Evidence map›Paper›PMID 9172080›Full record

ArticleJournal of muscle research and cell motility1997

Polymerization of myosin on activation of rat anococcygeus smooth muscle.

J Q Xu, J M Gillis, R Craig

Abstract read
PubMed Publisher
In one paragraph

Article in Journal of muscle research and cell motility, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
2.0field-weighted citation impact, top 14% 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

12 citing papers in PubMed, 53 citations in OpenAlex.

  1. Article
  2. Article
  3. Filament evanescence of myosin II and smooth muscle function.The Journal of general physiology · 2021
    Review
  4. Article
  5. Molecular Mechanisms for the Mechanical Modulation of Airway Responsiveness.Journal of engineering and science in medical diagnostics and therapy · 2019
    Article
  6. Interacting-heads motif has been conserved as a mechanism of myosin II inhibition since before the origin of animals.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  7. Reply from Chun Y. Seow.The Journal of physiology · 2015
    Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. 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 2 institutions in 2 countries.

J Q XuDepartment of Cell Biology, University of Massachusetts Medical School, Worcester 01655, USA.
J M Gillis
R Craig
UCLouvain · BEUniversity 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
SMOOTH MUSCLE FUNCTION--CELLULAR &MOLECULAR MECHANISMSP01HL047530 · NHLBI · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI FOGARTY, KEVIN E · 1993 to 1997
–
NHLBI NIH HHS HL 47530NIAMS NIH HHS AR 34711
6 · The paper itself

Abstract

The in vivo state of assembly of myosin in vertebrate smooth muscle is controversial. In vitro studies on purified smooth muscle myosin show that it is monomeric (10S) under relaxing conditions and filamentous under contraction conditions. Electron microscopic and antibody labelling studies of intact smooth muscles, on the other hand, suggest that myosin is filamentous in the relaxed as well as the contracting state and that 10S myosin occurs only in trace amounts. However, birefringence, conventional EM and X-ray diffraction evidence suggests that in certain smooth muscles in vivo (e.g. rat anococcygeus), while myosin filaments exist in the relaxed state, their number increases on contraction. Here, we have used low temperature electron microscopic techniques (rapid freezing followed by freeze-substitution), which preserve labile components in close to their in vivo state, to detect any change in filament number on contraction. The results from rat anococcygeus have been compared with those from guinea pig taenia coli, in which other techniques have revealed no change in filament number. In the anococcygeus, we find evidence for a 23% increase in filament density in transverse sections of contracting muscle compared with relaxed muscle. In the taenia coli we find no change. These results are in qualitative agreement with earlier findings. They provide evidence for polymerization of myosin in contracting rat anococcygeus, and suggest that this process is subtle and occurs only in some smooth muscles.

Indexed as

AnimalsGuinea PigsIsometric ContractionMaleMicroscopy, ElectronMuscle ContractionMuscle RelaxationMuscle, SmoothMyosinsRatsRats, WistarTissue PreservationMyosins

Identifiers

PMID9172080
OpenAlexW1695060755

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.