Evidence map›Paper›PMID 21687664›Full record

ArticlePloS one2011

Extending the aerolysin family: from bacteria to vertebrates.

Pawel Szczesny, Ioan Iacovache, Anna Muszewska, Krzysztof Ginalski, F Gisou van der Goot, Marcin Grynberg

Abstract read
In one paragraph

Article in PloS one, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 74 papers.

0numbers the graph read from it
0cells of the map it votes in
74citing 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

74 citing papers in PubMed.

  1. Article
  2. Review
  3. Aerolysin-like proteins fromFrontiers in fungal biology · 2026
    Article
  4. ThemBio · 2025
    Article
  5. A Comprehensive Structural and Functional Analysis ofbioRxiv : the preprint server for biology · 2025
    Article
  6. Chimerolectins: Classification, structural architecture, and functional perspectives.Protein science : a publication of the Protein Society · 2025
    Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Structure of theProceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  13. Horizontal gene transfer underlies the painful stings of asp caterpillars (Lepidoptera: Megalopygidae).Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Interaction ofToxins · 2022
    Article
  19. Article
  20. Article

14 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

6 authors.

Pawel SzczesnyInstitute of Biochemistry and Biophysics, Polish Academy of Sciences, Warsaw, Poland.
Ioan Iacovache
Anna Muszewska
Krzysztof Ginalski
F Gisou van der Goot
Marcin Grynberg

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A number of bacterial virulence factors have been observed to adopt structures similar to that of aerolysin, the principal toxin of Aeromonas species. However, a comprehensive description of architecture and structure of the aerolysin-like superfamily has not been determined. In this study, we define a more compact aerolysin-like domain--or aerolysin fold--and show that this domain is far more widely spread than anticipated since it can be found throughout kingdoms. The aerolysin-fold could be found in very diverse domain and functional contexts, although a toxic function could often be assigned. Due to this diversity, the borders of the superfamily could not be set on a sequence level. As a border-defining member, we therefore chose pXO2-60--a protein from the pathogenic pXO2 plasmid of Bacillus anthracis. This fascinating protein, which harbors a unique ubiquitin-like fold domain at the C-terminus of the aerolysin-domain, nicely illustrates the diversity of the superfamily. Its putative role in the virulence of B. anthracis and its three dimensional model are discussed.

Indexed as

BacteriaVertebratesAmino Acid SequenceAnimalsBacterial ToxinsConserved SequenceHumansModels, MolecularMolecular Sequence DataPore Forming Cytotoxic ProteinsProtein Structure, TertiarySequence AlignmentSpecies SpecificityaerolysinBacterial ToxinsPore Forming Cytotoxic Proteins

Identifiers

PMID21687664
PMCPMC3110756

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.