Insect Control: Biological and Synthetic Agents - Index of

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Valaitis, A.P., Jenkins, J.L., Lee, M.K., Dean, D.H., Garner, K.J., 2001. Isolation and partial characterization of Gypsy moth BTR-270 an anionic brush border membrane glycoconjugate that binds Bacillus thuringiensis Cry1A toxins with high affinity. Arch. Insect Biochem. Physiol. 46, 186–200. van Frankenhuyzen, K., 2000. Application of Bacillus thuringiensis in forestry. In: Charles, J.F., Delécluse, A., Nielsen-LeRoux, C. (Eds.), Entomopathogenic Bacteria: From Laboratory to Field Application. Kluwer, London, pp. 371–382. Vie, V., Van Mau, N., Pomarde, P., Dance, C., Schwartz, J.L., et al., 2001. Lipid-induced pore formation of the Bacillus thuringiensis Cry1Aa insecticidal toxin. J. Membr. Biol. 180, 195–203. Von-Tersch, M.A., Slatin, S.L., Kulesza, C.A., English, L.H., 1994. Membrane-permeabilizing activities of Bacillus thuringiensis coleopteran-active toxin CryIIIB2 and CryIIIB2 domain I peptide. Appl. Environ. Microbiol. 60, 3711–3717. Warren, G., 1997. Vegetative insecticidal proteins: novel proteins for control of corn pests. In: Carozzi, N., Koziel, M. (Eds.), Advances in Insect Control: The Role of Transgenic Plants. Taylor and Francis, London, pp. 109–121. Wei, J.-Z., Hale, K., Carta, L., Platzer, E., Wong, C., et al., 2003. Bacillus thuringiensis crystal proteins that target nematodes. Proc. Natl Acad. Sci. USA 100, 2760–2765. Widner, W.R., Whiteley, H.R., 1990. Location of the dipteran specific region in a lepidopteran–dipteran crystal protein from Bacillus thuringiensis. J. Bacteriol. 172, 2826–2832. Wirth, M.C., Georghiou, G.P., Federeci, B.A., 1997. CytA enables CryIV endotoxins of Bacillus thuringiensis to overcome high levels of CryIV resistance in the mosquito, Culex quinquefasciatus. Proc. Natl Acad. Sci. USA 94, 10536–10540. Wirth, M.C., Delécuse, A., Walton, W.E., 2001. CytAb1 and Cyt2Ba1 from Bacillus thuringiensis subsp. medellin and B. thuringiensis subsp. israelensis synergize Bacillus sphaericus against Aedes aegypti and resistant Culex quinquefasciatus (Diptera: Culicidae). Appl. Environ. Microbiol. 67, 3280–3284. 7: Bacillus thuringiensis: Mechanisms and Use 277 Wu, D., Aronson, A.I., 1992. Localized mutagenesis defines regions of the Bacillus thuringiensis d-endotoxin involved in toxicity and specificity. J. Biol. Chem. 267, 2311–2317. Wu, D., Johnson, J.J., Federeci, B.A., 1994. Synergism of mosquitocidal toxicity between CytA and CryIVD proteins using inclusions produced from cloned genes of Bacillus thuringiensis. Mol. Microbiol. 13, 965–972. Wu, S.-J., Dean, D.H., 1996. Functional significance of loops in the receptor binding domain of Bacillus thuringiensis CryIIIA d-endotoxin. J. Mol. Biol. 255, 628–640. Yamagiwa, M., Esaki, M., Otake, K., Inagaki, M., Komano, T., et al., 1999. Activation process of dipteran-specific insecticidal protein produced by Bacillus thuringiensis subsp. israelensis. Appl. Environ. Microbiol. 65, 3464–3469. Yaoi, K., Kadotani, T., Kuwana, H., Shinkawa, A., Takahashi, T., et al., 1997. Aminopeptidase N from Bombyx mori as a candidate for the receptor of Bacillus thuringiensis Cry1Aa toxin. Eur. J. Biochem. 246, 652–657. Yaoi, K., Nakanishi, K., Kadotani, T., Imamura, M., Koizumi, N., et al., 1999. Bacillus thuringiensis Cry1Aa toxin-binding region of Bombyx mori aminopeptidase N. FEBS Lett. 463, 221–224. Zangerl, A.R., McKenna, D., Wraight, C.L., Carroll, M., Ficarello, P., et al., 2001. Effects of exposure to event 176 Bacillus thuringiensis corn pollen on monarch and black swallowtail caterpillars under field conditions. Proc. Natl Acad. Sci. USA 98, 11908–11912. Zalunin, I.A., Revina, L.P., Kostina, L.I., Chestukhina, G.G., Stepanov, V.M., 1998. Limited proteolysis of Bacillus thuringiensis CryIG and CryIVB d-endotoxins leads to formation of active fragments that do not coincide with the structural domains. J. Protein Chem. 17, 463–471. Zhuang, M., Oltean, D.I., Gómez, I., Pullikuth, A.K., Soberón, 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.
A7 Addendum: Bacillus thuringiensis, with Resistance Mechanisms A Bravo and M Soberón, Universidad Nacional Auto´noma de Me´xico, Cuernavaca Morelos, Mexico S S Gill, University of California, Riverside, USA ß 2010 Elsevier B.V. All Rights Reserved A7.1. Mode of Action of Cry Toxins 278 A7.2. Conserved Cry Toxin-binding Proteins Among Different Insect Orders 279 A7.3. Other Cry Proteins Used in Insect Control 279 A7.4. Cyt1Aa Functions as a Surrogate Receptor for Cry11Aa 279 Since the publication of the chapter in 2005, there have been important developments in understanding the mode of action of Bacillus thuringiensis (Bt) toxins in different insect orders. Here we highlight some of these important developments. A7.1. Mode of Action of Cry Toxins The proposed model of the mode of action of Cry1A toxins involves sequential interaction of these toxins with at least two different receptor molecules, a transmembrane cadherin protein and GPI-anchored aminopeptidase-N (APN) (Bravo et al., 2005). In recent years, GPI-anchored alkaline phosphatase (ALP) was identified as a Cry toxin-receptor in different insect species (Jurat-Fuentes and Adang, 2004; Fernández et al., 2006). Monomeric Cry1A toxin binds to the cadherin receptor, facilitating additional cleavage of the N-terminal helix a-1 inducing oligomerization of the toxin (Bravo et al., 2005). Cry1A toxin oligomers then bind APN, due to its higher affinity, resulting in membrane insertion and pore formation (Figure A1). However, a second model proposed that insect cell death is triggered by the binding of the monomeric Cry1A toxin to cadherin, which in turn activates adenylyl cyclase resulting in increased cell levels of cAMP, that then activates protein kinase-A resulting in oncotic cell death (Zhang et al., 2006). In the signal transduction model, GPI-anchored receptors are involved neither in Cry toxicity nor in oligomer formation (Zhang et al., 2006). Oligomerization of Cry1Ab toxin was subsequently shown to be an indispensable step in its toxicity to Manduca sexta. Site directed mutagenesis of specific amino acids in domain I helix a-3 resulted in the isolation of Cry1Ab mutants that could not form oligomers, still bound cadherin receptor and lost toxicity to M. sexta (Jiménez-Juarez et al., 2007). It was also demonstrated that helix a-4 mutants affected in pore-formation have a dominant negative phenotype since they inhibited Cry1Ab toxicity and pore-formation when mixed in low ratios with wild-type Cry1Ab toxin, indicating that toxin hetero-oligomers were not functional (Rodriíguez-Almazan et al., 2009). Overall, these data indicate that Cry toxin oligomerization is an essential step in the mode of action of Cry toxins. In addition, it was shown in different insect species that GPI-anchored proteins are involved in Cry toxin action. In M. sexta, it was shown that an scFv antibody that bound Cry1Ab domain III and inhibited binding to APN but not to cadherin reduced Cry1Ab toxicity in bioassays (Gómez et al., 2006). Furthermore, populations of Spodoptera exigua and Helicoverpa armigera resistant to Cry1C and Cry1Ac, respectively, showed reduced levels of APN transcripts (Herrero et al., 2005; Zhang et al., 2009). These results demonstrate that binding to GPI-anchored proteins is an important step in the mode of action of Cry toxins. Finally, it was shown that modified Cry1Ab and Cry1Ac toxins (Cry1AbMod or Cry1AcMod) could skip cadherin binding and retain toxicity (Soberón et al., 2007). It was shown that these Cry1AbMod or Cry1AcMod toxins engineered to lack helix a-1 form oligomers in the absence of cadherin binding (Figure A1) and were toxic to a Pectinophora gossypiella population that is resistant to these toxins because of a mutation in the cadherin gene. These results show that cadherin binding alone is not sufficient for insect death. Cry1AMod
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INSECT CONTROL BIOLOGICAL AND SYNTH
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INSECT CONTROL BIOLOGICAL AND SYNTH
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CONTENTS Preface vii Contributors i
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PREFACE When Elsevier published the
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J T Andaloro E. I. Du Pont de Nemou
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1 Pyrethroids B P S Khambay and P J
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activity. In contrast to most other
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Figure 1 Commercial and novel pyret
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Figure 2 Pyrethroids referred to in
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4-position result in almost complet
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and their primary site of action is
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Figure 4 Folded and extended confor
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aromatic rings or methyl groups by
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pyrethroids) and consequently a sec
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1998), although the precise mechani
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polymorphisms in the protein. Of th
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observed resistance to pyrethroids,
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propoxur against Culex quinquefasci
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esistance in house fly. Insect Bioc
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Shan, G.M., Hammock, B.D., 2001. De
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A1.4. Resistance The increasing num
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B A IIS4-S5 linker, IIS5 helix and
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2 Indoxacarb and the Sodium Channel
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Figure 2 Structures of pyrazoline-l
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observed that both indoxacarb and i
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deflections resulting from stresses
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Figure 8 Dihydropyrazole block appe
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potential conduction in the CNS of
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known to affect blocker affinity, w
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Figure 13 Diagrammatic representati
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that the probable mechanism of ovil
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conventional chemistries and spinos
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Clare, J.J., Tate, S.N., Nobbs, M.,
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Tsurubuchi, Y., Karasawa, A., Nagat
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R1 N N O N H indoxacarb. Thus, whil
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3 Neonicotinoid Insecticides P Jesc
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esidues, like the pyrid-3-ylmethyl
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containing neonicotinoids, and neon
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Studies were also done using compar
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Becke, 1988; Klamt, 1995) level of
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sampling using forcefield methods (
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Figure 9 Stable conformations and p
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Figure 13 Binding to putative catio
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Figure 14 Systemicity of neonicotin
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site (Kayser et al., 2002). Clothia
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Figure 20 Important pest insects ta
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Barley yellow dwarf virus vectors s
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investigate the mode of action of n
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within the desensitized state over
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the accumulation of this acid in th
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3.8.1. Safety Profile The introduct
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Table 7 Environmental profile of co
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substance is bound irreversibly to
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imidacloprid conferring a high leve
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nAChR are comparable to the efficac
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Figure 25 Flea control achieved wit
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and the resolution of FAD was teste
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Brown, J.K., Perring, T.M., Cooper,
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In: Ishaaya, I. (Ed.), Biochemical
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Léna, C., Changeux, J.-P., 1993. A
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patterns in Colorado potato beetle
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nach Saatgutbeizung. Pflanzenschutz
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Today, photoaffinity labeling (e.g.
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for control of stinkbugs in soybean
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Biochem. Physiol., doi: 10.1016/j.p
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4 Insect Growth- and Development-Di
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The molting process is initiated by
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Table 1 Bisacylhydrazine insecticid
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4.2.2. Bisacylhydrazines as Tools o
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to the three EcRs with either muris
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of action of ecdysone agonists was
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thus inducing effects and symptomol
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and microsomes. Subsequently, Willi
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dipteran insects, like the midge, C
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eetle (Exomala orientalis) when app
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metabolic fate studies showed the i
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y specific proteins in signaling pa
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their reduced risk for the environm
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can be reversed by applying JH. JH
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door for a more rational approach t
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apparent that it was a bHLH-PAS and
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Table 9 Continued Bemisia tabaci (s
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Table 11 Insect control with some a
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Table 13 Ecotoxicological profile o
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Flucycloxuron Nonsystemic acaricide
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The discovery of diflubenzuron spaw
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Table 15 Environmental effects of s
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ecessive (R male S female) manner,
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esistance management programs due t
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IPS Paraconfusus lanier (Coleoptera
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larvae parasitized by Microplitis r
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Kostyukovsky, M., Chen, B., Atsmi,
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Three-dimensional quantitative stru
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Riddiford, L.M., 1994. Cellular and
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characterization of resistant clone
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Biological Approaches to Pest Contr
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M389 L308 M272 T304 T393 V404 L420
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5 Azadirachtin, a Natural Product i
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and Hemiptera and was related to ef
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eported, but this is rather nonspec
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important source of pest control at
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effects with physiological effects
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eing associated with an accumulatio
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et al., 1992). Salehzadeh et al. (2
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ehavior of Spodoptera littoralis (p
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indica A. Juss. IBH Publishing Comp
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Smith, S.L., Mitchell, M.J., 1988.
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which interact directly with azadir
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6 The Spinosyns: Chemistry, Biochem
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Table 1 Structures of the spinosyns
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Table 2 Biological activity of spin
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A large synthetic effort has gone i
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216 6: The Spinosyns: Chemistry, Bi
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Figure 4 Spinosad metabolism in avi
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A9 Addendum: Recent Advances in Pho
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330 A9: Addendum Lee, S.C., Stoilov
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332 10: Genetically Modified Baculo
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384 A10: Addendum cysteine protease
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388 11: Entomopathogenic Fungi and
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Zare, R., Gams, W., Culham, A., 200
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434 A11: Addendum although a number
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436 A11: Addendum Examination of ge
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440 12: Insect Transformation for U
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448 A12: Addendum genetic transform
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452 Subject Index Aphis gossypii (c
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454 Subject Index Bisacylhydrazine
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456 Subject Index Cry toxins (conti
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458 Subject Index Entomopathogenic
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460 Subject Index Homoptera molting
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462 Subject Index Kinoprene (ENSTAR
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464 Subject Index Muscle(s) sodium
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466 Subject Index Photorhabdus (con
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468 Subject Index Sodium channel bl
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470 Subject Index Toxocara cati, im
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