis toxins
    • Gould F, Anderson A, Reynolds A, Bumgarner L, Moar W, (1995) Selection and genetic analysis of a Heliothis virescens (Lepidoptera: noctuidae) strain with high levels of resistance to Bacillus thuringiensis toxins. J Econ Entomol 88: 1545-1559.
    • (1995) J Econ Entomol , vol.88 , pp. 1545-1559
    • Gould, F.1    Anderson, A.2    Reynolds, A.3    Bumgarner, L.4    Moar, W.5
  • 24
    • 33846623202 scopus 로고    scopus 로고
    • Analysis of midgut proteinases from Bacillus thuringiensis-susceptible and -resistant Heliothis virescens (Lepidoptera: Noctuidae)
    • Karumbaiah L, Oppert B, Jurat-Fuentes JL, Adang MJ, (2007) Analysis of midgut proteinases from Bacillus thuringiensis-susceptible and-resistant Heliothis virescens (Lepidoptera: Noctuidae). Comp Biochem Physiol Part B 146: 139-146.
    • (2007) Comp Biochem Physiol Part B , vol.146 , pp. 139-146
    • Karumbaiah, L.1    Oppert, B.2    Jurat-Fuentes, J.L.3    Adang, M.J.4
  • 25
    • 0036840198 scopus 로고    scopus 로고
    • Altered Glycosylation of 63- and 68-kilodalton microvillar proteins in Heliothis virescens correlates with reduced Cry1 toxin binding, decreased pore formation, and increased resistance to Bacillus thuringiensis Cry1 toxins
    • Jurat-Fuentes JL, Gould FL, Adang MJ, (2002) Altered Glycosylation of 63- and 68-kilodalton microvillar proteins in Heliothis virescens correlates with reduced Cry1 toxin binding, decreased pore formation, and increased resistance to Bacillus thuringiensis Cry1 toxins. Appl Environ Microbiol 68: 5711-5717.
    • (2002) Appl Environ Microbiol , vol.68 , pp. 5711-5717
    • Jurat-Fuentes, J.L.1    Gould, F.L.2    Adang, M.J.3
  • 26
    • 38349089582 scopus 로고    scopus 로고
    • Changes of inheritance mode and fitness in Helicoverpa armigera (Hubner) (Lepidoptera: Noctuidae) along with its resistance evolution to Cry1Ac toxin
    • Liang GM, Wu KM, Yu HK, Li KK, Feng X, et al. (2008) Changes of inheritance mode and fitness in Helicoverpa armigera (Hubner) (Lepidoptera: Noctuidae) along with its resistance evolution to Cry1Ac toxin. J Invertbr Pathol 97: 142-149.
    • (2008) J Invertbr Pathol , vol.97 , pp. 142-149
    • Liang, G.M.1    Wu, K.M.2    Yu, H.K.3    Li, K.K.4    Feng, X.5
  • 27
    • 78449281036 scopus 로고    scopus 로고
    • Susceptibility of isofamilies of Spodoptera frugiperda (Lepidoptera: Noctuidae) to Cry1Ac and Cry1Fa proteins of Bacillus thuringiensis
    • Blanco CA, Portilla M, Jurat-Fuentes JL, Sanchez JF, Viteri D, et al. (2010) Susceptibility of isofamilies of Spodoptera frugiperda (Lepidoptera: Noctuidae) to Cry1Ac and Cry1Fa proteins of Bacillus thuringiensis. Southwest Entomol 35: 409-415.
    • (2010) Southwest Entomol , vol.35 , pp. 409-415
    • Blanco, C.A.1    Portilla, M.2    Jurat-Fuentes, J.L.3    Sanchez, J.F.4    Viteri, D.5
  • 28
    • 45949125218 scopus 로고
    • Preparation and partial characterization of amino acid transporting brush border membrane vesicles from the larval midgut of the cabbage butterfly (Pieris brassicae)
    • Wolfersberger MG, Luthy P, Maurer A, Parenti P, Sacchi VF, et al. (1987) Preparation and partial characterization of amino acid transporting brush border membrane vesicles from the larval midgut of the cabbage butterfly (Pieris brassicae). Comp Biochem Physiol 86A: 301-308.
    • (1987) Comp Biochem Physiol , vol.86 A , pp. 301-308
    • Wolfersberger, M.G.1    Luthy, P.2    Maurer, A.3    Parenti, P.4    Sacchi, V.F.5
  • 29
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M, (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72: 248-254.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.1
  • 30
    • 33846821854 scopus 로고    scopus 로고
    • Identification of novel Cry1Ac binding proteins in midgut membranes from Heliothis virescens using proteomic analyses
    • Krishnamoorthy M, Jurat-Fuentes JL, McNall RJ, Andacht T, Adang MJ, (2007) Identification of novel Cry1Ac binding proteins in midgut membranes from Heliothis virescens using proteomic analyses. Insect Biochem Molec Biol 37: 189-201.
    • (2007) Insect Biochem Molec Biol , vol.37 , pp. 189-201
    • Krishnamoorthy, M.1    Jurat-Fuentes, J.L.2    McNall, R.J.3    Andacht, T.4    Adang, M.J.5
  • 31
    • 3242877290 scopus 로고    scopus 로고
    • Characterization of a Cry1Ac-receptor alkaline phosphatase in susceptible and resistant Heliothis virescens larvae
    • Jurat-Fuentes JL, Adang MJ, (2004) Characterization of a Cry1Ac-receptor alkaline phosphatase in susceptible and resistant Heliothis virescens larvae. Eur J Biochem 271: 3127-3135.
    • (2004) Eur J Biochem , vol.271 , pp. 3127-3135
    • Jurat-Fuentes, J.L.1    Adang, M.J.2
  • 32
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK, (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 33
    • 0031200935 scopus 로고    scopus 로고
    • The Heliothis virescens 170 kDa aminopeptidase functions as "receptor A" by mediating specific Bacillus thuringiensis Cry1A delta-endotoxin binding and pore formation
    • Luo K, Sangadala S, Masson L, Mazza A, Brousseau R, et al. (1997) The Heliothis virescens 170 kDa aminopeptidase functions as "receptor A" by mediating specific Bacillus thuringiensis Cry1A delta-endotoxin binding and pore formation. Insect Biochem Molec Biol 27: 735-743.
    • (1997) Insect Biochem Molec Biol , vol.27 , pp. 735-743
    • Luo, K.1    Sangadala, S.2    Masson, L.3    Mazza, A.4    Brousseau, R.5
  • 34
    • 62349124415 scopus 로고    scopus 로고
    • Cloning and characterization of the Cry1Ac-binding alkaline phosphatase (HvALP) from Heliothis virescens
    • Perera OP, Willis JD, Adang MJ, Jurat-Fuentes JL, (2009) Cloning and characterization of the Cry1Ac-binding alkaline phosphatase (HvALP) from Heliothis virescens. Insect Biochem Mol Biol 39: 294-302.
    • (2009) Insect Biochem Mol Biol , vol.39 , pp. 294-302
    • Perera, O.P.1    Willis, J.D.2    Adang, M.J.3    Jurat-Fuentes, J.L.4
  • 35
    • 0035710746 scopus 로고    scopus 로고
    • Analysis of relative gene expression data using real-time quantitative PCR and the 2(-Delta Delta C(T)) method
    • Livak KJ, Schmittgen TD, (2001) Analysis of relative gene expression data using real-time quantitative PCR and the 2(-Delta Delta C(T)) method. Methods 25: 402-408.
    • (2001) Methods , vol.25 , pp. 402-408
    • Livak, K.J.1    Schmittgen, T.D.2
  • 36
    • 33745743019 scopus 로고    scopus 로고
    • Cry toxin mode of action in susceptible and resistant Heliothis virescens larvae
    • Jurat-Fuentes JL, Adang MJ, (2006) Cry toxin mode of action in susceptible and resistant Heliothis virescens larvae. J Invertebr Pathol 92: 166-171.
    • (2006) J Invertebr Pathol , vol.92 , pp. 166-171
    • Jurat-Fuentes, J.L.1    Adang, M.J.2
  • 37
    • 34250629255 scopus 로고    scopus 로고
    • A proteomic approach to study Cry1Ac binding proteins and their alterations in resistant Heliothis virescens larvae
    • Jurat-Fuentes JL, Adang MJ, (2007) A proteomic approach to study Cry1Ac binding proteins and their alterations in resistant Heliothis virescens larvae. J Invertbr Pathol 95: 187-191.
    • (2007) J Invertbr Pathol , vol.95 , pp. 187-191
    • Jurat-Fuentes, J.L.1    Adang, M.J.2
  • 38
    • 60749089604 scopus 로고    scopus 로고
    • Bacillus thuringiensis Cry1Ac resistance frequency in tobacco budworm (Lepidoptera: Noctuidae)
    • Blanco CA, Andow DA, Abel CA, Sumerford DV, Hernandez G, et al. (2009) Bacillus thuringiensis Cry1Ac resistance frequency in tobacco budworm (Lepidoptera: Noctuidae). J Econ Entomol 102: 381-387.
    • (2009) J Econ Entomol , vol.102 , pp. 381-387
    • Blanco, C.A.1    Andow, D.A.2    Abel, C.A.3    Sumerford, D.V.4    Hernandez, G.5
  • 39
    • 4344675357 scopus 로고    scopus 로고
    • Selection and heritability of resistance to Bacillus thuringiensis subsp kurstaki and transgenic cotton in Helicoverpa armigera (Lepidoptera: Noctuidae)
    • Lu MG, Rui CH, Zhao JZ, Jian GL, Fan XL, et al. (2004) Selection and heritability of resistance to Bacillus thuringiensis subsp kurstaki and transgenic cotton in Helicoverpa armigera (Lepidoptera: Noctuidae). Pest Manag Sci 60: 887-893.
    • (2004) Pest Manag Sci , vol.60 , pp. 887-893
    • Lu, M.G.1    Rui, C.H.2    Zhao, J.Z.3    Jian, G.L.4    Fan, X.L.5
  • 40
    • 0842285384 scopus 로고    scopus 로고
    • Long-term selection for resistance to transgenic cotton expressing Bacillus thuringiensis toxin in Helicoverpa armigera (Hubner) (Lepidoptera: Noctuidae)
    • Meng F, Shen J, Zhou W, Cen H, (2004) Long-term selection for resistance to transgenic cotton expressing Bacillus thuringiensis toxin in Helicoverpa armigera (Hubner) (Lepidoptera: Noctuidae). Pest Manag Sci 60: 167-172.
    • (2004) Pest Manag Sci , vol.60 , pp. 167-172
    • Meng, F.1    Shen, J.2    Zhou, W.3    Cen, H.4
  • 41
    • 77956301012 scopus 로고    scopus 로고
    • Binding site alteration is responsible for field-isolated resistance to Bacillus thuringiensis Cry2A insecticidal proteins in two Helicoverpa species
    • Caccia S, Hernandez-Rodriguez CS, Mahon RJ, Downes S, James W, et al. (2010) Binding site alteration is responsible for field-isolated resistance to Bacillus thuringiensis Cry2A insecticidal proteins in two Helicoverpa species. PLoS ONE 5: e9975.
    • (2010) PLoS ONE , vol.5
    • Caccia, S.1    Hernandez-Rodriguez, C.S.2    Mahon, R.J.3    Downes, S.4    James, W.5
  • 42
    • 0002544072 scopus 로고    scopus 로고
    • Resistance to Bacillus thuringiensis Cry1Ac toxin in three strains of Heliothis virescens: proteolytic and SEM study of the larval midgut
    • Forcada C, Alcacer E, Garcerá MD, Tato A, Martinez R, (1999) Resistance to Bacillus thuringiensis Cry1Ac toxin in three strains of Heliothis virescens: proteolytic and SEM study of the larval midgut. Arch Insect Biochem Physiol 42: 51-63.
    • (1999) Arch Insect Biochem Physiol , vol.42 , pp. 51-63
    • Forcada, C.1    Alcacer, E.2    Garcerá, M.D.3    Tato, A.4    Martinez, R.5
  • 43
    • 18544403248 scopus 로고    scopus 로고
    • Histopathological effects and growth reduction in a susceptible and a resistant strain of Heliothis virescens (Lepidoptera: Noctuidae) caused by sublethal doses of pure Cry1A crystal proteins from Bacillus thuringiensis
    • Martinez-Ramirez AC, Gould F, Ferre J, (1999) Histopathological effects and growth reduction in a susceptible and a resistant strain of Heliothis virescens (Lepidoptera: Noctuidae) caused by sublethal doses of pure Cry1A crystal proteins from Bacillus thuringiensis. Biocont Sci Tech 9: 239-246.
    • (1999) Biocont Sci Tech , vol.9 , pp. 239-246
    • Martinez-Ramirez, A.C.1    Gould, F.2    Ferre, J.3
  • 44
    • 70549110902 scopus 로고    scopus 로고
    • Anti-insect potential of lectins from Arisaema species towards Bactrocera cucurbitae
    • Kaur M, Singh K, Rup PJ, Kamboj SS, Singh J, (2009) Anti-insect potential of lectins from Arisaema species towards Bactrocera cucurbitae. J Environ Biol 30: 1019-1023.
    • (2009) J Environ Biol , vol.30 , pp. 1019-1023
    • Kaur, M.1    Singh, K.2    Rup, P.J.3    Kamboj, S.S.4    Singh, J.5
  • 45
    • 0036231903 scopus 로고    scopus 로고
    • Studies on the activity of the alkaline phosphatase in the midgut of infected silkworm, Bombyx mori L
    • Miao Y-G, (2002) Studies on the activity of the alkaline phosphatase in the midgut of infected silkworm, Bombyx mori L. J Appl Ent 126: 138-142.
    • (2002) J Appl Ent , vol.126 , pp. 138-142
    • Miao, Y.-G.1
  • 46
    • 62349114903 scopus 로고
    • Alkaline-phosphatase in last larval instar of Barathra brassicae (Lepidoptera) infected by Nosema Plodiae
    • Kucera M, Weiser J, (1974) Alkaline-phosphatase in last larval instar of Barathra brassicae (Lepidoptera) infected by Nosema Plodiae. Acta Entomol Bohem 71: 289-293.
    • (1974) Acta Entomol Bohem , vol.71 , pp. 289-293
    • Kucera, M.1    Weiser, J.2
  • 47
    • 0028177991 scopus 로고
    • A mixture of Manduca sexta aminopeptidase and phosphatase enhances Bacillus thuringiensis insecticidal CryIA(c) toxin binding and 86Rb(+)-K+ efflux in vitro
    • Sangadala S, Walters FS, English LH, Adang MJ, (1994) A mixture of Manduca sexta aminopeptidase and phosphatase enhances Bacillus thuringiensis insecticidal CryIA(c) toxin binding and 86Rb(+)-K+ efflux in vitro. J Biol Chem 269: 10088-10092.
    • (1994) J Biol Chem , vol.269 , pp. 10088-10092
    • Sangadala, S.1    Walters, F.S.2    English, L.H.3    Adang, M.J.4
  • 48
    • 0000215798 scopus 로고
    • Delta endotoxin inhibits a phosphatase in midgut epithelial membranes of Heliothis virescens
    • English L, Readdy TL, (1989) Delta endotoxin inhibits a phosphatase in midgut epithelial membranes of Heliothis virescens. Insect Biochem 19: 145-152.
    • (1989) Insect Biochem , vol.19 , pp. 145-152
    • English, L.1    Readdy, T.L.2
  • 49
    • 0141958827 scopus 로고    scopus 로고
    • Identification of novel Bacillus thuringiensis Cry1Ac binding proteins in Manduca sexta midgut through proteomic analysis
    • McNall RJ, Adang MJ, (2003) Identification of novel Bacillus thuringiensis Cry1Ac binding proteins in Manduca sexta midgut through proteomic analysis. Insect Biochem Molec Biol 33: 999-1010.
    • (2003) Insect Biochem Molec Biol , vol.33 , pp. 999-1010
    • McNall, R.J.1    Adang, M.J.2
  • 50
    • 65249183895 scopus 로고    scopus 로고
    • Homodimeric alkaline phosphatase located at Helicoverpa armigera midgut, a putative receptor of Cry1Ac contains alpha-GalNAc in terminal glycan structure as interactive epitope
    • Sarkar A, Hess D, Mondal HA, Banerjee S, Sharma HC, et al. (2009) Homodimeric alkaline phosphatase located at Helicoverpa armigera midgut, a putative receptor of Cry1Ac contains alpha-GalNAc in terminal glycan structure as interactive epitope. J Proteome Res 8: 1838-1848.
    • (2009) J Proteome Res , vol.8 , pp. 1838-1848
    • Sarkar, A.1    Hess, D.2    Mondal, H.A.3    Banerjee, S.4    Sharma, H.C.5
  • 51
    • 77954860308 scopus 로고    scopus 로고
    • Characterization of a Cry1Ac toxin-binding alkaline phosphatase in the midgut from Helicoverpa armigera (Hubner) larvae
    • Ning C, Wu K, Liu C, Gao Y, Jurat-Fuentes JL, et al. (2010) Characterization of a Cry1Ac toxin-binding alkaline phosphatase in the midgut from Helicoverpa armigera (Hubner) larvae. J Insect Physiol 56: 666-672.
    • (2010) J Insect Physiol , vol.56 , pp. 666-672
    • Ning, C.1    Wu, K.2    Liu, C.3    Gao, Y.4    Jurat-Fuentes, J.L.5
  • 52
    • 32944464814 scopus 로고    scopus 로고
    • A GPI-anchored alkaline phosphatase is a functional midgut receptor of Cry11Aa toxin in Aedes aegypti larvae
    • Fernandez LE, Aimanova KG, Gill SS, Bravo A, Soberon M, (2006) A GPI-anchored alkaline phosphatase is a functional midgut receptor of Cry11Aa toxin in Aedes aegypti larvae. Biochem J 394: 77-84.
    • (2006) Biochem J , vol.394 , pp. 77-84
    • Fernandez, L.E.1    Aimanova, K.G.2    Gill, S.S.3    Bravo, A.4    Soberon, M.5
  • 53
    • 70350084958 scopus 로고    scopus 로고
    • Anopheles gambiae alkaline phosphatase is a functional receptor of Bacillus thuringiensis jegathesan Cry11Ba toxin
    • Hua G, Zhang R, Bayyareddy K, Adang MJ, (2009) Anopheles gambiae alkaline phosphatase is a functional receptor of Bacillus thuringiensis jegathesan Cry11Ba toxin. Biochemistry 48: 9785-9793.
    • (2009) Biochemistry , vol.48 , pp. 9785-9793
    • Hua, G.1    Zhang, R.2    Bayyareddy, K.3    Adang, M.J.4
  • 54
    • 77149124262 scopus 로고    scopus 로고
    • Midgut GPI-anchored proteins with alkaline phosphatase activity from the cotton boll weevil (Anthonomus grandis) are putative receptors for the Cry1B protein of Bacillus thuringiensis
    • Martins ES, Monnerat RG, Queiroz PR, Dumas VF, Braz SV, et al. (2010) Midgut GPI-anchored proteins with alkaline phosphatase activity from the cotton boll weevil (Anthonomus grandis) are putative receptors for the Cry1B protein of Bacillus thuringiensis. Insect Biochem Molec Biol 40: 138-145.
    • (2010) Insect Biochem Molec Biol , vol.40 , pp. 138-145
    • Martins, E.S.1    Monnerat, R.G.2    Queiroz, P.R.3    Dumas, V.F.4    Braz, S.V.5
  • 55
    • 0035172889 scopus 로고    scopus 로고
    • Importance of Cry1 delta-endotoxin domain II loops for binding specificity in Heliothis virescens (L.)
    • Jurat-Fuentes JL, Adang MJ, (2001) Importance of Cry1 delta-endotoxin domain II loops for binding specificity in Heliothis virescens (L.). Appl Environ Microbiol 67: 323-329.
    • (2001) Appl Environ Microbiol , vol.67 , pp. 323-329
    • Jurat-Fuentes, J.L.1    Adang, M.J.2
  • 56
    • 57449095370 scopus 로고    scopus 로고
    • Specific binding of Bacillus thuringiensis Cry2A insecticidal proteins to a common site in the midgut of Helicoverpa species
    • Hernandez-Rodriguez CS, Van Vliet A, Bautsoens N, Van Rie J, Ferre J, (2008) Specific binding of Bacillus thuringiensis Cry2A insecticidal proteins to a common site in the midgut of Helicoverpa species. Appl Environ Microbiol 74: 7654-7659.
    • (2008) Appl Environ Microbiol , vol.74 , pp. 7654-7659
    • Hernandez-Rodriguez, C.S.1    van Vliet, A.2    Bautsoens, N.3    van Rie, J.4    Ferre, J.5
  • 57
    • 0033304803 scopus 로고    scopus 로고
    • Regulation of alkaline phosphatase activity by p38 MAP kinase in response to activation of Gi protein-coupled receptors by epinephrine in osteoblast-like cells
    • Suzuki A, Palmer G, Bonjour JP, Caverzasio J, (1999) Regulation of alkaline phosphatase activity by p38 MAP kinase in response to activation of Gi protein-coupled receptors by epinephrine in osteoblast-like cells. Endocrinology 140: 3177-3182.
    • (1999) Endocrinology , vol.140 , pp. 3177-3182
    • Suzuki, A.1    Palmer, G.2    Bonjour, J.P.3    Caverzasio, J.4
  • 58
    • 0036138735 scopus 로고    scopus 로고
    • Evidence for a role of p38 MAP kinase in expression of alkaline phosphatase during osteoblastic cell differentiation
    • Suzuki A, Guicheux J, Palmer G, Miura Y, Oiso Y, et al. (2002) Evidence for a role of p38 MAP kinase in expression of alkaline phosphatase during osteoblastic cell differentiation. Bone 30: 91-98.
    • (2002) Bone , vol.30 , pp. 91-98
    • Suzuki, A.1    Guicheux, J.2    Palmer, G.3    Miura, Y.4    Oiso, Y.5
  • 59
    • 0034806431 scopus 로고    scopus 로고
    • Alterations of MAPK activities associated with intestinal cell differentiation
    • Ding Q, Wang Q, Evers BM, (2001) Alterations of MAPK activities associated with intestinal cell differentiation. Biochem Biophys Res Comm 284: 282-288.
    • (2001) Biochem Biophys Res Comm , vol.284 , pp. 282-288
    • Ding, Q.1    Wang, Q.2    Evers, B.M.3
  • 60
    • 55449127739 scopus 로고    scopus 로고
    • Activation of the unfolded protein response is required for defenses against bacterial pore-forming toxin in vivo
    • Bischof LJ, Kao CY, Los FC, Gonzalez MR, Shen Z, et al. (2008) Activation of the unfolded protein response is required for defenses against bacterial pore-forming toxin in vivo. PLoS Pathog 4: e1000176.
    • (2008) PLoS Pathog , vol.4
    • Bischof, L.J.1    Kao, C.Y.2    Los, F.C.3    Gonzalez, M.R.4    Shen, Z.5
  • 61
    • 3342901591 scopus 로고    scopus 로고
    • Mitogen-activated protein kinase pathways defend against bacterial pore-forming toxins
    • Huffman DL, Abrami L, Sasik R, Corbeil J, van der Goot FG, et al. (2004) Mitogen-activated protein kinase pathways defend against bacterial pore-forming toxins. Proc Natl Acad Sci USA 101: 10995-11000.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 10995-11000
    • Huffman, D.L.1    Abrami, L.2    Sasik, R.3    Corbeil, J.4    van der Goot, F.G.5
  • 62
    • 75949112991 scopus 로고    scopus 로고
    • The mitogen-activated protein kinase p38 is involved in insect defense against Cry toxins from Bacillus thuringiensis
    • Cancino-Rodezno A, Alexander C, Villasenor R, Pacheco S, Porta H, et al. (2010) The mitogen-activated protein kinase p38 is involved in insect defense against Cry toxins from Bacillus thuringiensis. Insect Biochem Mol Biol 40: 58-63.
    • (2010) Insect Biochem Mol Biol , vol.40 , pp. 58-63
    • Cancino-Rodezno, A.1    Alexander, C.2    Villasenor, R.3    Pacheco, S.4    Porta, H.5
  • 63
    • 1542357686 scopus 로고    scopus 로고
    • Induction and transmission of Bacillus thuringiensis tolerance in the flour moth Ephestia kuehniella
    • Rahman MM, Roberts HL, Sarjan M, Asgari S, Schmidt O, (2004) Induction and transmission of Bacillus thuringiensis tolerance in the flour moth Ephestia kuehniella. Proc Natl Acad Sci USA 101: 2696-2699.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 2696-2699
    • Rahman, M.M.1    Roberts, H.L.2    Sarjan, M.3    Asgari, S.4    Schmidt, O.5
  • 64
    • 0029026523 scopus 로고
    • Alkaline phosphatase isozymes in insects and comparison with mammalian enzyme
    • Eguchi M, (1995) Alkaline phosphatase isozymes in insects and comparison with mammalian enzyme. Comp Biochem Physiol 111B: 151-162.
    • (1995) Comp Biochem Physiol , vol.111 B , pp. 151-162
    • Eguchi, M.1
  • 65
    • 78650708942 scopus 로고    scopus 로고
    • An ABC transporter mutation is correlated with insect resistance to Bacillus thuringiensis Cry1Ac toxin
    • Gahan LJ, Pauchet Y, Vogel H, Heckel DG, (2010) An ABC transporter mutation is correlated with insect resistance to Bacillus thuringiensis Cry1Ac toxin. PLoS Genet 6: e1001248.
    • (2010) PLoS Genet , vol.6
    • Gahan, L.J.1    Pauchet, Y.2    Vogel, H.3    Heckel, D.G.4
  • 66
    • 64849104128 scopus 로고    scopus 로고
    • Using an F2 screen to monitor frequency of resistance alleles to Bt cotton in field populations of Helicoverpa armigera (Hübner) (Lepidoptera: Noctuidae)
    • Xu Z, Liu F, Chen J, Huang F, Andow DA, et al. (2009) Using an F2 screen to monitor frequency of resistance alleles to Bt cotton in field populations of Helicoverpa armigera (Hübner) (Lepidoptera: Noctuidae). Pest Manag Sci 65: 391-397.
    • (2009) Pest Manag Sci , vol.65 , pp. 391-397
    • Xu, Z.1    Liu, F.2    Chen, J.3    Huang, F.4    Andow, D.A.5
  • 68
    • 33845253149 scopus 로고    scopus 로고
    • DNA screening reveals pink bollworm resistance to Bt cotton remains rare after a decade of exposure
    • Tabashnik BE, Fabrick JA, Henderson S, Biggs RW, Yafuso CM, et al. (2006) DNA screening reveals pink bollworm resistance to Bt cotton remains rare after a decade of exposure. J Econ Entomol 99: 1525-1530.
    • (2006) J Econ Entomol , vol.99 , pp. 1525-1530
    • Tabashnik, B.E.1    Fabrick, J.A.2    Henderson, S.3    Biggs, R.W.4    Yafuso, C.M.5
  • 69
    • 34248658285 scopus 로고    scopus 로고
    • High-level resistance to Bacillus thuringiensis toxin cry1Ac and cadherin genotype in pink bollworm
    • Tabashnik BE, Biggs RW, Fabrick JA, Gassmann AJ, Dennehy TJ, et al. (2006) High-level resistance to Bacillus thuringiensis toxin cry1Ac and cadherin genotype in pink bollworm. J Econ Entomol 99: 2125-2131.
    • (2006) J Econ Entomol , vol.99 , pp. 2125-2131
    • Tabashnik, B.E.1    Biggs, R.W.2    Fabrick, J.A.3    Gassmann, A.J.4    Dennehy, T.J.5
  • 70
    • 76849113242 scopus 로고    scopus 로고
    • Diverse cadherin mutations conferring resistance to Bacillus thuringiensis toxin Cry1Ac in Helicoverpa armigera
    • Zhao J, Jin L, Yang Y, Wu Y, (2010) Diverse cadherin mutations conferring resistance to Bacillus thuringiensis toxin Cry1Ac in Helicoverpa armigera. Insect Biochem Mol Biol 40: 113-118.
    • (2010) Insect Biochem Mol Biol , vol.40 , pp. 113-118
    • Zhao, J.1    Jin, L.2    Yang, Y.3    Wu, Y.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.