Evidence map›Paper›PMID 12657740›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2003

Probing polymerization forces by using actin-propelled lipid vesicles.

Arpita Upadhyaya, Jeffrey R Chabot, Albina Andreeva, Azadeh Samadani, Alexander van Oudenaarden

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 72 papers.

0numbers the graph read from it
0cells of the map it votes in
72citing papers in PubMed
5.3field-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

72 citing papers in PubMed, 191 citations in OpenAlex.

  1. On the Assembly of Actin Polymerization-Powered Motors.Macromolecular rapid communications · 2026
    Article
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  3. Article
  4. Review
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  6. Article
  7. Review
  8. Encapsulated bacteria deform lipid vesicles into flagellated swimmers.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  9. Article
  10. On the adhesion-velocity relation and length adaptation of motile cells on stepped fibronectin lanes.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  11. Review
  12. Cytoskeleton Force Exertion in Bulk Cytoplasm.Frontiers in cell and developmental biology · 2020
    Review
  13. Article
  14. Article
  15. Review
  16. Review
  17. Article
  18. Artificial cell mimics as simplified models for the study of cell biology.Experimental biology and medicine (Maywood, N.J.) · 2017
    Review
  19. Article
  20. Review

12 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 at 1 institution in 1 country.

Arpita UpadhyayaDepartment of Physics, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge, MA 02139, USA.
Jeffrey R Chabot
Albina Andreeva
Azadeh Samadani
Alexander van Oudenaarden
Massachusetts Institute of Technology · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Actin polymerization provides a powerful propulsion force for numerous types of cell motility. Although tremendous progress has been made in identifying the biochemical components necessary for actin-based motility, the precise biophysical mechanisms of force generation remain unclear. To probe the polymerization forces quantitatively, we introduce an experimental system in which lipid vesicles coated with the Listeria monocytogenes virulence factor ActA are propelled by actin polymerization. The polymerization forces cause significant deformations of the vesicle. We have used these deformations to obtain a spatially resolved measure of the forces exerted on the membrane using a model based on the competition between osmotic pressure and membrane stretching. Our results indicate that actin exerts retractile or propulsive forces depending on the local membrane curvature and that the membrane is strongly bound to the actin gel. These results are consistent with the observed dynamics. After a slow elongation of the vesicle from a spherical shape, the strong bonds between the actin gel and the membrane rupture if the retractile forces exceed a critical value, leading to a rapid release of the vesicle's trailing edge.

Indexed as

ActinsAnimalsBacterial ProteinsBiophysical PhenomenaBiophysicsBiopolymersCattleGelsIn Vitro TechniquesLiposomesListeria monocytogenesMembrane ProteinsModels, BiologicalMolecular Motor ProteinsMovementactA protein, Listeria monocytogenesActinsBacterial ProteinsBiopolymersGelsLiposomesMembrane ProteinsMolecular Motor Proteins

Identifiers

PMID12657740
PMCPMC153588
OpenAlexW2145258422

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.