A. Ishijima

Direct measurement of stiffness of single actin filaments with and without tropomyosin by in vitro nanomanipulation.

Kojima, H, Ishijima, A, Yanagida, T

In order to explain the molecular mechanism of muscle contraction, it is crucial to know the distribution of the sarcomere compliance of active muscle. Here, we directly measure the stiffness of...

Charge-reversion mutagenesis of Dictyostelium actin to map the surface recognized by myosin during ATP-driven sliding motion.

Johara, M, Toyoshima, Y Y, Ishijima, A, Kojima, H, Yanagida, T, Sutoh, K

Amino acid residues D24/D25, E99/E100, E360/E361, and D363/E364 in subdomain 1 of Dictyostelium actin were replaced with histidine residues by site-directed mutagenesis. Mutant actins were expressed...

Multiple- and single-molecule analysis of the actomyosin motor by nanometer-piconewton manipulation with a microneedle: unitary steps and forces.

Ishijima, A, Kojima, H, Higuchi, H, Harada, Y, Funatsu, T, Yanagida, T

We have developed a new technique for measurements of piconewton forces and nanometer displacements in the millisecond time range caused by actin-myosin interaction in vitro by manipulating single...

Forces and steps generated by single myosin molecules.

Yanagida, T, Ishijima, A

Orientation dependence of displacements by a single one-headed myosin relative to the actin filament.

Tanaka, H, Ishijima, A, Honda, M, Saito, K, Yanagida, T

Displacements of single one-headed myosin molecules in a sparse myosin-rod cofilament were measured from bead displacements at various angles relative to an actin filament by dual optical trapping...

Direct measurement of stiffness of single actin filaments with and without tropomyosin by in vitro nanomanipulation.

Kojima, H, Ishijima, A, Yanagida, T

In order to explain the molecular mechanism of muscle contraction, it is crucial to know the distribution of the sarcomere compliance of active muscle. Here, we directly measure the stiffness of...

Charge-reversion mutagenesis of Dictyostelium actin to map the surface recognized by myosin during ATP-driven sliding motion.

Johara, M, Toyoshima, Y Y, Ishijima, A, Kojima, H, Yanagida, T, Sutoh, K

Amino acid residues D24/D25, E99/E100, E360/E361, and D363/E364 in subdomain 1 of Dictyostelium actin were replaced with histidine residues by site-directed mutagenesis. Mutant actins were expressed...

Multiple- and single-molecule analysis of the actomyosin motor by nanometer-piconewton manipulation with a microneedle: unitary steps and forces.

Ishijima, A, Kojima, H, Higuchi, H, Harada, Y, Funatsu, T, Yanagida, T

We have developed a new technique for measurements of piconewton forces and nanometer displacements in the millisecond time range caused by actin-myosin interaction in vitro by manipulating single...

Forces and steps generated by single myosin molecules.

Yanagida, T, Ishijima, A

Orientation dependence of displacements by a single one-headed myosin relative to the actin filament.

Tanaka, H, Ishijima, A, Honda, M, Saito, K, Yanagida, T

Displacements of single one-headed myosin molecules in a sparse myosin-rod cofilament were measured from bead displacements at various angles relative to an actin filament by dual optical trapping...

Single-motor mechanics and models of the myosin motor.

Yanagida, T, Esaki, S, Iwane, A H, Inoue, Y, Ishijima, A, Kitamura, K, ...

Recent progress in single-molecule detection techniques is remarkable. These techniques have allowed the accurate determination of myosin-head-induced displacements and how mechanical cycles are...