Evidence map›Paper›PMID 34680156›Full record

ReviewBiomolecules2021

Diversity in Sensing and Signaling of Bacterial Sensor Histidine Kinases.

Eiji Ishii, Yoko Eguchi

Abstract readReview
In one paragraph

Review in Biomolecules, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
–field-weighted citation impact
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

38 citing papers in PubMed.

  1. Review
  2. Review
  3. Review
  4. Article
  5. Article
  6. Development of covalent inhibitors for bacterial histidine kinases.Chemical communications (Cambridge, England) · 2026
    Article
  7. Programming Next-Generation Synthetic Biosensors by Genetic Circuit Design.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Review
  8. Protein-centric mechanisms of typhoidalFrontiers in cellular and infection microbiology · 2026
    Review
  9. Article
  10. Review
  11. Article
  12. Article
  13. Genome Mining ofBiomolecules · 2025
    Article
  14. Article
  15. Review
  16. Review
  17. Article
  18. Review
  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

2 authors.

Eiji IshiiDepartment of Bacterial Infections, Research Institute for Microbial Diseases, Osaka University, Osaka 565-0871, Japan.
Yoko EguchiFaculty of Biology-Oriented Science and Technology, Kindai University, Kinokawa 649-6493, Japan.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Two-component signal transduction systems (TCSs) are widely conserved in bacteria to respond to and adapt to the changing environment. Since TCSs are also involved in controlling the expression of virulence, biofilm formation, quorum sensing, and antimicrobial resistance in pathogens, they serve as candidates for novel drug targets. TCSs consist of a sensor histidine kinase (HK) and its cognate response regulator (RR). Upon perception of a signal, HKs autophosphorylate their conserved histidine residues, followed by phosphotransfer to their partner RRs. The phosphorylated RRs mostly function as transcriptional regulators and control the expression of genes necessary for stress response. HKs sense their specific signals not only in their extracytoplasmic sensor domain but also in their cytoplasmic and transmembrane domains. The signals are sensed either directly or indirectly via cofactors and accessory proteins. Accumulating evidence shows that a single HK can sense and respond to multiple signals in different domains. The underlying molecular mechanisms of how HK activity is controlled by these signals have been extensively studied both biochemically and structurally. In this article, we introduce the wide diversity of signal perception in different domains of HKs, together with their recently clarified structures and molecular mechanisms.

Indexed as

BacteriaBiofilmsCytoplasmHistidineHistidine KinasePhosphorylationProtein DomainsProtein Processing, Post-TranslationalQuorum SensingSignal TransductionVirulenceHistidineHistidine Kinaseautophosphorylationenvironmental signal sensinghistidine kinaseintramembrane sensingligand bindingPASphosphatasetwo-component signal transduction system

Identifiers

PMID34680156
PMCPMC8534201

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.