Satoshi Arai

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In various cellular membrane systems, vacuolar ATPases (V-ATPases) function as proton pumps, which are involved in many processes such as bone resorption and cancer metastasis, and these membrane proteins represent attractive drug targets for osteoporosis and cancer. The hydrophilic V(1) portion is known as a rotary motor, in which a central axis DF complex(More)
V-ATPases function as ATP-dependent ion pumps in various membrane systems of living organisms. ATP hydrolysis causes rotation of the central rotor complex, which is composed of the central axis D subunit and a membrane c ring that are connected by F and d subunits. Here we determined the crystal structure of the DF complex of the prokaryotic V-ATPase of(More)
Static analysis tools such as bug pattern tools are useful to detect bugs early in software development. However, existing tools sometimes yield so many warnings that developers tend to ignore such warnings. To deal with this problem, we propose a gamified tool for motivating developers to remove such warnings. Our tool employs the gamification technique(More)
Existing AOP tools, typified by AspectJ, are proposed as extensions of a single language. Therefore, most existing AOP tools cannot deal with cross-cutting concerns, which are scattered on many modules implemented in two or more languages. We propose a novel language-independent AOP framework named UniAspect. UniAspect translates programs written in various(More)
Vacuolar ATPases (V-ATPases) function as proton pumps in various cellular membrane systems. The hydrophilic V1 portion of the V-ATPase is a rotary motor, in which a central-axis DF complex rotates inside a hexagonally arranged catalytic A3B3 complex by using ATP hydrolysis energy. We have previously reported crystal structures of Enterococcushirae V-ATPase(More)
Vacuolar ATPase (V-ATPase) of Enterococcus hirae is composed of a soluble functional domain V1 (A3B3DF) and an integral membrane domain Vo (ac), where V1 and Vo domains are connected by a central stalk, composed of D-, F-, and d-subunits; and two peripheral stalks (E- and G-subunits). We identified 120 interacting residues of A3B3 heterohexamer with(More)
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