Evidence map›Paper›PMID 22729612›Full record

ReviewJournal of muscle research and cell motility2012

Residual force enhancement in skeletal muscles: one sarcomere after the other.

Dilson E Rassier

Abstract readReview
PubMed Publisher
In one paragraph

Review in Journal of muscle research and cell motility, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
–field-weighted citation impact
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

14 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Review
  5. Review
  6. Active Viscoelasticity of Sarcomeres.Frontiers in robotics and AI · 2018
    Review
  7. Article
  8. Article
  9. Article
  10. Review
  11. A new paradigm for muscle contraction.Frontiers in physiology · 2015
    Review
  12. Review
  13. Reply from K. A. P. Edman.The Journal of physiology · 2013
    Article
  14. Editorial on special issue "lifestyle and ageing in muscle disease".Journal of muscle research and cell motility · 2012
    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

1 author.

Dilson E RassierDepartments of Kinesiology and Physical Education, Physics and Physiology, McGill University, Montreal, Canada. dilson.rassier@mcgill.ca

Funding

Canadian Institutes of Health Research
6 · The paper itself

Abstract

The force-length relation is one of the most prominent features of striated muscles, and predicts that the force produced by a fully activated muscle is proportional to the overlap between myosin and actin filaments within sarcomeres. However, there are situations in which the force-length relation deviates from predictions based purely on filament overlap. Notably, stretch of activated skeletal muscles induces a long-lasting increase in force, which is larger than the force produced during isometric contractions at a similar length. The mechanism behind this residual force enhancement and deviations from the original force-length relation are unknown, generating heated debate in the literature. We performed a series of experiments with short segments of myofibrils and isolated sarcomeres to investigating the mechanisms of the residual force enhancement and the force length-relation. In this paper, evidence will be presented showing that force enhancement is caused by: (i) half-sarcomere non-uniformities, and (ii) a sarcomeric component, which may be associated with Ca(2+)-induced stiffness of titin molecules. These mechanisms have large implications for understanding the basic mechanisms of muscle contraction.

Indexed as

Biomechanical PhenomenaHumansMuscle, SkeletalMyofibrilsSarcomeres

Identifiers

PMID22729612

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.