ArticleJournal of the Royal Society, Interface2020
Dynamics of ATP-dependent and ATP-independent steppings of myosin-V on actin: catch-bond characteristics.
Article in Journal of the Royal Society, Interface, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
2 citing papers in PubMed.
- Polarity sorting of actin filaments by motor-driven cargo transport.Biophysical journal · 2025Article
- Validate the force-velocity relation of the Hill's muscle model from a molecular perspective.Frontiers in bioengineering and biotechnology · 2022Article
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Authors and funding
1 author.
Funding
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Abstract
An analytical theory is presented for the dynamics of myosin-V molecular motor, where both ATP-dependent and ATP-independent steppings are taken into account. Specifically, the dependences of velocity, run length and unbinding rate upon both forward and backward loads and ATP concentration are studied, explaining quantitatively the diverse available single-molecule data and providing predicted results. The results show that the unbinding rate increases with the increase of ATP concentration and levels off at both low and high ATP concentrations. More interestingly, at an ATP concentration that is not very low, the unbinding rate exhibits characteristics of a catch-slip bond under backward load, with the unbinding rate decreasing rapidly with the increase of the backward load in the range smaller than about 2.5 pN and then increasing slowly with the further increase of the backward load. By contrast, under forward load the unbinding rate exhibits a slip-bond characteristic.
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