Evidence map›Paper›PMID 18631239›Full record

ArticleMolecular microbiology2008

Characterization of CetA and CetB, a bipartite energy taxis system in Campylobacter jejuni.

Kathryn T Elliott, Victor J Dirita

Abstract read
In one paragraph

Article in Molecular microbiology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing 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

27 citing papers in PubMed.

  1. AcceleratingProceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  2. Review
  3. Article
  4. ThemBio · 2025
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. PAS domains in bacterial signal transduction.Current opinion in microbiology · 2021
    Review
  11. Review
  12. Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  13. Article
  14. Frontiers in microbiology · 2019
    Article
  15. Sensory Repertoire of Bacterial Chemoreceptors.Microbiology and molecular biology reviews : MMBR · 2017
    Review
  16. Review
  17. Article
  18. Article
  19. Article
  20. Chemotaxis in Campylobacter jejuni.European journal of microbiology & immunology · 2012
    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

2 authors.

Kathryn T ElliottDepartment of Microbiology and Immunology, University of Michigan, Ann Arbor, MI 48109, USA.
Victor J Dirita

Funding

Howard Hughes Medical Institute
6 · The paper itself

Abstract

The energy taxis receptor Aer, in Escherichia coli, senses changes in the redox state of the electron transport system via an flavin adenine dinucleotide cofactor bound to a PAS domain. The PAS domain (a sensory domain named after three proteins Per, ARNT and Sim, where it was first identified) is thought to interact directly with the Aer HAMP domain to transmit this signal to the highly conserved domain (HCD) found in chemotaxis receptors. An apparent energy taxis system in Campylobacter jejuni is composed of two proteins, CetA and CetB, that have the domains of Aer divided between them. CetB has a PAS domain, while CetA has a predicted transmembrane region, HAMP domain and the HCD. In this study, we examined the expression of cetA and cetB and the biochemical properties of the proteins they encode. cetA and cetB are co-transcribed independently of the flagellar regulon. CetA has two transmembrane helices in a helical hairpin while CetB is a peripheral membrane protein tightly associated with the membrane. CetB levels are CetA dependent. Additionally, we demonstrated that both CetA and CetB participate in complexes, including a likely CetB dimer and a complex that may include both CetA and CetB. This study provides a foundation for further characterization of signal transduction mechanisms within CetA/CetB.

Indexed as

Signal TransductionBacterial ProteinsCampylobacter jejuniChemotaxisFlagellaGene ExpressionMembrane ProteinsPeriplasmic ProteinsProtein Structure, TertiaryProtein TransportRegulonTranscription, GeneticBacterial ProteinsMembrane ProteinsPeriplasmic Proteins

Identifiers

PMID18631239
PMCPMC2628428

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

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.