Evidence map›Paper›PMID 19114664›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2009

Force generation by a dynamic Z-ring in Escherichia coli cell division.

Jun F Allard, Eric N Cytrynbaum

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
5.5field-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

36 citing papers in PubMed, 85 citations in OpenAlex.

  1. Article
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  8. Beyond force generation: Why is a dynamic ring of FtsZ polymers essential for bacterial cytokinesis?BioEssays : news and reviews in molecular, cellular and developmental biology · 2017
    Review
  9. Z-ring Structure and Constriction Dynamics inFrontiers in microbiology · 2017
    Article
  10. Review
  11. Review
  12. Targeting the Bacterial Division Protein FtsZ.Journal of medicinal chemistry · 2016
    Review
  13. Defining the rate-limiting processes of bacterial cytokinesis.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  14. Article
  15. Review
  16. Review
  17. Review
  18. Article
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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

2 authors at 1 institution in 1 country.

Jun F AllardDepartment of Mathematics, University of British Columbia, Vancouver, BC, Canada V6T 1Z2.
Eric N Cytrynbaum
University of British Columbia · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

FtsZ, a bacterial homologue of tubulin, plays a central role in bacterial cell division. It is the first of many proteins recruited to the division site to form the Z-ring, a dynamic structure that recycles on the time scale of seconds and is required for division to proceed. FtsZ has been recently shown to form rings inside tubular liposomes and to constrict the liposome membrane without the presence of other proteins, particularly molecular motors that appear to be absent from the bacterial proteome. Here, we propose a mathematical model for the dynamic turnover of the Z-ring and for its ability to generate a constriction force. Force generation is assumed to derive from GTP hydrolysis, which is known to induce curvature in FtsZ filaments. We find that this transition to a curved state is capable of generating a sufficient force to drive cell-wall invagination in vivo and can also explain the constriction seen in the in vitro liposome experiments. Our observations resolve the question of how FtsZ might accomplish cell division despite the highly dynamic nature of the Z-ring and the lack of molecular motors.

Indexed as

Cell DivisionBacterial ProteinsBiomechanical PhenomenaCytoskeletal ProteinsEscherichia coliEscherichia coli ProteinsGuanosine TriphosphateLiposomesModels, BiologicalBacterial ProteinsCytoskeletal ProteinsEscherichia coli ProteinsFtsZ protein, BacteriaGuanosine TriphosphateLiposomes

Identifiers

PMID19114664
PMCPMC2629190
OpenAlexW2160337123

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.