Evidence map›Paper›PMID 30875878›Full record

ReviewInternational journal of molecular sciences2019

Toxins Utilize the Endoplasmic Reticulum-Associated Protein Degradation Pathway in Their Intoxication Process.

Jowita Nowakowska-Gołacka, Hanna Sominka, Natalia Sowa-Rogozińska, Monika Słomińska-Wojewódzka

Open access · goldAbstract readReview
In one paragraph

Review in International journal of molecular sciences, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
2.2field-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

25 citing papers in PubMed, 45 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Review
  5. Structural basis for neutralizing antibody binding to pertussis toxin.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  6. Structural Basis for Antibody Neutralization of Pertussis Toxin.bioRxiv : the preprint server for biology · 2024
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Viruses Hijack ERAD to Regulate Their Replication and Propagation.International journal of molecular sciences · 2022
    Review
  15. Article
  16. ABToxins · 2022
    Review
  17. Article
  18. Review
  19. Smuggle tau through a secret(ory) pathway.The Biochemical journal · 2021
    Article
  20. 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

4 authors at 1 institution in 1 country.

Jowita Nowakowska-GołackaDepartment of Medical Biology and Genetics, Faculty of Biology, University of Gdańsk, Wita Stwosza 59, 80-308 Gdańsk, Poland. jowita.nowakowska@phdstud.ug.edu.pl.
Hanna SominkaDepartment of Medical Biology and Genetics, Faculty of Biology, University of Gdańsk, Wita Stwosza 59, 80-308 Gdańsk, Poland. hanna.sominka@phdstud.ug.edu.pl.
Natalia Sowa-RogozińskaDepartment of Medical Biology and Genetics, Faculty of Biology, University of Gdańsk, Wita Stwosza 59, 80-308 Gdańsk, Poland. natalia.sowa@phdstud.ug.edu.pl.
Monika Słomińska-WojewódzkaDepartment of Medical Biology and Genetics, Faculty of Biology, University of Gdańsk, Wita Stwosza 59, 80-308 Gdańsk, Poland. monika.slominska@biol.ug.edu.pl.ORCID 0000-0001-6609-6381
Gdańsk Medical University · PL

Funding

Narodowe Centrum Nauki 2015/19/B/NZ3/03266
6 · The paper itself

Abstract

Several bacterial and plant AB-toxins are delivered by retrograde vesicular transport to the endoplasmic reticulum (ER), where the enzymatically active A subunit is disassembled from the holotoxin and transported to the cytosol. In this process, toxins subvert the ER-associated degradation (ERAD) pathway. ERAD is an important part of cellular regulatory mechanism that targets misfolded proteins to the ER channels, prior to their retrotranslocation to the cytosol, ubiquitination and subsequent degradation by a protein-degrading complex, the proteasome. In this article, we present an overview of current understanding of the ERAD-dependent transport of AB-toxins to the cytosol. We describe important components of ERAD and discuss their significance for toxin transport. Toxin recognition and disassembly in the ER, transport through ER translocons and finally cytosolic events that instead of overall proteasomal degradation provide proper folding and cytotoxic activity of AB-toxins are discussed as well. We also comment on recent reports presenting medical applications for toxin transport through the ER channels.

Indexed as

Endoplasmic Reticulum-Associated DegradationProteolysisCytosolEndoplasmic ReticulumHumansProteasome Endopeptidase ComplexProtein FoldingProtein TransportToxins, BiologicalUbiquitinationProteasome Endopeptidase ComplexToxins, BiologicalAB-toxinsendoplasmic reticulum (ER)ER-associated degradation (ERAD)

Identifiers

PMID30875878
PMCPMC6471375
OpenAlexW2922133411

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.