Evidence map›Paper›PMID 25426803›Full record

ArticleeLife2014

Structure and transport mechanism of the sodium/proton antiporter MjNhaP1.

Cristina Paulino, David Wöhlert, Ekaterina Kapotova, Özkan Yildiz, Werner Kühlbrandt

Open access · goldAbstract read
In one paragraph

Article in eLife, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.

0numbers the graph read from it
0cells of the map it votes in
57citing papers in PubMed
5.4field-weighted citation impact, top 4% 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

57 citing papers in PubMed, 92 citations in OpenAlex.

  1. Cryo-EM structure of human NaNature communications · 2026
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  4. Structure and Inhibition of the Human NaInternational journal of molecular sciences · 2025
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  5. PIPNature communications · 2025
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  6. Structure and mechanism of the KNature communications · 2024
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  7. Review
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  14. Article
  15. Article
  16. Article
  17. Allosteric links between the hydrophilic N-terminus and transmembrane core of human NaProtein science : a publication of the Protein Society · 2022
    Article
  18. Article
  19. Article
  20. Prokaryotic NaInternational journal of molecular sciences · 2022
    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

5 authors at 1 institution in 1 country.

Cristina PaulinoDepartment of Structural Biology, Max Planck Institute of Biophysics, Frankfurt am Main, Germany.
David WöhlertDepartment of Structural Biology, Max Planck Institute of Biophysics, Frankfurt am Main, Germany.
Ekaterina KapotovaDepartment of Structural Biology, Max Planck Institute of Biophysics, Frankfurt am Main, Germany.
Özkan YildizDepartment of Structural Biology, Max Planck Institute of Biophysics, Frankfurt am Main, Germany.
Werner KühlbrandtDepartment of Structural Biology, Max Planck Institute of Biophysics, Frankfurt am Main, Germany.
Max Planck Institute of Biophysics · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Sodium/proton antiporters are essential for sodium and pH homeostasis and play a major role in human health and disease. We determined the structures of the archaeal sodium/proton antiporter MjNhaP1 in two complementary states. The inward-open state was obtained by x-ray crystallography in the presence of sodium at pH 8, where the transporter is highly active. The outward-open state was obtained by electron crystallography without sodium at pH 4, where MjNhaP1 is inactive. Comparison of both structures reveals a 7° tilt of the 6 helix bundle. (22)Na(+) uptake measurements indicate non-cooperative transport with an activity maximum at pH 7.5. We conclude that binding of a Na(+) ion from the outside induces helix movements that close the extracellular cavity, open the cytoplasmic funnel, and result in a ∼5 Å vertical relocation of the ion binding site to release the substrate ion into the cytoplasm.

Indexed as

Cell MembraneCrystallography, X-RayMethanocaldococcusModels, MolecularMutant ProteinsProtein BindingProtein MultimerizationProtein Structure, SecondaryProtein TransportSodiumSodium-Hydrogen ExchangersSubstrate SpecificityMutant ProteinsSodiumSodium-Hydrogen Exchangersbiochemistrybiophysicselectron cryo-microscopymembrane transportMethanocaldococcus jannaschiisodium/proton antiportstructural biologytransport mechanismx-ray crystallography

Identifiers

PMID25426803
PMCPMC4381896
OpenAlexW2037562571

What OpenQuestion holds

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LicenceCC BY
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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.