Evidence map›Paper›PMID 22411981›Full record

ReviewPhilosophical transactions of the Royal Society of London. Series B, Biological sciences2012

Structural biology of type VI secretion systems.

Eric Cascales, Christian Cambillau

Abstract readReview
In one paragraph

Review in Philosophical transactions of the Royal Society of London. Series B, Biological sciences, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 135 papers.

0numbers the graph read from it
0cells of the map it votes in
135citing papers in PubMed
–field-weighted citation impact
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

135 citing papers in PubMed.

  1. Article
  2. Review
  3. Megaplasmids associate withbioRxiv : the preprint server for biology · 2025
    Article
  4. Review
  5. Two cysteines control Tse1 secretion by H1-T6SS in Pseudomonas aeruginosa.Protein science : a publication of the Protein Society · 2025
    Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Type VI secretion systems promote intraspecific competition and host interactions in a bee gut symbiont.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. The Anti-Listeria Activity ofPathogens (Basel, Switzerland) · 2023
    Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. Article

75 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

2 authors.

Eric CascalesCNRS, Laboratoire d'Ingénierie des Systèmes Macromoléculaires, UMR 7255, Institut de Microbiologie de la Méditerranée, Aix-Marseille Université, 31 Chemin Joseph Aiguier, 13402 Marseille Cedex 20, France. cascales@imm.cnrs.fr
Christian Cambillau

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Type VI secretion systems (T6SSs) are transenvelope complexes specialized in the transport of proteins or domains directly into target cells. These systems are versatile as they can target either eukaryotic host cells and therefore modulate the bacteria-host interaction and pathogenesis or bacterial cells and therefore facilitate access to a specific niche. These molecular machines comprise at least 13 proteins. Although recent years have witnessed advances in the role and function of these secretion systems, little is known about how these complexes assemble in the cell envelope. Interestingly, the current information converges to the idea that T6SSs are composed of two subassemblies, one resembling the contractile bacteriophage tail, whereas the other subunits are embedded in the inner and outer membranes and anchor the bacteriophage-like structure to the cell envelope. In this review, we summarize recent structural information on individual T6SS components emphasizing the fact that T6SSs are composite systems, adapting subunits from various origins.

Indexed as

Bacterial Secretion SystemsBacterial ProteinsCell MembraneEscherichia coliEscherichia coli ProteinsLipopeptidesMembrane ProteinsModels, MolecularMolecular ChaperonesMultiprotein ComplexesPeriplasmProtein FoldingProtein Structure, TertiaryProtein TransportBacterial ProteinsBacterial Secretion SystemsEscherichia coli ProteinsLipopeptidesMembrane ProteinsMolecular ChaperonesMultiprotein ComplexesTssJ protein, E coli

Identifiers

PMID22411981
PMCPMC3297440

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.