T
Takayuki Kato
Researcher at Osaka University
Publications - 107
Citations - 4347
Takayuki Kato is an academic researcher from Osaka University. The author has contributed to research in topics: Chemistry & ATP hydrolysis. The author has an hindex of 29, co-authored 98 publications receiving 3686 citations. Previous affiliations of Takayuki Kato include National Institute for Materials Science & Wayne State University.
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Journal ArticleDOI
Cooperation between mDia1 and ROCK in Rho-induced actin reorganization
TL;DR: It is shown that GTP-bound Rho activates its effector mDia1 by disrupting mDIA1’s intramolecular interactions, which may induce the formation of different actin structures affected by the balance between mDía1 and ROCK signalling.
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Coordination of microtubules and the actin cytoskeleton by the Rho effector mDia1.
Toshimasa Ishizaki,Yosuke Morishima,Muneo Okamoto,Tomoyuki Furuyashiki,Takayuki Kato,Shuh Narumiya +5 more
TL;DR: Results indicate that mDia1 may coordinate microtubules and F-actin through its FH2 and FH1 regions, respectively.
Journal ArticleDOI
Cdc42 and mDia3 regulate microtubule attachment to kinetochores
Shingo Yasuda,Fabian Oceguera-Yanez,Takayuki Kato,Takayuki Kato,Muneo Okamoto,Shigenobu Yonemura,Yasuhiko Terada,Toshimasa Ishizaki,Shuh Narumiya +8 more
TL;DR: Small GTPases of the Rho family regulate cell morphogenesis by organizing the actin cytoskeleton and regulating MT alignment and stabilization and it is shown that one member of this family, Cdc42, and its effector, mDia3, regulate MT attachment to kinetochores.
Journal ArticleDOI
Common architecture of the flagellar type III protein export apparatus and F- and V-type ATPases.
Tatsuya Ibuki,Katsumi Imada,Tohru Minamino,Tohru Minamino,Takayuki Kato,Tomoko Miyata,Keiichi Namba +6 more
TL;DR: It is shown that the structure of FliJ derived from Salmonella enterica serovar Typhimurium is remarkably similar to that of the two-stranded α-helical coiled-coil part of the γ subunit of FoF1-ATP synthase and thatFliJ promotes the formation of FloI hexamer rings by binding to the center of the ring.
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An infectivity-enhancing site on the SARS-CoV-2 spike protein targeted by antibodies
Yafei Liu,Wai Tuck Soh,Jun-ichi Kishikawa,Mika Hirose,Emi E. Nakayama,Songling Li,Miwa Sasai,Tatsuya Suzuki,Asa Tada,Akemi Arakawa,Sumiko Matsuoka,Kanako Akamatsu,Makoto Matsuda,Chikako Ono,Shiho Torii,Kazuki Kishida,Hui Jin,Wataru Nakai,Noriko Arase,Atsushi Nakagawa,Maki Matsumoto,Yukoh Nakazaki,Yasuhiro Shindo,Masako Kohyama,Keisuke Tomii,Koichiro Ohmura,Shiro Ohshima,Toru Okamoto,Masahiro Yamamoto,Hironori Nakagami,Yoshiharu Matsuura,Takayuki Kato,Masato Okada,Daron M. Standley,Tatsuo Shioda,Hisashi Arase +35 more
TL;DR: In this paper, a series of anti-spike monoclonal antibodies from coronavirus disease 2019 (COVID-19) patients were screened and found that some of the antibodies against the N-terminal domain induced the open conformation of RBD and thus enhanced the binding capacity of the spike protein to ACE2 and infectivity of SARS-CoV-2.