Evidence map›Paper›PMID 2503537›Full record

ArticleJournal of muscle research and cell motility1989

Myosin filaments isolated from skinned amphibian smooth muscle cells are side-polar.

P H Cooke, F S Fay, R Craig

Abstract read
PubMed Publisher
In one paragraph

Article in Journal of muscle research and cell motility, 1989. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
3.9field-weighted citation impact, top 6% 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

21 citing papers in PubMed, 58 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Article
  6. Velocities of unloaded muscle filaments are not limited by drag forces imposed by myosin cross-bridges.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  7. Article
  8. Article
  9. Article
  10. Caldesmon and the regulation of cytoskeletal functions.Advances in experimental medicine and biology · 2008
    Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Calmodulin and the regulation of smooth muscle contraction.Molecular and cellular biochemistry · 1994
    Review
  17. Article
  18. The molecular anatomy of caldesmon.The Biochemical journal · 1991
    Review
  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.

P H CookeDepartment of Cell Biology, University of Massachusetts Medical School, Worcester 01655.
F S Fay
R Craig
University of Massachusetts Chan Medical School · US

Funding

STRUCTURE OF CONTRACTILE FILAMENTS OF MUSCLER01AR034711 · NIAMS · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI CRAIG, ROGER W · 1986 to 2013
$3.6M
GENERATION AND REGULATION OF FORCE IN SMOOTH MUSCLER01HL014523 · NHLBI · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI TUFT, RICHARD ALLAN · 1985 to 1996
–
GENERATION AND REGULATION OF FORCE IN SMOOTH MUSCLER37HL014523 · NHLBI · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI FAY, FREDRIC S · 1990 to 1996
–
NHLBI NIH HHS HL 14523NIAMS NIH HHS AR 34711
6 · The paper itself

Abstract

The structure of myosin filaments isolated from skinned toad stomach smooth muscle cells has been examined by electron microscopy as a step toward identifying the in vivo structure. When negatively stained following exposure to relaxing conditions, the filaments exhibited a continuous 14-nm axial repeat of crossbridge projections with no central bare zone. The filaments thus differed from the bipolar filaments found in striated muscle and displayed instead features resembling side-polar and mixed-polarity filament models. By rotation of isolated filaments around their longitudinal axes it was found that cross bridges occurred only along two sides of the filament, an arrangement consistent with the side-polar but not the mixed-polarity model. The polarity is thus similar to that proposed for ribbons (Small & Squire, J. molec. Biol. 67, (1972) 17-149) and for synthetic smooth muscle myosin filaments (Craig and Megerman, J. Cell Biol. 75, (1977) 990-996); their appearance in cross-section, however, shows that these structures are filaments (i.e. with two axes of similar dimensions) and not broad ribbons. As the filaments were derived directly from skinned cells which contracted and relaxed in response to physiological levels of MgATP and Ca2+ at rates comparable to those of native, isolated cells, this unusual arrangement of cross bridges appears to be an effective, functional form of myosin in the contractile apparatus. Side-polar filaments therefore merit consideration as plausible candidates for the native organization of myosin in vertebrate smooth muscle cells.

Indexed as

Actin CytoskeletonActomyosinAnimalsBufo marinusMacromolecular SubstancesMicroscopy, ElectronMuscle ContractionMuscle, SmoothMyosinsActomyosinMacromolecular SubstancesMyosins

Identifiers

PMID2503537
OpenAlexW2027662372

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.