Delayed Toxicity of Two Chitinolytic Enzyme Inhibitors (Psammaplin A and Pentoxifylline) Against Eastern Subterranean Termites (Isoptera: Rhinotermitidae)
暂无分享,去创建一个
[1] G. Henderson,et al. Toxicity of Seven Termiticides on the Formosan and Eastern Subterranean Termites , 2011, Journal of economic entomology.
[2] S. Muthukrishnan,et al. Insect chitinase and chitinase-like proteins , 2009, Cellular and Molecular Life Sciences.
[3] J. Lewis. Transfer efficiency by the subterranean termite Reticulitermes flavipes (Isoptera: Rhinotermitidae) of food-borne bait formulations containing benzoylphenyl urea chitin synthesis inhibitor , 2008 .
[4] B. Sangwan-Norreel,et al. Differential aphicidal effects of chitinase inhibitors on the polyphagous homopteran Myzus persicae (Sulzer). , 2006, Pest management science.
[5] S. Kamble,et al. A characterization of subterranean termites in nebraska using micro-morphological and molecular techniques , 2006 .
[6] D. V. van Aalten,et al. Methylxanthine drugs are chitinase inhibitors: investigation of inhibition and binding modes. , 2005, Chemistry & biology.
[7] S. Ōmura,et al. Specificity and affinity of natural product cyclopentapeptide inhibitors against A. fumigatus, human, and bacterial chitinases. , 2004, Chemistry & biology.
[8] B. Sipes,et al. Control of the big-headed ant, Pheidole megacephala (Hemonoptera: Formicidae) in pineapple cultivation using Amdro in bait stations , 2005 .
[9] J. King,et al. Comparative laboratory efficacy of noviflumuron and diflubenzuron on Reticulitermes flavipes (Isoptera: Rhinotermitidae) , 2005 .
[10] W. Bridges,et al. Temperature effect on survival and cellulose consumption of noviflumuron- or hexaflumuron-fed Reticulitermes flavipes (Isoptera: Rhinotermitidae) , 2005 .
[11] S. Ōmura,et al. High-resolution structures of a chitinase complexed with natural product cyclopentapeptide inhibitors: Mimicry of carbohydrate substrate , 2002, Proceedings of the National Academy of Sciences of the United States of America.
[12] B. Synstad,et al. Psammaplin A, a chitinase inhibitor isolated from the Fijian marine sponge Aplysinella rhax. , 2002, Bioorganic & medicinal chemistry.
[13] Rebecca D. Vahabzadeh. Effects of four chitin synthesis inhibitors on feeding and mortality of the Eastern subterranean termite, Reticulitermes flavipes Kollar (Isoptera:Rhinotermitidae) , 2002 .
[14] N. Su. Novel technologies for subterranean termite control , 2002 .
[15] Satoshi Omura,et al. Argadin, a new chitinase inhibitor, produced by Clonostachys sp. FO-7314. , 2000, Chemical & pharmaceutical bulletin.
[16] J. Dripps,et al. Kinetics of Uptake, Clearance, Transfer, and Metabolism of Hexaflumuron by Eastern Subterranean Termites (Isoptera: Rhinotermitidae) , 2000, Journal of economic entomology.
[17] E. Vargo,et al. Polymorphism at trinucleotide microsatellite loci in the subterranean termite Reticulitermes flavipes , 2000, Molecular ecology.
[18] S. Ōmura,et al. Structure of argifin, a new chitinase inhibitor produced by Gliocladium sp. , 2000 .
[19] K. Kramer,et al. Insect chitinases: molecular biology and potential use as biopesticides. , 1997, Insect biochemistry and molecular biology.
[20] M. Spindler-Barth,et al. Synthesis and Biological Activity of Allosamidin and Allosamidin Analogues , 1997 .
[21] M. Lennartz,et al. Characterization and Inhibitor Studies of Chitinases from a Parasitic Blowfly (Lucilia cuprina), a Tick (Boophilus microplus), an Intestinal Nematode (Haemonchus contortus) and a Bean (Phaseolus vulgaris) , 1996 .
[22] D. L. Dindal. Soil biology guide , 1990 .
[23] W. S. Abbott,et al. A method of computing the effectiveness of an insecticide. 1925. , 1925, Journal of the American Mosquito Control Association.
[24] M. Lenz,et al. Influence of container, matrix volume and group size on survival and feeding activity in species of Coptotermes and Nasutitermes (Isoptera: Rhinotermitidae, Termitidae). , 1980 .
[25] J. Breznak,et al. Heterotrophic bacteria present in hindguts of wood-eating termites [Reticulitermes flavipes (Kollar)] , 1978, Applied and environmental microbiology.