Evidence map›Paper›PMID 19959992›Full record

ArticleThe EMBO journal2010

Bactofilins, a ubiquitous class of cytoskeletal proteins mediating polar localization of a cell wall synthase in Caulobacter crescentus.

Juliane Kühn, Ariane Briegel, Erhard Mörschel, Jörg Kahnt, Katja Leser, Stephanie Wick, Grant J Jensen, Martin Thanbichler

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 86 papers.

0numbers the graph read from it
0cells of the map it votes in
86citing papers in PubMed
2.0field-weighted citation impact, top 14% 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

86 citing papers in PubMed, 154 citations in OpenAlex.

  1. Article
  2. DUF4004 protein BacR (YhbD) ofFrontiers in microbiology · 2026
    Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Halofilins as emerging bactofilin families of archaeal cell shape plasticity orchestrators.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. VirB, a key transcriptional regulator ofbioRxiv : the preprint server for biology · 2023
    Article
  16. Article
  17. Review
  18. MultipleFrontiers in microbiology · 2023
    Article
  19. Article
  20. Distinct regions ofeLife · 2022
    Article

26 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

8 authors at 4 institutions in 2 countries.

Juliane KühnMax Planck Institute for Terrestrial Microbiology, Marburg, Germany.
Ariane Briegel
Erhard Mörschel
Jörg Kahnt
Katja Leser
Stephanie Wick
Grant J Jensen
Martin Thanbichler
Philipps University of Marburg · DEMax Planck Institute for Terrestrial Microbiology · DECalifornia Institute of Technology · USHoward Hughes Medical Institute · US

Funding

Structure and function of the prokaryotic cytoskeleton by electron cryotomographyR01AI067548 · NIAID · CALIFORNIA INSTITUTE OF TECHNOLOGY · PI JENSEN, GRANT J · 2006 to 2010
$1.6M
Howard Hughes Medical InstituteNIAID NIH HHS R01 AI067548
6 · The paper itself

Abstract

The cytoskeleton has a key function in the temporal and spatial organization of both prokaryotic and eukaryotic cells. Here, we report the identification of a new class of polymer-forming proteins, termed bactofilins, that are widely conserved among bacteria. In Caulobacter crescentus, two bactofilin paralogues cooperate to form a sheet-like structure lining the cytoplasmic membrane in proximity of the stalked cell pole. These assemblies mediate polar localization of a peptidoglycan synthase involved in stalk morphogenesis, thus complementing the function of the actin-like cytoskeleton and the cell division machinery in the regulation of cell wall biogenesis. In other bacteria, bactofilins can establish rod-shaped filaments or associate with the cell division apparatus, indicating considerable structural and functional flexibility. Bactofilins polymerize spontaneously in the absence of additional cofactors in vitro, forming stable ribbon- or rod-like filament bundles. Our results suggest that these structures have evolved as an alternative to intermediate filaments, serving as versatile molecular scaffolds in a variety of cellular pathways.

Indexed as

Bacterial ProteinsCaulobacter crescentusCell WallConserved SequenceCytoskeletal ProteinsCytoskeletonPenicillin-Binding ProteinsPhylogenyProtein TransportBacterial ProteinsCytoskeletal ProteinsPenicillin-Binding Proteins

Identifiers

PMID19959992
PMCPMC2824468
OpenAlexW2136079705

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.