Evidence map›Paper›PMID 16167182›Full record

ArticleJournal of bioenergetics and biomembranes2005

Sodium, potassium-atpases in algae and oomycetes.

Javier Barrero-Gil, Blanca Garciadeblás, Begoña Benito

Abstract read
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In one paragraph

Article in Journal of bioenergetics and biomembranes, 2005. 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
–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

13 citing papers in PubMed.

  1. Article
  2. An animal-type NaFrontiers in plant science · 2025
    Article
  3. NaFrontiers in plant science · 2022
    Article
  4. NaThe Journal of membrane biology · 2020
    Review
  5. Article
  6. Article
  7. Mechanisms of Sodium Transport in Plants-Progresses and Challenges.International journal of molecular sciences · 2018
    Review
  8. Article
  9. Article
  10. Evolution of plant p-type ATPases.Frontiers in plant science · 2012
    Article
  11. 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

3 authors.

Javier Barrero-GilDepartamento de Biotecnología, Escuela Técnica Superior de Ingenieros Agrónomos, Universidad Politécnica de Madrid, Madrid, Spain.
Blanca Garciadeblás
Begoña Benito

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We have investigated the presence of K(+)-transporting ATPases that belong to the phylogenetic group of animal Na(+),K(+)-ATPases in the Pythium aphanidermatum Stramenopile oomycete, the Porphyra yezoensis red alga, and the Udotea petiolata green alga, by molecular cloning and expression in heterologous systems. PCR amplification and search in EST databases allowed one gene to be identified in each species that could encode ATPases of this type. Phylogenetic analysis of the sequences of these ATPases revealed that they cluster with ATPases of animal origin, and that the algal ATPases are closer to animal ATPases than the oomycete ATPase is. The P. yezoensis and P. aphanidermatum ATPases were functionally expressed in Saccharomyces cerevisiae and Escherichia coli alkali cation transport mutants. The aforementioned cloning and complementary searches in silicio for H(+)- and Na(+),K(+)-ATPases revealed a great diversity of strategies for plasma membrane energization in eukaryotic cells different from typical animal, plant, and fungal cells.

Indexed as

Amino Acid SequenceAnimalsEukaryotaMolecular Sequence DataOomycetesPhylogenyPolymerase Chain ReactionPorphyraProton-Translocating ATPasesPythiumSodium-Potassium-Exchanging ATPaseProton-Translocating ATPasesSodium-Potassium-Exchanging ATPase

Identifiers

What OpenQuestion holds

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Registered trials

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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.