Evidence map›Paper›PMID 3435453›Full record

ArticleThe Biochemical journal1987

Activity of a gelsolin-like actin modulator in rat skeletal muscle under protein catabolic conditions.

J D'Haese, M Rutschmann, B Dahlmann, H Hinssen

Open access · greenAbstract read
In one paragraph

Article in The Biochemical journal, 1987. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.3field-weighted citation impact, top 40% 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

1 citing paper in PubMed, 8 citations in OpenAlex.

  1. Mechanisms of exercise-induced muscle fibre injury.Sports medicine (Auckland, N.Z.) · 1991
    Review
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 3 institutions in 2 countries.

J D'HaeseInstitut für Zoologie II, Universität Düsseldorf, Federal Republic of Germany.
M Rutschmann
B Dahlmann
H Hinssen
Deutsches Diabetes-Zentrum e.V. · DEAustrian Academy of Sciences · ATHeinrich Heine University Düsseldorf · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A gelsolin-like actin-modulating protein was isolated from rat skeletal muscle and characterized with respect to its interaction with actin. The protein, with a molecular mass of approx. 85 kDa, forms a stoichiometric complex with two actin molecules and is activated by micromolar concentrations of Ca2+. It effectively severs actin filaments and promotes nucleation of actin polymerization. The activity of this protein is detectable already in crude extracts by its capability to reduce the steady state viscosity of actin. Actin-modulating activities were determined in muscle extracts of rats kept under protein catabolic conditions, i.e. as generated by corticosterone treatment and starvation. In both cases we found a marked increase of modulator activity. The possibility is discussed that the increased activity of actin modulator indicates a fragmentation of actin filaments prior to the proteolytic degradation of actin.

Indexed as

ActinsAnimalsCalciumCalcium-Binding ProteinsChromatography, Ion ExchangeCorticosteroneElectrophoresis, Polyacrylamide GelMacromolecular SubstancesMaleMusclesProtein BindingRatsRats, Inbred StrainsActinsCalciumCalcium-Binding ProteinsCorticosteroneMacromolecular Substances

Identifiers

PMID3435453
PMCPMC1148554
OpenAlexW2418545986

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.