Insect Control: Biological and Synthetic Agents - Index of

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Cry toxins CryMod toxins Cadherin receptor Synergism between Cry and Cyt toxins toxins will be useful in countering the potential problem of insect resistance in the field (Bravo and Soberón, 2008). Overall, the results discussed here clearly indicate that toxicity of Cry toxins involves formation of oligomers and binding to GPI-anchored proteins. It remains to be determined whether signal transduction is involved in toxin action but if so, it should be triggered by pore-formation and not by binding to cellular receptors. A7.2. Conserved Cry Toxin-binding Proteins Among Different Insect Orders In the past few years, significant progress has been made in the identification of Cry toxin receptors in coleopteran and dipteran species. Cadherin proteins in the coleopterans Tenebrio molitor and Diabrotica virgifera were identified as Cry3A receptors (Fabrick et al., 2009; Park et al., 2009). In the case of T. molitor, it was shown that binding of Cry3Aa to cadherin induced oligomerization of the toxin, while in D. virgifera a cadherin fragment containing a Cry3Aa binding region enhanced Cry3Aa toxicity (Fabrick et al., 2009; Park et al., 2009). Regarding GPI-anchored receptors, an ADAM-metalloprotease was identified as a Cry3Aa receptor in Leptinotarsa decemlineata (Ochoa-Campuzano et al., 2007). In the case of mosquitocidal Cry toxins, it is proposed that the mechanism of action is also conserved, since similar Cry-binding molecules have been identified in their midgut cells, such as cadherin of Anopheles gambiae and Aedes aegypti, thatbindCry4Baor Cry11Aa, respectively (Hua et al., 2008; Chen et al., Cry Cyt Pore formation model of Cry toxins, CryMod toxins and synergism between Cry and Cyt toxins Helix α-1 Oligomerization GPI- anchored receptors Pore formation A7: Addendum 279 Figure A1 Mode of action of Cry1A toxin. Upper panel, Mode of action of Cry1A toxins. Middle panel, Mode of action of Cry1AMod toxins that skip cadherin binding. Lower panel, Cyt1A functions as Cry11Aa receptor explaining synergism between these toxins. The proteins depicted in the figure are hypothetical structures except for Cry and Cyt1Aa toxins. 2009a), or GPI-anchored APN in A. quadrimaculatus, A. gambiae, andAe. aegypti that binds Cry11Ba or Cry11Aa (Abdulla et al., 1996; Zhang et al., 2008; Chen et al., 2009b), and ALP in Ae. aegypti or A. gambiae that binds Cry11Aa toxin or Cry11Ba, respectively (Fernández et al., 2006; Hua et al., 2009). A7.3. Other Cry Proteins Used in Insect Control Besides the three-domain Cry toxins, several Bt strains produce other Cry toxins that are active against different insect pests. In particular, the binary toxin Cry34/Cry35 that has activity against the western corn rootworm (D. virgifera virgifera) has been successfully produced in transgenic maize and shown to protect corn roots from insect attack (Moellenbeck et al., 2001). A7.4. Cyt1Aa Functions as a Surrogate Receptor for Cry11Aa Bacillus thuringiensis subs israelensis (Bti) is used worldwide in the control of mosquitoes that are vectors of important human diseases. Despite the large-scale use of Bti in mosquito control programs, there are no reports of resistance to Bti under field conditions. The lack of insect resistance development to Bti is mainly due to the fact that this strain produces at least four different crystal proteins that belong to two unrelated family of toxins, namely Cry (Cry4Aa, Cry4Ba, Cry11Aa) and Cyt (Cyt1Aa). Interestingly, the insecticidal activity of the isolated Bti
280 A7: Addendum toxins is magnitudes of order less toxic than the crystal inclusion containing all toxins (Bravo et al., 2005). This synergistic effect and the lack of resistance is mainly due to Cyt1Aa that enhances the activity of Cry4Aa, Cry4Ba, or Cry11Aa (Bravo et al., 2005). The mechanism of synergism of Cyt1Aa and Cry11Aa depends on specific interaction between these toxins since single point mutations on Cyt1Aa affected Cry11Aa binding and synergism (Pérez et al., 2005). Also, it was shown that Cry11Aa domain II loop regions involved in receptor binding were also involved in binding and synergism with Cyt1Aa (Pérez et al., 2005). These data led to the hypothesis that Cyt1Aa functions as a membrane-bound receptor for Cry11Aa (Perez et al. 2005). Furthermore, binding of Cry11Aa to Cyt1Aa facilitates formation of Cry11Aa oligomers, which were efficient in pore-formation indicating Cyt1Aa fulfils the role of the primary cadherin receptor facilitating oligomer formation (Pérez et al., 2007). This is the first example of an insect pathogenic bacterium that carries a toxin and also its functional receptor, promoting toxin binding to target membranes and toxicity (Figure A1). References Abdullah, M.A., Valaitis, A.P., Dean, D.H., 1996. Identification of a Bacillus thuringiensis Cry11Ba toxin-binding aminopeptidase from the mosquito. Anopheles quadrimaculatus. BMC Biochem 22, 7–16. Bravo, A., Soberón, M., 2008. How to cope with resistance to Bt toxins? Trends Biotechnol. 26, 573–579. Bravo, A., Gill, S.S., Soberón, M., 2005. Bacillus thuringiensis mechanisms and use. In: Gilbert, L.I., Iatrou, K., Gill, S.S. (Eds.), Comprehensive Molecluar Insect Science. Elsevier, pp. 175–206 ß2005 Elsevier BV ISBN (Set): 0–44–451516-X. Chen, J., Aimanova, K.G., Pan, S., Gill, S.S., 2009a. Identification and characterization of Aedes aegypti aminopeptidase N as a putative receptor of Bacillus thuringiensis Cry11A toxin. Insect Biochem Mol Biol. 39, 688–696. Chen, J., Aimanova, K.G., Fernandez, L.E., Bravo, A., Soberón, M., Gill, S.S., 2009b. Aedes aegypti cadherin serves as a putative receptor of the Cry11Aa toxin from Bacillus thuringiensis subsp. israelensis. Biochem. J. doi:10.1042/BJ20090730. Fabrick, J., Oppert, C., Lorenzen, M.D., Morris, K., Oppert, B., Jurat-Fuentes, J.L., 2009. A novel Tenebrio molitor cadherin is a functional receptor for Bacillus thuringiensis Cry3Aa toxin. J. Biol. Chem. 284, 18401–18410. Fernández, L.E., Aimaniova, K.G., Gill, S.S., Bravo, A., Soberón, M., 2006. A GPI-anchored alkaline phosphatase is a functional midgut receptor of Cry11Aa toxin in Aedes aegypti larvae. Biochem. J. 394, 77–84. Fernández, L.E., Martinez-Anaya, C., Lira, E., Chen, J., Evans, J., Hernández-Martiínez, S., Lanz-Mendoza, H., Bravo, A., Gill, S.S., Soberón, M., 2009. Cloning and epitope mapping of Cry11Aa-binding sites in the Cry11Aa-receptor alkaline phosphatase from Aedes aegypti. Biochemistry 48, 8899–8907. Gómez, I., Arenas, I., Benitez, I., Miranda-Riíos, J., Becerril, B., Grande, G., Almagro, J.C., Bravo, A., Soberón, M., 2006. 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, 34032–34039. Herrero, S., Gechev, T., Bakker, P.L., Moar, W.J., de Maagd, R.A., 2005. Bacillus thuringiensis Cry1Caresistant Spodoptera exigua lacks expression of one of four Aminopeptidase N genes. BMC Genomics 24, 6–96. Hua, G., Zhang, R., Abdullah, M.A., Adang, M.J., 2008. Anopheles gambiae cadherin AgCad1 binds the Cry4Ba toxin of Bacillus thuringiensis israelensis and a fragment of AgCad1 synergizes toxicity. Biochemistry 47, 5101–5110. Hua, G., Zhang, R., Bayyareddy, K., Adang, M.J., 2009. Anopheles gambiae alkaline phosphatase is a functional receptor of Bacillus thuringiensis jegathesan Cry11Ba toxin. Biochemistry 48, 9785–9793. Jiménez-Juárez, A., Muñoz-Garay, C., Gómez, I., Saab- Rincon, G., Damian-Alamazo, J.Y., Gill, S.S., Soberón, M., Bravo, A., 2007. Bacillus thuringiensis Cry1Ab mutants affecting oligomer formation are non-toxic to Manduca sexta larvae. J. Biol. Chem. 282, 21222–21229. Jurat-Fuentes, J.L., Adang, M.J., 2004. Characterization of a Cry1Ac-receptor alkaline phosphatase in susceptible and resistant Heliothis virescens larvae. Eur. J. Biochem. 271, 3127–3135. Ochoa-Campuzano, C., Real, M.D., Martiínez-Ramiírez, A.C., Bravo, A., Rausell, C., 2007. An ADAM metalloprotease is a Cry3Aa Bacillus thuringiensis toxin receptor. Biochem. Biophys. Res. Commun. 362, 437–442. Moellenbeck, D.J., Peters, M.L., Bing, J.W., Rouse, J.R., Higgins, L.S., Sims, L., Neveshmal, T., Marshall, L., Ellis, R.T., Bystrak, P.G., Lang, B.A., Stewart, J.L., Kouba, K., Sondag, V., Gustafson, V., Nour, K., Xu, D., Swenson, J., Zhang, J., Czpala, T., Schwab, G., Jayne, S., Dtorckhoff, B.A., Narva, K., Schnepf, H.E., Stelman, S.J., Poutre, C., Koziel, M., Duck, N., 2001. Insecticidal proteins from Bacillus thuringiensis protect corn from corn rootworms. Nat. Biotechnol. 19, 668–672. Park, Y., Abdullah, M.A., Taylor, M.D., Rahman, K., Adang, M.J., 2009. Enhancement of Bacillus thuringiensis Cry3Aa and Cry3Bb toxicities to coleopteran larvae by a toxin-binding fragment of an insect cadherin. Appl. Environ. Microbiol. 75, 3086–3092. Pérez, C., Fernandez, L.E., Sun, J., Folch, J.L., Gill, S.S., Soberón, M., Bravo, A., 2005. Bacillus thuringiensis subsp. israeliensis Cyt1Aa synergizes Cry11Aa toxin
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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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Page 295 and 296: Table 1 Comparative properties of s
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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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