Evidence map›Paper›PMID 26839186›Full record

ArticleScientific reports2016

A novel Hsp70 inhibitor prevents cell intoxication with the actin ADP-ribosylating Clostridium perfringens iota toxin.

Katharina Ernst, Markus Liebscher, Sebastian Mathea, Anton Granzhan, Johannes Schmid, Michel R Popoff, Heiko Ihmels, Holger Barth, Cordelia Schiene-Fischer

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

19 citing papers in PubMed, 33 citations in OpenAlex.

  1. Review
  2. Review
  3. Domperidone InhibitsToxins · 2023
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  7. Review
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  10. Heat Shock Proteins in Lymphoma Immunotherapy.Frontiers in immunology · 2021
    Review
  11. Review
  12. Article
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  16. Review
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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

9 authors at 4 institutions in 2 countries.

Katharina ErnstInstitute of Pharmacology and Toxicology, University of Ulm Medical Center, Ulm, Germany.
Markus LiebscherMax Planck Research Unit for Enzymology of Protein Folding Halle, Halle (Saale), Germany.
Sebastian MatheaMax Planck Research Unit for Enzymology of Protein Folding Halle, Halle (Saale), Germany.
Anton GranzhanDepartment of Chemistry and Biology, University of Siegen, Germany.
Johannes SchmidInstitute of Pharmacology and Toxicology, University of Ulm Medical Center, Ulm, Germany.
Michel R PopoffDepartment of Anaerobic Bacteria, Pasteur Institute, Paris, France.
Heiko IhmelsDepartment of Anaerobic Bacteria, Pasteur Institute, Paris, France.
Holger BarthInstitute of Pharmacology and Toxicology, University of Ulm Medical Center, Ulm, Germany.
Cordelia Schiene-FischerMax Planck Research Unit for Enzymology of Protein Folding Halle, Halle (Saale), Germany.
Max Planck Research Unit for Enzymology of Protein Folding · DEUniversität Ulm · DEInstitut Pasteur · FRUniversity of Siegen · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Hsp70 family proteins are folding helper proteins involved in a wide variety of cellular pathways. Members of this family interact with key factors in signal transduction, transcription, cell-cycle control, and stress response. Here, we developed the first Hsp70 low molecular weight inhibitor specifically targeting the peptide binding site of human Hsp70. After demonstrating that the inhibitor modulates the Hsp70 function in the cell, we used the inhibitor to show for the first time that the stress-inducible chaperone Hsp70 functions as molecular component for entry of a bacterial protein toxin into mammalian cells. Pharmacological inhibition of Hsp70 protected cells from intoxication with the binary actin ADP-ribosylating iota toxin from Clostridium perfringens, the prototype of a family of enterotoxins from pathogenic Clostridia and inhibited translocation of its enzyme component across cell membranes into the cytosol. This finding offers a starting point for novel therapeutic strategies against certain bacterial toxins.

Indexed as

ADP Ribose TransferasesAnimalsApoptosisBacterial ToxinsBinding SitesCell LineCell SurvivalChlorocebus aethiopsHEK293 CellsHeLa CellsHSP70 Heat-Shock ProteinsHT29 CellsHumansSmall Molecule LibrariesVero CellsADP Ribose TransferasesBacterial ToxinsHSP70 Heat-Shock Proteinsiota toxin, Clostridium perfringensSmall Molecule Libraries

Identifiers

PMID26839186
PMCPMC4738285
OpenAlexW2401505531

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.