Evidence map›Paper›PMID 16963567›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2006

Cytoskeletal polymer networks: the molecular structure of cross-linkers determines macroscopic properties.

B Wagner, R Tharmann, I Haase, M Fischer, A R Bausch

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 71 papers.

0numbers the graph read from it
0cells of the map it votes in
71citing 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

71 citing papers in PubMed.

  1. Measuring the Elastic Properties of Living Cells.Methods in molecular biology (Clifton, N.J.) · 2027
    Article
  2. Form and function in biological filaments: a physicist's review.Philosophical transactions. Series A, Mathematical, physical, and engineering sciences · 2025
    Review
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  16. The role of the Arp2/3 complex in shaping the dynamics and structures of branched actomyosin networks.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  17. Mimicry of a biophysical pathway leads to diverse pollen-like surface patterns.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
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11 more citing papers are in PubMed but not listed here.

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.

B WagnerLehrstühle für Biophysik E22 and Organische Chemie und Biochemie, Technische Universität München, 80333 Munich, Germany.
R Tharmann
I Haase
M Fischer
A R Bausch

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In living cells the mechanical properties of the actin cytoskeleton are defined by the local activation of different actin cross-linking proteins. These proteins consist of actin-binding domains that are separated and geometrically organized by different numbers of rod domains. The detailed molecular structure of the cross-linking molecules determines the structural and mechanical properties of actin networks in vivo. In this study, we systematically investigate the impact of the length of the spacing unit between two actin-binding domains on in vitro actin networks. Such synthetic cross-linkers reveal that the shorter the constructs are, the greater the elastic modulus changes in the linear response regime. Because the same binding domains are used in all constructs, only the differences in the number of rod domains determine their mechanical effectiveness. Structural rearrangements of the networks show that bundling propensity is highest for the shortest construct. The nonlinear mechanical response is affected by the molecular structure of the cross-linker molecules, and the observed critical strains and fracture stress increase proportional to the length of the spacing unit.

Indexed as

ActinsAnimalsCytoskeletal ProteinsCytoskeletonElasticityModels, MolecularMolecular Sequence DataPolymersProtein ConformationRabbitsActinsCytoskeletal ProteinsPolymers

Identifiers

PMID16963567
PMCPMC1599898

What OpenQuestion holds

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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.