Evidence map›Paper›PMID 24726887›Full record

ArticleJournal of molecular and cellular cardiology2014

Ventricular myosin modifies in vitro step-size when phosphorylated.

Yihua Wang, Katalin Ajtai, Thomas P Burghardt

Abstract read
In one paragraph

Article in Journal of molecular and cellular cardiology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
3.6field-weighted citation impact, top 7% 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

30 citing papers in PubMed, 39 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Sarcomere maturation: function acquisition, molecular mechanism, and interplay with other organelles.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2022
    Review
  6. Article
  7. Article
  8. Article
  9. Regulatory Light Chains in Cardiac Development and Disease.International journal of molecular sciences · 2021
    Review
  10. Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. Myosin light chain phosphorylation enhances contraction of heart muscle via structural changes in both thick and thin filaments.Proceedings of the National Academy of Sciences of the United States of America · 2016
    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.

Yihua WangDepartment of Biochemistry and Molecular Biology, United States.
Katalin AjtaiDepartment of Biochemistry and Molecular Biology, United States.
Thomas P BurghardtDepartment of Biochemistry and Molecular Biology, United States; Department of Physiology and Biomedical Engineering, United States. Electronic address: burghardt@mayo.edu.
Mayo Clinic in Arizona · US

Funding

Tumor BiologyP30CA125123 · NCI · BAYLOR COLLEGE OF MEDICINE · PI Michael M Ittmann · 2007 to 2026
$73.9M
Visualizing Actomyosin Transients by Data MergingR01AR049277 · NIAMS · MAYO CLINIC ROCHESTER · PI BURGHARDT, THOMAS P · 2004 to 2013
$3.2M
In Situ Sensing of Single Myosin Function in Hypertrophy DiseaseR01HL095572 · NHLBI · MAYO CLINIC ROCHESTER · PI BURGHARDT, THOMAS P · 2010 to 2013
$1.5M
NCI NIH HHS P30 CA125123NHLBI NIH HHS R01 HL095572NHLBI NIH HHS R01HL095572NIAMS NIH HHS R01 AR049277NIAMS NIH HHS R01AR049277
6 · The paper itself

Abstract

Cardiac and skeletal muscle myosins have the central role in contraction transducing ATP free energy into the mechanical work of moving actin. Myosin has a motor domain containing ATP and actin binding sites and a lever-arm that undergoes rotation impelling bound actin. The lever-arm converts torque generated in the motor into the linear displacement known as step-size. The myosin lever-arm is stabilized by bound essential and regulatory light chains (ELC and RLC). RLC phosphorylation at S15 is linked to modified lever-arm mechanical characteristics contributing to myosin filament based contraction regulation and to the response of the muscle to disease. Myosin step-size was measured using a novel quantum dot (Qdot) assay that previously confirmed a 5nm step-size for fast skeletal myosin and multiple unitary steps, most frequently 5 and 8nm, and a rare 3nm displacement for β cardiac myosin (βMys). S15 phosphorylation in βMys is now shown to change step-size distribution by advancing the 8nm step frequency. After phosphorylation, the 8nm step is the dominant myosin step-size resulting in significant gain in the average step-size. An increase in myosin step-size will increase the amount of work produced per ATPase cycle. The results indicate that RLC phosphorylation modulates work production per ATPase cycle suggesting the mechanism for contraction regulation by the myosin filament.

Indexed as

ActinsAdenosine TriphosphateAnimalsBiomechanical PhenomenaCell MovementHeart VentriclesMuscle, SkeletalMyocardial ContractionMyocardiumMyosin Light ChainsPhosphorylationQuantum DotsRabbitsSwineVentricular MyosinsActinsAdenosine TriphosphateMyosin Light ChainsVentricular MyosinsActin-activated ATPaseCardiac myosin RLC phosphorylationIn vitro motilityQdot assayVentricular myosin step-size

Identifiers

PMID24726887
PMCPMC4037356
OpenAlexW2016005073

What OpenQuestion holds

Textmetadata
LicenceTDM
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.