Zobrazeno 1 - 10
of 182
pro vyhledávání: '"Taro Q.P. Uyeda"'
Publikováno v:
Biophys Rev
Biophysics in Waseda University was started in 1965 as one of the three key research areas that constitute the Physics Department. In the biophysics group, one theoretical lab and two experimental labs are now working on the cutting-edge themes on bi
Autor:
Azuma Taoka, Tohru Minamino, Isil Tulum, Yoshiaki Kinosita, Kentaro Kato, Robert Robinson, Kazuo Inaba, Hirofumi Wada, Hiroyuki Mori, Seiji Kojima, Ken-ichi Wakabayashi, Shuichi Nakamura, Chikara Kaito, Masayoshi Nishiyama, Katsuya Shimabukuro, Shin Haruta, Koji Nakayama, Yosuke Tashiro, Shun ichi Fukushima, Masatada Tamakoshi, Yoshihiro Fukumori, Taro Q.P. Uyeda, Masahiro Ito, Tsuyoshi Kenri, Michio Homma, Satoshi Shibata, Daisuke Nakane, Makoto Miyata
Publikováno v:
Genes to Cells
Motility often plays a decisive role in the survival of species. Five systems of motility have been studied in depth: those propelled by bacterial flagella, eukaryotic actin polymerization and the eukaryotic motor proteins myosin, kinesin and dynein.
Autor:
Keitaro Shibata, Naoki Hosokawa, Taro Q.P. Uyeda, Kiyotaka Tokuraku, Atsuki Yoshino, Masahiro Kuragano
Publikováno v:
Biochemical and biophysical research communications. 552
Fimbrin forms bundles of parallel actin filaments in filopodia, but it remains unclear how fimbrin forms well-ordered bundles. To address this issue, we focused on the cooperative interaction between the actin-binding domain of fimbrin and actin fila
Publikováno v:
International Journal of Molecular Sciences, Vol 21, Iss 3209, p 3209 (2020)
International Journal of Molecular Sciences
International Journal of Molecular Sciences
A wide variety of uniquely localized actin-binding proteins (ABPs) are involved in various cellular activities, such as cytokinesis, migration, adhesion, morphogenesis, and intracellular transport. In a micrometer-scale space such as the inside of ce
Actin binding domain of Rng2 sparsely bound on F-actin strongly inhibits actin movement on myosin II
Autor:
Yuuki Hayakawa, Masak Takaine, Kien Xuan Ngo, Taiga Imai, Masafumi D. Yamada, Arash Badami Behjat, Kenichi Umeda, Keiko Hirose, Ayhan Yurtsever, Noriyuki Kodera, Kiyotaka Tokuraku, Osamu Numata, Takeshi Fukuma, Toshio Ando, Kentaro Nakano, Taro Q.P. Uyeda
Substoichiometric binding of certain actin-binding proteins induces conformational changes in a disproportionally large number of actin protomers in actin filaments. Here, we report a case in which such conformational changes in actin filaments have
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d20e9b24f576f8194dfdc137a6f24a30
https://doi.org/10.1101/2020.04.14.041046
https://doi.org/10.1101/2020.04.14.041046
Autor:
Jeongsu Ahn, Noriyuki Suetsugu, Akira Takano, Taro Q.P. Uyeda, Keiko Hirose, Kaoru Katoh, Sam-Geun Kong, Saku T. Kijima, Yuki Nakamura, Daisuke Kohda, Atsushi Shimada, Masamitsu Wada, Takeshi Higa
SUMMARYPlants have evolved unique responses to fluctuating light conditions in their environment. One such response, chloroplast photorelocation movement, optimizes photosynthesis under weak light and prevents photodamage under strong light. CHLOROPL
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ab5a3d697d8d5629bd4416de4b5168e7
https://doi.org/10.1101/2020.01.14.905984
https://doi.org/10.1101/2020.01.14.905984
Publikováno v:
Cytoskeleton. 74:482-489
Heavy meromyosin (HMM) forms clusters along actin filaments under low ATP concentrations. Here, we observed the growth of HMM clusters under low concentrations of ATP in real time using fluorescence microscopy. When actin filaments were loosely immob
Autor:
Maciej S. Lesniak, Bin Liu, Yu Cheng, Gustavo R. Plaza, Congyu Wu, Taro Q.P. Uyeda, Yu Han, Yajing Shen
Publikováno v:
Theranostics
Magnetic nanoparticles (MNPs) functionalized with targeting moieties can recognize specific cell components and induce mechanical actuation under magnetic field. Their size is adequate for reaching tumors and targeting cancer cells. However, due to t
Dynamin-Like Protein B of Dictyostelium Contributes to Cytokinesis Cooperatively with Other Dynamins
Autor:
Koushiro Fujimoto, Taro Q.P. Uyeda, Go Itoh, A. Y. K. Md. Masud Rana, Masatsune Tsujioka, Masahito Tanaka, Shin-ya Miyagishima, Md. Golam Sarowar Jahan, Shigehiko Yumura
Publikováno v:
Cells, Vol 8, Iss 8, p 781 (2019)
Cells
Volume 8
Issue 8
Cells
Volume 8
Issue 8
Dynamin is a large GTPase responsible for diverse cellular processes, such as endocytosis, division of organelles, and cytokinesis. The social amoebozoan, Dictyostelium discoideum, has five dynamin-like proteins: dymA, dymB, dlpA, dlpB, and dlpC. Dym
Publikováno v:
Biophysics and Physicobiology. 13:321-331
Conflicts of Interest All the authors declare that they have no conflict of interest. Author Contributions K. S. and T. U. conceived and planned the experiments. K. S., A. N. and T. U. performed the experiments. K. S. analyzed the data. K. S., A. N.,