메뉴 건너뛰기




Volumn 6, Issue 8, 2014, Pages 2393-2423

Molecular approaches to improve the insecticidal activity of Bacillus thuringiensis cry toxins

Author keywords

Biocontrol; Cry toxins; Display; DNA shuffling; Evolution; In silico studies; Insect pests; Phage; Specific mutation

Indexed keywords

BACILLUS THURINGIENSIS TOXIN; CRY1AB TOXIN; CRY1AC TOXIN; BACTERIAL PROTEIN; ENDOTOXIN; HEMOLYSIN; INSECTICIDAL CRYSTAL PROTEIN, BACILLUS THURINGIENSIS; INSECTICIDE;

EID: 84926126882     PISSN: None     EISSN: 20726651     Source Type: Journal    
DOI: 10.3390/toxins6082393     Document Type: Review
Times cited : (23)

References (102)
  • 1
    • 0036208040 scopus 로고    scopus 로고
    • Role of Bacillus thuringiensis Cry1 d-endotoxin binding in determining potency during Lepidopteran Larval development
    • Gilliand, A.; Chambers, C.; Bones, E.; Ellar, D. Role of Bacillus thuringiensis Cry1 d-endotoxin binding in determining potency during Lepidopteran Larval development. Appl. Environ. Microbiol. 2002, 68, 1509-1515.
    • (2002) Appl. Environ. Microbiol , vol.68 , pp. 1509-1515
    • Gilliand, A.1    Chambers, C.2    Bones, E.3    Ellar, D.4
  • 2
    • 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, N.B.; Taussig, R.; Bulla, L.A., Jr. 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 2006, 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
  • 3
    • 33847624102 scopus 로고    scopus 로고
    • Mode of action of Bacillus thuringiensis Cry and Cyt and their potential for insect control
    • Bravo, A.; Gill, S.; Soberón, M. Mode of action of Bacillus thuringiensis Cry and Cyt and their potential for insect control. Toxicon 2007, 49, 423-435.
    • (2007) Toxicon , vol.49 , pp. 423-435
    • Bravo, A.1    Gill, S.2    Soberón, M.3
  • 4
    • 0026050639 scopus 로고
    • Crystal structure of insecticidal d-endotoxin from Bacillus thuringiensis at 2.5A resolution
    • Li, J.; Carroll, J.; Ellar, D. Crystal structure of insecticidal d-endotoxin from Bacillus thuringiensis at 2.5A resolution. Nature (London) 1991, 353, 815-821.
    • (1991) Nature (London) , vol.353 , pp. 815-821
    • Li, J.1    Carroll, J.2    Ellar, D.3
  • 6
    • 0035214724 scopus 로고    scopus 로고
    • Crystallization of the Bacillus thuringiensis toxin Cry1Ac and its complex with the receptor ligand N-acetyl-D-galactosamine
    • Derbyshire, D.; Ellar, D.; Li, J. Crystallization of the Bacillus thuringiensis toxin Cry1Ac and its complex with the receptor ligand N-acetyl-D-galactosamine. Acta Crystallogr. Sect. D 2001, 57, 1938-1944.
    • (2001) Acta Crystallogr. Sect. D , vol.57 , pp. 1938-1944
    • Derbyshire, D.1    Ellar, D.2    Li, J.3
  • 8
    • 0034980642 scopus 로고    scopus 로고
    • Structure of Cry2Aa suggests an unexpected receptor binding epitope
    • Morse, R.; Yamamoto, T.; Stud, R. Structure of Cry2Aa suggests an unexpected receptor binding epitope. Structure 2001, 9, 409-417.
    • (2001) Structure , vol.9 , pp. 409-417
    • Morse, R.1    Yamamoto, T.2    Stud, R.3
  • 9
    • 16244392435 scopus 로고    scopus 로고
    • Crystal structure of the mosquito-larvicidal toxin Cry4Ba and its biological implications
    • Boonserm, P.; Davis, P.; Ellar, D.; Li, J. Crystal structure of the mosquito-larvicidal toxin Cry4Ba and its biological implications. J. Mol. Biol. 2005, 348, 363.
    • (2005) J. Mol. Biol , vol.348 , pp. 363
    • Boonserm, P.1    Davis, P.2    Ellar, D.3    Li, J.4
  • 10
    • 70349617068 scopus 로고    scopus 로고
    • Crystal structure of Bacillus thuringiensis Cry8Ea1: An insecticidal toxin toxic to underground pests, the larvae of Holotrichia parallela
    • Guo, S.; Ye, S.; Liu, Y.; Wei, L.; Xue, J. Crystal structure of Bacillus thuringiensis Cry8Ea1: An insecticidal toxin toxic to underground pests, the larvae of Holotrichia parallela. J. Struct. Biol. 2009, 168, 259-266.
    • (2009) J. Struct. Biol , vol.168 , pp. 259-266
    • Guo, S.1    Ye, S.2    Liu, Y.3    Wei, L.4    Xue, J.5
  • 11
    • 84870919631 scopus 로고    scopus 로고
    • Structure and glycolipid properties of the nematicidal protein Cry5B
    • Hui, F.; Scheib, U.; Hu, Y.; Sommer, R.J.; Aroian, R.V.; Ghosh, P. Structure and glycolipid properties of the nematicidal protein Cry5B. Biochemistry. 2012, 51, 9911-9921.
    • (2012) Biochemistry , vol.51 , pp. 9911-9921
    • Hui, F.1    Scheib, U.2    Hu, Y.3    Sommer, R.J.4    Aroian, R.V.5    Ghosh, P.6
  • 12
    • 0030574275 scopus 로고    scopus 로고
    • Probing the mechanism of action of Bacillus thuringiensis insecticidal proteins by site-directed mutagenesis-A minireview
    • Dean, D.; Rajamohan, F.; Lee, M.; Wu, S.-J.; Chen, X.-J.; Alcantara, E.; Hussain, S. Probing the mechanism of action of Bacillus thuringiensis insecticidal proteins by site-directed mutagenesis-A minireview. Gene 1996, 179, 111-117.
    • (1996) Gene , vol.179 , pp. 111-117
    • Dean, D.1    Rajamohan, F.2    Lee, M.3    Wu, S.-J.4    Chen, X.-J.5    Alcantara, E.6    Hussain, S.7
  • 16
    • 0028050350 scopus 로고
    • Rapid evolution of a protein in vitro by DNA shuffling
    • Stemmer, W. Rapid evolution of a protein in vitro by DNA shuffling. Nature (London) 1994, 370, 389-391.
    • (1994) Nature (London) , vol.370 , pp. 389-391
    • Stemmer, W.1
  • 17
    • 0030754926 scopus 로고    scopus 로고
    • Optimization for DNA shuffling for high fidelity recombination
    • Zhao, H.; Arnold, F. Optimization for DNA shuffling for high fidelity recombination. Nucleic Acids Res. 1997, 25, 1307-1308.
    • (1997) Nucleic Acids Res , vol.25 , pp. 1307-1308
    • Zhao, H.1    Arnold, F.2
  • 20
    • 85006751997 scopus 로고    scopus 로고
    • Bacillus thuringiensis: Mechanisms and use
    • Elsevier: Oxford, UK
    • Bravo, A.; Soberón, M.; Gill, S. Bacillus thuringiensis: Mechanisms and use. In Comprehensive Molecular Insect Science; Elsevier: Oxford, UK, 2005; Volume 6, pp. 175-206.
    • (2005) Comprehensive Molecular Insect Science , vol.6 , pp. 175-206
    • Bravo, A.1    Soberón, M.2    Gill, S.3
  • 21
    • 0030903162 scopus 로고    scopus 로고
    • Phylogenetic relationship of Bacillus thuringiensis δ-endotoxin family proteins and their functional domains
    • Bravo, A. Phylogenetic relationship of Bacillus thuringiensis δ-endotoxin family proteins and their functional domains. J. Bacteriol. 1997, 179, 2793-2801.
    • (1997) J. Bacteriol , vol.179 , pp. 2793-2801
    • Bravo, A.1
  • 22
    • 0035313205 scopus 로고    scopus 로고
    • How Bacillus thuringiensis has evolved specific toxins to colonize the insect world
    • De Maagd, R.A.; Bravo, A.; Crickmore, N. How Bacillus thuringiensis has evolved specific toxins to colonize the insect world. Trends Genet. 2001, 17, 193-199.
    • (2001) Trends Genet , vol.17 , pp. 193-199
    • de Maagd, R.A.1    Bravo, A.2    Crickmore, N.3
  • 23
    • 0001904607 scopus 로고    scopus 로고
    • The diversity of Bacillus thuringiensis d-endotoxins
    • Charles, J.-F., Delécluse, A., Nielsen-LeRoux, C., Eds.; Kluwer Academic Publishers: Dordrecht, The Netherland
    • Crickmore, N. The diversity of Bacillus thuringiensis d-endotoxins. In Enthomopathogenic Bacteria: From Laboratory to Field Application; Charles, J.-F., Delécluse, A., Nielsen-LeRoux, C., Eds.; Kluwer Academic Publishers: Dordrecht, The Netherland, 2000; Volume 1, pp. 65-79.
    • (2000) Enthomopathogenic Bacteria: From Laboratory to Field Application , vol.1 , pp. 65-79
    • Crickmore, N.1
  • 24
    • 34548760723 scopus 로고    scopus 로고
    • Adaptative evolution of cry genes in Bacillus thuringiensis: Implications for their specificity determination
    • Wu, J.-Y.; Zhao, F.-Q.; Bai, J.; Deng, G.; Qin, S.; Bao, Q.-Y. Adaptative evolution of cry genes in Bacillus thuringiensis: Implications for their specificity determination. Genomics Protemics Bioinform. 2007, 5, 102-110.
    • (2007) Genomics Protemics Bioinform , vol.5 , pp. 102-110
    • Wu, J.-Y.1    Zhao, F.-Q.2    Bai, J.3    Deng, G.4    Qin, S.5    Bao, Q.-Y.6
  • 26
    • 11144278658 scopus 로고    scopus 로고
    • Targeted mutagenesis of loop residues in the receptor-binding domain of the Bacillus thuringiensis Cry4Ba toxin affects larvicidal activity
    • Tuntitippawan, T.; Boonserm, P.; Katzenmeier, G.; Angsuthanasombat, C. Targeted mutagenesis of loop residues in the receptor-binding domain of the Bacillus thuringiensis Cry4Ba toxin affects larvicidal activity. FEBS Lett. 2005, 242, 325-332.
    • (2005) FEBS Lett , vol.242 , pp. 325-332
    • Tuntitippawan, T.1    Boonserm, P.2    Katzenmeier, G.3    Angsuthanasombat, C.4
  • 27
    • 0035808893 scopus 로고    scopus 로고
    • Why Bacillus thuringienis insecticidal toxins are so effective: Unique features of their mode of action
    • Aronson, A.; Shai, Y. Why Bacillus thuringienis insecticidal toxins are so effective: Unique features of their mode of action. FEMS Microbiol. Lett. 2001, 195, 1-8.
    • (2001) FEMS Microbiol. Lett , vol.195 , pp. 1-8
    • Aronson, A.1    Shai, Y.2
  • 28
    • 0003090545 scopus 로고
    • Immunocytochemical analysis of specific binding of Bacillus thuringiensis insecticidal stal proteins to lepidopteran and coleopteran midgutmembranes
    • Bravo, A.; Hendrickx, K.; Jansens, S.; Peferoen, M. Immunocytochemical analysis of specific binding of Bacillus thuringiensis insecticidal stal proteins to lepidopteran and coleopteran midgutmembranes. J. Invertebr. Pathol. 1992, 60, 247-253.
    • (1992) J. Invertebr. Pathol , vol.60 , pp. 247-253
    • Bravo, A.1    Hendrickx, K.2    Jansens, S.3    Peferoen, M.4
  • 29
    • 7744222624 scopus 로고    scopus 로고
    • Oligomerization triggers binding of a Bacillus thuringiensis 1Ab pore-forming toxin to aminopeptidase N receptor leading to insertion into membrane microdomains
    • Bravo, A.; Gómez, I.; Muñoz-Garay, C.; Sánchez, J.; Miranda, R.; Zhuang, M.; Gill, S.; Sóberon, M. Oligomerization triggers binding of a Bacillus thuringiensis 1Ab pore-forming toxin to aminopeptidase N receptor leading to insertion into membrane microdomains. Biochim. Biophys. Acta 2004, 1667, 38-46.
    • (2004) Biochim. Biophys. Acta , vol.1667 , pp. 38-46
    • Bravo, A.1    Gómez, I.2    Muñoz-Garay, C.3    Sánchez, J.4    Miranda, R.5    Zhuang, M.6    Gill, S.7    Sóberon, M.8
  • 31
    • 0348047325 scopus 로고    scopus 로고
    • Structure diversity, and evolution of protein toxins from spore-forming entomopathogenic bacteria
    • De Maagd, R.A.; Bravo, A.; Berry, C.; Crickmore, N.; Schnepf, H. Structure diversity, and evolution of protein toxins from spore-forming entomopathogenic bacteria. Annu. Rev. Genet. 2003, 37, 409-433.
    • (2003) Annu. Rev. Genet , vol.37 , pp. 409-433
    • de Maagd, R.A.1    Bravo, A.2    Berry, C.3    Crickmore, N.4    Schnepf, H.5
  • 33
    • 33745743019 scopus 로고    scopus 로고
    • Toxin mode of action in susceptible and resistant Heliothis virescens larvae
    • Jurat-Fuentes, J.; Adang, M. Toxin mode of action in susceptible and resistant Heliothis virescens larvae. J. Invertebr. Pathol. 2006, 92, 166-171.
    • (2006) J. Invertebr. Pathol , vol.92 , pp. 166-171
    • Jurat-Fuentes, J.1    Adang, M.2
  • 34
    • 34250782646 scopus 로고    scopus 로고
    • Role of receptors in Bacillus thuringiensis crystal toxin activity
    • Pigott, C.; Ellar, D. Role of receptors in Bacillus thuringiensis crystal toxin activity. Microbiol. Mol. Biol. Rev. 2007, 71, 255-281.
    • (2007) Microbiol. Mol. Biol. Rev , vol.71 , pp. 255-281
    • Pigott, C.1    Ellar, D.2
  • 35
    • 70450265465 scopus 로고    scopus 로고
    • Domain II loop 3 of Bacillus thuringiensis Cry1Ab toxin is involved in a "ping pong" binding mechanism with Manduca sexta aminopeptidase-N and cadherin receptors
    • Pacheco, S.; Gomez, I.; Arenas, I.; Saab-Rincon, G.; Rodriguez-Almazan, C. Domain II loop 3 of Bacillus thuringiensis Cry1Ab toxin is involved in a "ping pong" binding mechanism with Manduca sexta aminopeptidase-N and cadherin receptors. J. Biol. Chem. 2009, 284, 32750-32757.
    • (2009) J. Biol. Chem , vol.284 , pp. 32750-32757
    • Pacheco, S.1    Gomez, I.2    Arenas, I.3    Saab-Rincon, G.4    Rodriguez-Almazan, C.5
  • 37
    • 51249121783 scopus 로고    scopus 로고
    • How to cope with insect resistance to Bt toxins?
    • Bravo, A.; Soberon, M. How to cope with insect resistance to Bt toxins? Trends Biotechnol. 2008, 26, 573-579.
    • (2008) Trends Biotechnol , vol.26 , pp. 573-579
    • Bravo, A.1    Soberon, M.2
  • 38
    • 39149092363 scopus 로고    scopus 로고
    • The pore-pore from Bacillus thuringiensis Cry1Ab toxin is necessary to induce insect death in Manduca sexta
    • Jiménez-Juárez, N.; Munoz-Garay, C.; Gómez, I.; Gill, S.; Soberón, M.; Bravo, A. The pore-pore from Bacillus thuringiensis Cry1Ab toxin is necessary to induce insect death in Manduca sexta. Peptides 2008, 29, 318-323.
    • (2008) Peptides , vol.29 , pp. 318-323
    • Jiménez-Juárez, N.1    Munoz-Garay, C.2    Gómez, I.3    Gill, S.4    Soberón, M.5    Bravo, A.6
  • 40
    • 67349236660 scopus 로고    scopus 로고
    • Signaling versus punching hole: How do Bacillus thuringiensis toxins kill insect midgut cells?
    • Soberón, M.; Gill, S.; Bravo, A. Signaling versus punching hole: How do Bacillus thuringiensis toxins kill insect midgut cells? Cell Mol. Life Sci. 2009, 66, 1337-1349.
    • (2009) Cell Mol. Life Sci , vol.66 , pp. 1337-1349
    • Soberón, M.1    Gill, S.2    Bravo, A.3
  • 41
    • 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. Role of alkaline phosphatase from Manduca sexta in the mechanism of action of Bacillus thuringiensis Cry1Ab toxin. J. Biol. Chem. 2010, 285, 12497-12503.
    • (2010) J. Biol. Chem , vol.285 , pp. 12497-12503
    • Arenas, I.1    Bravo, A.2    Soberon, M.3    Gomez, I.4
  • 42
    • 0041817553 scopus 로고    scopus 로고
    • Molecular basis for Bacillus thuringiensis Cry1Ab toxin specificity: Two structural determinants in the Manduca sexta Bt-R1 receptor interact wit loops alpha8 and 2 in domain II of Cry1Ab toxin
    • Gómez, I.; Dean, D.; Bravo, A.; Soberón, M. Molecular basis for Bacillus thuringiensis Cry1Ab toxin specificity: Two structural determinants in the Manduca sexta Bt-R1 receptor interact wit loops alpha8 and 2 in domain II of Cry1Ab toxin. Biochemistry 2003, 42, 10482-10489.
    • (2003) Biochemistry , vol.42 , pp. 10482-10489
    • Gómez, I.1    Dean, D.2    Bravo, A.3    Soberón, M.4
  • 43
    • 33845947968 scopus 로고    scopus 로고
    • Specific epitopes of domains II and III of Bacillus thuringiensis Cry1Ab toxin involved in the sequential interaction with cadherin and aminopeptidase-N receptors in Manduca sexta
    • Gómez, I.; Arenas, I.; Benitez, I.; Miranda-Ríos, J.; Becerril, B.; Grande, G. Specific epitopes of domains II and III of Bacillus thuringiensis Cry1Ab toxin involved in the sequential interaction with cadherin and aminopeptidase-N receptors in Manduca sexta. J. Biol. Chem. 2006, 281, 34032-34039.
    • (2006) J. Biol. Chem , vol.281 , pp. 34032-34039
    • Gómez, I.1    Arenas, I.2    Benitez, I.3    Miranda-Ríos, J.4    Becerril, B.5    Grande, G.6
  • 46
    • 8744315849 scopus 로고    scopus 로고
    • Display of biologically functional insecticidal toxin on the surface of Xphage
    • Vílchez, S.; Jacoby, J.; Ellar, D. Display of biologically functional insecticidal toxin on the surface of Xphage. Appl. Environ. Microbiol. 2004, 70, 6587-6594.
    • (2004) Appl. Environ. Microbiol , vol.70 , pp. 6587-6594
    • Vílchez, S.1    Jacoby, J.2    Ellar, D.3
  • 47
    • 33646154885 scopus 로고    scopus 로고
    • Functioinal display of Bacillus thuringiensis Cry1Ac toxin on T7 phage
    • Pacheco, S.; Gómez, I.; Sato, R.; Bravo, A.; Soberón, M. Functioinal display of Bacillus thuringiensis Cry1Ac toxin on T7 phage. J. Invertebr. Pathol. 2006, 92, 45-49.
    • (2006) J. Invertebr. Pathol , vol.92 , pp. 45-49
    • Pacheco, S.1    Gómez, I.2    Sato, R.3    Bravo, A.4    Soberón, M.5
  • 49
    • 0035118386 scopus 로고    scopus 로고
    • Directed molecular evolution in plant improvement
    • Lassner, M.; Bedbrook, J. Directed molecular evolution in plant improvement. Curr. Opin. Plant Biol. 2001, 4, 152-156.
    • (2001) Curr. Opin. Plant Biol , vol.4 , pp. 152-156
    • Lassner, M.1    Bedbrook, J.2
  • 50
    • 12344256195 scopus 로고    scopus 로고
    • A strategy for shiffling numerous Bacillus thuringiensis crystal protein domains
    • Knight, J.; Broadwell, A.; Grant, W.; Shoemaker, C. A strategy for shiffling numerous Bacillus thuringiensis crystal protein domains. J. Econ. Entomol. 2004, 97, 1805-1813.
    • (2004) J. Econ. Entomol , vol.97 , pp. 1805-1813
    • Knight, J.1    Broadwell, A.2    Grant, W.3    Shoemaker, C.4
  • 51
    • 79151472976 scopus 로고    scopus 로고
    • A Cry1Ac toxin variant generated by directed evolution has enhanced toxicity against Lepidopteran insects
    • Shan, S.; Zhang, Y.; Ding, X.; Hu, S.; Sun, Y.; Yu, Z.; Liu, S.; Zhu, Z.; Xia, L. A Cry1Ac toxin variant generated by directed evolution has enhanced toxicity against Lepidopteran insects. Curr. Microbiol. 2011, 62, 358-365.
    • (2011) Curr. Microbiol , vol.62 , pp. 358-365
    • Shan, S.1    Zhang, Y.2    Ding, X.3    Hu, S.4    Sun, Y.5    Yu, Z.6    Liu, S.7    Zhu, Z.8    Xia, L.9
  • 52
    • 84882856233 scopus 로고    scopus 로고
    • Affinity maturation of Cry1Aa toxin to the Bombys mori cadherin-like receptor by directed evolution
    • Fujii, Y.; Tanaka, S.; Otsuki, M.; Hoshino, Y.; Endo, H.; Sato, R. Affinity maturation of Cry1Aa toxin to the Bombys mori cadherin-like receptor by directed evolution. Mol. Biotechnol. 2013, 54, 11.
    • (2013) Mol. Biotechnol , vol.54 , pp. 11
    • Fujii, Y.1    Tanaka, S.2    Otsuki, M.3    Hoshino, Y.4    Endo, H.5    Sato, R.6
  • 54
    • 78650346116 scopus 로고    scopus 로고
    • Participation of valine 171 in a-helix 5 of Bacillus thuringiensis Cry1Ab 6-endotoxin in translocation of toxin into Lymantria dispar midgut membranes
    • Alzate, O.; Osorio, C.; Florez, A.; Dean, D. Participation of valine 171 in a-helix 5 of Bacillus thuringiensis Cry1Ab 6-endotoxin in translocation of toxin into Lymantria dispar midgut membranes. Appl. Environ. Microbiol. 2010, 76, 7878-7880.
    • (2010) Appl. Environ. Microbiol , vol.76 , pp. 7878-7880
    • Alzate, O.1    Osorio, C.2    Florez, A.3    Dean, D.4
  • 55
    • 0028907322 scopus 로고
    • Cloning and expression of a receptor for an insecticidal toxin of Bacillus thuringiensis
    • Vadlamudi, R.K.; Weber, E.; Ji, I.; Ji, T.H.; Bulla, L.A. Jr. Cloning and expression of a receptor for an insecticidal toxin of Bacillus thuringiensis. J. Biol. Chem. 1995, 270, 5490-5499.
    • (1995) J. Biol. Chem , vol.270 , pp. 5490-5499
    • Vadlamudi, R.K.1    Weber, E.2    Ji, I.3    Ji, T.H.4    Bulla Jr., L.A.5
  • 56
    • 0037119455 scopus 로고    scopus 로고
    • Hydropathic complementarity determines interaction of epitope (869)HITDTNNK(876) in Manduca sexta Bt-R(1) receptor with loop 2 of domain II of Bacillus thuringiensis Cry1A toxins
    • Gomez, I.; Miranda-Rios, J.; Rudino-Pinera, E.; Oltean, D.I.; Gill, S.S.; Bravo, A.; Soberon, M. Hydropathic complementarity determines interaction of epitope (869)HITDTNNK(876) in Manduca sexta Bt-R(1) receptor with loop 2 of domain II of Bacillus thuringiensis Cry1A toxins. J. Biol. Chem. 2002, 277, 30137-30143.
    • (2002) J. Biol. Chem , vol.277 , pp. 30137-30143
    • Gomez, I.1    Miranda-Rios, J.2    Rudino-Pinera, E.3    Oltean, D.I.4    Gill, S.S.5    Bravo, A.6    Soberon, M.7
  • 57
    • 51749115730 scopus 로고    scopus 로고
    • Location of the Bombyx mori 175 kDa cadherin-like protein-binding site on Bacillus thuringiensis Cry1Aa toxin
    • Atsumi, S.; Inoue, Y.; Ishizaka, T.; Mizuno, E.; Yoshizawa, Y. Location of the Bombyx mori 175 kDa cadherin-like protein-binding site on Bacillus thuringiensis Cry1Aa toxin. FEBS J. 2008, 275, 4913-4926.
    • (2008) FEBS J , vol.275 , pp. 4913-4926
    • Atsumi, S.1    Inoue, Y.2    Ishizaka, T.3    Mizuno, E.4    Yoshizawa, Y.5
  • 58
    • 0029908854 scopus 로고    scopus 로고
    • Protein engineering of Bacillus thuringiensis 6-endotoxin: Mutations at domain II of CryIAb enhance receptor affinity and toxicity toward gypsy moth larvae
    • Rajamohan, F.; Alzate, O.; Cotrill, J.A.; Curtiss, A.; Dean, D.H. Protein engineering of Bacillus thuringiensis 6-endotoxin: Mutations at domain II of CryIAb enhance receptor affinity and toxicity toward gypsy moth larvae. Proc. Natl. Acad. Sci. USA 1996, 93, 14338-14343.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 14338-14343
    • Rajamohan, F.1    Alzate, O.2    Cotrill, J.A.3    Curtiss, A.4    Dean, D.H.5
  • 59
    • 44949153683 scopus 로고    scopus 로고
    • Investigating the properties of Bacillus thuringiensis Cry proteins with noval loop replacements created using combinatorial molecular biology
    • Pigott, C.; King, M.; Ellar, D. Investigating the properties of Bacillus thuringiensis Cry proteins with noval loop replacements created using combinatorial molecular biology. Appl. Environ. Microbiol. 2008, 74, 3497-3512.
    • (2008) Appl. Environ. Microbiol , vol.74 , pp. 3497-3512
    • Pigott, C.1    King, M.2    Ellar, D.3
  • 60
    • 0141816832 scopus 로고    scopus 로고
    • Introduction of Culex toxicity into Bacillus thuringiensis Cry4Ba by protein engineering
    • Abdullah, M.; Alzate, O.; Mohammad, M.; McNall, R.; Adang, M.; Dean, D. Introduction of Culex toxicity into Bacillus thuringiensis Cry4Ba by protein engineering. Appl. Environ. Microbiol. 2003, 69, 5343-5353.
    • (2003) Appl. Environ. Microbiol , vol.69 , pp. 5343-5353
    • Abdullah, M.1    Alzate, O.2    Mohammad, M.3    McNall, R.4    Adang, M.5    Dean, D.6
  • 61
    • 0034114535 scopus 로고    scopus 로고
    • Domain III substitution in Bacillus thuringiensis δ-endotoxin Cry1C domain III can function as a specific determinant for Spodoptera exigua in different, but not all, Cry1-Cry1C hybrids
    • Maagd, R.D.; Weemen-Hendriks, M.; Siekema, W.; Bosch, D. Domain III substitution in Bacillus thuringiensis δ-endotoxin Cry1C domain III can function as a specific determinant for Spodoptera exigua in different, but not all, Cry1-Cry1C hybrids. Appl. Environ. Microbiol. 2000, 66, 1559-1563.
    • (2000) Appl. Environ. Microbiol , vol.66 , pp. 1559-1563
    • Maagd, R.D.1    Weemen-Hendriks, M.2    Siekema, W.3    Bosch, D.4
  • 62
    • 0035512206 scopus 로고    scopus 로고
    • Bacillus thuringiensis δ-endotoxin Cry1 hybrid proteins with increased activity against the Colorado potato beetle
    • Naimov, S.; Weemen-Hendriks, M.; Dukiandjiev, S.; Maagd, R.D. Bacillus thuringiensis δ-endotoxin Cry1 hybrid proteins with increased activity against the Colorado potato beetle. Appl. Environ. Microbiol. 2001, 67, 5328-5330.
    • (2001) Appl. Environ. Microbiol , vol.67 , pp. 5328-5330
    • Naimov, S.1    Weemen-Hendriks, M.2    Dukiandjiev, S.3    Maagd, R.D.4
  • 63
    • 77952255387 scopus 로고    scopus 로고
    • Lepidopteran-active variable-region sequence imparts coleopteran activity in eCry3.1Ab, an engineered Bacillus thuringiensis hybrid insecticidal protein
    • Walters, F.; deFontes, C.; Hart, H.; Warren, G.; Chen, J. Lepidopteran-active variable-region sequence imparts coleopteran activity in eCry3.1Ab, an engineered Bacillus thuringiensis hybrid insecticidal protein. Appl. Environ. Microbiol. 2010, 76, 3082-3088.
    • (2010) Appl. Environ. Microbiol , vol.76 , pp. 3082-3088
    • Walters, F.1    Defontes, C.2    Hart, H.3    Warren, G.4    Chen, J.5
  • 64
    • 80053967140 scopus 로고    scopus 로고
    • Mortality impact of Bt transgenic maize roots expressing eCry3.1Ab, mCry3A, and eCry3.1Ab plus mCry3A on western corn rootworm larvae in the field
    • Hibbard, B.; Frank, D.; Kurtz, R.; Boudreau, E.; Ellersieck, M.; Odhiambo, J. Mortality impact of Bt transgenic maize roots expressing eCry3.1Ab, mCry3A, and eCry3.1Ab plus mCry3A on western corn rootworm larvae in the field. J. Econ. Entomol. 2011, 104, 1584-1591.
    • (2011) J. Econ. Entomol , vol.104 , pp. 1584-1591
    • Hibbard, B.1    Frank, D.2    Kurtz, R.3    Boudreau, E.4    Ellersieck, M.5    Odhiambo, J.6
  • 65
    • 0029152148 scopus 로고
    • The Cry1A(c) receptor purified from Manduca sexta displays multiple specificities
    • Masson, L.; Lu, Y.; Mazza, A.; Brousseau, R.; Adang, M. The Cry1A(c) receptor purified from Manduca sexta displays multiple specificities. J. Biol. Chem. 1995, 270, 20309-20315.
    • (1995) J. Biol. Chem , vol.270 , pp. 20309-20315
    • Masson, L.1    Lu, Y.2    Mazza, A.3    Brousseau, R.4    Adang, M.5
  • 66
    • 43049150073 scopus 로고    scopus 로고
    • Cysteine scanning mutagenesis of alpha4, a putative pore-lining helix of the Bacillus thuringiensis insecticidal toxin Cry1Aa
    • Girard, F.; Vachon, V. Cysteine scanning mutagenesis of alpha4, a putative pore-lining helix of the Bacillus thuringiensis insecticidal toxin Cry1Aa. Appl. Environ. Microbiol. 2008, 74, 2565-2572.
    • (2008) Appl. Environ. Microbiol , vol.74 , pp. 2565-2572
    • Girard, F.1    Vachon, V.2
  • 67
    • 8144229487 scopus 로고    scopus 로고
    • Helix 4 mutants of the Bacillus thuringiensis insecticidal toxin Cry1Aa display altered pore-forming abilities
    • Vachon, V.; Prefontaine, G. Helix 4 mutants of the Bacillus thuringiensis insecticidal toxin Cry1Aa display altered pore-forming abilities. Appl. Environ. Microbiol. 2004, 70, 6123-6130.
    • (2004) Appl. Environ. Microbiol , vol.70 , pp. 6123-6130
    • Vachon, V.1    Prefontaine, G.2
  • 69
    • 65849141019 scopus 로고    scopus 로고
    • Dominant negative mutants of Bacillus thuringiensis Cry1Ab toxin function as anti-toxins: Demonstration of the role of oligomerization in toxicity
    • Rodríguez-Almazán, C.; Zavala, L.E.; Muñoz-Garay, C.; Jiménez-Juárez, N.; Pacheco, S.; Masson, L.; Soberón, M.; Bravo, A. Dominant negative mutants of Bacillus thuringiensis Cry1Ab toxin function as anti-toxins: Demonstration of the role of oligomerization in toxicity. PLoS One 2009, 4, e5545.
    • (2009) PLoS One , vol.e5545 , pp. 4
    • Rodríguez-Almazán, C.1    Zavala, L.E.2    Muñoz-Garay, C.3    Jiménez-Juárez, N.4    Pacheco, S.5    Masson, L.6    Soberón, M.7    Bravo, A.8
  • 70
    • 0035656776 scopus 로고    scopus 로고
    • The α-Helix 4 Residue, Asn135, is involved in the oligomerization of Cry1Ac1 and Cry1Ab5 Bacillus thuringiensis toxins
    • Tigue, N.J.; Jacoby, J.; Ellar, D.J. The α-Helix 4 Residue, Asn135, is involved in the oligomerization of Cry1Ac1 and Cry1Ab5 Bacillus thuringiensis toxins. Appl. Environ. Microbiol. 2001, 67, 5715-5720.
    • (2001) Appl. Environ. Microbiol , vol.67 , pp. 5715-5720
    • Tigue, N.J.1    Jacoby, J.2    Ellar, D.J.3
  • 71
    • 33751008673 scopus 로고    scopus 로고
    • Effects of disulfide bridges in domain I of Bacillus thuringiensis Cry1Aa δ-endotoxin on ion-channel formation in biological membranes
    • Alzate, O.; You, T. Effects of disulfide bridges in domain I of Bacillus thuringiensis Cry1Aa δ-endotoxin on ion-channel formation in biological membranes. Biochemistry 2006, 45, 13597-13605.
    • (2006) Biochemistry , vol.45 , pp. 13597-13605
    • Alzate, O.1    You, T.2
  • 72
    • 0032743862 scopus 로고    scopus 로고
    • Binding of Bacillus thuringiensis Cry1Ac toxin to Manduca sexta aminopeptidase-N receptor is not directly related to toxicity
    • Jenkins, J.L.; Lee, M.K.; Sangadala, S.; Adang, M.J.; Dean, D.H. Binding of Bacillus thuringiensis Cry1Ac toxin to Manduca sexta aminopeptidase-N receptor is not directly related to toxicity. FEBS Lett. 1999, 462, 373-376.
    • (1999) FEBS Lett , vol.462 , pp. 373-376
    • Jenkins, J.L.1    Lee, M.K.2    Sangadala, S.3    Adang, M.J.4    Dean, D.H.5
  • 73
    • 84886255558 scopus 로고    scopus 로고
    • New insight to structure-function relationship of GalNAc mediated primary interaction between insecticidal Cry1Ac toxin and HaALP receptor of Helicoverpa armigera
    • Sengupta, A.; Sarkar, A.; Priya, P.; Ghosh Dastidar, S.; Das, S. New insight to structure-function relationship of GalNAc mediated primary interaction between insecticidal Cry1Ac toxin and HaALP receptor of Helicoverpa armigera. PLoS One 2013, 8, e78249.
    • (2013) PLoS One , vol.8
    • Sengupta, A.1    Sarkar, A.2    Priya, P.3    Ghosh Dastidar, S.4    Das, S.5
  • 74
    • 0032937987 scopus 로고    scopus 로고
    • Domain III of the Bacillus thuringiensis δ-endotoxin Cry1Ac is involved in binding to Manduca sexta brush border membranes and to its purified aminopeptidase N
    • De Maagd, R.A.; Bakker, P.L.; Masson, L.; Adang, M.J.; Sangadala, S.; Stiekema, W.; Bosch, D. Domain III of the Bacillus thuringiensis δ-endotoxin Cry1Ac is involved in binding to Manduca sexta brush border membranes and to its purified aminopeptidase N. Mol. Microbiol. 1999, 31, 463-471.
    • (1999) Mol. Microbiol , vol.31 , pp. 463-471
    • de Maagd, R.A.1    Bakker, P.L.2    Masson, L.3    Adang, M.J.4    Sangadala, S.5    Stiekema, W.6    Bosch, D.7
  • 75
    • 0033574601 scopus 로고    scopus 로고
    • N-acetylgalactosamine on the putative insect receptor aminopeptidase N is recognised by a site on the domain III lectin-like fold of a Bacillus thuringiensis insecticidal toxin
    • Burton, S.; Ellar, D.; Li, J.; Derbyshire, D. N-acetylgalactosamine on the putative insect receptor aminopeptidase N is recognised by a site on the domain III lectin-like fold of a Bacillus thuringiensis insecticidal toxin. J. Mol. Biol. 1999, 287, 1011-1022.
    • (1999) J. Mol. Biol , vol.287 , pp. 1011-1022
    • Burton, S.1    Ellar, D.2    Li, J.3    Derbyshire, D.4
  • 76
    • 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, J.L.; Gao, X. Characterization of a Cry1Ac toxin-binding alkaline phosphatase in the midgut from Helicoverpa armigera (Hubner) larvae. J. Insect Phys. 2010, 56, 666-672.
    • (2010) J. Insect Phys , vol.56 , pp. 666-672
    • Ning, C.1    Wu, K.2    Liu, C.3    Gao, Y.4    Jurat-Fuentes, J.L.5    Gao, X.6
  • 77
    • 35348875436 scopus 로고    scopus 로고
    • Susceptibility of Anthonomus grandis (cotton boll weevil) and Spodoptera frugiperda (fall armyworm) to a Cry1Ia-type toxin from a Brazilian Bacillus thuringiensis strain
    • Grossi-de-Sa, M.; Magahães, M.; Silva, M.; Silva, S.; Dias, S.; Nakasu, E.; Brunetta, P.; Oliveira, G.; Neto, O.O.; Oliveira, R. et al. Susceptibility of Anthonomus grandis (cotton boll weevil) and Spodoptera frugiperda (fall armyworm) to a Cry1Ia-type toxin from a Brazilian Bacillus thuringiensis strain. J. Biochem. Moel. Biol. 2007,40, 10.
    • (2007) J. Biochem. Moel. Biol , vol.40 , pp. 10
    • Grossi-de-Sa, M.1    Magahães, M.2    Silva, M.3    Silva, S.4    Dias, S.5    Nakasu, E.6    Brunetta, P.7    Oliveira, G.8    Neto, O.O.9    Oliveira, R.10
  • 79
    • 34247140927 scopus 로고    scopus 로고
    • Safety assessment of transgenic Bacillus thuringiensis with VIP insecticidal protein gene by feeding studies
    • Peng, D.; Chen, S.; Ruan, L.; Li, L.; Yu, Z.; Sun, M. Safety assessment of transgenic Bacillus thuringiensis with VIP insecticidal protein gene by feeding studies. Food Chem. Toxicol. 2007, 45, 1179-1185.
    • (2007) Food Chem. Toxicol , vol.45 , pp. 1179-1185
    • Peng, D.1    Chen, S.2    Ruan, L.3    Li, L.4    Yu, Z.5    Sun, M.6
  • 80
    • 0028980926 scopus 로고
    • A comparative review of the mammalian toxicity of Bacillus thuringiensis-based pesticides
    • McClintock, J.; Schaffer, C.; Sjoblad, R. A comparative review of the mammalian toxicity of Bacillus thuringiensis-based pesticides. Pestic. Sci. 1995, 45, 95-105.
    • (1995) Pestic. Sci , vol.45 , pp. 95-105
    • McClintock, J.1    Schaffer, C.2    Sjoblad, R.3
  • 82
    • 58149400440 scopus 로고    scopus 로고
    • Helix alpha 4 of the Bacillus thuringiensis Cry1Aa toxin plays a critical role in the post binding steps of pore formation
    • Girard, F.; Vachon, V. Helix alpha 4 of the Bacillus thuringiensis Cry1Aa toxin plays a critical role in the post binding steps of pore formation. Appl. Environ. Microbiol. 2009, 75, 359-365.
    • (2009) Appl. Environ. Microbiol , vol.75 , pp. 359-365
    • Girard, F.1    Vachon, V.2
  • 83
    • 0028905149 scopus 로고
    • Mutations in domain I of Bacilllus thuringiensis δ-endotoxin Cry1Ab reduce the irreversible binding of toxin to Manduca sexta brush border membrane vesicles
    • Chen, X.; Curtiss, A.; Alcantara, E.; Dean, D. Mutations in domain I of Bacilllus thuringiensis δ-endotoxin Cry1Ab reduce the irreversible binding of toxin to Manduca sexta brush border membrane vesicles. J. Biol. Chem. 1995, 270, 6412-6419.
    • (1995) J. Biol. Chem , vol.270 , pp. 6412-6419
    • Chen, X.1    Curtiss, A.2    Alcantara, E.3    Dean, D.4
  • 84
    • 84899034273 scopus 로고    scopus 로고
    • A conserved tetrameric interaction of cry toxin helix α3 suggests a funciontal role for toxin oligomerization
    • Lin, X.; Parthasarathy, K.; Surya, W.; Zhang, T.; Mu, Y.; Torres, J. A conserved tetrameric interaction of cry toxin helix α3 suggests a funciontal role for toxin oligomerization. Biochim. Biophys. Acta 2014, 1838, 1777-1784.
    • (2014) Biochim. Biophys. Acta , vol.1838 , pp. 1777-1784
    • Lin, X.1    Parthasarathy, K.2    Surya, W.3    Zhang, T.4    Mu, Y.5    Torres, J.6
  • 85
    • 0037181168 scopus 로고    scopus 로고
    • Cadherin-like receptor binding facilitates proteolytic cleavage of helix α-1 in domain I and oligomer pre-pore formation of Bacillus thuringiensis Cry1Ab toxin
    • Gomez, I.; Sanchez, J.; Miranda, R.; Bravo, A.; Soberon, M. Cadherin-like receptor binding facilitates proteolytic cleavage of helix α-1 in domain I and oligomer pre-pore formation of Bacillus thuringiensis Cry1Ab toxin. FEBS Lett. 2002, 513, 242-246.
    • (2002) FEBS Lett , vol.513 , pp. 242-246
    • Gomez, I.1    Sanchez, J.2    Miranda, R.3    Bravo, A.4    Soberon, M.5
  • 86
    • 0031559920 scopus 로고    scopus 로고
    • Isolated domain II and III from the Bacillus thuringiensis Cry1Ab δ-endotoxin binds to lepidopteran midgut membranes
    • Flores, H.; Soberón, X.; Sánches, J.; Bravo, A. Isolated domain II and III from the Bacillus thuringiensis Cry1Ab δ-endotoxin binds to lepidopteran midgut membranes. FEBS Lett. 1997, 414, 313-318.
    • (1997) FEBS Lett , vol.414 , pp. 313-318
    • Flores, H.1    Soberón, X.2    Sánches, J.3    Bravo, A.4
  • 87
    • 67349279272 scopus 로고    scopus 로고
    • N546 in b18-b19 loop is important for binding and toxicity of the Bacillus thuringiensis Cry1Ac toxin
    • Xiang, W.; Qiu, X.; Zhi, D.; Min, Z. N546 in b18-b19 loop is important for binding and toxicity of the Bacillus thuringiensis Cry1Ac toxin. J. Invertabr. Pathol. 2009, 101, 119-123.
    • (2009) J. Invertabr. Pathol , vol.101 , pp. 119-123
    • Xiang, W.1    Qiu, X.2    Zhi, D.3    Min, Z.4
  • 89
    • 0024337104 scopus 로고
    • Insecticidal crystal proteins of Bacillus thuringiensis
    • Hofte, H.; Whiteley, H. Insecticidal crystal proteins of Bacillus thuringiensis. Microbiol. Rev. 1989, 53, 242-255.
    • (1989) Microbiol. Rev , vol.53 , pp. 242-255
    • Hofte, H.1    Whiteley, H.2
  • 90
    • 0035929648 scopus 로고    scopus 로고
    • Role of interdomain salt bridges in the pore-forming ability of the Bacillus thuringiensis toxins Cry1Aa and Cry1Ac
    • Coux, F.; Vachon, V. Role of interdomain salt bridges in the pore-forming ability of the Bacillus thuringiensis toxins Cry1Aa and Cry1Ac. J. Biol. Chem. 2001, 276, 35546-35551.
    • (2001) J. Biol. Chem , vol.276 , pp. 35546-35551
    • Coux, F.1    Vachon, V.2
  • 91
    • 0035831331 scopus 로고    scopus 로고
    • Structural and functional studies of α-helix 5 region from Bacillus thuringiensis Cry1Ab δ-endotoxin
    • Nunez-Valdez, M.; Sanchez, J.; Lina, L.; Guereca, L.; Bravo, A. Structural and functional studies of α-helix 5 region from Bacillus thuringiensis Cry1Ab δ-endotoxin. Biochim. Biophys. Acta 2001, 1546, 122-131.
    • (2001) Biochim. Biophys. Acta , vol.1546 , pp. 122-131
    • Nunez-Valdez, M.1    Sanchez, J.2    Lina, L.3    Guereca, L.4    Bravo, A.5
  • 92
    • 0037076528 scopus 로고    scopus 로고
    • Role of helix 3 in pore formation by the Bacillus thuringiensis insecticidal toxin Cry1Aa
    • Vachon, V.; Orefontaine, G. Role of helix 3 in pore formation by the Bacillus thuringiensis insecticidal toxin Cry1Aa. Biochemistry 2002, 41, 6178-6184.
    • (2002) Biochemistry , vol.41 , pp. 6178-6184
    • Vachon, V.1    Orefontaine, G.2
  • 93
    • 0037952941 scopus 로고    scopus 로고
    • Specific mutations witihn the alpha4-alpha5 loop of Bacillus thuringiensis Cry4B toxin reveal a crucial role for Asn-166 and Tyr-170
    • Kanintronkul, Y.; Sramala, I.; Katzenmeier, G.; Panyim, S.; Angsuthanasombat, C. Specific mutations witihn the alpha4-alpha5 loop of Bacillus thuringiensis Cry4B toxin reveal a crucial role for Asn-166 and Tyr-170. Mol. Biotechnol. 2003, 24, 11-20.
    • (2003) Mol. Biotechnol , vol.24 , pp. 11-20
    • Kanintronkul, Y.1    Sramala, I.2    Katzenmeier, G.3    Panyim, S.4    Angsuthanasombat, C.5
  • 94
    • 0023885305 scopus 로고    scopus 로고
    • The Protein Kinase Family: Conserved Features and Deduced Phylogeny of the Catalytic Domains
    • Hank, S.K.; Quinn, A.M.; Hunter, T. The Protein Kinase Family: Conserved Features and Deduced Phylogeny of the Catalytic Domains. Science1988, 241, 42-52.
    • Science1988 , vol.241 , pp. 42-52
    • Hank, S.K.1    Quinn, A.M.2    Hunter, T.3
  • 95
    • 84870955143 scopus 로고    scopus 로고
    • Bacillus thuringiensis insecticidal three-domain Cry toxins: Mode of action, insect resistance and consequences for crop protection
    • Pardo-Lopez, L.; Soberon, M.; Bravo, A. Bacillus thuringiensis insecticidal three-domain Cry toxins: Mode of action, insect resistance and consequences for crop protection. FEMS Microbiol. Rev. 2012, 37, 3-22.
    • (2012) FEMS Microbiol. Rev , vol.37 , pp. 3-22
    • Pardo-Lopez, L.1    Soberon, M.2    Bravo, A.3
  • 96
    • 84865563394 scopus 로고    scopus 로고
    • Current models of the mode of action of Bacillus thuringiensis insecticidal crystal proteins: A critical review
    • Vachon, V.; Laprade, R.; Schwartz, J. Current models of the mode of action of Bacillus thuringiensis insecticidal crystal proteins: A critical review. J. Invertabr. Pathol. 2012, 111, 1-12.
    • (2012) J. Invertabr. Pathol , vol.111 , pp. 1-12
    • Vachon, V.1    Laprade, R.2    Schwartz, J.3
  • 98
    • 0029850471 scopus 로고    scopus 로고
    • High-resolution crystal structures of human cyclin-dependent kinase 2 with and without ATP: Bound waters and natural ligand as guides for inhibitor design
    • Schulze-Gahmen, U.; de Bondt, H.L.; Kim, S.H. High-resolution crystal structures of human cyclin-dependent kinase 2 with and without ATP: Bound waters and natural ligand as guides for inhibitor design. J. Med. Chem. 1996, 39, 4540-4546.
    • (1996) J. Med. Chem , vol.39 , pp. 4540-4546
    • Schulze-Gahmen, U.1    de Bondt, H.L.2    Kim, S.H.3
  • 99
    • 79151475987 scopus 로고    scopus 로고
    • The role of b20-b21 loop structure in insecticidal activity of Cry1Ac toxin from Bacillus thuringiensis
    • Lv, Y.; Tang, Y.; Zhang, Y.; Xia, L.; Wang, F.; Ding, X. The role of b20-b21 loop structure in insecticidal activity of Cry1Ac toxin from Bacillus thuringiensis. Curr. Microbiol. 2011, 62, 665-670.
    • (2011) Curr. Microbiol , vol.62 , pp. 665-670
    • Lv, Y.1    Tang, Y.2    Zhang, Y.3    Xia, L.4    Wang, F.5    Ding, X.6
  • 100
    • 77956267389 scopus 로고    scopus 로고
    • Residue 544 in domain III of the Bacillus thuringiensis Cry1Ac toxin is involved in protein structure stability
    • Liu, Y.; Wang, Q.; Wang, F.; Ding, X.; Xia, L. Residue 544 in domain III of the Bacillus thuringiensis Cry1Ac toxin is involved in protein structure stability. Protein J. 2010, 29, 440-445.
    • (2010) Protein J , vol.29 , pp. 440-445
    • Liu, Y.1    Wang, Q.2    Wang, F.3    Ding, X.4    Xia, L.5
  • 101
    • 84940286518 scopus 로고    scopus 로고
    • Foundation, I.R. GM Crop Database, accessed on 5 May 2014
    • Foundation, I.R. GM Crop Database. Available online: http://cera-gmc.org/index.php?action=gm_crop_database (accessed on 5 May 2014).
  • 102
    • 0036057181 scopus 로고    scopus 로고
    • Anticipatory evolution nd DNA shuffling
    • Bacher, J.; Reiss, B.; Ellington, A. Anticipatory evolution nd DNA shuffling. Genome Biol. 2002, 3, 1021:1-1021:4.
    • (2002) Genome Biol , vol.3
    • Bacher, J.1    Reiss, B.2    Ellington, A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.