Evidence map›Paper›PMID 17604319›Full record

ArticleBiophysical journal2007

Molecular motor-induced instabilities and cross linkers determine biopolymer organization.

D Smith, F Ziebert, D Humphrey, C Duggan, M Steinbeck, W Zimmermann, J Käs

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
4.7field-weighted citation impact, top 4% 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

38 citing papers in PubMed, 111 citations in OpenAlex.

  1. Review
  2. Microscopic interactions control a structural transition in active mixtures of microtubules and molecular motors.Proceedings of the National Academy of Sciences of the United States of America · 2024
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  3. Article
  4. Article
  5. Article
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  7. Large and stable: actin aster networks formedFrontiers in chemistry · 2022
    Article
  8. Tuning the Properties of Active Microtubule Networks by Depletion Forces.Langmuir : the ACS journal of surfaces and colloids · 2021
    Article
  9. Effect of DNA Origami Nanostructures on hIAPP Aggregation.Nanomaterials (Basel, Switzerland) · 2020
    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. Variations of Elastic Modulus and Cell Volume with Temperature for Cortical Neurons.Langmuir : the ACS journal of surfaces and colloids · 2019
    Article
  15. Article
  16. DNA Nanotubes as a Versatile Tool to Study Semiflexible Polymers.Journal of visualized experiments : JoVE · 2017
    Article
  17. Single Actin Bundle Rheology.Molecules (Basel, Switzerland) · 2017
    Article
  18. Review
  19. Article
  20. Actomyosin dynamics drive local membrane component organization in an in vitro active composite layer.Proceedings of the National Academy of Sciences of the United States of America · 2016
    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

7 authors at 4 institutions in 2 countries.

D SmithInstitute for Soft Matter Physics, University of Leipzig, Germany.
F Ziebert
D Humphrey
C Duggan
M Steinbeck
W Zimmermann
J Käs
The University of Texas at Austin · USArgonne National Laboratory · USLeipzig University · DEUniversity of Bayreuth · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

All eukaryotic cells rely on the active self-organization of protein filaments to form a responsive intracellular cytoskeleton. The necessity of motility and reaction to stimuli additionally requires pathways that quickly and reversibly change cytoskeletal organization. While thermally driven order-disorder transitions are, from the viewpoint of physics, the most obvious method for controlling states of organization, the timescales necessary for effective cellular dynamics would require temperatures exceeding the physiologically viable temperature range. We report a mechanism whereby the molecular motor myosin II can cause near-instantaneous order-disorder transitions in reconstituted cytoskeletal actin solutions. When motor-induced filament sliding diminishes, the actin network structure rapidly and reversibly self-organizes into various assemblies. Addition of stable cross linkers was found to alter the architectures of ordered assemblies. These isothermal transitions between dynamic disorder and self-assembled ordered states illustrate that the interplay between passive crosslinking and molecular motor activity plays a substantial role in dynamic cellular organization.

Indexed as

Models, ChemicalActinsBinding SitesBiopolymersComputer SimulationCross-Linking ReagentsCrystallizationModels, MolecularMolecular Motor ProteinsMultiprotein ComplexesMyosin Type IIProtein BindingProtein ConformationActinsBiopolymersCross-Linking ReagentsMolecular Motor ProteinsMultiprotein ComplexesMyosin Type II

Identifiers

PMID17604319
PMCPMC2098725
OpenAlexW2123404147

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.