Evidence map›Paper›PMID 15102823›Full record

ArticleInfection and immunity2004

The host cell chaperone Hsp90 is necessary for cytotoxic action of the binary iota-like toxins.

Gerd Haug, Klaus Aktories, Holger Barth

Open access · greenAbstract read
In one paragraph

Article in Infection and immunity, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
1.0field-weighted citation impact, top 25% 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

34 citing papers in PubMed, 72 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Domperidone InhibitsToxins · 2023
    Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Proline Isomerization as a Key Determinant for Hsp90-Toxin Interactions.Frontiers in cellular and infection microbiology · 2021
    Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. The chaperonin TRiC/CCT is essential for the action of bacterial glycosylating protein toxins likeProceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  16. Article
  17. Article
  18. Review
  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

3 authors at 1 institution in 1 country.

Gerd HaugInstitut für Experimentelle und Klinische Pharmakologie und Toxikologie, Albert-Ludwigs-Universität Freiburg, D-79104 Freiburg, Germany.
Klaus Aktories
Holger Barth
University of Freiburg · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The heat shock protein Hsp90 is essential for uptake of the binary actin ADP-ribosylating toxins Clostridium perfringens iota-toxin and Clostridium difficile transferase into eukaryotic cells. Inhibition of Hsp90 by its specific inhibitor radicicol delayed intoxication of Vero cells by these toxins. A common Hsp90-dependent mechanism for their translocation is discussed.

Indexed as

ADP Ribose TransferasesAnimalsBacterial ToxinsChlorocebus aethiopsClostridioides difficileClostridium perfringensHSP90 Heat-Shock ProteinsLactonesMacrolidesVero CellsADP Ribose TransferasesBacterial ToxinsHSP90 Heat-Shock Proteinsiota toxin, Clostridium perfringensLactonesMacrolidesmonorden

Identifiers

PMID15102823
PMCPMC387881
OpenAlexW2098644179

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.