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Volumn 168, Issue 2, 2009, Pages 259-266

Crystal structure of Bacillus thuringiensis Cry8Ea1: An insecticidal toxin toxic to underground pests, the larvae of Holotrichia parallela

Author keywords

Bacillus thuringiensis; Bioinsecticide; Cry protein; Crystal structure

Indexed keywords

BACILLUS THURINGIENSIS TOXIN; CRY8EA1 TOXIN; INSECT VENOM; INSECTICIDE; PROLINE; UNCLASSIFIED DRUG;

EID: 70349617068     PISSN: 10478477     EISSN: 10958657     Source Type: Journal    
DOI: 10.1016/j.jsb.2009.07.004     Document Type: Article
Times cited : (74)

References (54)
  • 1
    • 58249113980 scopus 로고    scopus 로고
    • Mammalian nicotinic acetylcholine receptors: from structure to function
    • Albuquerque E.X., Pereira E.F., Alkondon M., and Rogers S.W. Mammalian nicotinic acetylcholine receptors: from structure to function. Physiol. Rev. 89 1 (2009) 73-120
    • (2009) Physiol. Rev. , vol.89 , Issue.1 , pp. 73-120
    • Albuquerque, E.X.1    Pereira, E.F.2    Alkondon, M.3    Rogers, S.W.4
  • 2
    • 0024278714 scopus 로고
    • Helix geometry in proteins
    • Barlow D.J., and Thornton J.M. Helix geometry in proteins. J. Mol. Biol. 201 3 (1988) 601-619
    • (1988) J. Mol. Biol. , vol.201 , Issue.3 , pp. 601-619
    • Barlow, D.J.1    Thornton, J.M.2
  • 3
    • 16244392435 scopus 로고    scopus 로고
    • Crystal structure of the mosquito-larvicidal toxin Cry4Ba and its biological implications
    • Boonserm P., Davis P., Ellar D.J., and Li J. Crystal structure of the mosquito-larvicidal toxin Cry4Ba and its biological implications. J. Mol. Biol. 348 2 (2005) 363-382
    • (2005) J. Mol. Biol. , vol.348 , Issue.2 , pp. 363-382
    • Boonserm, P.1    Davis, P.2    Ellar, D.J.3    Li, J.4
  • 4
    • 33646257356 scopus 로고    scopus 로고
    • Structure of the functional form of the mosquito larvicidal Cry4Aa toxin from Bacillus thuringiensis at a 2.8-Å resolution
    • Boonserm P., Mo M., Angsuthanasombat C., and Lescar J. Structure of the functional form of the mosquito larvicidal Cry4Aa toxin from Bacillus thuringiensis at a 2.8-Å resolution. J. Bacteriol. 188 9 (2006) 3391-3401
    • (2006) J. Bacteriol. , vol.188 , Issue.9 , pp. 3391-3401
    • Boonserm, P.1    Mo, M.2    Angsuthanasombat, C.3    Lescar, J.4
  • 5
    • 0026514429 scopus 로고
    • SecA insertion into phospholipids is stimulated by negatively charged lipids and inhibited by ATP: a monolayer study
    • Breukink E., Demel R.A., de Korte-Kool G., and de Kruijff B. SecA insertion into phospholipids is stimulated by negatively charged lipids and inhibited by ATP: a monolayer study. Biochemistry 31 4 (1992) 1119-1124
    • (1992) Biochemistry , vol.31 , Issue.4 , pp. 1119-1124
    • Breukink, E.1    Demel, R.A.2    de Korte-Kool, G.3    de Kruijff, B.4
  • 7
    • 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.L., Ellar D.J., Li J., and Derbyshire D.J. 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. 287 5 (1999) 1011-1022
    • (1999) J. Mol. Biol. , vol.287 , Issue.5 , pp. 1011-1022
    • Burton, S.L.1    Ellar, D.J.2    Li, J.3    Derbyshire, D.J.4
  • 8
    • 0012789571 scopus 로고    scopus 로고
    • Proline-induced kink in a helix arises primarily from dihedral angle energy: a molecular dynamics simulation on alamethicin
    • Cheng S.F., and Chang D.K. Proline-induced kink in a helix arises primarily from dihedral angle energy: a molecular dynamics simulation on alamethicin. Chem. Phys. Lett. 301 5-6 (1999) 453-457
    • (1999) Chem. Phys. Lett. , vol.301 , Issue.5-6 , pp. 453-457
    • Cheng, S.F.1    Chang, D.K.2
  • 9
    • 0025337108 scopus 로고
    • Unusual proteolysis of the protoxin and toxin from Bacillus thuringiensis. Structural implications
    • Choma C.T., Surewicz W.K., Carey P.R., Pozsgay M., Raynor T., and Kaplan H. Unusual proteolysis of the protoxin and toxin from Bacillus thuringiensis. Structural implications. Eur. J. Biochem. 189 3 (1990) 523-527
    • (1990) Eur. J. Biochem. , vol.189 , Issue.3 , pp. 523-527
    • Choma, C.T.1    Surewicz, W.K.2    Carey, P.R.3    Pozsgay, M.4    Raynor, T.5    Kaplan, H.6
  • 10
    • 0032884932 scopus 로고    scopus 로고
    • Identification of Bacillus thuringiensis delta-endotoxin Cry1C domain III amino acid residues involved in insect specificity
    • de Maagd R.A., Bakker P., Staykov N., Dukiandjiev S., Stiekema W., and Bosch D. Identification of Bacillus thuringiensis delta-endotoxin Cry1C domain III amino acid residues involved in insect specificity. Appl. Environ. Microbiol. 65 10 (1999) 4369-4374
    • (1999) Appl. Environ. Microbiol. , vol.65 , Issue.10 , pp. 4369-4374
    • de Maagd, R.A.1    Bakker, P.2    Staykov, N.3    Dukiandjiev, S.4    Stiekema, W.5    Bosch, D.6
  • 11
    • 0016369116 scopus 로고
    • Monolayers-description of use and interaction
    • Demel R.A. Monolayers-description of use and interaction. Methods Enzymol. 32 (1974) 539-544
    • (1974) Methods Enzymol. , vol.32 , pp. 539-544
    • Demel, R.A.1
  • 12
    • 0016717097 scopus 로고
    • Relation between various phospholipase actions on human red cell membranes and the interfacial phospholipid pressure in monolayers
    • Demel R.A., Geurts van Kessel W.S., Zwaal R.F., Roelofsen B., and van Deenen L.L. Relation between various phospholipase actions on human red cell membranes and the interfacial phospholipid pressure in monolayers. Biochim. Biophys. Acta 406 1 (1975) 97-107
    • (1975) Biochim. Biophys. Acta , vol.406 , Issue.1 , pp. 97-107
    • Demel, R.A.1    Geurts van Kessel, W.S.2    Zwaal, R.F.3    Roelofsen, B.4    van Deenen, L.L.5
  • 14
    • 0004116672 scopus 로고
    • Cambridge University Press, Cambridge, United Kingdom
    • Finney D.J. Probit Analysis (1971), Cambridge University Press, Cambridge, United Kingdom
    • (1971) Probit Analysis
    • Finney, D.J.1
  • 16
    • 0032514753 scopus 로고    scopus 로고
    • The structure and organization within the membrane of the helices composing the pore-forming domain of Bacillus thuringiensis delta-endotoxin are consistent with an "umbrella-like" structure of the pore
    • Gazit E., La Rocca P., Sansom M.S., and Shai Y. The structure and organization within the membrane of the helices composing the pore-forming domain of Bacillus thuringiensis delta-endotoxin are consistent with an "umbrella-like" structure of the pore. Proc. Natl. Acad. Sci. USA 95 21 (1998) 12289-12294
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , Issue.21 , pp. 12289-12294
    • Gazit, E.1    La Rocca, P.2    Sansom, M.S.3    Shai, Y.4
  • 17
    • 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
    • Gomez I., Arenas I., Benitez I., Miranda-Rios J., Becerril B., Grande R., Almagro J.C., Bravo A., and Soberon M. 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. 281 45 (2006) 34032-34039
    • (2006) J. Biol. Chem. , vol.281 , Issue.45 , pp. 34032-34039
    • Gomez, I.1    Arenas, I.2    Benitez, I.3    Miranda-Rios, J.4    Becerril, B.5    Grande, R.6    Almagro, J.C.7    Bravo, A.8    Soberon, M.9
  • 19
    • 10944245296 scopus 로고    scopus 로고
    • Mutations in the Bacillus thuringiensis Cry1Ca toxin demonstrate the role of domains II and III in specificity towards Spodoptera exigua larvae
    • Herrero S., Gonzalez-Cabrera J., Ferre J., Bakker P.L., and de Maagd R.A. Mutations in the Bacillus thuringiensis Cry1Ca toxin demonstrate the role of domains II and III in specificity towards Spodoptera exigua larvae. Biochem. J. 384 Pt. 3 (2004) 507-513
    • (2004) Biochem. J. , vol.384 , Issue.PART 3 , pp. 507-513
    • Herrero, S.1    Gonzalez-Cabrera, J.2    Ferre, J.3    Bakker, P.L.4    de Maagd, R.A.5
  • 20
    • 0024337104 scopus 로고
    • Insecticidal crystal proteins of Bacillus thuringiensis
    • Hofte H., and Whiteley H.R. Insecticidal crystal proteins of Bacillus thuringiensis. Microbiol. Rev. 53 2 (1989) 242-255
    • (1989) Microbiol. Rev. , vol.53 , Issue.2 , pp. 242-255
    • Hofte, H.1    Whiteley, H.R.2
  • 21
    • 34250631991 scopus 로고    scopus 로고
    • Microbial control and biotechnology research on Bacillus thuringiensis in China
    • Huang D.F., Zhang J., Song F.P., and Lang Z.H. Microbial control and biotechnology research on Bacillus thuringiensis in China. J. Invertebr. Pathol. 95 3 (2007) 175-180
    • (2007) J. Invertebr. Pathol. , vol.95 , Issue.3 , pp. 175-180
    • Huang, D.F.1    Zhang, J.2    Song, F.P.3    Lang, Z.H.4
  • 22
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch W., and Sander C. Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers 22 12 (1983) 2577-2637
    • (1983) Biopolymers , vol.22 , Issue.12 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 23
    • 0004098818 scopus 로고    scopus 로고
    • Identification of residues in domain III of Bacillus thuringiensis Cry1Ac toxin that affect binding and toxicity
    • Lee M.K., You T.H., Gould F.L., and Dean D.H. Identification of residues in domain III of Bacillus thuringiensis Cry1Ac toxin that affect binding and toxicity. Appl. Environ. Microbiol. 65 10 (1999) 4513-4520
    • (1999) Appl. Environ. Microbiol. , vol.65 , Issue.10 , pp. 4513-4520
    • Lee, M.K.1    You, T.H.2    Gould, F.L.3    Dean, D.H.4
  • 24
    • 0026050639 scopus 로고
    • Crystal structure of insecticidal delta-endotoxin from Bacillus thuringiensis at 2.5 Å resolution
    • Li J.D., Carroll J., and Ellar D.J. Crystal structure of insecticidal delta-endotoxin from Bacillus thuringiensis at 2.5 Å resolution. Nature 353 6347 (1991) 815-821
    • (1991) Nature , vol.353 , Issue.6347 , pp. 815-821
    • Li, J.D.1    Carroll, J.2    Ellar, D.J.3
  • 25
    • 0032974991 scopus 로고    scopus 로고
    • Toxicity, binding, and permeability analyses of four Bacillus thuringiensis Cry1 delta-endotoxins using brush border membrane vesicles of Spodoptera exigua and Spodoptera frugiperda
    • Luo K., Banks D., and Adang M.J. Toxicity, binding, and permeability analyses of four Bacillus thuringiensis Cry1 delta-endotoxins using brush border membrane vesicles of Spodoptera exigua and Spodoptera frugiperda. Appl. Environ. Microbiol. 65 2 (1999) 457-464
    • (1999) Appl. Environ. Microbiol. , vol.65 , Issue.2 , pp. 457-464
    • Luo, K.1    Banks, D.2    Adang, M.J.3
  • 26
    • 0037060461 scopus 로고    scopus 로고
    • Polydispersity of Bacillus thuringiensis Cry1 toxins in solution and its effect on receptor binding kinetics
    • Masson L., Mazza A., Sangadala S., Adang M.J., and Brousseau R. Polydispersity of Bacillus thuringiensis Cry1 toxins in solution and its effect on receptor binding kinetics. Biochim. Biophys. Acta 1594 2 (2002) 266-275
    • (2002) Biochim. Biophys. Acta , vol.1594 , Issue.2 , pp. 266-275
    • Masson, L.1    Mazza, A.2    Sangadala, S.3    Adang, M.J.4    Brousseau, R.5
  • 27
    • 69949170335 scopus 로고
    • Bacillus thuringiensis toxins active against scarab pests
    • US Patent 5554534
    • Michaels, T., Narva, K., Foncerrada, L., 1994. Bacillus thuringiensis toxins active against scarab pests. US Patent 5554534.
    • (1994)
    • Michaels, T.1    Narva, K.2    Foncerrada, L.3
  • 28
    • 0034980642 scopus 로고    scopus 로고
    • Structure of Cry2Aa suggests an unexpected receptor binding epitope
    • Morse R.J., Yamamoto T., and Stroud R.M. Structure of Cry2Aa suggests an unexpected receptor binding epitope. Structure 9 5 (2001) 409-417
    • (2001) Structure , vol.9 , Issue.5 , pp. 409-417
    • Morse, R.J.1    Yamamoto, T.2    Stroud, R.M.3
  • 29
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov G.N., Vagin A.A., and Dodson E.J. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr. D Biol. Crystallogr. 53 Pt. 3 (1997) 240-255
    • (1997) Acta Crystallogr. D Biol. Crystallogr. , vol.53 , Issue.PART 3 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 30
    • 0028926284 scopus 로고
    • Nucleotide sequence of the gene encoding novel delta-endotoxin from Bacillus thuringiensis serovar japonensis strain Buibui specific to scarabaeid beetles
    • Ogiwara K., Hori H., Minami M., Takeuchi K., Sato R., Ohba M., and Iwahana H. Nucleotide sequence of the gene encoding novel delta-endotoxin from Bacillus thuringiensis serovar japonensis strain Buibui specific to scarabaeid beetles. Curr. Microbiol. 30 4 (1995) 227-235
    • (1995) Curr. Microbiol. , vol.30 , Issue.4 , pp. 227-235
    • Ogiwara, K.1    Hori, H.2    Minami, M.3    Takeuchi, K.4    Sato, R.5    Ohba, M.6    Iwahana, H.7
  • 31
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z., and Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276 (1997) 307-326
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 32
    • 0032212015 scopus 로고    scopus 로고
    • Incorporation of prior phase information strengthens maximum-likelihood structure refinement
    • PART 6
    • Pannu N.S., Murshudov G.N., Dodson E.J., and Read R.J. Incorporation of prior phase information strengthens maximum-likelihood structure refinement. Acta Crystallogr. D Biol. Crystallogr. 54 Pt. 6, 2 (1998) 1285-1294
    • (1998) Acta Crystallogr. D Biol. Crystallogr. , vol.54 , Issue.2 , pp. 1285-1294
    • Pannu, N.S.1    Murshudov, G.N.2    Dodson, E.J.3    Read, R.J.4
  • 33
    • 0027443116 scopus 로고
    • Rendering a membrane protein soluble in water: a common packing motif in bacterial protein toxins
    • Parker M.W., and Pattus F. Rendering a membrane protein soluble in water: a common packing motif in bacterial protein toxins. Trends Biochem. Sci. 18 10 (1993) 391-395
    • (1993) Trends Biochem. Sci. , vol.18 , Issue.10 , pp. 391-395
    • Parker, M.W.1    Pattus, F.2
  • 34
    • 34250782646 scopus 로고    scopus 로고
    • Role of receptors in Bacillus thuringiensis crystal toxin activity
    • Pigott C.R., and Ellar D.J. Role of receptors in Bacillus thuringiensis crystal toxin activity. Microbiol. Mol. Biol. Rev. 71 2 (2007) 255-281
    • (2007) Microbiol. Mol. Biol. Rev. , vol.71 , Issue.2 , pp. 255-281
    • Pigott, C.R.1    Ellar, D.J.2
  • 35
    • 0029792870 scopus 로고    scopus 로고
    • Mutations at domain II, loop 3, of Bacillus thuringiensis CryIAa and CryIAb delta-endotoxins suggest loop 3 is involved in initial binding to lepidopteran midguts
    • Rajamohan F., Hussain S.R., Cotrill J.A., Gould F., and Dean D.H. Mutations at domain II, loop 3, of Bacillus thuringiensis CryIAa and CryIAb delta-endotoxins suggest loop 3 is involved in initial binding to lepidopteran midguts. J. Biol. Chem. 271 41 (1996) 25220-25226
    • (1996) J. Biol. Chem. , vol.271 , Issue.41 , pp. 25220-25226
    • Rajamohan, F.1    Hussain, S.R.2    Cotrill, J.A.3    Gould, F.4    Dean, D.H.5
  • 37
    • 0027957473 scopus 로고
    • Cloning, heterologous expression, and localization of a novel crystal protein gene from Bacillus thuringiensis serovar japonensis strain buibui toxic to scarabaeid insects
    • Sato R., Takeuchi K., Ogiwara K., Minami M., Kaji Y., Suzuki N., Hori H., Asano S., Ohba M., and Iwahana H. Cloning, heterologous expression, and localization of a novel crystal protein gene from Bacillus thuringiensis serovar japonensis strain buibui toxic to scarabaeid insects. Curr. Microbiol. 28 1 (1994) 15-19
    • (1994) Curr. Microbiol. , vol.28 , Issue.1 , pp. 15-19
    • Sato, R.1    Takeuchi, K.2    Ogiwara, K.3    Minami, M.4    Kaji, Y.5    Suzuki, N.6    Hori, H.7    Asano, S.8    Ohba, M.9    Iwahana, H.10
  • 39
    • 0343196687 scopus 로고    scopus 로고
    • Ion channels formed in planar lipid bilayers by Bacillus thuringiensis toxins in the presence of Manduca sexta midgut receptors
    • Schwartz J.L., Lu Y.J., Sohnlein P., Brousseau R., Laprade R., Masson L., and Adang M.J. Ion channels formed in planar lipid bilayers by Bacillus thuringiensis toxins in the presence of Manduca sexta midgut receptors. FEBS Lett. 412 2 (1997) 270-276
    • (1997) FEBS Lett. , vol.412 , Issue.2 , pp. 270-276
    • Schwartz, J.L.1    Lu, Y.J.2    Sohnlein, P.3    Brousseau, R.4    Laprade, R.5    Masson, L.6    Adang, M.J.7
  • 40
    • 0141453334 scopus 로고    scopus 로고
    • A strain of Bacillus thuringiensis subsp. galleriae containing a novel cry8 gene highly toxic to Anomala cuprea (Coleoptera: Scarabaeidae)
    • Shin-ichiro A., Yamashita C., Iizuka T., Takeuchi K., Yamanaka S., Cerf D., and Yamamoto T. A strain of Bacillus thuringiensis subsp. galleriae containing a novel cry8 gene highly toxic to Anomala cuprea (Coleoptera: Scarabaeidae). Biol. Control 28 (2003) 191-196
    • (2003) Biol. Control , vol.28 , pp. 191-196
    • Shin-ichiro, A.1    Yamashita, C.2    Iizuka, T.3    Takeuchi, K.4    Yamanaka, S.5    Cerf, D.6    Yamamoto, T.7
  • 42
    • 0029945751 scopus 로고    scopus 로고
    • Cholesterol-induced interfacial area condensations of galactosylceramides and sphingomyelins with identical acyl chains
    • Smaby J.M., Momsen M., Kulkarni V.S., and Brown R.E. Cholesterol-induced interfacial area condensations of galactosylceramides and sphingomyelins with identical acyl chains. Biochemistry 35 18 (1996) 5696-5704
    • (1996) Biochemistry , vol.35 , Issue.18 , pp. 5696-5704
    • Smaby, J.M.1    Momsen, M.2    Kulkarni, V.S.3    Brown, R.E.4
  • 43
    • 0029993089 scopus 로고    scopus 로고
    • Mutagenesis of three surface-exposed loops of a Bacillus thuringiensis insecticidal toxin reveals residues important for toxicity, receptor recognition and possibly membrane insertion
    • Smedley D.P., and Ellar D.J. Mutagenesis of three surface-exposed loops of a Bacillus thuringiensis insecticidal toxin reveals residues important for toxicity, receptor recognition and possibly membrane insertion. Microbiology 142 Pt. 7 (1996) 1617-1624
    • (1996) Microbiology , vol.142 , Issue.PART 7 , pp. 1617-1624
    • Smedley, D.P.1    Ellar, D.J.2
  • 44
    • 39049188731 scopus 로고    scopus 로고
    • Gaussian mixture modeling of alpha-helix subclasses: structure and sequence variations
    • Tendulkar A.V., Ogunnaike B., and Wangikar P.P. Gaussian mixture modeling of alpha-helix subclasses: structure and sequence variations. Pac. Symp. Biocomput. 291 (2006) 302
    • (2006) Pac. Symp. Biocomput. , vol.291 , pp. 302
    • Tendulkar, A.V.1    Ogunnaike, B.2    Wangikar, P.P.3
  • 45
    • 0031972865 scopus 로고    scopus 로고
    • Kinked-helices model of the nicotinic acetylcholine receptor ion channel and its complexes with blockers: simulation by the Monte Carlo minimization method
    • Tikhonov D.B., and Zhorov B.S. Kinked-helices model of the nicotinic acetylcholine receptor ion channel and its complexes with blockers: simulation by the Monte Carlo minimization method. Biophys. J. 74 1 (1998) 242-255
    • (1998) Biophys. J. , vol.74 , Issue.1 , pp. 242-255
    • Tikhonov, D.B.1    Zhorov, B.S.2
  • 46
    • 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., and Angsuthanasombat C. Targeted mutagenesis of loop residues in the receptor-binding domain of the Bacillus thuringiensis Cry4Ba toxin affects larvicidal activity. FEMS Microbiol. Lett. 242 2 (2005) 325-332
    • (2005) FEMS Microbiol. Lett. , vol.242 , Issue.2 , pp. 325-332
    • Tuntitippawan, T.1    Boonserm, P.2    Katzenmeier, G.3    Angsuthanasombat, C.4
  • 47
    • 0036015624 scopus 로고    scopus 로고
    • Characterization of the proteolytic enzymes in the midgut of the European Cockchafer, Melolontha melolontha (Coleoptera: Scarabaeidae)
    • Wagner W., Mohrlen F., and Schnetter W. Characterization of the proteolytic enzymes in the midgut of the European Cockchafer, Melolontha melolontha (Coleoptera: Scarabaeidae). Insect Biochem. Mol. Biol. 32 7 (2002) 803-814
    • (2002) Insect Biochem. Mol. Biol. , vol.32 , Issue.7 , pp. 803-814
    • Wagner, W.1    Mohrlen, F.2    Schnetter, W.3
  • 49
    • 0032531992 scopus 로고    scopus 로고
    • The insertion of human apolipoprotein H into phospholipid membranes: a monolayer study
    • Wang S.X., Cai G.P., and Sui S.F. The insertion of human apolipoprotein H into phospholipid membranes: a monolayer study. Biochem. J. 335 Pt. 2 (1998) 225-232
    • (1998) Biochem. J. , vol.335 , Issue.PART 2 , pp. 225-232
    • Wang, S.X.1    Cai, G.P.2    Sui, S.F.3
  • 50
    • 0008032049 scopus 로고
    • Biological control of white grubs (Coleopera: Scarabaeidae) by larvae of Promachus yesonicus (Diptera: Asilidae) in China
    • Wei X.T., Xu X.D., and Deloach C.J. Biological control of white grubs (Coleopera: Scarabaeidae) by larvae of Promachus yesonicus (Diptera: Asilidae) in China. Biol. Control 5 2 (1995) 290-296
    • (1995) Biol. Control , vol.5 , Issue.2 , pp. 290-296
    • Wei, X.T.1    Xu, X.D.2    Deloach, C.J.3
  • 51
    • 0035182073 scopus 로고    scopus 로고
    • Use of TLS parameters to model anisotropic displacements in macromolecular refinement
    • Winn M.D., Isupov M.N., and Murshudov G.N. Use of TLS parameters to model anisotropic displacements in macromolecular refinement. Acta Crystallogr. D Biol. Crystallogr. 57 Pt. 1 (2001) 122-133
    • (2001) Acta Crystallogr. D Biol. Crystallogr. , vol.57 , Issue.PART 1 , pp. 122-133
    • Winn, M.D.1    Isupov, M.N.2    Murshudov, G.N.3
  • 52
    • 0034254839 scopus 로고    scopus 로고
    • The membrane insertion of trichosanthin is membrane-surface-pH dependent
    • Xia X.F., and Sui S.F. The membrane insertion of trichosanthin is membrane-surface-pH dependent. Biochem. J. 349 Pt. 3 (2000) 835-841
    • (2000) Biochem. J. , vol.349 , Issue.PART 3 , pp. 835-841
    • Xia, X.F.1    Sui, S.F.2
  • 53
    • 54849430509 scopus 로고    scopus 로고
    • Discovery of a novel Bacillus thuringiensis Cry8D protein and the unique toxicity of the Cry8D-class proteins against scarab beetles
    • Yamaguchi T., Sahara K., Bando H., and Asano S.I. Discovery of a novel Bacillus thuringiensis Cry8D protein and the unique toxicity of the Cry8D-class proteins against scarab beetles. J. Invertebr. Pathol. 99 3 (2008) 257-262
    • (2008) J. Invertebr. Pathol. , vol.99 , Issue.3 , pp. 257-262
    • Yamaguchi, T.1    Sahara, K.2    Bando, H.3    Asano, S.I.4
  • 54
    • 33746421012 scopus 로고    scopus 로고
    • Characterization of Bacillus thuringiensis strain Bt185 toxic to the Asian cockchafer: Holotrichia parallela
    • Yu H., Zhang J., Huang D., Gao J., and Song F. Characterization of Bacillus thuringiensis strain Bt185 toxic to the Asian cockchafer: Holotrichia parallela. Curr. Microbiol. 53 1 (2006) 13-17
    • (2006) Curr. Microbiol. , vol.53 , Issue.1 , pp. 13-17
    • Yu, H.1    Zhang, J.2    Huang, D.3    Gao, J.4    Song, F.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.