Evidence map›Paper›PMID 28681850›Full record

ArticleNature communications2017

Coordinated force generation of skeletal myosins in myofilaments through motor coupling.

Motoshi Kaya, Yoshiaki Tani, Takumi Washio, Toshiaki Hisada, Hideo Higuchi

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
5.9field-weighted citation impact, top 3% of its field
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

43 citing papers in PubMed, 73 citations in OpenAlex.

  1. Article
  2. Article
  3. A Catalysis-Driven Dual Molecular Motor.Journal of the American Chemical Society · 2025
    Article
  4. Article
  5. Measuring emergent mechanical changes in cytoskeletal ensemblesFrontiers in cell and developmental biology · 2025
    Article
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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

5 authors at 2 institutions in 1 country.

Motoshi KayaDeparment of Physics, Graduate School of Science, University of Tokyo, 7-3-1 Hongo Bunkyo-ku, Tokyo 113-0033, Japan.
Yoshiaki TaniDeparment of Physics, Graduate School of Science, University of Tokyo, 7-3-1 Hongo Bunkyo-ku, Tokyo 113-0033, Japan.
Takumi WashioDepartment of Human and Engineered Environmental Studies, Graduate School of Frontier Science, University of Tokyo, Kashiwanoha Kashiwa, Chiba 277-0882, Japan.
Toshiaki HisadaDepartment of Human and Engineered Environmental Studies, Graduate School of Frontier Science, University of Tokyo, Kashiwanoha Kashiwa, Chiba 277-0882, Japan.
Hideo HiguchiDeparment of Physics, Graduate School of Science, University of Tokyo, 7-3-1 Hongo Bunkyo-ku, Tokyo 113-0033, Japan.
The University of Tokyo · JPTokyo University of Science · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In contrast to processive molecular motors, skeletal myosins form a large motor ensemble for contraction of muscles against high loads. Despite numerous information on the molecular properties of skeletal myosin, its ensemble effects on collective force generation have not been rigorously clarified. Here we show 4 nm stepwise actin displacements generated by synthetic myofilaments beyond a load of 30 pN, implying that steps cannot be driven exclusively by single myosins, but potentially by coordinated force generations among multiple myosins. The simulation model shows that stepwise actin displacements are primarily caused by coordinated force generation among myosin molecules. Moreover, the probability of coordinated force generation can be enhanced against high loads by utilizing three factors: strain-dependent kinetics between force-generating states; multiple power stroke steps; and high ATP concentrations. Compared with other molecular motors, our findings reveal how the properties of skeletal myosin are tuned to perform cooperative force generation for efficient muscle contraction.

Indexed as

Models, BiologicalActin CytoskeletonAdenosine DiphosphateAdenosine TriphosphateAnimalsBiomechanical PhenomenaComputer SimulationHumansKineticsMuscle Fibers, SkeletalMyofibrilsMyosinsAdenosine DiphosphateAdenosine TriphosphateMyosins

Identifiers

PMID28681850
PMCPMC5504292
OpenAlexW2731130848

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.