Evidence map›Paper›PMID 21569202›Full record

ReviewThe FEBS journal2011

Cellular and molecular action of the mitogenic protein-deamidating toxin from Pasteurella multocida.

Brenda A Wilson, Mengfei Ho

Abstract readReview
In one paragraph

Review in The FEBS journal, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
3.3field-weighted citation impact, top 10% 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

20 citing papers in PubMed, 23 citations in OpenAlex.

  1. Article
  2. Oral and intestinal bacterial exotoxins: Potential linked to carcinogenesis.Progress in molecular biology and translational science · 2020
    Review
  3. Pasteurella multocida: Genotypes and Genomics.Microbiology and molecular biology reviews : MMBR · 2019
    Review
  4. Article
  5. Is submucosal fat injection effective in atrophic rhinitis? An experimental animal study.European archives of oto-rhino-laryngology : official journal of the European Federation of Oto-Rhino-Laryngological Societies (EUFOS) : affiliated with the German Society for Oto-Rhino-Laryngology - Head and Neck Surgery · 2017
    Article
  6. Article
  7. Frontiers in immunology · 2017
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Review
  15. Article
  16. Article
  17. Structure of the catalytic domain of the Salmonella virulence factor SseI.Acta crystallographica. Section D, Biological crystallography · 2012
    Article
  18. Article
  19. Article
  20. Review
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 at 1 institution in 1 country.

Brenda A WilsonDepartment of Microbiology and Host-Microbe Systems Theme of the Institute for Genomic Biology, University of Illinois at Urbana-Champaign, Urbana, IL 61801, USA. bawilson@life.illinois.edu
Mengfei Ho
University of Illinois Urbana-Champaign · US

Funding

Pasteurella multocida toxin: Structure and ActivityR01AI038396 · NIAID · UNIVERSITY OF ILLINOIS URBANA-CHAMPAIGN · PI WILSON, BRENDA A. · 2004 to 2008
$1.7M
PASTEURELLA MULTOCIDA TOXIN--STRUCTURE AND ACTIVITYR29AI038396 · NIAID · WRIGHT STATE UNIVERSITY · PI WILSON, BRENDA A. · 1996 to 2000
$105k
NIAID NIH HHS AI038396NIAID NIH HHS R01 AI038396NIAID NIH HHS R29 AI038396
6 · The paper itself

Abstract

The mitogenic toxin from Pasteurella multocida (PMT) is a member of the dermonecrotic toxin family, which includes toxins from Bordetella, Escherichia coli and Yersinia. Members of the dermonecrotic toxin family modulate G-protein targets in host cells through selective deamidation and/or transglutamination of a critical active site Gln residue in the G-protein target, which results in the activation of intrinsic GTPase activity. Structural and biochemical data point to the uniqueness of PMT among these toxins in its structure and action. Whereas the other dermonecrotic toxins act on small Rho GTPases, PMT acts on the α subunits of heterotrimeric G(q) -, G(i) - and G(12/13) -protein families. To date, experimental evidence supports a model in which PMT potently stimulates various mitogenic and survival pathways through the activation of G(q) and G(12/13) signaling, ultimately leading to cellular proliferation, whilst strongly inhibiting pathways involved in cellular differentiation through the activation of G(i) signaling. The resulting cellular outcomes account for the global physiological effects observed during infection with toxinogenic P. multocida, and hint at potential long-term sequelae that may result from PMT exposure.

Indexed as

AdipogenesisBacterial ToxinsCell ProliferationCyclic AMPCytotoxinsGTP-Binding ProteinsMitosisOsteogenesisPasteurella InfectionsPasteurella multocidarho GTP-Binding ProteinsSignal TransductionSubstrate SpecificityBacterial ToxinsCyclic AMPCytotoxinsGTP-Binding Proteinsrho GTP-Binding Proteins

Identifiers

PMID21569202
PMCPMC3166354
OpenAlexW1488612260

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.