Evidence map›Paper›PMID 31374212›Full record

ReviewBiochimica et biophysica acta. Biomembranes2020

Regulation of the chemotaxis histidine kinase CheA: A structural perspective.

Alise R Muok, Ariane Briegel, Brian R Crane

Abstract readReview
In one paragraph

Review in Biochimica et biophysica acta. Biomembranes, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing 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

39 citing papers in PubMed.

  1. Signaling mechanism of the transmembrane energy receptor Aer.bioRxiv : the preprint server for biology · 2026
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  6. Microorganisms · 2025
    Review
  7. Article
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  13. A flagellar accessory protein links chemotaxis to surface sensing.bioRxiv : the preprint server for biology · 2024
    Article
  14. Article
  15. Article
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  18. Bacterial chemoreceptor signaling complexes control kinase activity by stabilizing the catalytic domain of CheA.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  19. Article
  20. Review
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.

Alise R MuokInstitute for Biology, Leiden University, Sylviusweg 72, 2333 BE Leiden, the Netherlands.
Ariane BriegelInstitute for Biology, Leiden University, Sylviusweg 72, 2333 BE Leiden, the Netherlands.
Brian R CraneDepartment of Chemistry and Chemical Biology, Cornell University, Ithaca, NY 14850, United States of America. Electronic address: bc69@cornell.edu.

Funding

Molecular Mechanisms of Signal Transduction Involving Light, Redox and Transmembrane ComplexesR35GM122535 · NIGMS · CORNELL UNIVERSITY · PI BRIAN R CRANE · 2017 to 2026
$7.1M
NIGMS NIH HHS R35 GM122535
6 · The paper itself

Abstract

Bacteria sense and respond to their environment through a highly conserved assembly of transmembrane chemoreceptors (MCPs), the histidine kinase CheA, and the coupling protein CheW, hereafter termed "the chemosensory array". In recent years, great strides have been made in understanding the architecture of the chemosensory array and how this assembly engenders sensitive and cooperative responses. Nonetheless, a central outstanding question surrounds how receptors modulate the activity of the CheA kinase, the enzymatic output of the sensory system. With a focus on recent advances, we summarize the current understanding of array structure and function to comment on the molecular mechanism by which CheA, receptors and CheW generate the high sensitivity, gain and dynamic range emblematic of bacterial chemotaxis. The complexity of the chemosensory arrays has motivated investigation with many different approaches. In particular, structural methods, genetics, cellular activity assays, nanodisc technology and cryo-electron tomography have provided advances that bridge length scales and connect molecular mechanism to cellular function. Given the high degree of component integration in the chemosensory arrays, we ultimately aim to understand how such networked molecular interactions generate a whole that is truly greater than the sum of its parts. This article is part of a Special Issue entitled: Molecular biophysics of membranes and membrane proteins.

Indexed as

ChemotaxisBacterial ProteinsEscherichia coli ProteinsHistidine KinaseMethyl-Accepting Chemotaxis ProteinsModels, MolecularBacterial ProteinscheA protein, E coliEscherichia coli ProteinsHistidine KinaseMethyl-Accepting Chemotaxis ProteinsEnzymologyHistidine kinaseMembrane proteinsPhosphorelayProtein structureSignal transduction

Identifiers

PMID31374212
PMCPMC7212787

What OpenQuestion holds

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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.