Evidence map›Paper›PMID 3159750›Full record

ArticleJournal of muscle research and cell motility1985

Dual effect of filamin on actomyosin ATPase activity.

R Dabrowska, A Goch, H Osińska, A Szpacenko, J Sosinski

Abstract read
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In one paragraph

Article in Journal of muscle research and cell motility, 1985. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
0.9field-weighted citation impact, top 28% 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

6 citing papers in PubMed, 26 citations in OpenAlex.

  1. Article
  2. Slow cycling of unphosphorylated myosin is inhibited by calponin, thus keeping smooth muscle relaxed.Proceedings of the National Academy of Sciences of the United States of America · 1997
    Article
  3. Article
  4. Article
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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

5 authors at 1 institution in 1 country.

R Dabrowska
A Goch
H Osińska
A Szpacenko
J Sosinski
Instytut Biologii Doświadczalnej im. Marcelego Nenckiego · PL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Filamin binds to F-actin and influences the myosin-actin interaction. At relatively low concentrations, filamin activates actomyosin Mg2+-ATPase, whereas higher concentrations of filamin exert an inhibitory effect. Activation of ATPase activity occurs under conditions where a loose meshwork of actin filaments is present and inhibition is associated with the appearance of closely apposed bundles of actin filaments. Maximum activation (about fourfold) of actomyosin ATPase activity by filamin occurs between 30 and 65 mM KCl, at pH 6.5, and at temperatures not less than 30 degrees C. ATPase activation requires higher concentrations of filamin in the presence than in the absence of tropomyosin. Filamin does not activate Mg2+-ATPase activity of acto-subfragment-1 and has only a slight effect on the Mg2+-ATPase of acto-heavy meromyosin, but it inhibits the activity of both these systems under conditions similar to those that inhibit actomyosin ATPase activity.

Indexed as

ActinsActomyosinAdenosine TriphosphatasesAnimalsCa(2+) Mg(2+)-ATPaseCarrier ProteinsChickensContractile ProteinsEnzyme ActivationFilaminsKineticsMagnesiumMagnesium ChlorideMicrofilament ProteinsMicroscopy, ElectronMusclesActinsActomyosinAdenosine TriphosphatasesCa(2+) Mg(2+)-ATPaseCarrier ProteinsContractile ProteinsFilaminsMagnesiumMagnesium ChlorideMicrofilament Proteins

Identifiers

PMID3159750
OpenAlexW1977806010

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.