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Your search keyword '"Kimura, Kanako Terakado"' showing total 12 results
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12 results on '"Kimura, Kanako Terakado"'

2. Virological characteristics of the SARS-CoV-2 Omicron XBB.1.5 variant

Author

Tamura, Tomokazu, Irie, Takashi, Deguchi, Sayaka, Yajima, Hisano, Tsuda, Masumi, Nasser, Hesham, Mizuma, Keita, Plianchaisuk, Arnon, Suzuki, Saori, Uriu, Keiya, Begum, Mst Monira, Shimizu, Ryo, Jonathan, Michael, Suzuki, Rigel, Kondo, Takashi, Ito, Hayato, Kamiyama, Akifumi, Yoshimatsu, Kumiko, Shofa, Maya, Hashimoto, Rina, Anraku, Yuki, Kimura, Kanako Terakado, Kita, Shunsuke, Sasaki, Jiei, Sasaki-Tabata, Kaori, Maenaka, Katsumi, Nao, Naganori, Wang, Lei, Oda, Yoshitaka, Ikeda, Terumasa, Saito, Akatsuki, Matsuno, Keita, Ito, Jumpei, Tanaka, Shinya, Sato, Kei, Hashiguchi, Takao, Takayama, Kazuo, and Fukuhara, Takasuke

Published
2024
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3. Convergent evolution of SARS-CoV-2 Omicron subvariants leading to the emergence of BQ.1.1 variant

Author

Ito, Jumpei, Suzuki, Rigel, Uriu, Keiya, Itakura, Yukari, Zahradnik, Jiri, Kimura, Kanako Terakado, Deguchi, Sayaka, Wang, Lei, Lytras, Spyros, Tamura, Tomokazu, Kida, Izumi, Nasser, Hesham, Shofa, Maya, Begum, Mst Monira, Tsuda, Masumi, Oda, Yoshitaka, Suzuki, Tateki, Sasaki, Jiei, Sasaki-Tabata, Kaori, Fujita, Shigeru, Yoshimatsu, Kumiko, Ito, Hayato, Nao, Naganori, Asakura, Hiroyuki, Nagashima, Mami, Sadamasu, Kenji, Yoshimura, Kazuhisa, Yamamoto, Yuki, Nagamoto, Tetsuharu, Kuramochi, Jin, Schreiber, Gideon, Saito, Akatsuki, Matsuno, Keita, Takayama, Kazuo, Hashiguchi, Takao, Tanaka, Shinya, Fukuhara, Takasuke, Ikeda, Terumasa, and Sato, Kei

Published
2023
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4. Structure of the bile acid transporter and HBV receptor NTCP

Author

Asami, Jinta, Kimura, Kanako Terakado, Fujita-Fujiharu, Yoko, Ishida, Hanako, Zhang, Zhikuan, Nomura, Yayoi, Liu, Kehong, Uemura, Tomoko, Sato, Yumi, Ono, Masatsugu, Yamamoto, Masaki, Noda, Takeshi, Shigematsu, Hideki, Drew, David, Iwata, So, Shimizu, Toshiyuki, Nomura, Norimichi, and Ohto, Umeharu

Published
2022
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6. Virological characteristics of the SARS-CoV-2 Omicron XBB.1.5 variant

Author

50632098, 10759509, Tamura, Tomokazu, Irie, Takashi, Deguchi, Sayaka, Yajima, Hisano, Tsuda, Masumi, Nasser, Hesham, Mizuma, Keita, Plianchaisuk, Arnon, Suzuki, Saori, Uriu, Keiya, Begum, Mst Monira, Shimizu, Ryo, Jonathan, Michael, Suzuki, Rigel, Kondo, Takashi, Ito, Hayato, Kamiyama, Akifumi, Yoshimatsu, Kumiko, Shofa, Maya, Hashimoto, Rina, Anraku, Yuki, Kimura, Kanako Terakado, Kita, Shunsuke, Sasaki, Jiei, Sasaki-Tabata, Kaori, Maenaka, Katsumi, Nao, Naganori, Wang, Lei, Oda, Yoshitaka, The Genotype to Phenotype Japan (G2P-Japan) Consortium, Ikeda, Terumasa, Saito, Akatsuki, Matsuno, Keita, Ito, Jumpei, Tanaka, Shinya, Sato, Kei, Hashiguchi, Takao, Takayama, Kazuo, Fukuhara, Takasuke, 50632098, 10759509, Tamura, Tomokazu, Irie, Takashi, Deguchi, Sayaka, Yajima, Hisano, Tsuda, Masumi, Nasser, Hesham, Mizuma, Keita, Plianchaisuk, Arnon, Suzuki, Saori, Uriu, Keiya, Begum, Mst Monira, Shimizu, Ryo, Jonathan, Michael, Suzuki, Rigel, Kondo, Takashi, Ito, Hayato, Kamiyama, Akifumi, Yoshimatsu, Kumiko, Shofa, Maya, Hashimoto, Rina, Anraku, Yuki, Kimura, Kanako Terakado, Kita, Shunsuke, Sasaki, Jiei, Sasaki-Tabata, Kaori, Maenaka, Katsumi, Nao, Naganori, Wang, Lei, Oda, Yoshitaka, The Genotype to Phenotype Japan (G2P-Japan) Consortium, Ikeda, Terumasa, Saito, Akatsuki, Matsuno, Keita, Ito, Jumpei, Tanaka, Shinya, Sato, Kei, Hashiguchi, Takao, Takayama, Kazuo, and Fukuhara, Takasuke

Abstract

Circulation of SARS-CoV-2 Omicron XBB has resulted in the emergence of XBB.1.5, a new Variant of Interest. Our phylogenetic analysis suggests that XBB.1.5 evolved from XBB.1 by acquiring the S486P spike (S) mutation, subsequent to the acquisition of a nonsense mutation in ORF8. Neutralization assays showed similar abilities of immune escape between XBB.1.5 and XBB.1. We determine the structural basis for the interaction between human ACE2 and the S protein of XBB.1.5, showing similar overall structures between the S proteins of XBB.1 and XBB.1.5. We provide the intrinsic pathogenicity of XBB.1 and XBB.1.5 in hamsters. Importantly, we find that the ORF8 nonsense mutation of XBB.1.5 resulted in impairment of MHC suppression. In vivo experiments using recombinant viruses reveal that the XBB.1.5 mutations are involved with reduced virulence of XBB.1.5. Together, our study identifies the two viral functions defined the difference between XBB.1 and XBB.1.5.

Published
2024

7. Crystal Structures of Human Orexin 2 Receptor Bound to the Subtype-Selective Antagonist EMPA

Author

Suno, Ryoji, Kimura, Kanako Terakado, Nakane, Takanori, Yamashita, Keitaro, Wang, Junmei, Fujiwara, Takaaki, Yamanaka, Yasuaki, Im, Dohyun, Horita, Shoichiro, Tsujimoto, Hirokazu, Tawaramoto, Maki S., Hirokawa, Takatsugu, Nango, Eriko, Tono, Kensuke, Kameshima, Takashi, Hatsui, Takaki, Joti, Yasumasa, Yabashi, Makina, Shimamoto, Keiko, Yamamoto, Masaki, Rosenbaum, Daniel M., Iwata, So, Shimamura, Tatsuro, and Kobayashi, Takuya

Published
2018
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10. Convergent evolution of SARS-CoV-2 Omicron subvariants leading to the emergence of BQ.1.1 variant

Author

80833334, 10759509, 50632098, Ito, Jumpei, Suzuki, Rigel, Uriu, Keiya, Itakura, Yukari, Zahradnik, Jiri, Kimura, Kanako Terakado, Deguchi, Sayaka, Wang, Lei, Lytras, Spyros, Tamura, Tomokazu, Kida, Izumi, Nasser, Hesham, Shofa, Maya, Begum, Mst Monira, Tsuda, Masumi, Oda, Yoshitaka, Suzuki, Tateki, Sasaki, Jiei, Sasaki-Tabata, Kaori, Fujita, Shigeru, Yoshimatsu, Kumiko, Ito, Hayato, Nao, Naganori, Asakura, Hiroyuki, Nagashima, Mami, Sadamasu, Kenji, Yoshimura, Kazuhisa, Yamamoto, Yuki, Nagamoto, Tetsuharu, Kuramochi, Jin, Schreiber, Gideon, The Genotype to Phenotype Japan (G2P-Japan) Consortium, Saito, Akatsuki, Matsuno, Keita, Takayama, Kazuo, Hashiguchi, Takao, Tanaka, Shinya, Fukuhara, Takasuke, Ikeda, Terumasa, Sato, Kei, 80833334, 10759509, 50632098, Ito, Jumpei, Suzuki, Rigel, Uriu, Keiya, Itakura, Yukari, Zahradnik, Jiri, Kimura, Kanako Terakado, Deguchi, Sayaka, Wang, Lei, Lytras, Spyros, Tamura, Tomokazu, Kida, Izumi, Nasser, Hesham, Shofa, Maya, Begum, Mst Monira, Tsuda, Masumi, Oda, Yoshitaka, Suzuki, Tateki, Sasaki, Jiei, Sasaki-Tabata, Kaori, Fujita, Shigeru, Yoshimatsu, Kumiko, Ito, Hayato, Nao, Naganori, Asakura, Hiroyuki, Nagashima, Mami, Sadamasu, Kenji, Yoshimura, Kazuhisa, Yamamoto, Yuki, Nagamoto, Tetsuharu, Kuramochi, Jin, Schreiber, Gideon, The Genotype to Phenotype Japan (G2P-Japan) Consortium, Saito, Akatsuki, Matsuno, Keita, Takayama, Kazuo, Hashiguchi, Takao, Tanaka, Shinya, Fukuhara, Takasuke, Ikeda, Terumasa, and Sato, Kei

Abstract

In late 2022, various Omicron subvariants emerged and cocirculated worldwide. These variants convergently acquired amino acid substitutions at critical residues in the spike protein, including residues R346, K444, L452, N460, and F486. Here, we characterize the convergent evolution of Omicron subvariants and the properties of one recent lineage of concern, BQ.1.1. Our phylogenetic analysis suggests that these five substitutions are recurrently acquired, particularly in younger Omicron lineages. Epidemic dynamics modelling suggests that the five substitutions increase viral fitness, and a large proportion of the fitness variation within Omicron lineages can be explained by these substitutions. Compared to BA.5, BQ.1.1 evades breakthrough BA.2 and BA.5 infection sera more efficiently, as demonstrated by neutralization assays. The pathogenicity of BQ.1.1 in hamsters is lower than that of BA.5. Our multiscale investigations illuminate the evolutionary rules governing the convergent evolution for known Omicron lineages as of 2022.

Published
2023

11. Virological characteristics of the SARS-CoV-2 Omicron BA.2 subvariants, including BA.4 and BA.5

Author

Kimura, Izumi, primary, Yamasoba, Daichi, additional, Tamura, Tomokazu, additional, Nao, Naganori, additional, Suzuki, Tateki, additional, Oda, Yoshitaka, additional, Mitoma, Shuya, additional, Ito, Jumpei, additional, Nasser, Hesham, additional, Zahradnik, Jiri, additional, Uriu, Keiya, additional, Fujita, Shigeru, additional, Kosugi, Yusuke, additional, Wang, Lei, additional, Tsuda, Masumi, additional, Kishimoto, Mai, additional, Ito, Hayato, additional, Suzuki, Rigel, additional, Shimizu, Ryo, additional, Begum, MST Monira, additional, Yoshimatsu, Kumiko, additional, Kimura, Kanako Terakado, additional, Sasaki, Jiei, additional, Sasaki-Tabata, Kaori, additional, Yamamoto, Yuki, additional, Nagamoto, Tetsuharu, additional, Kanamune, Jun, additional, Kobiyama, Kouji, additional, Asakura, Hiroyuki, additional, Nagashima, Mami, additional, Sadamasu, Kenji, additional, Yoshimura, Kazuhisa, additional, Shirakawa, Kotaro, additional, Takaori-Kondo, Akifumi, additional, Kuramochi, Jin, additional, Schreiber, Gideon, additional, Ishii, Ken J., additional, Hashiguchi, Takao, additional, Ikeda, Terumasa, additional, Saito, Akatsuki, additional, Fukuhara, Takasuke, additional, Tanaka, Shinya, additional, Matsuno, Keita, additional, and Sato, Kei, additional

Published
2022
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12. Structures of the 5-HT2Areceptor in complex with the antipsychotics risperidone and zotepine

Author

Kimura, Kanako Terakado, Asada, Hidetsugu, Inoue, Asuka, Kadji, Francois Marie Ngako, Im, Dohyun, Mori, Chihiro, Arakawa, Takatoshi, Hirata, Kunio, Nomura, Yayoi, Nomura, Norimichi, Aoki, Junken, Iwata, So, and Shimamura, Tatsuro

Abstract

Many drugs target the serotonin 2A receptor (5-HT2AR), including second-generation antipsychotics that also target the dopamine D2receptor (D2R). These drugs often produce severe side effects due to non-selective binding to other aminergic receptors. Here, we report the structures of human 5-HT2AR in complex with the second-generation antipsychotics risperidone and zotepine. These antipsychotics effectively stabilize the inactive conformation by forming direct contacts with the residues at the bottom of the ligand-binding pocket, the movements of which are important for receptor activation. 5-HT2AR is structurally similar to 5-HT2CR but possesses a unique side-extended cavity near the orthosteric binding site. A docking study and mutagenic studies suggest that a highly 5-HT2AR-selective antagonist binds the side-extended cavity. The conformation of the ligand-binding pocket in 5-HT2AR significantly differs around extracellular loops 1 and 2 from that in D2R. These findings are beneficial for the rational design of safer antipsychotics and 5-HT2AR-selective drugs.

Published
2019
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