Evidence map›Paper›PMID 24967582›Full record

ArticlePloS one2014

Vimentin mediates uptake of C3 exoenzyme.

Astrid Rohrbeck, Anke Schröder, Sandra Hagemann, Andreas Pich, Markus Höltje, Gudrun Ahnert-Hilger, Ingo Just

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2014. 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
2.1field-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

19 citing papers in PubMed, 36 citations in OpenAlex.

  1. Peptide-Incorporated Biomaterials Promote Regeneration of Peripheral Nerve Injuries.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
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  5. Secreted Phospholipases AInternational journal of biological sciences · 2022
    Review
  6. Article
  7. Article
  8. Review
  9. Article
  10. Lentiviral Vector-Mediated Expression of Exoenzyme C3 Transferase Lowers Intraocular Pressure in Monkeys.Molecular therapy : the journal of the American Society of Gene Therapy · 2019
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Cell Entry of C3 Exoenzyme from Clostridium botulinum.Current topics in microbiology and immunology
    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

7 authors at 2 institutions in 1 country.

Astrid RohrbeckInstitute of Toxicology, Hannover Medical School, Charité-Universitätsmedizin Berlin, Germany.
Anke SchröderInstitute of Toxicology, Hannover Medical School, Charité-Universitätsmedizin Berlin, Germany.
Sandra HagemannInstitute of Toxicology, Hannover Medical School, Charité-Universitätsmedizin Berlin, Germany.
Andreas PichInstitute of Toxicology, Hannover Medical School, Charité-Universitätsmedizin Berlin, Germany.
Markus HöltjeCenter for Anatomy, Functional Cell Biology, Charité-Universitätsmedizin Berlin, Germany.
Gudrun Ahnert-HilgerCenter for Anatomy, Functional Cell Biology, Charité-Universitätsmedizin Berlin, Germany.
Ingo JustInstitute of Toxicology, Hannover Medical School, Charité-Universitätsmedizin Berlin, Germany.
Charité - Universitätsmedizin Berlin · DEMedizinische Hochschule Hannover · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Clostridium botulinum C3 exoenzyme (C3) selectively inactivates RhoA/B/C GTPases by ADP-ribosylation. Based on this substrate specificity C3 is a well-established tool in cell biology. C3 is taken up by eukaryotic cells although lacking an uptake and translocation domain. Based on different approaches vimentin was identified as membranous C3-interaction partner by mass spectrometry. Vimentin in fact was partly localized at the outer surface of hippocampal HT22 cells and J744A.1 macrophages. Domain analysis identified the rod domain as binding partner of C3. Vimentin was also involved in uptake of C3 as shown by knock down of vimentin in HT22 and J774A.1 cells. The involvement of vimentin in uptake of C3 was further supported by the findings that the vimentin disruptor acrylamide blocked uptake of C3. Vimentin is not only a major organizing element of the intermediate filament network but is also involved in both binding and uptake of C3 exoenzyme.

Indexed as

ADP Ribose TransferasesAnimalsBotulinum ToxinsCarrier ProteinsCell LineCell MembraneGene ExpressionGene Knockdown TechniquesMiceProtein BindingProtein Interaction Domains and MotifsProtein Interaction MappingRecombinant ProteinsRNA InterferenceRNA, Small InterferingVimentinADP Ribose TransferasesBotulinum ToxinsCarrier Proteinsexoenzyme C3, Clostridium botulinumRecombinant ProteinsRNA, Small InterferingVimentin

Identifiers

PMID24967582
PMCPMC4072758
OpenAlexW2022185453

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.