Evidence map›Paper›PMID 24187092›Full record

ArticleJournal of bacteriology2014

Outside-in assembly pathway of the type IV pilus system in Myxococcus xanthus.

Carmen Friedrich, Iryna Bulyha, Lotte Søgaard-Andersen

Open access · bronzeAbstract read
In one paragraph

Article in Journal of bacteriology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.

0numbers the graph read from it
0cells of the map it votes in
55citing 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

55 citing papers in PubMed, 101 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Electron Cryo-Tomography Reveals thebioRxiv : the preprint server for biology · 2025
    Article
  5. Integrative Structure and Function of thebioRxiv : the preprint server for biology · 2025
    Article
  6. Article
  7. Milestones in the development ofJournal of bacteriology · 2025
    Review
  8. Article
  9. Article
  10. Type IV pili ofEcoSal Plus · 2024
    Review
  11. Article
  12. Article
  13. Article
  14. Bacterial flagella hijack type IV pili proteins to control motility.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Article
  20. Article
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

3 authors at 1 institution in 1 country.

Carmen FriedrichDepartment of Ecophysiology, Max Planck Institute for Terrestrial Microbiology, Marburg, Germany.
Iryna Bulyha
Lotte Søgaard-Andersen
Max Planck Institute for Terrestrial Microbiology · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Type IV pili (T4P) are ubiquitous bacterial cell surface structures that undergo cycles of extension, adhesion, and retraction. T4P function depends on a highly conserved envelope-spanning macromolecular machinery consisting of 10 proteins that localizes polarly in Myxococcus xanthus. Using this localization, we investigated the entire T4P machinery assembly pathway by systematically profiling the stability of all and the localization of eight of these proteins in the absence of other T4P machinery proteins as well as by mapping direct protein-protein interactions. Our experiments uncovered a sequential, outside-in pathway starting with the outer membrane (OM) PilQ secretin ring. PilQ recruits a subcomplex consisting of the inner membrane (IM) lipoprotein PilP and the integral IM proteins PilN and PilO by direct interaction with the periplasmic domain of PilP. The PilP/PilN/PilO subcomplex recruits the cytoplasmic PilM protein, by direct interaction between PilN and PilM, and the integral IM protein PilC. The PilB/PilT ATPases that power extension/retraction localize independently of other T4P machinery proteins. Thus, assembly of the T4P machinery initiates with formation of the OM secretin ring and continues inwards over the periplasm and IM to the cytoplasm.

Indexed as

Protein MultimerizationBacterial Outer Membrane ProteinsCell MembraneFimbriae, BacterialFimbriae ProteinsMacromolecular SubstancesMyxococcus xanthusProtein Interaction MappingProtein TransportBacterial Outer Membrane ProteinsFimbriae ProteinsMacromolecular Substances

Identifiers

PMID24187092
PMCPMC3911261
OpenAlexW2169277660

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.