Evidence map›Paper›PMID 18591676›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2008

Measuring molecular rupture forces between single actin filaments and actin-binding proteins.

Jorge M Ferrer, Hyungsuk Lee, Jiong Chen, Benjamin Pelz, Fumihiko Nakamura, Roger D Kamm, Matthew J Lang

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 98 papers.

0numbers the graph read from it
0cells of the map it votes in
98citing papers in PubMed
10.5field-weighted citation impact, top 1% 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

98 citing papers in PubMed, 216 citations in OpenAlex.

  1. Article
  2. Sono-Mechanogenetics: Linking Ultrasound Physics With Cellular Mechanobiology.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
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  6. Bending Dynamics of Magnetic Filaments at a Curved Bacterial Bath Interface.Langmuir : the ACS journal of surfaces and colloids · 2025
    Article
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  10. Review
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  12. Review
  13. Coupling during collective cell migration is controlled by a vinculin mechanochemical switch.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

38 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

7 authors at 3 institutions in 2 countries.

Jorge M FerrerDepartment of Biological Engineering, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.
Hyungsuk Lee
Jiong Chen
Benjamin Pelz
Fumihiko Nakamura
Roger D Kamm
Matthew J Lang
Massachusetts Institute of Technology · USHarvard University · USStony Brook University · US

Funding

Subcellular Mechanotransduction in Vascular Smooth Muscle CellsP01HL064858 · NHLBI · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI KAMM, ROGER D. · 2001 to 2005
$7.6M
NHLBI NIH HHS P01 HL064858NHLBI NIH HHS P01HL064858
6 · The paper itself

Abstract

Actin-binding proteins (ABPs) regulate the assembly of actin filaments (F-actin) into networks and bundles that provide the structural integrity of the cell. Two of these ABPs, filamin and alpha-actinin, have been extensively used to model the mechanical properties of actin networks grown in vitro; however, there is a lack in the understanding of how the molecular interactions between ABPs and F-actin regulate the dynamic properties of the cytoskeleton. Here, we present a native-like assay geometry to test the rupture force of a complex formed by an ABP linking two quasiparallel actin filaments. We readily demonstrate the adaptability of this assay by testing it with two different ABPs: filamin and alpha-actinin. For filamin/actin and alpha-actinin/actin, we measured similar rupture forces of 40-80 pN for loading rates between 4 and 50 pN/s. Both ABP unfolding and conformational transition events were observed, demonstrating that both are important and may be a significant mechanism for the temporal regulation of the mechanical properties of the actin cytoskeleton. With this modular, single-molecule assay, a wide range of ABP/actin interactions can be studied to better understand cytoskeletal and cell dynamics.

Indexed as

Actin CytoskeletonActininAnimalsBiomechanical PhenomenaContractile ProteinsFilaminsGelsolinHumansMicrofilament ProteinsModels, MolecularRabbitsActininContractile ProteinsFilaminsGelsolinMicrofilament Proteins

Identifiers

PMID18591676
PMCPMC2453742
OpenAlexW2069030820

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.