AbstractDynamics of sliding were explored in isolated actin and myosin filaments. Sliding occurs in steps. The steps are integer multiples of 2.7nm, which is equal to the monomeric repeat along the actin filament. When filaments were forced to slide in the reverse direction, the size paradigm was the same. This size paradigm is parallel to that seen in the kinesin-microtubule system, where step size is an integer multiple of the tubulin repeat along the microtubule
AbstractWe present a model study of gliding assays in which actin filaments are moved by nonprocessi...
AbstractNaturally occurring groups of muscle myosin behave differently from individual myosins or sm...
Using in vitro motility assays, we examined the sliding velocity of actin filaments generated by pai...
AbstractDynamics of sliding were explored in isolated actin and myosin filaments. Sliding occurs in ...
Movement of single myosin filaments, synthesized by copolymerization of intact myosin and fluorescen...
The movement produced by a small number of myosin molecular motors was measured with nanometre preci...
The movement produced by a small number of myosin molecular motors was measured with nanometre preci...
We have developed a new technique for measurements of piconewton forces and nanometer displacements ...
Movement of single myosin filaments, synthesized by copolymerization of intact myosin and fluorescen...
AbstractMyosin X is a molecular motor that is adapted to select bundled actin filaments over single ...
We have analyzed the dependence of actin filament sliding movement on the mode of myosin attachment ...
AbstractMyosin X is a molecular motor that is adapted to select bundled actin filaments over single ...
AbstractMyosin V is biomolecular motor with two actin-binding domains (heads) that take multiple ste...
AbstractMyosin VI walks in a hand-over-hand fashion with an average step size of 30nm, which is much...
AbstractMyosin V is a homodimeric motor protein involved in trafficking of vesicles in the cell. It ...
AbstractWe present a model study of gliding assays in which actin filaments are moved by nonprocessi...
AbstractNaturally occurring groups of muscle myosin behave differently from individual myosins or sm...
Using in vitro motility assays, we examined the sliding velocity of actin filaments generated by pai...
AbstractDynamics of sliding were explored in isolated actin and myosin filaments. Sliding occurs in ...
Movement of single myosin filaments, synthesized by copolymerization of intact myosin and fluorescen...
The movement produced by a small number of myosin molecular motors was measured with nanometre preci...
The movement produced by a small number of myosin molecular motors was measured with nanometre preci...
We have developed a new technique for measurements of piconewton forces and nanometer displacements ...
Movement of single myosin filaments, synthesized by copolymerization of intact myosin and fluorescen...
AbstractMyosin X is a molecular motor that is adapted to select bundled actin filaments over single ...
We have analyzed the dependence of actin filament sliding movement on the mode of myosin attachment ...
AbstractMyosin X is a molecular motor that is adapted to select bundled actin filaments over single ...
AbstractMyosin V is biomolecular motor with two actin-binding domains (heads) that take multiple ste...
AbstractMyosin VI walks in a hand-over-hand fashion with an average step size of 30nm, which is much...
AbstractMyosin V is a homodimeric motor protein involved in trafficking of vesicles in the cell. It ...
AbstractWe present a model study of gliding assays in which actin filaments are moved by nonprocessi...
AbstractNaturally occurring groups of muscle myosin behave differently from individual myosins or sm...
Using in vitro motility assays, we examined the sliding velocity of actin filaments generated by pai...