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Phosphate enhances myosin-powered actin filament velocity under acidic conditions in a motility assay.
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.
Direct observation of phosphate inhibiting the force-generating capacity of a miniensemble of Myosin molecules.
Ca++-sensitizing mutations in troponin, P(i), and 2-deoxyATP alter the depressive effect of acidosis on regulated thin-filament velocity.
Acidosis affects muscle contraction by slowing the rates myosin attaches to and detaches from actin.
Acidosis decreases the Ca2+ sensitivity of thin filaments by preventing the first actomyosin interaction.
FRET and optical trapping reveal mechanisms of actin activation of the power stroke and phosphate release in myosin V.