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Makoto Ihara

Researcher at Kindai University

Publications -  58
Citations -  1870

Makoto Ihara is an academic researcher from Kindai University. The author has contributed to research in topics: Nicotinic agonist & Neonicotinoid. The author has an hindex of 21, co-authored 53 publications receiving 1497 citations. Previous affiliations of Makoto Ihara include Tokyo University of Agriculture and Technology & Okayama University.

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Neonicotinoids Show Selective and Diverse Actions on Their Nicotinic Receptor Targets: Electrophysiology, Molecular Biology, and Receptor Modeling Studies

TL;DR: A rich diversity of neonicotinoid-nAChR interactions has been demonstrated using voltage-clamp electrophysiology, and Computational modeling of nA ChR-imidacloprid interaction has assisted in the interpretation of these results.
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Neonicotinoid Insecticides: Molecular Targets, Resistance, and Toxicity.

TL;DR: This work addresses the current understanding of neonicotinoid target site interactions, selectivity, and metabolism not only in pests but also in beneficial insects such as bees.
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Neonicotinoid insecticides display partial and super agonist actions on native insect nicotinic acetylcholine receptors.

TL;DR: Recordings of cholinergic neurons cultured from the central nervous system of 3rd instar Drosophila larvae indicate that super agonism results from more frequent openings at the largest conductance state observed, the first demonstration of ‘super’ agonist actions of an insecticide on native insect nAChRs.
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Crystal structures of Lymnaea stagnalis AChBP in complex with neonicotinoid insecticides imidacloprid and clothianidin

TL;DR: IMI showed higher binding affinity for Ls-AChBP than that of CTD, consistent with weaker CH–π interactions in the Ls, AChBP–CTD complex than in the MIMI–IMI complex and the lack of the nitro group-Gln55 hydrogen bond in CTD.
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Role in the selectivity of neonicotinoids of insect-specific basic residues in loop D of the nicotinic acetylcholine receptor agonist binding site.

TL;DR: The models indicate that the nitro group of imidacloprid interacts directly with the introduced basic residues at position 77, whereas those at position 79 either prevent or permit such interactions depending on their electrostatic properties, thereby explaining the observed functional changes resulting from site-directed mutagenesis.