Evidence map›Paper›PMID 12080126›Full record

ArticleBiophysical journal2002

Kinetic effects of myosin regulatory light chain phosphorylation on skeletal muscle contraction.

Julien S Davis, Colleen L Satorius, Neal D Epstein

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
2.1field-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

31 citing papers in PubMed, 59 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Neurophysiology of ACL Injury.Orthopedic reviews · 2025
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Heavy and light roles: myosin in the morphogenesis of the heart.Cellular and molecular life sciences : CMLS · 2013
    Review
  14. Article
  15. Review
  16. Human skeletal muscle: transition between fast and slow fibre types.Pflugers Archiv : European journal of physiology · 2011
    Article
  17. Signaling to myosin regulatory light chain in sarcomeres.The Journal of biological chemistry · 2011
    Review
  18. The molecular effects of skeletal muscle myosin regulatory light chain phosphorylation.American journal of physiology. Regulatory, integrative and comparative physiology · 2009
    Article
  19. Article
  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

3 authors at 1 institution in 1 country.

Julien S DavisMolecular Physiology Section, Laboratory of Molecular Cardiology, National Heart Lung and Blood Institute, National Institutes of Health, Bethesda, Maryland 20892-1760, USA. davisjs@nhlbi.nih.gov
Colleen L Satorius
Neal D Epstein
National Heart Lung and Blood Institute · US

Funding

MOLECULAR BIOLOGY AND PATHOPHYSIOLOGY OF HYPERTROPHIC CARDIOMYOPATHYZ01HL004996 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI EPSTEIN, NEAL DAVID · 1996 to 2008
$1.2M
Molecular Biology And Pathophysiology Of CardiomyopathyZIAHL004996 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI EPSTEIN, NEAL DAVID · 2009 to 2012
$1.0M
6 · The paper itself

Abstract

Kinetic analysis of contracting fast and slow rabbit muscle fibers in the presence of the tension inhibitor 2,3-butanedione monoxime suggests that regulatory light chain (RLC) phosphorylation up-regulates the flux of weakly attached cross-bridges entering the contractile cycle by increasing the actin-catalyzed release of phosphate from myosin. This step appears to be separate from earlier Ca(2+) regulated steps. Small step-stretches of single skinned fibers were used to study the effect of phosphorylation on fiber mechanics. Subdivision of the resultant tension transients into the Huxley-Simmons phases 1, 2(fast), 2(slow), 3, and 4 reveals that phosphorylation reduces the normalized amplitude of the delayed rise in tension (stretch activation response) by decreasing the amplitudes of phase 3 and, to a lesser extent, phase 2(slow). In slow fibers, the RLC P1 isoform phosphorylates at least 4-fold faster than the P2 isoform, complicating the role of RLC phosphorylation in heart and slow muscle. We discuss the functional relevance of the regulation of stretch activation by RLC phosphorylation for cardiac and other oscillating muscles and speculate how the interaction of the two heads of myosin could account for the inverse effect of Ca(2+) levels on isometric tension and rate of force redevelopment (k(TR)).

Indexed as

Muscle ContractionAnimalsBiophysical PhenomenaBiophysicsCalciumCloning, MolecularHumansKineticsModels, ChemicalMuscle, SkeletalMyosin Light ChainsPhosphorylationProtein IsoformsRabbitsTime FactorsUp-RegulationCalciumMyosin Light ChainsProtein Isoforms

Identifiers

PMID12080126
PMCPMC1302153
OpenAlexW1979694848

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.