Evidence map›Paper›PMID 22695678›Full record

ReviewCellular and molecular life sciences : CMLS2013

Na(+),K (+)-ATPase as a docking station: protein-protein complexes of the Na(+),K (+)-ATPase.

Linda Reinhard, Henning Tidow, Michael J Clausen, Poul Nissen

Open access · greenAbstract readReview
In one paragraph

Review in Cellular and molecular life sciences : CMLS, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 86 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
86citing papers in PubMed, 1 pooled it
4.8field-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

86 citing papers in PubMed, 1 synthesis or guideline pooled it, 147 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. An Alkaloid from MarinePharmaceuticals (Basel, Switzerland) · 2026
    Article
  4. Article
  5. NaFrontiers in chemistry · 2026
    Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. The NamBio · 2025
    Article
  12. Review
  13. Article
  14. Review
  15. Digoxin and its NaBioorganic & medicinal chemistry · 2024
    Review
  16. Sensational site: the sodium pump ouabain-binding site and its ligands.American journal of physiology. Cell physiology · 2024
    Review
  17. Article
  18. Article
  19. Article
  20. Article

26 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

4 authors at 2 institutions in 2 countries.

Linda ReinhardDanish National Research Foundation, Centre for Membrane Pumps in Cells and Disease-PUMPKIN, Department of Molecular Biology and Genetics, 8000, Aarhus C, Denmark.
Henning Tidow
Michael J Clausen
Poul Nissen
Danish National Research Foundation · DKNational Research Foundation · ZA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The Na(+),K(+)-ATPase, or sodium pump, is well known for its role in ion transport across the plasma membrane of animal cells. It carries out the transport of Na(+) ions out of the cell and of K(+) ions into the cell and thus maintains electrolyte and fluid balance. In addition to the fundamental ion-pumping function of the Na(+),K(+)-ATPase, recent work has suggested additional roles for Na(+),K(+)-ATPase in signal transduction and biomembrane structure. Several signaling pathways have been found to involve Na(+),K(+)-ATPase, which serves as a docking station for a fast-growing number of protein interaction partners. In this review, we focus on Na(+),K(+)-ATPase as a signal transducer, but also briefly discuss other Na(+),K(+)-ATPase protein-protein interactions, providing a comprehensive overview of the diverse signaling functions ascribed to this well-known enzyme.

Indexed as

AnimalsBiological Transport, ActiveCell MembraneHumansIon TransportMultiprotein ComplexesPotassiumProtein BindingProtein Structure, TertiarySignal TransductionSodiumSodium-Potassium-Exchanging ATPaseMultiprotein ComplexesPotassiumSodiumSodium-Potassium-Exchanging ATPase

Identifiers

PMID22695678
PMCPMC11113973
OpenAlexW2004464633

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.