A
Akito Maeda
Researcher at Osaka University
Publications - 55
Citations - 5756
Akito Maeda is an academic researcher from Osaka University. The author has contributed to research in topics: Tyrosine phosphorylation & Muscarinic acetylcholine receptor. The author has an hindex of 26, co-authored 55 publications receiving 5591 citations. Previous affiliations of Akito Maeda include Boehringer Ingelheim & Kyoto University.
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Journal ArticleDOI
Cloning, sequencing and expression of complementary DNA encoding the muscarinic acetylcholine receptor
Tai Kubo,Kazuhiko Fukuda,Atsushi Mikami,Akito Maeda,Hideo Takahashi,Masayoshi Mishina,Tatsuya Haga,Kazuko Haga,Arata Ichiyama,Kenji Kangawa,Masayasu Kojima,Hisayuki Matsuo,Tadaaki Hirose,Shosaku Numa +13 more
TL;DR: Cloning and sequence analysis of DNA complementary to porcine cerebral messenger RNA encoding the muscarinic acetylcholine receptor predict the complete amino-acid sequence of this protein.
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PD-1 immunoreceptor inhibits B cell receptor-mediated signaling by recruiting src homology 2-domain-containing tyrosine phosphatase 2 to phosphotyrosine
TL;DR: Results show that PD-1 can inhibit B CR signaling by recruiting SHP-2 to its phosphotyrosine and dephosphorylating key signal transducers of BCR signaling.
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RAPL, a Rap1-binding molecule that mediates Rap1-induced adhesion through spatial regulation of LFA-1.
TL;DR: Human RAPL stimulated lymphocyte polarization and the patch-like redistribution of lymphocyte-function-associated antigen 1 (LFA-1) to the leading edge, resulting in enhanced adhesion to intercellular adhesion molecule 1 (ICAM-1).
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Molecular and Functional Characterization of a Novel Mouse Transient Receptor Potential Protein Homologue TRP7 Ca2+-PERMEABLE CATION CHANNEL THAT IS CONSTITUTIVELY ACTIVATED AND ENHANCED BY STIMULATION OF G PROTEIN-COUPLED RECEPTOR
Takaharu Okada,Ryuji Inoue,Kazuto Yamazaki,Akito Maeda,Tomohiro Kurosaki,Tohru Yamakuni,Isao Tanaka,Shunichi Shimizu,Kazuhiro Ikenaka,Keiji Imoto,Yasuo Mori +10 more
TL;DR: These findings reveal an interesting correspondence of TRP7 to the background and receptor stimulation-induced cation currents in various native systems and suggest that the TRP6 channel is a new member of diacylglycerol-activated cation channels.
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Encoding of Ca2+ signals by differential expression of IP3 receptor subtypes
TL;DR: It is demonstrated that differential expression of IP3R subtypes helps to encode IP3‐mediated Ca2+ signalling, and for the first time functional interactions between coexpressed subtypes are shown.