Evidence map›Paper›PMID 17704177›Full record

ArticleBiophysical journal2007

High-resolution structure of a Na+/H+ antiporter dimer obtained by pulsed electron paramagnetic resonance distance measurements.

D Hilger, Y Polyhach, E Padan, H Jung, G Jeschke

Abstract read
In one paragraph

Article in Biophysical journal, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing 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

46 citing papers in PubMed.

  1. Article
  2. Protein Modeling with DEER Spectroscopy.Annual review of biophysics · 2025
    Review
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Sub-Micromolar Pulse Dipolar EPR Spectroscopy Reveals Increasing CuAngewandte Chemie (International ed. in English) · 2019
    Article
  18. Article
  19. The contribution of modern EPR to structural biology.Emerging topics in life sciences · 2018
    Article
  20. MMM: A toolbox for integrative structure modeling.Protein science : a publication of the Protein Society · 2018
    Article
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

5 authors.

D HilgerLudwig-Maximilians-Universität München, Department Biologie I, D-80638 Munich, Germany.
Y Polyhach
E Padan
H Jung
G Jeschke

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Transient or partial formation of complexes between biomacromolecules is a general mechanism used to control cellular functions. Several of these complexes escape structure determination by crystallographic means. We developed a new approach for determining the structure of protein dimers in the native environment (e.g., in the membrane) with high resolution in cases where the structure of the two monomers is known. The approach is based on measurements of distance distributions between spin labels in the range between 2 and 6 nanometers by a pulsed electron paramagnetic resonance technique and explicit modeling of spin label conformations. By applying this method to the membrane protein homodimer of the Na(+)/H(+) antiporter NhaA of Escherichia coli, the structure of the presumably physiological dimer was determined. It reveals two points of contact between the two monomers, with one of them confirming results of earlier cross-linking experiments.

Indexed as

AllelesBinding SitesCryoelectron MicroscopyCysteineDatabases, ProteinDimerizationElectron Spin Resonance SpectroscopyEscherichia coliEscherichia coli ProteinsHydrogen-Ion ConcentrationModels, StatisticalMolecular ConformationMutagenesis, Site-DirectedProtein ConformationSodium-Hydrogen ExchangersCysteineEscherichia coli ProteinsNhaA protein, E coliSodium-Hydrogen Exchangers

Identifiers

PMID17704177
PMCPMC2072073

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.