Evidence map›Paper›PMID 28937631›Full record

ArticleToxins2017

Cellular Entry of the Diphtheria Toxin Does Not Require the Formation of the Open-Channel State by Its Translocation Domain.

Alexey S Ladokhin, Mauricio Vargas-Uribe, Mykola V Rodnin, Chiranjib Ghatak, Onkar Sharma

Open access · goldAbstract read
In one paragraph

Article in Toxins, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
0.7field-weighted citation impact, top 32% 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

13 citing papers in PubMed, 15 citations in OpenAlex.

  1. Article
  2. Article
  3. Targeting the Inside of Cells with Biologicals: Toxin Routes in a Therapeutic Context.BioDrugs : clinical immunotherapeutics, biopharmaceuticals and gene therapy · 2023
    Review
  4. Article
  5. How Do Biomolecules Cross the Cell Membrane?Accounts of chemical research · 2022
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. 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

5 authors at 2 institutions in 1 country.

Alexey S LadokhinDepartment of Biochemistry and Molecular Biology, University of Kansas Medical Center, Kansas City, KS 66160, USA. aladokhin@kumc.edu.
Mauricio Vargas-UribeDepartment of Biochemistry and Molecular Biology, University of Kansas Medical Center, Kansas City, KS 66160, USA. mauricio.vargasu@gmail.com.
Mykola V RodninDepartment of Biochemistry and Molecular Biology, University of Kansas Medical Center, Kansas City, KS 66160, USA. mrodnin@kumc.edu.
Chiranjib GhatakDepartment of Biochemistry and Molecular Biology, University of Kansas Medical Center, Kansas City, KS 66160, USA. c.ghatak79@gmail.com.
Onkar SharmaDepartment of Microbiology and Immunobiology, Harvard Medical School, Boston, MA 02115, USA. Onkar_Sharma@hms.harvard.edu.
University of Kansas Medical Center · USHarvard University · US

Funding

Protein Structure Laboratory P30GM110761 · NIGMS · UNIVERSITY OF KANSAS LAWRENCE · PI HANZLIK, ROBERT P · 2014 to 2018
$5.6M
NIGMS NIH HHS P30 GM110761
6 · The paper itself

Abstract

Cellular entry of diphtheria toxin is a multistage process involving receptor targeting, endocytosis, and translocation of the catalytic domain across the endosomal membrane into the cytosol. The latter is ensured by the translocation (T) domain of the toxin, capable of undergoing conformational refolding and membrane insertion in response to the acidification of the endosomal environment. While numerous now classical studies have demonstrated the formation of an ion-conducting conformation-the Open-Channel State (OCS)-as the final step of the refolding pathway, it remains unclear whether this channel constitutes an in vivo translocation pathway or is a byproduct of the translocation. To address this question, we measure functional activity of known OCS-blocking mutants with H-to-Q replacements of

Indexed as

Catalytic DomainDiphtheria ToxinEndocytosisHistidineIntracellular MembranesMutant ProteinsProtein ConformationDiphtheria ToxinHistidineMutant Proteinsbilayer insertiondepth-dependent fluorescence quenchingmembrane translocationpH-dependent refoldingtryptophan fluorescence

Identifiers

PMID28937631
PMCPMC5666346
OpenAlexW2758060015

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.