Evidence map›Paper›PMID 27050261›Full record

ArticleActa crystallographica. Section F, Structural biology communications2016

Isolation, crystallization and crystal structure determination of bovine kidney Na(+),K(+)-ATPase.

Jonas Lindholt Gregersen, Daniel Mattle, Natalya U Fedosova, Poul Nissen, Linda Reinhard

Open access · bronzeAbstract read
In one paragraph

Article in Acta crystallographica. Section F, Structural biology communications, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

13 citing papers in PubMed, 29 citations in OpenAlex.

  1. Active conformations of neuronal NaNature communications · 2026
    Article
  2. Molecular Structure of the NaInternational journal of molecular sciences · 2024
    Article
  3. NaInternational journal of molecular sciences · 2024
    Review
  4. The NaThe Journal of biological chemistry · 2022
    Article
  5. The Non-Gastric HInternational journal of molecular sciences · 2022
    Article
  6. Article
  7. NaMolecules (Basel, Switzerland) · 2021
    Review
  8. Displacement of the NaProceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  9. Article
  10. Article
  11. Na⁺Molecules (Basel, Switzerland) · 2017
    Review
  12. Article
  13. 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

5 authors at 2 institutions in 1 country.

Jonas Lindholt GregersenCentre for Membrane Pumps in Cells and Disease - PUMPkin, Danish National Research Foundation, Denmark.
Daniel MattleCentre for Membrane Pumps in Cells and Disease - PUMPkin, Danish National Research Foundation, Denmark.
Natalya U FedosovaCentre for Membrane Pumps in Cells and Disease - PUMPkin, Danish National Research Foundation, Denmark.
Poul NissenCentre for Membrane Pumps in Cells and Disease - PUMPkin, Danish National Research Foundation, Denmark.
Linda ReinhardCentre for Membrane Pumps in Cells and Disease - PUMPkin, Danish National Research Foundation, Denmark.
Danish National Research Foundation · DKAarhus University · DK

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Na(+),K(+)-ATPase is responsible for the transport of Na(+) and K(+) across the plasma membrane in animal cells, thereby sustaining vital electrochemical gradients that energize channels and secondary transporters. The crystal structure of Na(+),K(+)-ATPase has previously been elucidated using the enzyme from native sources such as porcine kidney and shark rectal gland. Here, the isolation, crystallization and first structure determination of bovine kidney Na(+),K(+)-ATPase in a high-affinity E2-BeF3(-)-ouabain complex with bound magnesium are described. Crystals belonging to the orthorhombic space group C2221 with one molecule in the asymmetric unit exhibited anisotropic diffraction to a resolution of 3.7 Å with full completeness to a resolution of 4.2 Å. The structure was determined by molecular replacement, revealing unbiased electron-density features for bound BeF3(-), ouabain and Mg(2+) ions.

Indexed as

AnimalsCattleCrystallizationCrystallography, X-RayKidneyModels, MolecularSodium-Potassium-Exchanging ATPaseSodium-Potassium-Exchanging ATPasecardiotonic steroidsNa+,K+-ATPasenative source isolationouabainP-type ATPase

Identifiers

PMID27050261
PMCPMC4822984
OpenAlexW2322503225

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.