T
Toshio Shono
Researcher at University of Tsukuba
Publications - 74
Citations - 2173
Toshio Shono is an academic researcher from University of Tsukuba. The author has contributed to research in topics: Housefly & Permethrin. The author has an hindex of 26, co-authored 74 publications receiving 2066 citations. Previous affiliations of Toshio Shono include Cornell University & National Institutes of Health.
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Journal ArticleDOI
Mechanisms of Pyrethroid Resistance in the Dengue Mosquito Vector, Aedes aegypti: Target Site Insensitivity, Penetration, and Metabolism
Shinji Kasai,Osamu Komagata,Kentaro Itokawa,Toshio Shono,Lee Ching Ng,Mutsuo Kobayashi,Takashi Tomita +6 more
TL;DR: In vivo metabolism studies showed that the SP strain excreted permethrin metabolites more rapidly than a susceptible SMK strain, and in vitro metabolism studies indicated an association of P450s with resistance, suggesting that cytochrome P450 monooxygenases (P450s) play an important role in resistance development.
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Spinosad resistance in the housefly, Musca domestica, is due to a recessive factor on autosome 1
Toshio Shono,Jeffrey G. Scott +1 more
TL;DR: Results suggest spinosad resistance in the housefly is due to a unique resistance mechanism that cannot be overcome with the insecticide synergists piperonyl butoxide, S, S , S -tributylphosphorotrithioate nor diethyl maleate.
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Indoxacarb resistance in the house fly, Musca domestica
TL;DR: Indoxacarb resistance in the NYINDR strain was inherited primarily as a completely recessive trait, and only limited levels of cross-resistance were detected to pyrethroid, organophosphate, carbamate or chlorinated hydrocarbon insecticides in NYInDR.
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Fenitroxon insensitive acetylcholinesterases of the housefly, Musca domestica associated with point mutations.
TL;DR: The cDNA of AChE in the housefly, Musca domestica, was sequenced and individual flies were genotyped by this gene in an inhibition assay of A ChE activity with an organophaspate, fenitroxon, and mutations at Gly and Tyr were associated with the insensitivity.
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Molecular cloning, nucleotide sequence and gene expression of a cytochrome P450 (CYP6F1) from the pyrethroid-resistant mosquito, Culex quinquefasciatus Say.
TL;DR: The deduced amino acid of CYP6F1 showed that it has conserved domains of a membrane-anchoring signal, reductase binding sites, a heme-binding site, ETLR motif and substrate recognition sites in P450s, which is strongly related to CyP6D1 involved in pyrethroid detoxification.