Evidence map›Paper›PMID 8063856›Full record

ArticleThe Journal of cell biology1994

Antibodies probe for folded monomeric myosin in relaxed and contracted smooth muscle.

A Horowitz, K M Trybus, D S Bowman, F S Fay

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.1field-weighted citation impact, top 24% 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

14 citing papers in PubMed, 41 citations in OpenAlex.

  1. Filament evanescence of myosin II and smooth muscle function.The Journal of general physiology · 2021
    Review
  2. 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
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Folding and regulation in myosins II and V.Journal of muscle research and cell motility · 2007
    Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Polymerization of myosin on activation of rat anococcygeus smooth muscle.Journal of muscle research and cell motility · 1997
    Article
  14. 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 at 1 institution in 1 country.

A HorowitzRosentiel Basic Medical Sciences Research Center, Brandeis University, Waltham, Massachusetts 02254.
K M Trybus
D S Bowman
F S Fay
Brandeis University · US

Funding

SMOOTH MUSCLE MYOSIN--CONFORMATION AND ACTIVITYR01HL038113 · NHLBI · UNIVERSITY OF VERMONT &ST AGRIC COLLEGE · PI TRYBUS, KATHLEEN M · 1993 to 2011
$3.9M
GENERATION AND REGULATION OF FORCE IN SMOOTH MUSCLER01HL014523 · NHLBI · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI TUFT, RICHARD ALLAN · 1985 to 1996
–
VASCULAR SMOOTH MUSCLE MYOSIN--CONFORMATION &ACTIVITYR29HL038113 · NHLBI · BRANDEIS UNIVERSITY · PI TRYBUS, KATHLEEN M · 1987 to 1991
–
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 HL14523NHLBI NIH HHS HL 38113
6 · The paper itself

Abstract

Regulatory light chain phosphorylation is required for assembly of smooth and non-muscle myosins in vitro, but its effect on polymerization within the cell is not understood. Relaxed smooth muscle cells contain dephosphorylated thick filaments, but this does not exclude the presence of a pool of folded myosin monomers which could be recruited to assemble when phosphorylated, thus forming part of smooth muscle's activation pathway. To test this hypothesis, relaxed and contracted avian gizzard cryosections were labeled with a fluorescently conjugated monoclonal antibody specific for the folded monomeric conformation, or with an antibody against the tip of the tail whose epitope is accessible in the monomeric but not the filamentous state. Fluorescence intensity observed in the two physiological states was quantitated by digital imaging microscopy. Only trace amounts of folded monomeric myosin were detected in both the relaxed and contracted states. The amount of monomer also did not increase when alpha-toxin permeabilized gizzard was equilibrated in a solvent that disassembles filaments in vitro. Assembly/disassembly is therefore unlikely to play a major role in regulating the contraction/relaxation cycle in smooth muscle cells.

Indexed as

Muscle ContractionAnimalsAntibodies, MonoclonalChickensGizzard, AvianImmunologic TechniquesIn Vitro TechniquesMacromolecular SubstancesMuscle, SmoothMyosinsProtein BindingAntibodies, MonoclonalMacromolecular SubstancesMyosins

Identifiers

PMID8063856
PMCPMC2120169
OpenAlexW2020967667

What OpenQuestion holds

Textmetadata
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.