Evidence map›Paper›PMID 15792977›Full record

ArticleBiophysical journal2005

Elastic lever-arm model for myosin V.

Andrej Vilfan

Abstract read
In one paragraph

Article in Biophysical journal, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.

0numbers the graph read from it
0cells of the map it votes in
47citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

47 citing papers in PubMed.

  1. Article
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  11. Simulating the dynamics of the mechanochemical cycle of myosin-V.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  12. Flexural Stiffness of Myosin Va Subdomains as Measured from Tethered Particle Motion.Journal of biophysics (Hindawi Publishing Corporation : Online) · 2015
    Article
  13. Motor coupling through lipid membranes enhances transport velocities for ensembles of myosin Va.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  14. Article
  15. Myosin directionality results from coupling between ATP hydrolysis, lever motion, and actin binding.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  16. Article
  17. Motor proteins and molecular motors: how to operate machines at the nanoscale.Journal of physics. Condensed matter : an Institute of Physics journal · 2013
    Review
  18. Review
  19. Design principles governing the motility of myosin V.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

1 author.

Andrej VilfanJ. Stefan Institute, Ljubljana, Slovenia. andrej.vilfan@ijs.si

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We present a mechanochemical model for myosin V, a two-headed processive motor protein. We derive the properties of a dimer from those of an individual head, which we model both with a four-state cycle (detached; attached with ADP.Pi; attached with ADP; and attached without nucleotide) and alternatively with a five-state cycle (where the powerstroke is not tightly coupled to the phosphate release). In each state the lever arm leaves the head at a different, but fixed, angle. The lever arm itself is described as an elastic rod. The chemical cycles of both heads are coordinated exclusively by the mechanical connection between the two lever arms. The model explains head coordination by showing that the lead head only binds to actin after the powerstroke in the trail head and that it only undergoes its powerstroke after the trail head unbinds from actin. Both models (four- and five-state) reproduce the observed hand-over-hand motion and fit the measured force-velocity relations. The main difference between the two models concerns the load dependence of the run length, which is much weaker in the five-state model. We show how systematic processivity measurement under varying conditions could be used to distinguish between both models and to determine the kinetic parameters.

Indexed as

Models, BiologicalAdenosine DiphosphateAdenosine TriphosphateBiophysical PhenomenaBiophysicsDimerizationElasticityEnergy MetabolismIn Vitro TechniquesKineticsModels, MolecularMolecular Motor ProteinsMyosin Type VPhosphatesProtein Structure, QuaternaryThermodynamicsAdenosine DiphosphateAdenosine TriphosphateMolecular Motor ProteinsMyosin Type VPhosphates

Identifiers

PMID15792977
PMCPMC1305614

What OpenQuestion holds

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Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.