Tomohiro Shima
University of Tokyo
12 Papers
12 Citations
Tomohiro Shima is an academic researcher from University of Tokyo. The author has contributed to research in topics: Dynein & Microtubule. The author has an hindex of 5, co-authored 12 publications. Previous affiliations of Tomohiro Shima include RIKEN Quantitative Biology Center.
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Papers
Small stepping motion of processive dynein revealed by load-free high-speed single-particle tracking.
Jun Ando,Jun Ando,Tomohiro Shima,Riko Kanazawa,Rieko Shimo-Kon,Akihiko Nakamura,Akihiko Nakamura,Mayuko Yamamoto,Takahide Kon,Ryota Iino,Ryota Iino +10 more
TL;DR: The results indicate dynein mainly moves with biased small stepping motion in which only backward steps are slightly suppressed, which is consistent with on- and off-axes pitches of binding cleft between αβ-tubulin dimers on the microtubule.
Second harmonic generation polarization microscopy as a tool for protein structure analysis
Junichi Kaneshiro,Yasushi Okada,Tomohiro Shima,Mika Tsujii,Katsumi Imada,Taro Ichimura,Taro Ichimura,Tomonobu M. Watanabe +7 more
TL;DR: It is demonstrated that a conformational change as well as its dynamics in protein macromolecular assemblies can be detected by means of SHG polarization measurement, and the potential of this method for protein structure analysis in physiological solutions at room temperature without any labeling is illustrated.
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Real-time observation of flexible domain movements in Cas9
Saki Osuka,Kazushi Isomura,Shohei Kajimoto,Tomotaka Komori,Hiroshi Nishimasu,Tomohiro Shima,Osamu Nureki,Sotaro Uemura +7 more
TL;DR: This work directly observed dynamic fluctuations of multiple Cas9 domains, using single-molecule FRET, and revealed the conformational flexibility of apo-Cas9, which may play a role in the assembly with the sgRNA.
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How Cytoplasmic Dynein Couples ATP Hydrolysis Cycle to Diverse Stepping Motions: Kinetic Modeling
TL;DR: The model reproduced key experimental motility-related properties, including velocity and run length, as functions of the ATP concentration and external force, therefore providing a plausible explanation of how dynein achieves various stepping manners with explicit characterization of nucleotide states.
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Second harmonic generation polarization microscopy as a tool for protein structure analysis
Junichi Kaneshiro,Yasushi Okada,Tomohiro Shima,Mika Tsujii,Katsumi Imada,Taro Ichimura,Taro Ichimura,Tomonobu M. Watanabe +7 more
TL;DR: Polarization measurement for second-harmonic generation is reported for the detection of protein conformational changes in solutions of macromolecular protein assemblies such as microtubules and protein crystals.