Evidence map›Paper›PMID 28193897›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2017

Simulating the dynamics of the mechanochemical cycle of myosin-V.

Shayantani Mukherjee, Raphael Alhadeff, Arieh Warshel

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing 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

13 citing papers in PubMed.

  1. Article
  2. Article
  3. Understanding hypertrophic cardiomyopathy and its regulation by myosin drugs.Protein science : a publication of the Protein Society · 2025
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. How kinesin waits for ATP affects the nucleotide and load dependence of the stepping kinetics.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  9. Article
  10. Review
  11. Article
  12. The FPhotosynthesis research · 2017
    Review
  13. Reexamining the origin of the directionality of myosin V.Proceedings of the National Academy of Sciences of the United States of America · 2017
    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

3 authors.

Shayantani MukherjeeDepartment of Chemistry, University of Southern California, Los Angeles, CA 90089.
Raphael AlhadeffDepartment of Chemistry, University of Southern California, Los Angeles, CA 90089.
Arieh WarshelDepartment of Chemistry, University of Southern California, Los Angeles, CA 90089 warshel@usc.edu.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The detailed dynamics of the cycle of myosin-V are explored by simulation approaches, examining the nature of the energy-driven motion. Our study started with Langevin dynamics (LD) simulations on a very coarse landscape with a single rate-limiting barrier and reproduced the stall force and the hand-over-hand dynamics. We then considered a more realistic landscape and used time-dependent Monte Carlo (MC) simulations that allowed trajectories long enough to reproduce the force/velocity characteristic sigmoidal correlation, while also reproducing the hand-over-hand motion. Overall, our study indicated that the notion of a downhill lever-up to lever-down process (popularly known as the powerstroke mechanism) is the result of the energetics of the complete myosin-V cycle and is not the source of directional motion or force generation on its own. The present work further emphasizes the need to use well-defined energy landscapes in studying molecular motors in general and myosin in particular.

Indexed as

ActinsAdenosine DiphosphateAdenosine TriphosphateBinding SitesBiomechanical PhenomenaHumansKineticsMolecular Dynamics SimulationMonte Carlo MethodMyosin Type VPhosphatesProtein BindingProtein Conformation, alpha-HelicalProtein Conformation, beta-StrandProtein Interaction Domains and MotifsThermodynamicsActinsAdenosine DiphosphateAdenosine TriphosphateMyosin Type VPhosphatesbrownian ratchetchemomechanical couplingcytoskeletonmolecular motorspowerstroke

Identifiers

PMID28193897
PMCPMC5338489

What OpenQuestion holds

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Registered trials

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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.