Evidence map›Paper›PMID 26786569›Full record

ArticleScientific reports2016

Temperature effect on the chemomechanical regulation of substeps within the power stroke of a single Myosin II.

Chenling Dong, Bin Chen

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.4field-weighted citation impact, top 32% 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

4 citing papers in PubMed, 5 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
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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

2 authors at 1 institution in 1 country.

Chenling DongDepartment of Engineering Mechanics, Zhejiang University, Hangzhou, P.R. China.
Bin ChenDepartment of Engineering Mechanics, Zhejiang University, Hangzhou, P.R. China.
Zhejiang University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Myosin IIs in the skeletal muscle are highly efficient nanoscale machines evolved in nature. Understanding how they function can not only bring insights into various biological processes but also provide guidelines to engineer synthetic nanoscale motors working in the vicinity of thermal noise. Though it was clearly demonstrated that the behavior of a skeletal muscle fiber, or that of a single myosin was strongly affected by the temperature, how exactly the temperature affects the kinetics of a single myosin is not fully understood. By adapting the newly developed transitional state model, which successfully explained the intriguing motor force regulation during skeletal muscle contraction, here we systematically explain how exactly the power stroke of a single myosin proceeds, with the consideration of the chemomechanical regulation of sub-steps within the stroke. The adapted theory is then utilized to investigate the temperature effect on various aspects of the power stroke. Our analysis suggests that, though swing rates, the isometric force, and the maximal stroke size all strongly vary with the temperature, the temperature can have a very small effect on the releasable elastic energy within the power stroke.

Indexed as

Models, BiologicalMuscle ContractionTemperatureAlgorithmsComputer SimulationMyosin Type IIMyosin Type II

Identifiers

PMID26786569
PMCPMC4726395
OpenAlexW2414229362

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.