Evidence map›Paper›PMID 27930316›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2016

Structural basis for glutathione-mediated activation of the virulence regulatory protein PrfA in Listeria.

Michael Hall, Christin Grundström, Afshan Begum, Mikael J Lindberg, Uwe H Sauer, Fredrik Almqvist, Jörgen Johansson, A Elisabeth Sauer-Eriksson

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.

0numbers the graph read from it
0cells of the map it votes in
54citing papers in PubMed
13.9field-weighted citation impact, top 1% 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

54 citing papers in PubMed, 91 citations in OpenAlex.

  1. Review
  2. Article
  3. Listeria monocytogenes: from a saprophytic to a cytosolic virulent pathogen.World journal of microbiology & biotechnology · 2025
    Review
  4. Article
  5. Article
  6. Article
  7. Comparative Analysis ofMicroorganisms · 2025
    Article
  8. Long-chain unsaturated free fatty acids reduce the host cell invasion ofFrontiers in cellular and infection microbiology · 2025
    Article
  9. Article
  10. Article
  11. Article
  12. Infection and immunity · 2024
    Article
  13. Diverse roles of low-molecular weight thiol GSH inCurrent research in microbial sciences · 2024
    Article
  14. Microbiology spectrum · 2023
    Article
  15. How Bacterial Pathogens Coordinate Appetite with Virulence.Microbiology and molecular biology reviews : MMBR · 2023
    Review
  16. Review
  17. Article
  18. Human Listeriosis.Clinical microbiology reviews · 2023
    Review
  19. Article
  20. Microorganisms · 2022
    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

8 authors at 1 institution in 1 country.

Michael HallDepartment of Chemistry, Umeå University, 901 87 Umeå, Sweden.
Christin GrundströmDepartment of Chemistry, Umeå University, 901 87 Umeå, Sweden.
Afshan BegumDepartment of Chemistry, Umeå University, 901 87 Umeå, Sweden.
Mikael J LindbergDepartment of Chemistry, Umeå University, 901 87 Umeå, Sweden.
Uwe H SauerDepartment of Chemistry, Umeå University, 901 87 Umeå, Sweden.
Fredrik AlmqvistDepartment of Chemistry, Umeå University, 901 87 Umeå, Sweden.
Jörgen JohanssonUmeå Centre for Microbial Research, Umeå University, 901 87 Umeå, Sweden.
A Elisabeth Sauer-ErikssonDepartment of Chemistry, Umeå University, 901 87 Umeå, Sweden; elisabeth.sauer-eriksson@umu.se.
Umeå University · SE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Infection by the human bacterial pathogen Listeria monocytogenes is mainly controlled by the positive regulatory factor A (PrfA), a member of the Crp/Fnr family of transcriptional activators. Published data suggest that PrfA requires the binding of a cofactor for full activity, and it was recently proposed that glutathione (GSH) could fulfill this function. Here we report the crystal structures of PrfA in complex with GSH and in complex with GSH and its cognate DNA, the hly operator PrfA box motif. These structures reveal the structural basis for a GSH-mediated allosteric mode of activation of PrfA in the cytosol of the host cell. The crystal structure of PrfA

Indexed as

Amino Acid MotifsBacterial ProteinsCrystallography, X-RayDNA, BacterialGene Expression Regulation, BacterialGlutathioneGlycineListeria monocytogenesPeptide Termination FactorsProtein BindingProtein MultimerizationTrans-ActivatorsTranscription FactorsVirulenceBacterial ProteinsDNA, BacterialGlutathioneGlycinePeptide Termination FactorsPrfA protein, Listeria monocytogenesTrans-ActivatorsTranscription FactorsactivationglutathioneListeriaPrfAvirulence

Identifiers

PMID27930316
PMCPMC5187702
OpenAlexW2559749948

What OpenQuestion holds

Textmetadata
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.