Evidence map›Paper›PMID 30204203›Full record

ArticleSoft matter2018

Nonequilibrium phase diagrams for actomyosin networks.

Simon L Freedman, Glen M Hocky, Shiladitya Banerjee, Aaron R Dinner

Abstract read
In one paragraph

Article in Soft matter, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing 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

19 citing papers in PubMed.

  1. Article
  2. An active matter model captures spatial dynamics of actomyosin oscillations in larval epithelial cells duringProceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  3. Article
  4. Morphometric analysis of actin networks.Molecular biology of the cell · 2024
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. The Actin Cytoskeleton as an Active Adaptive Material.Annual review of condensed matter physics · 2020
    Article
  14. Article
  15. Article
  16. Mechanical and kinetic factors drive sorting of F-actin cross-linkers on bundles.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  17. Article
  18. Article
  19. 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.

Simon L FreedmanDepartment of Physics, The University of Chicago, 929 East 57th Street, Chicago, IL 60637, USA.
Glen M Hocky
Shiladitya Banerjee
Aaron R Dinner

Funding

Robust rare event simulation for protein folding and disease-related aggregationR01GM109455 · NIGMS · UNIVERSITY OF CHICAGO · PI DINNER, AARON · 2013 to 2017
$1.7M
Computational studies of Arp2/3 activation and deactivationF32GM113415 · NIGMS · UNIVERSITY OF CHICAGO · PI HOCKY, GLEN · 2015 to 2017
$162k
NIGMS NIH HHS F32 GM113415NIGMS NIH HHS R01 GM109455
6 · The paper itself

Abstract

Living cells dynamically modulate the local morphologies of their actin networks to perform biological functions, including force transduction, intracellular transport, and cell division. A major challenge is to understand how diverse structures of the actin cytoskeleton are assembled from a limited set of molecular building blocks. Here we study the spontaneous self-assembly of a minimal model of cytoskeletal materials, consisting of semiflexible actin filaments, crosslinkers, and molecular motors. Using coarse-grained simulations, we demonstrate that by changing concentrations and kinetics of crosslinkers and motors, as well as filament lengths, we can generate three distinct structural phases of actomyosin assemblies: bundled, polarity-sorted, and contracted. We introduce new metrics to distinguish these structural phases and demonstrate their functional roles. We find that the binding kinetics of motors and crosslinkers can be tuned to optimize contractile force generation, motor transport, and mechanical response. By quantitatively characterizing the relationships between the modes of cytoskeletal self-assembly, the resulting structures, and their functional consequences, our work suggests new principles for the design of active materials.

Indexed as

Models, BiologicalActinsActomyosinElasticityViscosityActinsActomyosin

Identifiers

PMID30204203
PMCPMC6192427

What OpenQuestion holds

Textmetadata
LicenceTDM
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.