Evidence map›Paper›PMID 17158704›Full record

ReviewMicrobiology and molecular biology reviews : MMBR2006

Stimulus perception in bacterial signal-transducing histidine kinases.

Thorsten Mascher, John D Helmann, Gottfried Unden

Open access · greenAbstract readReview
In one paragraph

Review in Microbiology and molecular biology reviews : MMBR, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 358 papers.

0numbers the graph read from it
0cells of the map it votes in
358citing papers in PubMed
25.2field-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

358 citing papers in PubMed, 701 citations in OpenAlex.

  1. Trial
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  12. Structural modeling reveals the allosteric switch controlling the chitin utilization program ofProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  13. Review
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  15. Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

298 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 3 institutions in 2 countries.

Thorsten MascherDepartment of General Microbiology, Georg-August-University, Grisebachstr. 8, D-37077 Göttingen, Germany. tmasche@gwdg.de
John D Helmann
Gottfried Unden
Cornell University · USJohannes Gutenberg University Mainz · DEUniversity of Göttingen · DE

Funding

STRUCTURAL STUDIES OF BACILLUS SUBTILIS SIGMA FACTORSR01GM047446 · NIGMS · CORNELL UNIVERSITY ITHACA · PI HELMANN, JOHN D · 1992 to 2016
$6.7M
NIGMS NIH HHS GM047446NIGMS NIH HHS R01 GM047446
6 · The paper itself

Abstract

Two-component signal-transducing systems are ubiquitously distributed communication interfaces in bacteria. They consist of a histidine kinase that senses a specific environmental stimulus and a cognate response regulator that mediates the cellular response, mostly through differential expression of target genes. Histidine kinases are typically transmembrane proteins harboring at least two domains: an input (or sensor) domain and a cytoplasmic transmitter (or kinase) domain. They can be identified and classified by virtue of their conserved cytoplasmic kinase domains. In contrast, the sensor domains are highly variable, reflecting the plethora of different signals and modes of sensing. In order to gain insight into the mechanisms of stimulus perception by bacterial histidine kinases, we here survey sensor domain architecture and topology within the bacterial membrane, functional aspects related to this topology, and sequence and phylogenetic conservation. Based on these criteria, three groups of histidine kinases can be differentiated. (i) Periplasmic-sensing histidine kinases detect their stimuli (often small solutes) through an extracellular input domain. (ii) Histidine kinases with sensing mechanisms linked to the transmembrane regions detect stimuli (usually membrane-associated stimuli, such as ionic strength, osmolarity, turgor, or functional state of the cell envelope) via their membrane-spanning segments and sometimes via additional short extracellular loops. (iii) Cytoplasmic-sensing histidine kinases (either membrane anchored or soluble) detect cellular or diffusible signals reporting the metabolic or developmental state of the cell. This review provides an overview of mechanisms of stimulus perception for members of all three groups of bacterial signal-transducing histidine kinases.

Indexed as

Bacterial Physiological PhenomenaBacterial ProteinsHistidine KinaseProtein KinasesSignal TransductionBacterial ProteinsHistidine KinaseProtein Kinases

Identifiers

PMID17158704
PMCPMC1698512
OpenAlexW2107093868

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.