Evidence map›Paper›PMID 10775270›Full record

ArticleThe EMBO journal2000

A small protein that mediates the activation of a two-component system by another two-component system.

L F Kox, M M Wösten, E A Groisman

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 134 papers.

0numbers the graph read from it
0cells of the map it votes in
134citing papers in PubMed
5.7field-weighted citation impact, top 4% 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

134 citing papers in PubMed, 265 citations in OpenAlex.

  1. Review
  2. Article
  3. Engineering low-endotoxin lipid A in a double auxotrophFrontiers in cellular and infection microbiology · 2026
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  4. Review
  5. Article
  6. Analysis of stress-induced small proteins inbioRxiv : the preprint server for biology · 2025
    Article
  7. Review
  8. Review
  9. Antibiotic resistance mediated by gene amplifications.npj antimicrobials and resistance · 2024
    Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. How Bacterial Pathogens Coordinate Appetite with Virulence.Microbiology and molecular biology reviews : MMBR · 2023
    Review
  15. Article
  16. Article
  17. Frontiers in microbiology · 2023
    Review
  18. TheMicrobiology spectrum · 2022
    Article
  19. Review
  20. Review

74 more citing papers are in PubMed but not listed here.

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.

L F KoxDepartment of Molecular Microbiology, Howard Hughes Medical Institute, Washington University School of Medicine, St Louis, MO 63110-1093, USA.
M M Wösten
E A Groisman
Howard Hughes Medical Institute · US

Funding

MOLECULAR AND STRUCTURAL BASES OF POLYMYXIN RESISTANCER01AI042236 · NIAID · YALE UNIVERSITY · PI GROISMAN, EDUARDO · 1998 to 2013
$3.0M
Co-opting ancestral regulatory systems to control bacterial virulenceR56AI042236 · NIAID · YALE UNIVERSITY · PI GROISMAN, EDUARDO · 2015 to 2015
$368k
NIAID NIH HHS AI42236NIAID NIH HHS R01 AI042236NIAID NIH HHS R56 AI042236
6 · The paper itself

Abstract

The PmrA-PmrB two-component system of Salmonella enterica controls resistance to the peptide antibiotic polymyxin B and to several antimicrobial proteins from human neutrophils. Transcription of PmrA-activated genes is induced by high iron, but can also be promoted by growth in low magnesium in a process that requires another two-component system, PhoP-PhoQ. Here, we define the genetic basis for the interaction between the PhoP-PhoQ and PmrA-PmrB systems. We have identified pmrD as a PhoP-activated gene that mediates the transcriptional activation of PmrA-regulated genes during growth in low magnesium. When transcription of pmrD is driven from a heterologous promoter, expression of PmrA-activated genes occurs even at repressing magnesium concentrations and becomes independent of the phoP and phoQ genes. The PmrD effect is specific for PmrA-regulated genes and requires functional PmrA and PmrB proteins. A pmrD mutant is sensitive to polymyxin if grown in low magnesium, but resistant if grown in high iron. The PmrD protein controls the activity of the PmrA-PmrB system at a post-transcriptional level.

Indexed as

Anti-Bacterial AgentsBacterial ProteinsBase SequenceDrug Resistance, MicrobialIronMagnesiumModels, BiologicalMolecular Sequence DataMutagenesisMutationPhosphorylationPlasmidsPolymyxinsProtein BindingRecombinant ProteinsRNA Processing, Post-TranscriptionalAnti-Bacterial AgentsBacterial ProteinsIronMagnesiumPhoP protein, BacteriaPhoQ protein, BacteriapmrA protein, BacteriaPmrB protein, bacteriaPolymyxinsRecombinant ProteinsSingle-Strand Specific DNA and RNA EndonucleasesTranscription Factors

Identifiers

PMID10775270
PMCPMC302009
OpenAlexW2157217625

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.