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Phosphate enhances myosin-powered actin filament velocity under acidic conditions in a motility assay.
Mechanical coupling between myosin molecules causes differences between ensemble and single-molecule measurements.
The effects of phosphate and acidosis on regulated thin-filament velocity in an in vitro motility assay.
Slip sliding away: load-dependence of velocity generated by skeletal muscle myosin molecules in the laser trap.
Human actin mutations associated with hypertrophic and dilated cardiomyopathies demonstrate distinct thin filament regulatory properties in vitro.
The molecular basis of thin filament activation: from single molecule to muscle.
Acidosis decreases the Ca2+ sensitivity of thin filaments by preventing the first actomyosin interaction.
Myosin's powerstroke occurs prior to the release of phosphate from the active site.
Recent insights into the relative timing of myosin's powerstroke and release of phosphate.