Evidence map›Paper›PMID 18936178›Full record

ArticleInfection and immunity2009

The cytoplasmic domain of anthrax toxin receptor 1 affects binding of the protective antigen.

Mandy Y Go, Edith M C Chow, Jeremy Mogridge

Abstract read
In one paragraph

Article in Infection and immunity, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
1.9field-weighted citation impact, top 14% 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

24 citing papers in PubMed, 34 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Cell autonomous ANTXR1-mediated regulation of extracellular matrix components in primary fibroblasts.Matrix biology : journal of the International Society for Matrix Biology · 2017
    Article
  6. Article
  7. Article
  8. Calpain-dependent cytoskeletal rearrangement exploited for anthrax toxin endocytosis.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  9. Article
  10. Review
  11. Review
  12. Anthrax toxin protective antigen--insights into molecular switching from prepore to pore.Protein science : a publication of the Protein Society · 2012
    Review
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. Receptors of anthrax toxin and cell entry.Molecular aspects of medicine · 2009
    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

3 authors at 1 institution in 1 country.

Mandy Y GoDepartment of Laboratory Medicine and Pathobiology, Medical Sciences Building, Rm. 6308, 1 King's College Circle, University of Toronto, Toronto, ON, Canada M5S 1A8.
Edith M C Chow
Jeremy Mogridge
University of Toronto · CA

Funding

Characterization of Anthrax Lethal ToxinR01AI067683 · NIAID · UNIVERSITY OF TORONTO · PI MOGRIDGE, JEREMY S · 2006 to 2010
$1.3M
NIAID NIH HHS R01 AI067683
6 · The paper itself

Abstract

The protective antigen (PA) component of anthrax toxin binds the I domain of the receptor ANTXR1. Integrin I domains convert between open and closed conformations that bind ligand with high and low affinities, respectively; this process is regulated by signaling from the cytoplasmic domains. To assess whether intracellular signals might influence the interaction between ANTXR1 and PA, we compared two splice variants of ANTXR1 that differ only in their cytoplasmic domains. We found that cells expressing ANTXR1 splice variant 1 (ANTXR1-sv1) bound markedly less PA than did cells expressing a similar level of the shorter splice variant ANTXR1-sv2. ANTXR1-sv1 but not ANTXR1-sv2 associated with the actin cytoskeleton, although disruption of the cytoskeleton did not affect binding of ANTXR-sv1 to PA. Introduction of a cytoplasmic domain missense mutation found in the related receptor ANTXR2 in a patient with juvenile hyaline fibromatosis impaired actin association and increased binding of PA to ANTXR1-sv1. These results suggest that ANTXR1 has two affinity states that may be modulated by cytoplasmic signals.

Indexed as

Amino Acid SubstitutionAnimalsAntigens, BacterialBacterial ToxinsCHO CellsCricetinaeCricetulusMutagenesis, Site-DirectedMutation, MissenseProtein BindingProtein Structure, TertiaryReceptors, Peptideanthrax toxinanthrax toxin receptorsAntigens, BacterialBacterial ToxinsReceptors, Peptide

Identifiers

PMID18936178
PMCPMC2612287
OpenAlexW2169386966

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.