Evidence map›Paper›PMID 19217390›Full record

ArticleStructure (London, England : 1993)2009

Structural analysis of ligand stimulation of the histidine kinase NarX.

Jonah Cheung, Wayne A Hendrickson

Open access · bronzeAbstract read
In one paragraph

Article in Structure (London, England : 1993), 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 79 papers.

0numbers the graph read from it
0cells of the map it votes in
79citing papers in PubMed
6.9field-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

79 citing papers in PubMed, 141 citations in OpenAlex.

  1. Article
  2. Structure-informed engineering of plant-microbe interactions.The Plant journal : for cell and molecular biology · 2026
    Review
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  4. Article
  5. Article
  6. A Designed ZnJournal of the American Chemical Society · 2025
    Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Crystal structures of QseE and QseG: elements of a three-component system from Escherichia coli.Acta crystallographica. Section F, Structural biology communications · 2023
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. Review

19 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 2 institutions in 1 country.

Jonah CheungDepartment of Biochemistry and Molecular Biophysics, Columbia University, New York, NY 10032, USA.
Wayne A Hendrickson
Columbia University · USHoward Hughes Medical Institute · US

Funding

ANOMALOUS-SCATTERING STUDIES OF MACROMOLECULAR STRUCTURER37GM034102 · NIGMS · COLUMBIA UNIV NEW YORK MORNINGSIDE · PI HENDRICKSON, WAYNE A. · 1994 to 2003
$1.4M
ANOMALOUS-SCATTERING STUDIES OF PROTEIN STRUCTURER01GM034102 · NIGMS · COLUMBIA UNIV NEW YORK MORNINGSIDE · PI HENDRICKSON, WAYNE A. · 1985 to 2008
$1.3M
Howard Hughes Medical InstituteNIGMS NIH HHS GM34102NIGMS NIH HHS R01 GM034102NIGMS NIH HHS R37 GM034102
6 · The paper itself

Abstract

Histidine kinase receptors are a large family of membrane-spanning proteins found in many prokaryotes and some eukaryotes. They are a part of two-component signal transduction systems, which each comprise a sensor kinase and a response regulator and are involved with the regulation of many cellular processes. NarX is a histidine kinase receptor that responds to nitrate and nitrite to effect regulation of anaerobic respiration in various bacteria. We present high-resolution X-ray crystal structures of the periplasmic sensor domain from Escherichia coli NarX in a complex with nitrate and in the apo state. Our analysis reveals that nitrate-binding induces conformation changes that result in a piston-type displacement between the N- and C-terminal helices of the periplasmic domain. Such conformational changes might represent a conserved mechanism of signaling in histidine kinases by which ligand binding is communicated across the lipid bilayer.

Indexed as

LigandsAmino Acid SequenceBinding SitesCrystallography, X-RayEnzyme ActivationEscherichia coliEscherichia coli ProteinsHistidine KinaseModels, MolecularMolecular Sequence DataNitratesProtein FoldingProtein KinasesProtein MultimerizationProtein Structure, QuaternaryProtein Structure, TertiaryEscherichia coli ProteinsHistidine KinaseLigandsnarX protein, E coliNitratesProtein Kinases

Identifiers

PMID19217390
PMCPMC3749045
OpenAlexW2041844212

What OpenQuestion holds

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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.