Evidence map›Paper›PMID 22040088›Full record

ArticleMolecular microbiology2011

Ubiquitin and ubiquitin-modified proteins activate the Pseudomonas aeruginosa T3SS cytotoxin, ExoU.

David M Anderson, Katherine M Schmalzer, Hiromi Sato, Monika Casey, Scott S Terhune, Arthur L Haas, Jimmy B Feix, Dara W Frank

Open access · bronzeAbstract read
In one paragraph

Article in Molecular microbiology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 64 papers.

0numbers the graph read from it
0cells of the map it votes in
64citing papers in PubMed
4.8field-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

64 citing papers in PubMed, 85 citations in OpenAlex.

  1. Article
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  3. cUMP elicits interendothelial gap formation duringAmerican journal of physiology. Lung cellular and molecular physiology · 2024
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  4. Evidence for intracellularJournal of bacteriology · 2024
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  8. Cells · 2023
    Review
  9. Catheter-associated urinary tract infection byProceedings of the National Academy of Sciences of the United States of America · 2022
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  10. ThemBio · 2022
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  11. Article
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  13. UtilizingBiochemistry and biophysics reports · 2022
    Article
  14. Article
  15. Role of Host and Bacterial Lipids inFrontiers in immunology · 2022
    Review
  16. Perspectives on theToxins · 2021
    Review
  17. Article
  18. Article
  19. Article
  20. Article

4 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 2 institutions in 1 country.

David M AndersonDepartment of Microbiology and Molecular Genetics, Medical College of Wisconsin, Milwaukee, WI 53226, USA.
Katherine M Schmalzer
Hiromi Sato
Monika Casey
Scott S Terhune
Arthur L Haas
Jimmy B Feix
Dara W Frank
Medical College of Wisconsin · USLouisiana State University Health Sciences Center New Orleans · US

Funding

Activity of Pseudomonas Type III ToxinsR01AI049577 · NIAID · MEDICAL COLLEGE OF WISCONSIN · PI FRANK, DARA W. · 2001 to 2011
$3.6M
NIAID NIH HHS AI49577NIAID NIH HHS R01 AI049577
6 · The paper itself

Abstract

Pseudomonas aeruginosa is an opportunistic Gram-negative pathogen that possesses a type III secretion system (T3SS) critical for evading innate immunity and establishing acute infections in compromised patients. Our research has focused on the structure-activity relationships of ExoU, the most toxic and destructive type III effector produced by P. aeruginosa. ExoU possesses phospholipase activity, which is detectable in vitro only when a eukaryotic cofactor is provided with membrane substrates. We report here that a subpopulation of ubiquitylated yeast SOD1 and other ubiquitylated mammalian proteins activate ExoU. Phospholipase activity was detected using purified ubiquitin of various chain lengths and linkage types; however, free monoubiquitin is sufficient in a genetically engineered dual expression system. The use of ubiquitin by a bacterial enzyme as an activator is unprecedented and represents a new aspect in the manipulation of the eukaryotic ubiquitin system to facilitate bacterial replication and dissemination.

Indexed as

Bacterial Secretion SystemsAnimalsBacterial ProteinsCattleCell LineEnzyme ActivatorsHumansLeukocidinsPseudomonas aeruginosaPseudomonas InfectionsSuperoxide DismutaseSuperoxide Dismutase-1UbiquitinBacterial ProteinsBacterial Secretion SystemsEnzyme ActivatorsLeukocidinsPseudomonas aeruginosa Cytotoxinspseudomonas exoprotein A protein, Pseudomonas aeruginosaSOD1 protein, humanSuperoxide DismutaseSuperoxide Dismutase-1Ubiquitin

Identifiers

PMID22040088
PMCPMC3237844
OpenAlexW1539422958

What OpenQuestion holds

Textmetadata
LicenceTDM
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.