Evidence map›Paper›PMID 36558830›Full record

ArticlePathogens (Basel, Switzerland)2022

14-3-3 Activated Bacterial Exotoxins AexT and ExoT Share Actin and the SH2 Domains of CRK Proteins as Targets for ADP-Ribosylation.

Carmen Ebenwaldner, Peter Hornyak, Antonio Ginés García-Saura, Archimede Torretta, Saber Anoosheh, Anders Hofer, Herwig Schüler

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Pathogens (Basel, Switzerland), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.3field-weighted citation impact, top 44% 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

4 citing papers in PubMed, 4 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. PARP14 is a writer, reader, and eraser of mono-ADP-ribosylation.The Journal of biological chemistry · 2023
    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

7 authors at 3 institutions in 1 country.

Carmen EbenwaldnerCenter for Molecular Protein Science (CMPS), Department of Chemistry, Lund University, 22100 Lund, Sweden.ORCID 0000-0002-7919-2994
Peter HornyakDepartment of Biosciences, Karolinska Institutet, 14157 Huddinge, Sweden.
Antonio Ginés García-SauraCenter for Molecular Protein Science (CMPS), Department of Chemistry, Lund University, 22100 Lund, Sweden.
Archimede TorrettaCenter for Molecular Protein Science (CMPS), Department of Chemistry, Lund University, 22100 Lund, Sweden.
Saber AnooshehDepartment of Medical Biochemistry and Biophysics, Umeå University, 90736 Umeå, Sweden.
Anders HoferDepartment of Medical Biochemistry and Biophysics, Umeå University, 90736 Umeå, Sweden.
Herwig SchülerCenter for Molecular Protein Science (CMPS), Department of Chemistry, Lund University, 22100 Lund, Sweden.ORCID 0000-0003-4059-3501
Lund University · SEUmeå University · SEKarolinska Institutet · SE

Funding

Crafoord Foundation 2019-4871Swedish Research Council 2019-4871
6 · The paper itself

Abstract

Bacterial exotoxins with ADP-ribosyltransferase activity can be divided into distinct clades based on their domain organization. Exotoxins from several clades are known to modify actin at Arg177; but of the 14-3-3 dependent exotoxins only

Indexed as

14-3-3 activated bacterial exotoxinsactinADP-ribosylationAeromonas salmonicidprotein refoldingPseudomonas aeruginosatype III secretion system

Identifiers

PMID36558830
PMCPMC9787417
OpenAlexW4311961295

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.