Evidence map›Paper›PMID 21895797›Full record

ReviewMolecular microbiology2011

Negative control in two-component signal transduction by transmitter phosphatase activity.

TuAnh Ngoc Huynh, Valley Stewart

Open access · bronzeAbstract readReview
In one paragraph

Review in Molecular microbiology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 68 papers.

0numbers the graph read from it
0cells of the map it votes in
68citing papers in PubMed
3.9field-weighted citation impact, top 6% 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

68 citing papers in PubMed, 118 citations in OpenAlex.

  1. Article
  2. Two-Component Systems inVeterinary sciences · 2025
    Review
  3. Review
  4. Article
  5. AProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  6. Review
  7. ThemBio · 2025
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Transcriptomics ofFrontiers in bioengineering and biotechnology · 2023
    Article
  16. Article
  17. Role of Two-Component System Networks in Pseudomonas aeruginosa Pathogenesis.Advances in experimental medicine and biology · 2022
    Article
  18. Review
  19. Article
  20. Review

8 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.

TuAnh Ngoc HuynhFood Science Graduate Group Department of Microbiology, University of California, Davis, California, USA.
Valley Stewart
University of California, Davis · US

Funding

GENETIC CONTROL OF NITRATE RESPIRATION IN E. COLIR01GM036877 · NIGMS · UNIVERSITY OF CALIFORNIA DAVIS · PI STEWART, VALLEY J. · 1986 to 2010
$2.4M
NIGMS NIH HHS GM036877NIGMS NIH HHS R01 GM036877
6 · The paper itself

Abstract

Bifunctional sensor transmitter modules of two-component systems exert both positive and negative control on the receiver domain of the cognate response regulator. In negative control, the transmitter module accelerates the rate of phospho-receiver dephosphorylation. This transmitter phosphatase reaction serves the important physiological functions of resetting response regulator phosphorylation level and suppressing cross-talk. Although the biochemical reactions underlying positive control are reasonably well understood, the mechanism for transmitter phosphatase activity has been unknown. A recent hypothesis is that the transmitter phosphatase reaction is catalysed by a conserved Gln, Asn or Thr residue, via a hydrogen bond between the amide or hydroxyl group and the nucleophilic water molecule in acyl-phosphate hydrolysis. This hypothetical mechanism closely resembles the established mechanisms of auxiliary phosphatases such as CheZ and CheX, and may be widely conserved in two-component signal transduction. In addition to the proposed catalytic residues, transmitter phosphatase activity also requires the correct transmitter conformation and appropriate interactions with the receiver. Evidence suggests that the phosphatase-competent and autokinase-competent states are mutually exclusive, and the corresponding negative and positive activities are likely to be reciprocally regulated through dynamic control of transmitter conformations.

Indexed as

Down-RegulationSignal TransductionBacteriaBacterial ProteinsPhosphoric Monoester HydrolasesBacterial ProteinsPhosphoric Monoester Hydrolases

Identifiers

PMID21895797
PMCPMC3192241
OpenAlexW2145187544

What OpenQuestion holds

Textmetadata
LicenceTDM
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.