Evidence map›Paper›PMID 23169659›Full record

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

Mechanism for adaptive remodeling of the bacterial flagellar switch.

Pushkar P Lele, Richard W Branch, Vedhavalli S J Nathan, Howard C Berg

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 60 papers.

0numbers the graph read from it
0cells of the map it votes in
60citing 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

60 citing papers in PubMed.

  1. Article
  2. Article
  3. The dynamic response of the bacterial flagellar motor to its direct intracellular input signal.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  4. Article
  5. Article
  6. Review
  7. Reassessing the Standard Chemotaxis Framework for Understanding Biased Migration inAnnual review of chemical and biomolecular engineering · 2024
    Review
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Bacterial motility: machinery and mechanisms.Nature reviews. Microbiology · 2022
    Review
  15. Review
  16. Review
  17. Article
  18. Article
  19. Review
  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

4 authors.

Pushkar P LeleDepartment of Molecular and Cellular Biology, Harvard University, Cambridge, MA 02138, USA.
Richard W Branch
Vedhavalli S J Nathan
Howard C Berg

Funding

SENSORY TRANSDUCTION IN BACTERIAL CHEMOTAXISR01AI016478 · NIAID · HARVARD UNIVERSITY · PI BERG, HOWARD C · 1985 to 2019
$14.1M
SENSORY TRANSDUCTION IN BACTERIAL CHEMOTAXISR37AI016478 · NIAID · HARVARD UNIVERSITY · PI BERG, HOWARD C · 1990 to 1999
–
NIAID NIH HHS AI016478NIAID NIH HHS R01 AI016478NIAID NIH HHS R37 AI016478
6 · The paper itself

Abstract

The bacterial flagellar motor has been shown in previous work to adapt to changes in the steady-state concentration of the chemotaxis signaling molecule, CheY-P, by changing the FliM content. We show here that the number of FliM molecules in the motor and the fraction of FliM molecules that exchange depend on the direction of flagellar rotation, not on CheY-P binding per se. Our results are consistent with a model in which the structural differences associated with the direction of rotation modulate the strength of FliM binding. When the motor spins counterclockwise, FliM binding strengthens, the fraction of FliM molecules that exchanges decreases, and the ring content increases. The larger number of CheY-P binding sites enhances the motor's sensitivity, i.e., the motor adapts. An interesting unresolved question is how additional copies of FliM might be accommodated.

Indexed as

Models, ChemicalBacterial ProteinsEscherichia coliEscherichia coli ProteinsFlagellaFluorescence Recovery After PhotobleachingMembrane ProteinsMethyl-Accepting Chemotaxis ProteinsMicroscopy, FluorescenceMolecular Motor ProteinsProtein BindingRotationBacterial ProteinscheY protein, E coliEscherichia coli ProteinsFliM protein, BacteriaMembrane ProteinsMethyl-Accepting Chemotaxis ProteinsMolecular Motor Proteins

Identifiers

PMID23169659
PMCPMC3523824

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.