Evidence map›Paper›PMID 27618209›Full record

ReviewMolecular microbiology2017

Atypical modes of bacterial histidine kinase signaling.

Jonathan W Willett, Sean Crosson

Abstract readReview
In one paragraph

Review in Molecular microbiology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
4.2field-weighted citation impact, top 6% 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

26 citing papers in PubMed, 35 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Review
  5. Review
  6. Mode of autophosphorylation in bacteriophytochromes RpBphP2 and RpBphP3.Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology · 2023
    Article
  7. Review
  8. Article
  9. Article
  10. Review
  11. Review
  12. Article
  13. Article
  14. NME/NM23/NDPK and Histidine Phosphorylation.International journal of molecular sciences · 2020
    Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. A universal stress protein inThe Journal of biological chemistry · 2020
    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 at 1 institution in 1 country.

Jonathan W WillettDepartment of Biochemistry and Molecular Biology, University of Chicago, Chicago, IL, USA.ORCID 0000-0002-5467-4145
Sean CrossonDepartment of Biochemistry and Molecular Biology, University of Chicago, Chicago, IL, USA.
Argonne National Laboratory · US

Funding

Intergrated control of Caulobacter cell physiology by visible light and stressR01GM087353 · NIGMS · UNIVERSITY OF CHICAGO · PI CROSSON, SEAN · 2009 to 2018
$2.8M
Molecular mechanism of general stress signaling in Brucella abortusR01AI107159 · NIAID · UNIVERSITY OF CHICAGO · PI CROSSON, SEAN · 2014 to 2018
$2.2M
Structural Analysis of a Conserved Alphaproteobacterial Stress Response PathwayF32GM109661 · NIGMS · UNIVERSITY OF CHICAGO · PI WILLETT, JONATHAN W · 2014 to 2016
$160k
NIAID NIH HHS R01 AI107159NIGMS NIH HHS F32 GM109661NIGMS NIH HHS R01 GM087353
6 · The paper itself

Abstract

The environment of a cell has a profound influence on its physiology, development and evolution. Accordingly, the capacity to sense and respond to physical and chemical signals in the environment is an important feature of cellular biology. In bacteria, environmental sensory perception is often regulated by two-component signal transduction systems (TCSTs). Canonical TCST entails signal-induced autophosphorylation of a sensor histidine kinase (HK) followed by phosphoryl transfer to a cognate response regulator (RR) protein, which may affect gene expression at multiple levels. Recent studies provide evidence for systems that do not adhere to this archetypal TCST signaling model. We present selected examples of atypical modes of signal transduction including inactivation of HK activity via homo- and hetero oligomerization, and cross-phosphorylation between HKs. These examples highlight mechanisms bacteria use to integrate environmental signals to control complex adaptive processes.

Indexed as

BacteriaBacterial ProteinsEvolution, MolecularHistidine KinasePhosphorylationResponse ElementsSignal TransductionBacterial ProteinsHistidine Kinase

Identifiers

PMID27618209
PMCPMC5218898
OpenAlexW2521107885

What OpenQuestion holds

Textmetadata
LicenceTDM
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.