Evidence map›Paper›PMID 17217957›Full record

ArticleJournal of molecular biology2007

Physical responses of bacterial chemoreceptors.

Ady Vaknin, Howard C Berg

Open access · greenAbstract read
In one paragraph

Article in Journal of molecular biology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 62 papers.

0numbers the graph read from it
0cells of the map it votes in
62citing papers in PubMed
4.5field-weighted citation impact, top 5% 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

62 citing papers in PubMed, 89 citations in OpenAlex.

  1. Article
  2. Article
  3. Signal integration in chemoreceptor complexes.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  4. Article
  5. A nonequilibrium allosteric model for receptor-kinase complexes: The role of energy dissipation in chemotaxis signaling.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  6. Review
  7. Article
  8. A traveling-wave solution for bacterial chemotaxis with growth.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  9. Article
  10. Article
  11. Article
  12. Conformational shifts in a chemoreceptor helical hairpin control kinase signaling inProceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  13. Article
  14. Article
  15. Article
  16. The Role of Adaptation in Bacterial Speed Races.PLoS computational biology · 2016
    Article
  17. Information processing in bacteria: memory, computation, and statistical physics: a key issues review.Reports on progress in physics. Physical Society (Great Britain) · 2016
    Review
  18. The source of high signal cooperativity in bacterial chemosensory arrays.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  19. Article
  20. Article

2 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

2 authors at 1 institution in 1 country.

Ady VakninDepartment of Molecular and Cellular Biology, Harvard University, Cambridge, MA 02138, USA.
Howard C Berg
Harvard University · US

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

Chemoreceptors of the bacterium Escherichia coli are thought to form trimers of homodimers that undergo conformational changes upon ligand binding and thereby signal a cytoplasmic kinase. We monitored the physical responses of trimers in living cells lacking other chemotaxis proteins by fluorescently tagging receptors and measuring changes in fluorescence anisotropy. These changes were traced to changes in energy transfer between fluorophores on different dimers of a trimer: attractants move these fluorophores farther apart, and repellents move them closer together. These measurements allowed us to define the responses of bare receptor oligomers to ligand binding and compare them to the corresponding response in kinase activity. Receptor responses could be fit by a simple "two-state" model in which receptor dimers are in either active or inactive conformations, from which energy bias and dissociation constants could be estimated. Comparison with responses in kinase-activity indicated that higher-order interactions are dominant in receptor clusters.

Indexed as

ChemotaxisAnisotropyBacterial ProteinsChemoreceptor CellsDimerizationEscherichia coli K12Fluorescence PolarizationFluorescence Resonance Energy TransferLigandsMembrane ProteinsModels, ChemicalProtein BindingReceptors, Amino AcidReceptors, Cell SurfaceSignal TransductionBacterial ProteinsLigandsMembrane ProteinsReceptors, Amino AcidReceptors, Cell Surface

Identifiers

PMID17217957
PMCPMC1849981
OpenAlexW2084110947

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.