Evidence map›Paper›PMID 24653704›Full record

ReviewFrontiers in physiology2014

To understand muscle you must take it apart.

Christopher Batters, Claudia Veigel, Earl Homsher, James R Sellers

Open access · goldAbstract readReview
In one paragraph

Review in Frontiers in physiology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
2.0field-weighted citation impact, top 12% 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

21 citing papers in PubMed, 38 citations in OpenAlex.

  1. Article
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  9. Article
  10. Force Measurements From Myofibril to Filament.Frontiers in physiology · 2021
    Review
  11. Article
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  13. 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

4 authors at 3 institutions in 2 countries.

Christopher BattersDepartment of Cellular Physiology and Centre for Nanosciences (CeNS), Ludwig-Maximilians-Universität München München, Germany.
Claudia VeigelDepartment of Cellular Physiology and Centre for Nanosciences (CeNS), Ludwig-Maximilians-Universität München München, Germany.
Earl HomsherPhysiology Department, University of California Los Angeles Los Angeles, CA, USA.
James R SellersLaboratory of Molecular Physiology, National Heart, Lung and Blood Institute, National Institutes of Health Bethesda, MD, USA.
Ludwig-Maximilians-Universität München · DENational Heart Lung and Blood Institute · USUniversity of California, Los Angeles · US

Funding

Regulation Of Smooth and Nonmuscle MyosinZIAHL001786 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI SELLERS, JAMES · 2009 to 2025
$17.4M
Role of phosphorylation in cardiac muscle myosinZIAHL006174 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI SELLERS, JAMES · 2013 to 2017
$985k
6 · The paper itself

Abstract

Striated muscle is an elegant system for study at many levels. Much has been learned about the mechanism of contraction from studying the mechanical properties of intact and permeabilized (or skinned) muscle fibers. Structural studies using electron microscopy, X-ray diffraction or spectroscopic probes attached to various contractile proteins were possible because of the highly ordered sarcomeric arrangement of actin and myosin. However, to understand the mechanism of force generation at a molecular level, it is necessary to take the system apart and study the interaction of myosin with actin using in vitro assays. This reductionist approach has lead to many fundamental insights into how myosin powers muscle contraction. In addition, nature has provided scientists with an array of muscles with different mechanical properties and with a superfamily of myosin molecules. Taking advantage of this diversity in myosin structure and function has lead to additional insights into common properties of force generation. This review will highlight the development of the major assays and methods that have allowed this combined reductionist and comparative approach to be so fruitful. This review highlights the history of biochemical and biophysical studies of myosin and demonstrates how a broad comparative approach combined with reductionist studies have led to a detailed understanding of how myosin interacts with actin and uses chemical energy to generate force and movement in muscle contraction and motility in general.

Indexed as

actomyosinATPaseelectron microscopyin vitro modelmusclemyosin

Identifiers

PMID24653704
PMCPMC3949407
OpenAlexW2144857767

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.