Evidence map›Paper›PMID 17878301›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2007

Myosin V stepping mechanism.

Giovanni Cappello, Paolo Pierobon, Clémentine Symonds, Lorenzo Busoni, J Christof M Gebhardt, Matthias Rief, Jacques Prost

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing 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

26 citing papers in PubMed.

  1. Article
  2. On the Control of Directionality of Myosin.Journal of the American Chemical Society · 2024
    Article
  3. Article
  4. Review
  5. Information flow, gating, and energetics in dimeric molecular motors.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  6. Article
  7. Structural basis for power stroke vs. Brownian ratchet mechanisms of motor proteins.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  8. Mechanisms for achieving high speed and efficiency in biomolecular machines.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  9. Article
  10. Article
  11. Allocating dissipation across a molecular machine cycle to maximize flux.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  12. Article
  13. Design principles governing the motility of myosin V.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Direct observation of the myosin-Va power stroke and its reversal.Nature structural & molecular biology · 2010
    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

7 authors.

Giovanni CappelloInstitut Curie, Centre National de la Recherche Scientifique Unité Mixte de Recherche 168, 75231 Paris, France. giovanni.cappello@curie.fr
Paolo Pierobon
Clémentine Symonds
Lorenzo Busoni
J Christof M Gebhardt
Matthias Rief
Jacques Prost

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We observe the myosin V stepping mechanism by traveling wave tracking. This technique, associated with optical tweezers, allows one to follow a scattering particle in a two-dimensional plane, with nanometer accuracy and a temporal resolution in the microsecond range. We have observed that, at the millisecond time scale, the myosin V combines longitudinal and vertical motions during the step. Because at this time scale the steps appear heterogeneous, we deduce their general features by aligning and averaging a large number of them. Our data show that the 36-nm step occurs in three main stages. First, the myosin center of mass moves forward 5 nm; the duration of this short prestep depends on the ATP concentration. Second, the motor performs a fast motion over 23 nm; this motion is associated to a vertical movement of the myosin center of mass, whose distance from the actin filament increases by 6 nm. Third, the myosin head freely diffuses toward the next binding site and the vertical position is recovered. We propose a simple model to describe the step mechanism of the dimeric myosin V.

Indexed as

ActinsAnimalsChickensDimerizationKinesinsModels, MolecularModels, StatisticalMuscle, SkeletalMyosinsMyosin Type VPolystyrenesRabbitsSpectroscopy, Fourier Transform InfraredThermodynamicsActinsKinesinsMyosinsMyosin Type VPolystyrenes

Identifiers

PMID17878301
PMCPMC2000544

What OpenQuestion holds

Textmetadata
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.