Evidence map›Paper›PMID 24473071›Full record

ArticleeLife2014

pH- and sodium-induced changes in a sodium/proton antiporter.

Cristina Paulino, 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 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

17 citing papers in PubMed, 31 citations in OpenAlex.

  1. Article
  2. Crystal structure of the NaNature communications · 2022
    Article
  3. The Remaining Conundrum of the Role of the NaReviews in cardiovascular medicine · 2022
    Review
  4. Forty years in cryoEM of membrane proteins.Microscopy (Oxford, England) · 2022
    Article
  5. Article
  6. The change of intracellular zinc distribution after strong acid challenge.International journal of physiology, pathophysiology and pharmacology · 2021
    Article
  7. Structural and Functional Changes in the NaInternational journal of molecular sciences · 2019
    Review
  8. Article
  9. Article
  10. Article
  11. Dissecting the proton transport pathway in electrogenic NaProceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  12. Simulating the Function of the MjNhaP1 Transporter.The journal of physical chemistry. B · 2016
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. 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

2 authors at 1 institution in 1 country.

Cristina PaulinoDepartment of Structural Biology, Max Planck Institute of Biophysics, Frankfurt am Main, Germany.
Werner Kühlbrandt
Max Planck Institute of Biophysics · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We examined substrate-induced conformational changes in MjNhaP1, an archaeal electroneutral Na(+)/H(+)-antiporter resembling the human antiporter NHE1, by electron crystallography of 2D crystals in a range of physiological pH and Na(+) conditions. In the absence of sodium, changes in pH had no major effect. By contrast, changes in Na(+) concentration caused a marked conformational change that was largely pH-independent. Crystallographically determined, apparent dissociation constants indicated ∼10-fold stronger Na(+) binding at pH 8 than at pH 4, consistent with substrate competition for a common ion-binding site. Projection difference maps indicated helix movements by about 2 Å in the 6-helix bundle region of MjNhaP1 that is thought to contain the ion translocation site. We propose that these movements convert the antiporter from the proton-bound, outward-open state to the Na(+)-bound, inward-open state. Oscillation between the two states would result in rapid Na(+)/H(+) antiport. DOI: http://dx.doi.org/10.7554/eLife.01412.001.

Indexed as

ArchaeaCrystallographyHydrogen-Ion ConcentrationMicroscopy, ElectronProtein ConformationSodiumSodium-Hydrogen ExchangersSodiumSodium-Hydrogen Exchangersconformational changeselectron cryo-microscopyelectron crystallographymembrane protein structureNa+/H+ antiportertransport mechanism

Identifiers

PMID24473071
PMCPMC3900740
OpenAlexW2014090984

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.