Publications by authors named "Takuya Muto"

Aim: We focused on the preparation and activities of clinics for spectators and athletes in the Izu Velodrome in Shizuoka Prefecture, which was managed by the Tokyo Organizing Committee of the Olympic and Paralympic Games (TOC).

Methods: Two medical clinics were established for the track cycling competition: one for Olympians and their associates, and one for spectators, TOC-related individuals, and volunteers. Each medical clinic had two separate buildings.

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Structural characterization of fully unfolded proteins is essential for understanding not only protein-folding mechanisms, but also the structures of intrinsically disordered proteins. Because an unfolded protein can assume all possible conformations, statistical descriptions of its structure are most appropriate. For this purpose, we applied Förster resonance energy transfer (FRET) analysis to fully unfolded staphylococcal nuclease.

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A new method for evaluating thrust with high-frequency variations beyond the resonant frequency using a disturbance observer is presented. Setpoint control is applied to a conventional pendulum-type thrust stand to keep the pendulum at the target position using a solenoid actuator. During control, pendulum acceleration and solenoid-actuator current are measured, and the disturbance observer determines thrust with a wide range of frequency variations.

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The plant stress hormone abscisic acid (ABA) is critical for several abiotic stress responses. ABA signaling is normally repressed by group-A protein phosphatases 2C (PP2Cs), but stress-induced ABA binds Arabidopsis PYR/PYL/RCAR (PYL) receptors, which then bind and inhibit PP2Cs. X-ray structures of several receptor-ABA complexes revealed a tunnel above ABA's 3' ring CH that opens at the PP2C binding interface.

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A novel chemical tool compound that is an antagonist of brassinolide (BL, 1)-induced rice lamina joint inclination was developed. Although 2-O-, 3-O-, 22-O-, or 23-O-methylation of BL causes a critical decrease in biological activity,(5) a crystal structure of the extracellular leucine-rich repeat (LRR) domain of BRASSINOSTEROID-INSENSITIVE I (BRI1) bound to BL(3,4) indicates that the loss of activity of the O-methylated BL may result from not only the low affinity to BRI1, but also from blocking the interaction with another BR signaling factor, a partner protein of BRI1 (e.g.

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