Evidence map›Paper›PMID 32195198›Full record

ReviewFrontiers in cellular and infection microbiology2020

Diverse Localization and Protein Binding Abilities of Glyceraldehyde-3-Phosphate Dehydrogenase in Pathogenic Bacteria: The Key to its Multifunctionality?

Monika Kopeckova, Ivona Pavkova, Jiri Stulik

Open access · goldAbstract readReview
In one paragraph

Review in Frontiers in cellular and infection microbiology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
6.3field-weighted citation impact, top 3% 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

26 citing papers in PubMed, 58 citations in OpenAlex.

  1. Article
  2. Article
  3. The return of metabolism: biochemistry and physiology of glycolysis.Biological reviews of the Cambridge Philosophical Society · 2026
    Review
  4. Article
  5. Article
  6. Secretome Profiling ofAntibiotics (Basel, Switzerland) · 2026
    Article
  7. Article
  8. Roles and mechanisms ofVirulence · 2025
    Article
  9. Review
  10. TargetingVaccines · 2024
    Review
  11. Article
  12. Glyceraldehyde 3-Phosphate Dehydrogenase on the Surface ofInternational journal of molecular sciences · 2024
    Article
  13. Article
  14. Article
  15. SubcutaneousJournal of veterinary science · 2023
    Article
  16. Sticking to the Subject: Multifunctionality in Microbial Adhesins.Journal of fungi (Basel, Switzerland) · 2023
    Review
  17. Cells · 2023
    Article
  18. Article
  19. Article
  20. 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

3 authors at 1 institution in 1 country.

Monika KopeckovaDepartment of Molecular Pathology and Biology, Faculty of Military Health Science, University of Defence, Hradec Kralove, Czechia.
Ivona PavkovaDepartment of Molecular Pathology and Biology, Faculty of Military Health Science, University of Defence, Hradec Kralove, Czechia.
Jiri StulikDepartment of Molecular Pathology and Biology, Faculty of Military Health Science, University of Defence, Hradec Kralove, Czechia.
University of Defence · CZ

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Bacterial proteins exhibiting two or more unrelated functions, referred to as moonlighting proteins, are suggested to contribute to full virulence manifestation in pathogens. An expanding number of published studies have revealed the glycolytic enzyme glyceraldehyde-3-phosphate dehydrogenase (GAPDH) to be a multitasking protein with virulence impact in a number of pathogenic bacteria. This protein can be detected on the bacterial surface or outside the bacterial cell, where it interacts with host proteins. In this way, GAPDH is able to modulate various pathogenic processes. Moreover, it has been shown to be involved in non-enzymatic processes inside the bacterial cell. In this mini review, we summarize main findings concerning the multiple localization and protein interactions of GAPDH derived from bacterial pathogens of humans. We also briefly discuss problems associated with using GAPDH as a vaccine antigen and endeavor to inspire further research to fill gaps in the existing knowledge.

Indexed as

BacteriaBacterial InfectionsBacterial ProteinsBacterial VaccinesGlyceraldehyde-3-Phosphate DehydrogenasesHumansProtein BindingProteinsVirulenceBacterial ProteinsBacterial VaccinesGlyceraldehyde-3-Phosphate DehydrogenasesProteinsglyceraldehyde-3-phosphate dehydrogenaselocalizationmoonlighting proteinspathogenic bacteriaprotein-protein interaction (PPI)

Identifiers

PMID32195198
PMCPMC7062713
OpenAlexW3010555380

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.