Toyoyuki Ose
Hokkaido University
61 Papers
326 Citations
Toyoyuki Ose is an academic researcher from Hokkaido University. The author has contributed to research in topics: Biology & Protein domain. The author has an hindex of 17, co-authored 53 publications. Previous affiliations of Toyoyuki Ose include Kyushu University.
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Papers
Structure of the measles virus hemagglutinin bound to its cellular receptor SLAM
Takao Hashiguchi,Toyoyuki Ose,Marie Kubota,Nobuo Maita,Nobuo Maita,Jun Kamishikiryo,Katsumi Maenaka,Katsumi Maenaka,Yusuke Yanagi +8 more
TL;DR: In this paper, the head domain of the measles virus hemagglutinin (MV-H) was shown to attach to a β-sheet of the membrane-distal ectodomain of SLAM using the side of its β-propeller fold.
Insight into a natural Diels-Alder reaction from the structure of macrophomate synthase.
Toyoyuki Ose,Kenji Watanabe,Takashi Mie,Mamoru Honma,Hiromi Watanabe,Min Yao,Hideaki Oikawa,Isao Tanaka +7 more
TL;DR: The 1.70 Å resolution crystal structure of the natural Diels–Alderase, fungal macrophomate synthase (MPS), in complex with pyruvate is presented, and it is suggested that the reaction proceeds via a large-scale structural reorganization of the product.
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Structural analysis for glycolipid recognition by the C-type lectins Mincle and MCL.
Atsushi Furukawa,Jun Kamishikiryo,Daiki Mori,Kenji Toyonaga,Yuki Okabe,Aya Toji,R. Kanda,Yasunobu Miyake,Toyoyuki Ose,Sho Yamasaki,Katsumi Maenaka +10 more
TL;DR: In this article, the crystal structures of Mincle, MCL and the Mincle-citric acid complex were reported, showing that these receptors are capable of interacting with sugar in a Ca2+-dependent manner, as observed in other C-type lectins.
151
A Sialylated Voltage-Dependent Ca2+ Channel Binds Hemagglutinin and Mediates Influenza A Virus Entry into Mammalian Cells
Yoichiro Fujioka,Shin-ya Nishide,Toyoyuki Ose,Tadaki Suzuki,Izumi Kato,Hideo Fukuhara,Mari Fujioka,Kosui Horiuchi,Aya O. Satoh,Prabha Nepal,Sayaka Kashiwagi,Jing Wang,Mika Horiguchi,Yuko Sato,Sarad Paudel,Asuka Nanbo,Tadaaki Miyazaki,Hideki Hasegawa,Katsumi Maenaka,Yusuke Ohba,Yusuke Ohba +20 more
TL;DR: Cav1.2 is identified as a sialylated host cell surface receptor that binds HA and is critical for IAV entry and replication, and reintroduction of wild-type but not the glycosylation-deficient mutants of Cav1.
150
Interaction between a Domain of the Negative Regulator of the Ras-ERK Pathway, SPRED1 Protein, and the GTPase-activating Protein-related Domain of Neurofibromin Is Implicated in Legius Syndrome and Neurofibromatosis Type 1.
Yasuko Hirata,Hilde Brems,Mayu Suzuki,Mitsuhiro Kanamori,Masahiro Okada,Rimpei Morita,Isabel Llano-Rivas,Toyoyuki Ose,Ludwine Messiaen,Eric Legius,Akihiko Yoshimura +10 more
TL;DR: Data clearly demonstrate that SPRED1 inhibits the Ras-ERK pathway by recruiting neurofibromin to Ras through the EVH1-GRD interaction, and this study provides molecular basis for the pathogenic mutations of NF1 and Legius syndrome.
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