Zobrazeno 1 - 10
of 78
pro vyhledávání: '"Tomoko Masaike"'
Autor:
Yuh Hasimoto, Mitsuhiro Sugawa, Yoshihiro Nishiguchi, Fumihiro Aeba, Ayari Tagawa, Kenta Suga, Nobukiyo Tanaka, Hiroshi Ueno, Hiroki Yamashita, Ryuichi Yokota, Tomoko Masaike, Takayuki Nishizaka
Publikováno v:
Biophysical Journal. 122:554-564
Autor:
Yuh, Hasimoto, Mitsuhiro, Sugawa, Yoshihiro, Nishiguchi, Fumihiro, Aeba, Ayari, Tagawa, Kenta, Suga, Nobukiyo, Tanaka, Hiroshi, Ueno, Hiroki, Yamashita, Ryuichi, Yokota, Tomoko, Masaike, Takayuki, Nishizaka
Publikováno v:
Biophysical journal.
F
Autor:
Daisuke Nakane, Toshihito Iwase, Nariya Uchida, Tomoko Masaike, Koji Ikegami, Takanobu A. Katoh, Mitsutoshi Setou, Takayuki Nishizaka
Publikováno v:
Scientific Reports, Vol 8, Iss 1, Pp 1-9 (2018)
Scientific Reports
Scientific Reports
To study the properties of tracheal cilia beating under various conditions, we developed a method to monitor the movement of the ciliary tip. One end of a demembranated cilium was immobilized on the glass surface, while the other end was capped with
Autor:
Mitsuhiro Sugawa, Yoko Y. Toyoshima, Kei Saito, Keitaro Shibata, Fumihiko Fujii, Junichiro Yajima, Shin Yamaguchi, Tomoko Masaike, Nagisa Mikami, Takayuki Nishizaka
Publikováno v:
Biochemical and Biophysical Research Communications. 504:709-714
Single-molecule fluorescence polarization technique has been utilized to detect structural changes in biomolecules and intermolecular interactions. Here we developed a single-molecule fluorescence polarization measurement system, named circular orien
Autor:
Tomoko, MASAIKE
Publikováno v:
理大科学フォーラム. 34(5):30-35
Publikováno v:
Biophysical reviews. 11(4)
Motor proteins are molecular machines that convert chemical energy into mechanical work. In addition to existing studies performed on the linear motors found in eukaryotic cells, researchers in biophysics have also focused on rotary motors such as F(
Autor:
Kaoru A. Okada, Mitsuhiro Sugawa, Takayuki Nishizaka, Daisuke Nakane, Tomoko Masaike, Tatsuya Naito
Publikováno v:
Scientific Reports
Scientific Reports, Vol 9, Iss 1, Pp 1-9 (2019)
Scientific Reports, Vol 9, Iss 1, Pp 1-9 (2019)
F1-ATPase is a rotary motor protein in which the central γ-subunit rotates inside the cylinder made of α3β3 subunits. To investigate interactions between the γ shaft and the cylinder at the molecular scale, load was imposed on γ through a polyst
Autor:
Tomoko Masaike, Eiro Muneyuki, Tetsuaki Okamoto, Hiroshi Ueno, Shoichi Toyabe, Yusuke Naka, Yohsuke Kikuchi, Hidemitsu Osakabe
Publikováno v:
Biophysical Journal. 105:2541-2548
Rotation of the γ subunit of the F1-ATPase plays an essential role in energy transduction by F1-ATPase. Hydrolysis of an ATP molecule induces a 120° step rotation that consists of an 80° substep and 40° substep. ATP binding together with ADP rele
Autor:
Mitsutoshi Setou, Takanobu A. Katoh, Nariya Uchida, Takayuki Nishizaka, Koji Ikegami, Toshihito Iwase, Tomoko Masaike
Publikováno v:
Biophysical Journal. 110(3)
Highly coordinated dyneins generate asymmetric ciliary beating composed of clearly distinguished effective and recovery strokes. We herein aim to understand the mechanism of asymmetric beating of a single cilium by combining multiple optical-microsco
Publikováno v:
Biophysical Journal. 101(9):2201-2206
F(1)-ATPase is a water-soluble portion of F(o)F(1)-ATP synthase and rotary molecular motor that exhibits reversibility in chemical reactions. The rotational motion of the shaft subunit γ has been carefully scrutinized in previous studies, but a tilt