Evidence map›Paper›PMID 2143195›Full record

ArticleThe Journal of cell biology1990

Smooth muscle myosin cross-bridge interactions modulate actin filament sliding velocity in vitro.

D M Warshaw, J M Desrosiers, S S Work, K M Trybus

Abstract read
In one paragraph

Article in The Journal of cell biology, 1990. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 100 papers.

0numbers the graph read from it
0cells of the map it votes in
100citing 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

100 citing papers in PubMed.

  1. bioRxiv : the preprint server for biology · 2026
    Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Actomyosin Complex.Sub-cellular biochemistry · 2022
    Article
  10. Force Measurements From Myofibril to Filament.Frontiers in physiology · 2021
    Review
  11. Article
  12. Article
  13. Spreading of perturbations in myosin group kinetics along actin filaments.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  14. Article
  15. Review of cellular mechanotransduction on micropost substrates.Medical & biological engineering & computing · 2016
    Review
  16. Review
  17. 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
  18. Article
  19. Review
  20. Article

40 more citing papers are in PubMed but not listed here.

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.

D M WarshawDepartment of Physiology and Biophysics, University of Vermont, College of Medicine, Burlington 05405.
J M Desrosiers
S S Work
K M Trybus

Funding

SMOOTH MUSCLE MYOSIN--CONFORMATION AND ACTIVITYR01HL038113 · NHLBI · UNIVERSITY OF VERMONT &ST AGRIC COLLEGE · PI TRYBUS, KATHLEEN M · 1993 to 2011
$3.9M
SINGLE VASCULAR SMOOTH MUSCLE CELL MECHANICSR01HL035684 · NHLBI · UNIVERSITY OF VERMONT &ST AGRIC COLLEGE · PI WARSHAW, DAVID M · 1985 to 1989
–
VASCULAR SMOOTH MUSCLE MYOSIN--CONFORMATION &ACTIVITYR29HL038113 · NHLBI · BRANDEIS UNIVERSITY · PI TRYBUS, KATHLEEN M · 1987 to 1991
–
NHLBI NIH HHS HL35684NHLBI NIH HHS HL38113
6 · The paper itself

Abstract

Although it is generally believed that phosphorylation of the regulatory light chain of myosin is required before smooth muscle can develop force, it is not known if the overall degree of phosphorylation can also modulate the rate at which cross-bridges cycle. To address this question, an in vitro motility assay was used to observe the motion of single actin filaments interacting with smooth muscle myosin copolymers composed of varying ratios of phosphorylated and unphosphorylated myosin. The results suggest that unphosphorylated myosin acts as a load to slow down the rate at which actin is moved by the faster cycling phosphorylated cross-bridges. Myosin that was chemically modified to generate a noncycling analogue of the "weakly" bound conformation was similarly able to slow down phosphorylated myosin. The observed modulation of actin velocity as a function of copolymer composition can be accounted for by a model based on mechanical interactions between cross-bridges.

Indexed as

Actin CytoskeletonActinsAnimalsCytoskeletonGizzard, AvianKineticsMacromolecular SubstancesMicroscopy, ElectronMusclesMuscle, SmoothMyosinsTurkeysActinsMacromolecular SubstancesMyosins

Identifiers

PMID2143195
PMCPMC2116193

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.