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Loops D, E and G in the Drosophila Dα1 subunit contribute to high neonicotinoid sensitivity of Dα1‐chicken β2 nicotinic acetylcholine receptor
Author(s) -
Ihara Makoto,
Hikida Mai,
Matsushita Hiroyuki,
Yamanaka Kyosuke,
Kishimoto Yuya,
Kubo Kazuki,
Watanabe Shun,
Sakamoto Mifumi,
Matsui Koutaro,
Yamaguchi Akihiro,
Okuhara Daiki,
Furutani Shogo,
Sattelle David B,
Matsuda Kazuhiko
Publication year - 2018
Publication title -
british journal of pharmacology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.432
H-Index - 211
eISSN - 1476-5381
pISSN - 0007-1188
DOI - 10.1111/bph.13914
Subject(s) - thiacloprid , neonicotinoid , nicotinic acetylcholine receptor , imidacloprid , nicotinic agonist , protein subunit , receptor , acetylcholine receptor , agonist , biology , pharmacology , chemistry , biochemistry , thiamethoxam , pesticide , gene , agronomy
Neonicotinoid insecticides interact with the orthosteric site formed at subunit interfaces of insect nicotinic ACh (nACh) receptors. However, their interactions with the orthosteric sites at α-non α and α-α subunit interfaces remain poorly understood. The aim of this study was to elucidate the mechanism of neonicotinoid actions using the Drosophila Dα1-chicken β2 hybrid nACh receptor.