Evidence map›Paper›PMID 21179061›Full record

ReviewNature reviews. Molecular cell biology2011

A structural overview of the plasma membrane Na+,K+-ATPase and H+-ATPase ion pumps.

J Preben Morth, Bjørn P Pedersen, Morten J Buch-Pedersen, Jens Peter Andersen, Bente Vilsen, Michael G Palmgren, Poul Nissen

Abstract readReview
PubMed Publisher
In one paragraph

Review in Nature reviews. Molecular cell biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 162 papers.

0numbers the graph read from it
0cells of the map it votes in
162citing papers in PubMed
9.1field-weighted citation impact, top 1% 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

162 citing papers in PubMed, 406 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Review
  7. NaFrontiers in chemistry · 2026
    Article
  8. Article
  9. Review
  10. Article
  11. LncDARS-AS1 Regulates ATP1A1 Stability and Enhances NaAdvanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
    Article
  12. Strategies to Develop Na,K-ATPase-α4 Inhibitors as Male Contraceptives.International journal of molecular sciences · 2025
    Article
  13. Condenzymes: Biomolecular condensates with inherent catalytic activities.bioRxiv : the preprint server for biology · 2025
    Article
  14. Review
  15. Article
  16. Ethylene increases the NaHCOPlant biotechnology journal · 2025
    Article
  17. The NamBio · 2025
    Article
  18. Review
  19. An animal-type NaFrontiers in plant science · 2025
    Article
  20. NaResearch (Washington, D.C.) · 2025
    Article

102 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

7 authors at 2 institutions in 2 countries.

J Preben MorthDanish National Research Foundation, Centre for Membrane Pumps in Cells and Disease - PUMPKIN, Denmark.
Bjørn P Pedersen
Morten J Buch-Pedersen
Jens Peter Andersen
Bente Vilsen
Michael G Palmgren
Poul Nissen
Danish National Research Foundation · DKInstitutt for Eksperimentell Medisinsk Forskning · NO

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Plasma membrane ATPases are primary active transporters of cations that maintain steep concentration gradients. The ion gradients and membrane potentials derived from them form the basis for a range of essential cellular processes, in particular Na(+)-dependent and proton-dependent secondary transport systems that are responsible for uptake and extrusion of metabolites and other ions. The ion gradients are also both directly and indirectly used to control pH homeostasis and to regulate cell volume. The plasma membrane H(+)-ATPase maintains a proton gradient in plants and fungi and the Na(+),K(+)-ATPase maintains a Na(+) and K(+) gradient in animal cells. Structural information provides insight into the function of these two distinct but related P-type pumps.

Indexed as

AnimalsCell MembraneHumansProton-Translocating ATPasesSodium-Potassium-Exchanging ATPaseProton-Translocating ATPasesSodium-Potassium-Exchanging ATPase

Identifiers

PMID21179061
OpenAlexW2040615565

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.