<p>The same simulation as in <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0087638#pone-0087638-g004" target="_blank">Fig. 4</a>, but with a myosin contractility of 0.225 pN/µm<sup>2</sup> instead of 5.555 pN/µm<sup>2</sup>. (A) Position of the leading edge (black) and the gel boundary (blue). (B) Velocities of the leading edge (black) and the gel boundary (light blue) and retrograde flow velocity (red). Comparison with <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0087638#pone-0087638-g004" target="_blank">Fig. 4</a> shows that the measured increase in period (C) is reproduced by our simulation. Filament densities, filament lengths and SR depth show basically the same behavior as without myo...
Background: MyosinIIs are adenosine triphosphate-driven molecular motors that form part of a cell’s ...
We have analyzed the dependence of actin filament sliding movement on the mode of myosin attachment ...
BACKGROUND: MyosinIIs are adenosine triphosphate-driven molecular motors that form part of a cell's ...
<p>(A) Experimentally measured P<sub>1</sub> for different ramp velocities. Solid line: pCa<sup>2+</...
<p>The same simulation as in <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0...
<p>(A) Actin network as visualized by SDC-FSM using Alexa-568 actin after 5 minutes in vehicle (0.75...
<p><b>A.</b> Simulation snap-shots showing the emergence of sarcomeric order in an acto-myosin bundl...
Blebbistatin reversibly disrupted both stolon tip pulsations and gastrovascular flow in the colonial...
<p>(A) Comparison of the corrected layer line intensities (gray curves) from nearly full-overlap mus...
In a spatially explicit stochastic simulation of myosin S1 heads attaching to a single actin filamen...
It has been observed that heavy meromyosin (HMM) propels actin filaments to higher velocities than n...
The precise details of how myosin-V coordinates the biochemical reactions and mechanical motions of ...
The interaction of actin filaments with myosin is crucial to cell motility, muscular contraction, ce...
<p>A. Size scales in muscle. Muscle contracts due to the formation of transient links between thick ...
The proteins involved in smooth muscle's molecular contractile mechanism – the anti-parallel motion ...
Background: MyosinIIs are adenosine triphosphate-driven molecular motors that form part of a cell’s ...
We have analyzed the dependence of actin filament sliding movement on the mode of myosin attachment ...
BACKGROUND: MyosinIIs are adenosine triphosphate-driven molecular motors that form part of a cell's ...
<p>(A) Experimentally measured P<sub>1</sub> for different ramp velocities. Solid line: pCa<sup>2+</...
<p>The same simulation as in <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0...
<p>(A) Actin network as visualized by SDC-FSM using Alexa-568 actin after 5 minutes in vehicle (0.75...
<p><b>A.</b> Simulation snap-shots showing the emergence of sarcomeric order in an acto-myosin bundl...
Blebbistatin reversibly disrupted both stolon tip pulsations and gastrovascular flow in the colonial...
<p>(A) Comparison of the corrected layer line intensities (gray curves) from nearly full-overlap mus...
In a spatially explicit stochastic simulation of myosin S1 heads attaching to a single actin filamen...
It has been observed that heavy meromyosin (HMM) propels actin filaments to higher velocities than n...
The precise details of how myosin-V coordinates the biochemical reactions and mechanical motions of ...
The interaction of actin filaments with myosin is crucial to cell motility, muscular contraction, ce...
<p>A. Size scales in muscle. Muscle contracts due to the formation of transient links between thick ...
The proteins involved in smooth muscle's molecular contractile mechanism – the anti-parallel motion ...
Background: MyosinIIs are adenosine triphosphate-driven molecular motors that form part of a cell’s ...
We have analyzed the dependence of actin filament sliding movement on the mode of myosin attachment ...
BACKGROUND: MyosinIIs are adenosine triphosphate-driven molecular motors that form part of a cell's ...