Evidence map›Paper›PMID 26536259›Full record

ArticleBiophysical journal2015

A Combination of Actin Treadmilling and Cross-Linking Drives Contraction of Random Actomyosin Arrays.

Dietmar B Oelz, Boris Y Rubinstein, Alex Mogilner

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
3.3field-weighted citation impact, top 8% 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

31 citing papers in PubMed, 57 citations in OpenAlex.

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  11. Review
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  14. The Actin Cytoskeleton as an Active Adaptive Material.Annual review of condensed matter physics · 2020
    Article
  15. Review
  16. Article
  17. Molecular Mechanism of Cytokinesis.Annual review of biochemistry · 2019
    Review
  18. Review
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  20. 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

3 authors at 2 institutions in 1 country.

Dietmar B OelzCourant Institute of Mathematical Sciences, New York University, New York, New York.
Boris Y RubinsteinStowers Institute, Kansas City, Missouri.
Alex MogilnerCourant Institute of Mathematical Sciences, New York University, New York, New York; Department of Biology, New York University, New York, New York. Electronic address: mogilner@cims.nyu.edu.
Courant Institute of Mathematical Sciences · USStowers Institute for Medical Research · US

Funding

Modeling mitotic spindle assemblyR01GM068952 · NIGMS · UNIVERSITY OF CALIFORNIA DAVIS · PI MOGILNER, ALEXANDER · 2003 to 2014
$4.4M
Austrian Science Fund FWF J 3463NIGMS NIH HHS GM068952NIGMS NIH HHS R01 GM068952
6 · The paper itself

Abstract

We investigate computationally the self-organization and contraction of an initially random actomyosin ring. In the framework of a detailed physical model for a ring of cross-linked actin filaments and myosin-II clusters, we derive the force balance equations and solve them numerically. We find that to contract, actin filaments have to treadmill and to be sufficiently cross linked, and myosin has to be processive. The simulations reveal how contraction scales with mechanochemical parameters. For example, they show that the ring made of longer filaments generates greater force but contracts slower. The model predicts that the ring contracts with a constant rate proportional to the initial ring radius if either myosin is released from the ring during contraction and actin filaments shorten, or if myosin is retained in the ring, while the actin filament number decreases. We demonstrate that a balance of actin nucleation and compression-dependent disassembly can also sustain contraction. Finally, the model demonstrates that with time pattern formation takes place in the ring, worsening the contractile process. The more random the actin dynamics are, the higher the contractility will be.

Indexed as

Models, BiologicalActinsActomyosinAnimalsBiomechanical PhenomenaCaenorhabditis elegansComputer SimulationMyosin Type IINeurospora crassaSaccharomycetalesActinsActomyosinMyosin Type II

Identifiers

PMID26536259
PMCPMC4643270
OpenAlexW2227100252

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.