Evidence map›Paper›PMID 9380671›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1997

The Aer protein and the serine chemoreceptor Tsr independently sense intracellular energy levels and transduce oxygen, redox, and energy signals for Escherichia coli behavior.

A Rebbapragada, M S Johnson, G P Harding, A J Zuccarelli, H M Fletcher, I B Zhulin, B L Taylor

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 141 papers.

0numbers the graph read from it
0cells of the map it votes in
141citing papers in PubMed
5.7field-weighted citation impact, top 3% 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

141 citing papers in PubMed, 272 citations in OpenAlex.

  1. Article
  2. ZnbioRxiv : the preprint server for biology · 2026
    Article
  3. Signaling mechanism of the transmembrane energy receptor Aer.bioRxiv : the preprint server for biology · 2026
    Article
  4. Article
  5. Review
  6. Insights into Chemoreceptor MCP2201-Sensing D-Malate.International journal of molecular sciences · 2025
    Article
  7. ThemBio · 2025
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Multistep Signaling in Nature: A Close-Up ofInternational journal of molecular sciences · 2021
    Review
  18. Review
  19. Article
  20. PAS domains in bacterial signal transduction.Current opinion in microbiology · 2021
    Review

81 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

7 authors at 1 institution in 1 country.

A RebbapragadaDepartment of Microbiology and Molecular Genetics, School of Medicine, Loma Linda University, Loma Linda, CA 92350, USA.
M S Johnson
G P Harding
A J Zuccarelli
H M Fletcher
I B Zhulin
B L Taylor
Loma Linda University · US

Funding

SENSORY TRANSDUCTION IN BACTERIAR01GM029481 · NIGMS · LOMA LINDA UNIVERSITY · PI TAYLOR, BARRY L · 1985 to 2011
$2.9M
NIGMS NIH HHS GM29481NIGMS NIH HHS R01 GM029481
6 · The paper itself

Abstract

We identified a protein, Aer, as a signal transducer that senses intracellular energy levels rather than the external environment and that transduces signals for aerotaxis (taxis to oxygen) and other energy-dependent behavioral responses in Escherichia coli. Domains in Aer are similar to the signaling domain in chemotaxis receptors and the putative oxygen-sensing domain of some transcriptional activators. A putative FAD-binding site in the N-terminal domain of Aer shares a consensus sequence with the NifL, Bat, and Wc-1 signal-transducing proteins that regulate gene expression in response to redox changes, oxygen, and blue light, respectively. A double mutant deficient in aer and tsr, which codes for the serine chemoreceptor, was negative for aerotaxis, redox taxis, and glycerol taxis, each of which requires the proton motive force and/or electron transport system for signaling. We propose that Aer and Tsr sense the proton motive force or cellular redox state and thereby integrate diverse signals that guide E. coli to environments where maximal energy is available for growth.

Indexed as

Escherichia coli ProteinsSignal TransductionAmino Acid SequenceBacterial ProteinsCarrier ProteinsChemotaxisEscherichia coliIntercellular Signaling Peptides and ProteinsMembrane ProteinsMolecular Sequence DataOxidation-ReductionOxygenSequence Homology, Amino AcidAer protein, E coliBacterial ProteinsCarrier ProteinsEscherichia coli ProteinsIntercellular Signaling Peptides and ProteinsMembrane ProteinsOxygenTsr protein, Bacteria

Identifiers

PMID9380671
PMCPMC23396
OpenAlexW2090381756

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.