Evidence map›Paper›PMID 24644283›Full record

ArticleThe Journal of biological chemistry2014

Keeping it simple, transport mechanism and pH regulation in Na+/H+ exchangers.

Octavian Călinescu, Cristina Paulino, Werner Kühlbrandt, Klaus Fendler

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
7.9field-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

31 citing papers in PubMed, 45 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Structure and mechanism of the KNature communications · 2024
    Article
  8. Article
  9. Article
  10. Metabolic and Proteomic Profiles Reveal the Response of the ASD-Associated Resistant Strain 6-1 ofInternational journal of environmental research and public health · 2022
    Article
  11. Prokaryotic NaInternational journal of molecular sciences · 2022
    Review
  12. Article
  13. Article
  14. Ion Binding and Selectivity of the NaThe journal of physical chemistry. B · 2020
    Article
  15. Article
  16. Microbial response to acid stress: mechanisms and applications.Applied microbiology and biotechnology · 2020
    Review
  17. Article
  18. Analysis of seven putative NaPhysiology and molecular biology of plants : an international journal of functional plant biology · 2019
    Article
  19. Article
  20. 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

4 authors at 2 institutions in 1 country.

Octavian CălinescuFrom the Departments of Biophysical Chemistry and.
Cristina Paulino
Werner Kühlbrandt
Klaus Fendler
Max Planck Society · DEMax Planck Institute of Biophysics · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Na(+)/H(+) exchangers are essential for regulation of intracellular proton and sodium concentrations in all living organisms. We examined and experimentally verified a kinetic model for Na(+)/H(+) exchangers, where a single binding site is alternatively occupied by Na(+) or one or two H(+) ions. The proposed transport mechanism inherently down-regulates Na(+)/H(+) exchangers at extreme pH, preventing excessive cytoplasmic acidification or alkalinization. As an experimental test system we present the first electrophysiological investigation of an electroneutral Na(+)/H(+) exchanger, NhaP1 from Methanocaldococcus jannaschii (MjNhaP1), a close homologue of the medically important eukaryotic NHE Na(+)/H(+) exchangers. The kinetic model describes the experimentally observed substrate dependences of MjNhaP1, and the transport mechanism explains alkaline down-regulation of MjNhaP1. Because this model also accounts for acidic down-regulation of the electrogenic NhaA Na(+)/H(+) exchanger from Escherichia coli (EcNhaA, shown in a previous publication) we conclude that it applies generally to all Na(+)/H(+) exchangers, electrogenic as well as electroneutral, and elegantly explains their pH regulation. Furthermore, the electrophysiological analysis allows insight into the electrostatic structure of the translocation complex in electroneutral and electrogenic Na(+)/H(+) exchangers.

Indexed as

Archaeal ProteinsHydrogen-Ion ConcentrationIon TransportMethanocaldococcusSodium-Hydrogen ExchangersArchaeal ProteinsSodium-Hydrogen ExchangersArchaeaCation Proton AntiporterEcNhaAElectrophysiologyMembrane TransportMjNhaP1pH RegulationSodium Proton ExchangeSolid Supported Membrane

Identifiers

PMID24644283
PMCPMC4036328
OpenAlexW1992053703

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.