Evidence map›Paper›PMID 3937845›Full record

ReviewJournal of muscle research and cell motility1985

The thin filaments of smooth muscles.

S B Marston, C W Smith

Abstract readReview
PubMed Publisher
In one paragraph

Review in Journal of muscle research and cell motility, 1985. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.

0numbers the graph read from it
0cells of the map it votes in
54citing papers in PubMed
14.0field-weighted citation impact, top 1% 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

54 citing papers in PubMed, 195 citations in OpenAlex.

  1. Review
  2. Smooth muscle contractile cytoskeleton in health and disease.Journal of muscle research and cell motility · 2026
    Review
  3. MBNL loss of function in smooth muscle as a model for myotonic dystrophy associated gastrointestinal dysmotility.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Biochemistry of smooth muscle myosin light chain kinase.Archives of biochemistry and biophysics · 2011
    Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
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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 1 institution in 1 country.

S B Marston
C W Smith
Essex Cardiothoracic Centre · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Contraction in vertebrate smooth and striated muscles results from the interaction of the actin filaments with crossbridges arising from the myosin filaments. The functions of the actin based thin filaments are (1) interaction with myosin to produce force; (2) regulation of force generation in response to Ca2+ concentration; and (3) transmission of the force to the ends of the cell. The major protein components of smooth muscle thin filaments are actin, tropomyosin and caldesmon, present in molar ratios of 28:4:1 respectively. Other smooth muscle proteins which may be associated with the thin filaments in the cell are filamin, vinculin, alpha-actinin, myosin light chain kinase and calmodulin. We have reviewed the structural and functional properties of these proteins and where possible we have suggested what their function and mechanism of action may be. We propose that actin and tropomyosin are involved in the force producing interaction with myosin, and that this interaction is controlled by a Ca2+-dependent mechanism involving caldesmon, tropomyosin and calmodulin. Vinculin, alpha-actinin and filamin appear to be involved in the attachment of the thin filaments to the cell membrane and their spatial organization within the cell. We conclude that the filaments of smooth muscles share many common properties with those from skeletal muscle, but that they are also quite distinct in terms of both their caldesmon based regulatory mechanism and their mode of organization into a contractile apparatus.

Indexed as

ActininActinsAnimalsCalciumCalmodulinCalmodulin-Binding ProteinsContractile ProteinsFilaminsHumansMicrofilament ProteinsMolecular WeightMuscle ProteinsMuscle, SmoothMyosin-Light-Chain KinaseMyosinsPhosphorylationActininActinsCalciumCalmodulinCalmodulin-Binding ProteinsContractile ProteinsFilaminsMicrofilament ProteinsMuscle ProteinsMyosin-Light-Chain KinaseMyosinsProtein KinasesTropomyosinVinculin

Identifiers

PMID3937845
OpenAlexW2092991423

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.