Evidence map›Paper›PMID 30008469›Full record

ReviewNature reviews. Microbiology2018

Structural insights into the signalling mechanisms of two-component systems.

Françoise Jacob-Dubuisson, Ariel Mechaly, Jean-Michel Betton, Rudy Antoine

Abstract readReview
PubMed Publisher
In one paragraph

Review in Nature reviews. Microbiology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 166 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
166citing papers in PubMed, 1 pooled it
17.4field-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

166 citing papers in PubMed, 1 synthesis or guideline pooled it, 315 citations in OpenAlex.

  1. Meta-analysis of caries microbiome studies can improve upon disease prediction outcomes.APMIS : acta pathologica, microbiologica, et immunologica Scandinavica · 2022
    Pooled it
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Plant-Derived Melatonin Inhibits Bacterial Virulence via CpxA/R Two-Component System.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Article
  8. Structural and functional insights into the Rcs phosphorelay.bioRxiv : the preprint server for biology · 2026
    Article
  9. Article
  10. Article
  11. Hijacking competitor-derived signals: RcsB/C drivesApplied and environmental microbiology · 2026
    Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Review
  17. Article
  18. Article
  19. Review
  20. Review

106 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

4 authors at 1 institution in 1 country.

Françoise Jacob-DubuissonUniversité de Lille, CNRS, INSERM, CHU Lille, Institut Pasteur de Lille, U1019-UMR 8204 - Center for Infection and Immunity of Lille, Lille, France. francoise.jacob@ibl.cnrs.fr.ORCID http://orcid.org/0000-0002-5102-1704
Ariel MechalyInstitut Pasteur, Plateforme de Cristallographie, CNRS-UMR3528, Paris, France.
Jean-Michel BettonInstitut Pasteur, Unité de Microbiologie Structurale, CNRS-UMR3528, Paris, France.
Rudy AntoineUniversité de Lille, CNRS, INSERM, CHU Lille, Institut Pasteur de Lille, U1019-UMR 8204 - Center for Infection and Immunity of Lille, Lille, France.
Centre National de la Recherche Scientifique · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Two-component systems reprogramme diverse aspects of microbial physiology in response to environmental cues. Canonical systems are composed of a transmembrane sensor histidine kinase and its cognate response regulator. They catalyse three reactions: autophosphorylation of the histidine kinase, transfer of the phosphoryl group to the regulator and dephosphorylation of the phosphoregulator. Elucidating signal transduction between sensor and output domains is highly challenging given the size, flexibility and dynamics of histidine kinases. However, recent structural work has provided snapshots of the catalytic mechanisms of the three enzymatic reactions and described the conformation and dynamics of the enzymatic moiety in the kinase-competent and phosphatase-competent states. Insight into signalling mechanisms across the membrane is also starting to emerge from new crystal structures encompassing both sensor and transducer domains of sensor histidine kinases. In this Progress article, we highlight such important advances towards understanding at the molecular level the signal transduction mechanisms mediated by these fascinating molecular machines.

Indexed as

Bacterial ProteinsHistidine KinaseBacteriaCytoplasmModels, MolecularPhosphorylationSignal TransductionBacterial ProteinsHistidine Kinase

Identifiers

PMID30008469
OpenAlexW2884502717

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.