Evidence map›Paper›PMID 15647168›Full record

ReviewPhilosophical transactions of the Royal Society of London. Series B, Biological sciences2004

Smooth muscle myosin: regulation and properties.

Avril V Somlyo, Alexander S Khromov, Martin R Webb, Michael A Ferenczi, David R Trentham, Zhen-He He, Sitong Sheng, Zhifeng Shao, Andrew P Somlyo

Open access · greenAbstract readReview
In one paragraph

Review in Philosophical transactions of the Royal Society of London. Series B, Biological sciences, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
1.7field-weighted citation impact, top 16% 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

37 citing papers in PubMed, 51 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Airway smooth muscle tone increases actin filamentogenesis and contractile capacity.American journal of physiology. Lung cellular and molecular physiology · 2020
    Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. 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
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Smooth muscle-protein translocation and tissue function.Anatomical record (Hoboken, N.J. : 2007) · 2014
    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

9 authors at 4 institutions in 3 countries.

Avril V SomlyoMolecular Physiology and Biological Physics, University of Virginia, PO Box 800736, 1300 Jefferson Park Avenue, Charlottesville, VA 22908-0736, USA. avs5u@virginia.edu
Alexander S Khromov
Martin R Webb
Michael A Ferenczi
David R Trentham
Zhen-He He
Sitong Sheng
Zhifeng Shao
Andrew P Somlyo
University of Virginia · USInstitute of Molecular Biology and Biophysics · RUKing's College London · GBNIHR Imperial Biomedical Research Centre · GB

Funding

THE CONTRACTILE SYSTEM OF VASCULAR SMOOTH MUSCLEP01HL019242 · NHLBI · UNIVERSITY OF VIRGINIA CHARLOTTESVILLE · PI OWENS, GARY K · 1985 to 2009
$16.9M
THREE DIMENSIONAL DISTRIBUTION OF ION TRANSPORTING MEMBRANE CHANNELS/ORGANELLESP01HL048807 · NHLBI · UNIVERSITY OF VIRGINIA CHARLOTTESVILLE · PI SOMLYO, AVRIL V. · 1992 to 2008
$14.0M
Medical Research Council G0100150NHLBI NIH HHS P01 HL19242NHLBI NIH HHS P01 HL48807
6 · The paper itself

Abstract

The relationship of the biochemical states to the mechanical events in contraction of smooth muscle cross-bridges is reviewed. These studies use direct measurements of the kinetics of Pi and ADP release. The rate of release of Pi from thiophosphorylated cycling cross-bridges held isometric was biphasic with turnovers of 1.8 s-1 and 0.3 s-1, reflecting properties and forces directly acting on cross-bridges through mechanisms such as positive strain and inhibition by high-affinity MgADP binding. Fluorescent transients reporting release of an ADP analogue 3'-deac-edaADP were significantly faster in phasic than in tonic smooth muscles. Thiophosphorylation of myosin regulatory light chains (RLCs) increased and positive strain decreased the release rate around twofold. The rates of ADP release from rigor cross-bridges and the steady-state Pi release from cycling isometric cross-bridges are similar, indicating that the ADP-release step or an isomerization preceding it may limit the ATPase rate. Thus ADP release in phasic and tonic smooth muscles is a regulated step with strain- and dephosphorylation-dependence. High affinity of cross-bridges for ADP and slow ADP release prolong the fraction of the duty cycle occupied by strongly bound AM.ADP state(s) and contribute to the high economy of force that is characteristic of smooth muscle. RLC thiophosphorylation led to structural changes in smooth muscle cross-bridges consistent with our findings that thiophosphorylation and strain modulate product release.

Indexed as

Models, BiologicalActinsAdenosine DiphosphateAnimalsKineticsMuscle ContractionMuscle, SmoothMyosinsPhosphatesPhosphorylationProtein BindingActinsAdenosine DiphosphateMyosinsPhosphates

Identifiers

PMID15647168
PMCPMC1693473
OpenAlexW179885216

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.