Evidence map›Paper›PMID 7708709›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1995

Use of Saccharomyces cerevisiae for patch-clamp analysis of heterologous membrane proteins: characterization of Kat1, an inward-rectifying K+ channel from Arabidopsis thaliana, and comparison with endogeneous yeast channels and carriers.

A Bertl, J A Anderson, C L Slayman, R F Gaber

Open access · greenAbstract readComparative Study
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
7.0field-weighted citation impact, top 2% 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

23 citing papers in PubMed, 96 citations in OpenAlex.

  1. Article
  2. Article
  3. Heterelogous expression of plant genes.International journal of plant genomics · 2009
    Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Voltage-dependent gating characteristics of the K+ channel KAT1 depend on the N and C termini.Proceedings of the National Academy of Sciences of the United States of America · 1997
    Article
  18. Article
  19. Article
  20. Changes in voltage activation, Cs+ sensitivity, and ion permeability in H5 mutants of the plant K+ channel KAT1.Proceedings of the National Academy of Sciences of the United States of America · 1996
    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 at 1 institution in 1 country.

A BertlDepartment of Cellular and Molecular Physiology, Yale University, New Haven, CT 06510, USA.
J A Anderson
C L Slayman
R F Gaber
Yale University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Transport-deficient strains of the yeast Saccharomyces cerevisiae have recently proven useful for cloning, by functional complementation, of cDNAs encoding heterologous membrane transporters: specifically, H(+)-amino acid symporters and K+ channels from the higher plant Arabidopsis thaliana. The present study uses whole-cell patch-clamp experiments to show that yeast strains which grow poorly on submillimolar K+ due to the deletion of two K(+)-transporter genes (TRK1 and TRK2) are in fact missing a prominent K+ inward current present in wild-type cells. Rescue of such strains for growth on low K+ by transformation with a gene (KAT1) encoding an inward-rectifying K+ channel from Arabidopsis is accompanied by the appearance of an inward current whose characteristics are in qualitative agreement with previous studies in the Xenopus oocyte system, but differ in quantitative details. The ability to make such measurements directly on Saccharomyces should facilitate structure-function studies of any electrogenic or electrophoretic ion transporters which can be expressed in the plasma membrane (or tonoplast) of that organism.

Indexed as

Potassium Channels, Inwardly RectifyingAnimalsArabidopsisArabidopsis ProteinsCell MembraneCloning, MolecularCrosses, GeneticDNA, ComplementaryFemaleGenes, FungalGenes, PlantMembrane PotentialsOocytesPatch-Clamp TechniquesPlant ProteinsPotassiumArabidopsis ProteinsDNA, ComplementaryKAT1 protein, ArabidopsisPlant ProteinsPotassiumPotassium ChannelsPotassium Channels, Inwardly RectifyingSodium

Identifiers

PMID7708709
PMCPMC42286
OpenAlexW2086654946

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.