Evidence map›Paper›PMID 23150526›Full record

ArticleFASEB journal : official publication of the Federation of American Societies for Experimental Biology2013

Substrate specificity of Pasteurella multocida toxin for α subunits of heterotrimeric G proteins.

Joachim H C Orth, Ines Fester, Peter Siegert, Markus Weise, Ulrike Lanner, Shigeki Kamitani, Taro Tachibana, Brenda A Wilson, Andreas Schlosser, Yasuhiko Horiguchi and 1 more

Abstract read
In one paragraph

Article in FASEB journal : official publication of the Federation of American Societies for Experimental Biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
4.3field-weighted citation impact, top 5% 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

25 citing papers in PubMed, 42 citations in OpenAlex.

  1. CXCL8 Knockout: A Key to ResistingInternational journal of molecular sciences · 2024
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  2. Revealing the lethal effects ofFrontiers in microbiology · 2024
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  3. Review
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  5. In Vivo Targets ofInternational journal of molecular sciences · 2020
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  11. Review
  12. Article
  13. Frontiers in immunology · 2017
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  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

11 authors at 4 institutions in 3 countries.

Joachim H C OrthInstitut für Experimentelle und Klinische Pharmakologie und Toxikologie, Albert-Ludwigs-Universität Freiburg, Freiburg, Germany. joachim.orth@pharmakol.uni-freiburg.de
Ines Fester
Peter Siegert
Markus Weise
Ulrike Lanner
Shigeki Kamitani
Taro Tachibana
Brenda A Wilson
Andreas Schlosser
Yasuhiko Horiguchi
Klaus Aktories
University of Freiburg · DEOsaka University · JPOsaka City University · JPUrbana University · US

Funding

Pasteurella multocida toxin: Structure and ActivityR01AI038396 · NIAID · UNIVERSITY OF ILLINOIS URBANA-CHAMPAIGN · PI WILSON, BRENDA A. · 2004 to 2008
$1.7M
NIAID NIH HHS R01 AI038396NIAID NIH HHS R01-AI-038936
6 · The paper itself

Abstract

Pasteurella multocida is the causative agent of a number of epizootic and zoonotic diseases. Its major virulence factor associated with atrophic rhinitis in animals and dermonecrosis in bite wounds is P. multocida toxin (PMT). PMT stimulates signal transduction pathways downstream of heterotrimeric G proteins, leading to effects such as mitogenicity, blockade of apoptosis, or inhibition of osteoblast differentiation. On the basis of Gα(i2), it was demonstrated that the toxin deamidates an essential glutamine residue of the Gα(i2) subunit, leading to constitutive activation of the G protein. Here, we studied the specificity of PMT for its G-protein targets by mass spectrometric analyses and by utilizing a monoclonal antibody, which recognizes specifically G proteins deamidated by PMT. The studies revealed deamidation of 3 of 4 families of heterotrimeric G proteins (Gα(q/11), Gα(i1,2,3), and Gα(12/13) of mouse or human origin) by PMT but not by a catalytic inactive toxin mutant. With the use of G-protein fragments and chimeras of responsive or unresponsive G proteins, the structural basis for the discrimination of heterotrimeric G proteins was studied. Our results elucidate substrate specificity of PMT on the molecular level and provide evidence for the underlying structural reasons of substrate discrimination.

Indexed as

Amino Acid SequenceAmino Acid SubstitutionAnimalsBacterial ProteinsBacterial ToxinsBase SequenceBinding SitesCells, CulturedDNA, ComplementaryGlutamineGTP-Binding Protein alpha SubunitsGTP-Binding Protein alpha Subunits, Gi-GoGTP-Binding Protein alpha Subunits, Gq-G11HEK293 CellsHumansMiceBacterial ProteinsBacterial ToxinsDNA, ComplementaryGlutamineGTP-Binding Protein alpha SubunitsGTP-Binding Protein alpha Subunits, Gi-GoGTP-Binding Protein alpha Subunits, Gq-G11Pasteurella multocida toxinPeptide FragmentsRecombinant Fusion Proteins

Identifiers

PMID23150526
PMCPMC3545528
OpenAlexW2102426188

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.