Evidence map›Paper›PMID 27252653›Full record

ReviewFrontiers in physiology2016

Specialized Functional Diversity and Interactions of the Na,K-ATPase.

Vladimir V Matchkov, Igor I Krivoi

Open access · goldAbstract readReview
In one paragraph

Review in Frontiers in physiology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.

0numbers the graph read from it
0cells of the map it votes in
49citing papers in PubMed
4.5field-weighted citation impact, top 5% 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

49 citing papers in PubMed, 83 citations in OpenAlex.

  1. Article
  2. The machinery of healthy vasoconstriction: an overview.Pflugers Archiv : European journal of physiology · 2025
    Review
  3. Article
  4. Strategies to Develop Na,K-ATPase-α4 Inhibitors as Male Contraceptives.International journal of molecular sciences · 2025
    Article
  5. Cells · 2025
    Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Influence of Anticholinesterase Drugs on Activity and Properties of NaBulletin of experimental biology and medicine · 2024
    Article
  11. NaInternational journal of molecular sciences · 2024
    Review
  12. Sensational site: the sodium pump ouabain-binding site and its ligands.American journal of physiology. Cell physiology · 2024
    Review
  13. Review
  14. Article
  15. Review
  16. Article
  17. Article
  18. The NaFrontiers in endocrinology · 2023
    Review
  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

2 authors at 2 institutions in 2 countries.

Vladimir V MatchkovDepartment of Biomedicine, Aarhus University Aarhus, Denmark.
Igor I KrivoiDepartment of General Physiology, St. Petersburg State University St. Petersburg, Russia.
Aarhus University · DKSt Petersburg University · RU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Na,K-ATPase is a protein ubiquitously expressed in the plasma membrane of all animal cells and vitally essential for their functions. A specialized functional diversity of the Na,K-ATPase isozymes is provided by molecular heterogeneity, distinct subcellular localizations, and functional interactions with molecular environment. Studies over the last decades clearly demonstrated complex and isoform-specific reciprocal functional interactions between the Na,K-ATPase and neighboring proteins and lipids. These interactions are enabled by a spatially restricted ion homeostasis, direct protein-protein/lipid interactions, and protein kinase signaling pathways. In addition to its "classical" function in ion translocation, the Na,K-ATPase is now considered as one of the most important signaling molecules in neuronal, epithelial, skeletal, cardiac and vascular tissues. Accordingly, the Na,K-ATPase forms specialized sub-cellular multimolecular microdomains which act as receptors to circulating endogenous cardiotonic steroids (CTS) triggering a number of signaling pathways. Changes in these endogenous cardiotonic steroid levels and initiated signaling responses have significant adaptive values for tissues and whole organisms under numerous physiological and pathophysiological conditions. This review discusses recent progress in the studies of functional interactions between the Na,K-ATPase and molecular microenvironment, the Na,K-ATPase-dependent signaling pathways and their significance for diversity of cell function.

Indexed as

blood pressurecardiotonic steroidscell survivalK-ATPase molecular heterogeneityNasignaling pathwayssubcellular microdomains

Identifiers

PMID27252653
PMCPMC4879863
OpenAlexW2407506250

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.