Evidence map›Paper›PMID 19165498›Full record

ArticlePflugers Archiv : European journal of physiology2009

Insights into the kinetics of Ca2+-regulated contraction and relaxation from myofibril studies.

Robert Stehle, Johannes Solzin, Bogdan Iorga, Corrado Poggesi

Abstract read
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In one paragraph

Article in Pflugers Archiv : European journal of physiology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.

0numbers the graph read from it
0cells of the map it votes in
50citing papers in PubMed
3.2field-weighted citation impact, top 8% 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

50 citing papers in PubMed, 78 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Dysfunctional sarcomeric relaxation in the heart.Current opinion in physiology · 2022
    Article
  9. Article
  10. Why make a strong muscle weaker?The Journal of general physiology · 2021
    Article
  11. Article
  12. Article
  13. Article
  14. Force Measurements From Myofibril to Filament.Frontiers in physiology · 2021
    Review
  15. Review
  16. Review
  17. Article
  18. Article
  19. Frontiers in physiology · 2020
    Review
  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

4 authors at 3 institutions in 3 countries.

Robert StehleInstitute of Physiology, University of Cologne, Robert Koch Str. 39, 50931 Cologne, Germany. Robert.Stehle@Uni-Koeln.de
Johannes Solzin
Bogdan Iorga
Corrado Poggesi
University of Cologne · DERobert Koch Institute · DEUniversity of Florence · IT

Funding

Telethon GGP07133
6 · The paper itself

Abstract

Muscle contraction results from force-generating interactions between myosin cross-bridges on the thick filament and actin on the thin filament. The force-generating interactions are regulated by Ca(2+) via specialised proteins of the thin filament. It is controversial how the contractile and regulatory systems dynamically interact to determine the time course of muscle contraction and relaxation. Whereas kinetics of Ca(2+)-induced thin-filament regulation is often investigated with isolated proteins, force kinetics is usually studied in muscle fibres. The gap between studies on isolated proteins and structured fibres is now bridged by recent techniques that analyse the chemical and mechanical kinetics of small components of a muscle fibre, subcellular myofibrils isolated from skeletal and cardiac muscle. Formed of serially arranged repeating units called sarcomeres, myofibrils have a complete fully structured ensemble of contractile and Ca(2+) regulatory proteins. The small diameter of myofibrils (few micrometres) facilitates analysis of the kinetics of sarcomere contraction and relaxation induced by rapid changes of [ATP] or [Ca(2+)]. Among the processes studied on myofibrils are: (1) the Ca(2+)-regulated switch on/off of the troponin complex, (2) the chemical steps in the cross-bridge adenosine triphosphatase cycle, (3) the mechanics of force generation and (4) the length dynamics of individual sarcomeres. These studies give new insights into the kinetics of thin-filament regulation and of cross-bridge turnover, how cross-bridges transform chemical energy into mechanical work, and suggest that the cross-bridge ensembles of each half-sarcomere cooperate with each other across the half-sarcomere borders. Additionally, we now have a better understanding of muscle relaxation and its impairment in certain muscle diseases.

Indexed as

Adenosine DiphosphateAdenosine TriphosphateAnimalsCalciumCardiomyopathiesDiastoleHumansKineticsMuscle ContractionMuscle RelaxationMyofibrilsSarcomeresSystoleTroponinAdenosine DiphosphateAdenosine TriphosphateCalciumTroponin

Identifiers

PMID19165498
OpenAlexW2034286956

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.