Evidence map›Paper›PMID 8698822›Full record

ArticleThe Journal of cell biology1996

Myosin filament structure in vertebrate smooth muscle.

J Q Xu, B A Harder, P Uman, R Craig

Abstract read
In one paragraph

Article in The Journal of cell biology, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
–field-weighted citation impact
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

39 citing papers in PubMed.

  1. Smooth muscle contractile cytoskeleton in health and disease.Journal of muscle research and cell motility · 2026
    Review
  2. Article
  3. Review
  4. Article
  5. Article
  6. The myosin II coiled-coil domain atomic structure in its native environment.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  7. Filament evanescence of myosin II and smooth muscle function.The Journal of general physiology · 2021
    Review
  8. Review
  9. The Huxley crossbridge model as the basic mechanism for airway smooth muscle contraction.American journal of physiology. Lung cellular and molecular physiology · 2019
    Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. An invertebrate smooth muscle with striated muscle myosin filaments.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  16. 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
  17. Review
  18. 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

4 authors.

J Q XuDepartment of Cell Biology, University of Massachusetts Medical School, Worcester, 01655, USA.
B A Harder
P Uman
R Craig

Funding

STRUCTURE OF CONTRACTILE FILAMENTS OF MUSCLER01AR034711 · NIAMS · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI CRAIG, ROGER W · 1986 to 2013
$3.6M
SMOOTH MUSCLE FUNCTION--CELLULAR &MOLECULAR MECHANISMSP01HL047530 · NHLBI · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI FOGARTY, KEVIN E · 1993 to 1997
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CRYOELECTRON MICROSCOPE AND CRYO-ULTRAMICROTOMES10RR008426 · NCRR · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI CRAIG, ROGER W · 1993 to 1993
–
NCRR NIH HHS RR08426NHLBI NIH HHS HL47530NIAMS NIH HHS AR34711
6 · The paper itself

Abstract

The in vivo structure of the myosin filaments in vertebrate smooth muscle is unknown. Evidence from purified smooth muscle myosin and from some studies of intact smooth muscle suggests that they may have a nonhelical, side-polar arrangement of crossbridges. However, the bipolar, helical structure characteristic of myosin filaments in striated muscle has not been disproved for smooth muscle. We have used EM to investigate this question in a functionally diverse group of smooth muscles (from the vascular, gastrointestinal, reproductive, and visual systems) from mammalian, amphibian, and avian species. Intact muscle under physiological conditions, rapidly frozen and then freeze substituted, shows many myosin filaments with a square backbone in transverse profile. Transverse sections of fixed, chemically skinned muscles also show square backbones and, in addition, reveal projections (crossbridges) on only two opposite sides of the square. Filaments gently isolated from skinned smooth muscles and observed by negative staining show crossbridges with a 14.5-nm repeat projecting in opposite directions on opposite sides of the filament. Such filaments subjected to low ionic strength conditions show bare filament ends and an antiparallel arrangement of myosin tails along the length of the filament. All of these observations are consistent with a side-polar structure and argue against a bipolar, helical crossbridge arrangement. We conclude that myosin filaments in all smooth muscles, regardless of function, are likely to be side-polar. Such a structure could be an important factor in the ability of smooth muscles to contract by large amounts.

Indexed as

AnimalsBufo marinusChickensFourier AnalysisGuinea PigsImage Processing, Computer-AssistedMicroscopy, ElectronMuscle ContractionMuscle, SmoothMyosinsOsmolar ConcentrationRabbitsMyosins

Identifiers

PMID8698822
PMCPMC2120914

What OpenQuestion holds

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LicenceCC BY-NC-SA
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.