Evidence map›Paper›PMID 22355139›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2012

Bacterial chemoreceptor arrays are hexagonally packed trimers of receptor dimers networked by rings of kinase and coupling proteins.

Ariane Briegel, Xiaoxiao Li, Alexandrine M Bilwes, Kelly T Hughes, Grant J Jensen, Brian R Crane

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 174 papers.

0numbers the graph read from it
0cells of the map it votes in
174citing 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

174 citing papers in PubMed.

  1. Distinct roles of PilI and ChpC inApplied and environmental microbiology · 2026
    Article
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  4. Review
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  10. Microorganisms · 2025
    Review
  11. Article
  12. Review
  13. Review
  14. A chemoreceptor conformational equilibrium controlled by signaling inputs.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Article
  20. Signal integration in chemoreceptor complexes.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article

114 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

6 authors.

Ariane BriegelDivision of Biology, California Institute of Technology, Pasadena, CA 91125, USA.
Xiaoxiao Li
Alexandrine M Bilwes
Kelly T Hughes
Grant J Jensen
Brian R Crane

Funding

The Structure and Function of the Bacterial ChemosomeR01GM066775 · NIGMS · CORNELL UNIVERSITY ITHACA · PI CRANE, BRIAN R · 2003 to 2016
$4.3M
Howard Hughes Medical InstituteNIGMS NIH HHS GM066775NIGMS NIH HHS R01 GM066775
6 · The paper itself

Abstract

Chemoreceptor arrays are supramolecular transmembrane machines of unknown structure that allow bacteria to sense their surroundings and respond by chemotaxis. We have combined X-ray crystallography of purified proteins with electron cryotomography of native arrays inside cells to reveal the arrangement of the component transmembrane receptors, histidine kinases (CheA) and CheW coupling proteins. Trimers of receptor dimers lie at the vertices of a hexagonal lattice in a "two-facing-two" configuration surrounding a ring of alternating CheA regulatory domains (P5) and CheW couplers. Whereas the CheA kinase domains (P4) project downward below the ring, the CheA dimerization domains (P3) link neighboring rings to form an extended, stable array. This highly interconnected protein architecture underlies the remarkable sensitivity and cooperative nature of transmembrane signaling in bacterial chemotaxis.

Indexed as

Bacillus subtilisBacterial Physiological PhenomenaBacterial ProteinsChemoreceptor CellsChemotaxisCrystallizationCrystallography, X-RayCytoplasmDimerizationElectron Microscope TomographyEscherichia coliEscherichia coli ProteinsHistidine KinaseMembrane ProteinsMethyl-Accepting Chemotaxis ProteinsProtein BindingBacterial ProteinscheA protein, E coliCheW protein, E coliEscherichia coli ProteinsHistidine KinaseMembrane ProteinsMethyl-Accepting Chemotaxis Proteins

Identifiers

PMID22355139
PMCPMC3309718

What OpenQuestion holds

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Registered trials

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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.