Evidence map›Paper›PMID 16909198›Full record

ReviewJournal of muscle research and cell motility2006

Use of thin filament reconstituted muscle fibres to probe the mechanism of force generation.

Masataka Kawai, Shin'ichi Ishiwata

Open access · greenAbstract readReview
In one paragraph

Review in Journal of muscle research and cell motility, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
0.8field-weighted citation impact, top 24% 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

17 citing papers in PubMed, 28 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Alpha-tropomyosin mutations in inherited cardiomyopathies.Journal of muscle research and cell motility · 2013
    Review
  8. Article
  9. Evolving concepts on the age-related changes in "muscle quality".Journal of cachexia, sarcopenia and muscle · 2012
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. 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

2 authors at 2 institutions in 2 countries.

Masataka KawaiDepartment of Anatomy and Cell Biology, College of Medicine, The University of Iowa, Iowa City, IA 52242, USA. masataka-kawai@uiowa.edu
Shin'ichi Ishiwata
University of Iowa · USWaseda University · JP

Funding

Role of actin domains in force generation in myocardiumR01HL070041 · NHLBI · UNIVERSITY OF IOWA · PI KAWAI, MASATAKA · 2002 to 2011
$2.5M
NHLBI NIH HHS HL70041NHLBI NIH HHS R01 HL070041
6 · The paper itself

Abstract

The technique of selective removal of the thin filament by gelsolin in bovine cardiac muscle fibres, and reconstitution of the thin filament from isolated proteins is reviewed, and papers that used reconstituted preparations are discussed. By comparing the results obtained in the absence/presence of regulatory proteins tropomyosin (Tm) and troponin (Tn), it is concluded that the role of Tm and Tn in force generation is not only to expose the binding site of actin to myosin, but also to modify actin for better stereospecific and hydrophobic interaction with myosin. This conclusion is further supported by experiments that used a truncated Tm mutant and the temperature study of reconstituted fibres. The conclusion is consistent with the hypothesis that there are three states in the thin filament: blocked state, closed state, and open state. Tm is the major player to produce these effects, with Tn playing the role of Ca2+ sensing and signal transmission mechanism. Experiments that changed the number of negative charges at the N-terminal finger of actin demonstrates that this part of actin is essential to promote the strong interaction between actin and myosin molecules, in addition to the well-known weak interaction that positions the myosin head at the active site of actin prior to force generation.

Indexed as

ActinsAllosteric RegulationAnimalsBinding SitesCattleCytoskeletonGelsolinMuscle Fibers, SkeletalMyocardial ContractionMyocardiumMyosinsTropomyosinTroponinActinsGelsolinMyosinsTropomyosinTroponin

Identifiers

PMID16909198
PMCPMC2896216
OpenAlexW2050836758

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.