Evidence map›Paper›PMID 35163054›Full record

ArticleInternational journal of molecular sciences2022

Effect of Myosin Isoforms on Cardiac Muscle Twitch of Mice, Rats and Humans.

Momcilo Prodanovic, Michael A Geeves, Corrado Poggesi, Michael Regnier, Srboljub M Mijailovich

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2022. 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
2.3field-weighted citation impact, top 11% 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

13 citing papers in PubMed, 14 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Article
  6. Myosin in autoinhibitedProceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  7. Article
  8. Article
  9. Structural and Functional Properties of Kappa Tropomyosin.International journal of molecular sciences · 2023
    Article
  10. Article
  11. Article
  12. Article
  13. Review
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 5 institutions in 4 countries.

Momcilo ProdanovicInstitute for Information Technologies, University of Kragujevac, 34000 Kragujevac, Serbia.ORCID 0000-0003-0556-1213
Michael A GeevesDepartment of Biosciences, University of Kent, Canterbury CT2 7NJ, Kent, UK.ORCID 0000-0002-9364-8898
Corrado PoggesiDepartment of Experimental & Clinical Medicine, University of Florence, 20134 Florence, Italy.ORCID 0000-0003-2624-4778
Michael RegnierDepartment of Bioengineering, University of Washington, Seattle, WA 98105, USA.
Srboljub M MijailovichFilamenTech, Inc., Newtown, MA 02458, USA.ORCID 0000-0003-2640-3548
Illinois Institute of Technology · USUniversity of Florence · ITUniversity of Kent · GBUniversity of Kragujevac · RSUniversity of Washington · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

To understand how pathology-induced changes in contractile protein isoforms modulate cardiac muscle function, it is necessary to quantify the temporal-mechanical properties of contractions that occur under various conditions. Pathological responses are much easier to study in animal model systems than in humans, but extrapolation between species presents numerous challenges. Employing computational approaches can help elucidate relationships that are difficult to test experimentally by translating the observations from rats and mice, as model organisms, to the human heart. Here, we use the spatially explicit MUSICO platform to model twitch contractions from rodent and human trabeculae collected in a single laboratory. This approach allowed us to identify the variations in kinetic characteristics of α- and β-myosin isoforms across species and to quantify their effect on cardiac muscle contractile responses. The simulations showed how the twitch transient varied with the ratio of the two myosin isoforms. Particularly, the rate of tension rise was proportional to the fraction of α-myosin present, while the β-isoform dominated the rate of relaxation unless α-myosin was >50%. Moreover, both the myosin isoform and the Ca

Indexed as

AnimalsCalciumComputer SimulationHeartHumansMaleMiceMyocardial ContractionMyosinsProtein IsoformsRatsCalciumMyosinsProtein Isoformscalcium sensitivitycross-species simulationlevel of incorporationMUSICO platformtension relaxationtrabeculae

Identifiers

PMID35163054
PMCPMC8835009
OpenAlexW4206251963

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.