Evidence map›Paper›PMID 18849964›Full record

ArticleNature2008

The ion pathway through the opened Na(+),K(+)-ATPase pump.

Ayako Takeuchi, Nicolás Reyes, Pablo Artigas, David C Gadsby

Abstract read
In one paragraph

Article in Nature, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
–field-weighted citation impact
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

38 citing papers in PubMed.

  1. Designable van der Waals Crystal for Artificial Neuronal Cell Mimicking.Advanced materials (Deerfield Beach, Fla.) · 2026
    Article
  2. NaFrontiers in chemistry · 2026
    Article
  3. How palytoxin transforms the NaProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  4. NaInternational journal of molecular sciences · 2024
    Review
  5. Article
  6. Role of NaJournal of molecular medicine (Berlin, Germany) · 2022
    Review
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Structures and characterization of digoxin- and bufalin-bound Na+,K+-ATPase compared with the ouabain-bound complex.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  18. 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.

Ayako TakeuchiLaboratory of Cardiac/Membrane Physiology, The Rockefeller University, New York, New York 10065, USA.
Nicolás Reyes
Pablo Artigas
David C Gadsby

Funding

NA/K PUMP CURRENT IN ISOLATED HEART CELLSR01HL036783 · NHLBI · ROCKEFELLER UNIVERSITY · PI GADSBY, DAVID C · 1987 to 2011
$3.3M
NHLBI NIH HHS R01 HL036783
6 · The paper itself

Abstract

P-type ATPases pump ions across membranes, generating steep electrochemical gradients that are essential for the function of all cells. Access to the ion-binding sites within the pumps alternates between the two sides of the membrane to avoid the dissipation of the gradients that would occur during simultaneous access. In Na(+),K(+)-ATPase pumps treated with the marine agent palytoxin, this strict alternation is disrupted and binding sites are sometimes simultaneously accessible from both sides of the membrane, transforming the pumps into ion channels (see, for example, refs 2, 3). Current recordings in these channels can monitor accessibility of introduced cysteine residues to water-soluble sulphydryl-specific reagents. We found previously that Na(+),K(+) pump-channels open to the extracellular surface through a deep and wide vestibule that emanates from a narrower pathway between transmembrane helices 4 and 6 (TM4 and TM6). Here we report that cysteine scans from TM1 to TM6 reveal a single unbroken cation pathway that traverses palytoxin-bound Na(+),K(+) pump-channels from one side of the membrane to the other. This pathway comprises residues from TM1, TM2, TM4 and TM6, passes through ion-binding site II, and is probably conserved in structurally and evolutionarily related P-type pumps, such as sarcoplasmic- and endoplasmic-reticulum Ca(2+)-ATPases and H(+),K(+)-ATPases.

Indexed as

AcrylamidesAnimalsBinding SitesCell MembraneCnidarian VenomsConserved SequenceCysteineElectric ConductivityIon TransportModels, MolecularPolyether ToxinsProtein ConformationSodium-Potassium-Exchanging ATPaseXenopusAcrylamidesCnidarian VenomsCysteinepalytoxinPolyether ToxinsSodium-Potassium-Exchanging ATPase

Identifiers

PMID18849964
PMCPMC2585603

What OpenQuestion holds

Textmetadata
LicenceTDM
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.