Evidence map›Paper›PMID 9786970›Full record

ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience1998

The epithelial inward rectifier channel Kir7.1 displays unusual K+ permeation properties.

F Döring, C Derst, E Wischmeyer, C Karschin, R Schneggenburger, J Daut, A Karschin

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 73 papers.

0numbers the graph read from it
0cells of the map it votes in
73citing papers in PubMed
3.2field-weighted citation impact, top 7% 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

73 citing papers in PubMed, 151 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Relative biological effectiveness and neural stem cell fate in carbon ion-irradiated human brain organoids.Radiotherapy and oncology : journal of the European Society for Therapeutic Radiology and Oncology · 2026
    Article
  5. Hypothalamic opsin 3 suppresses MC4R signaling and potentiates Kir7.1 to promote food consumption.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Review
  14. Inward rectifier potassium (Kir) channels in the retina: living our vision.American journal of physiology. Cell physiology · 2022
    Review
  15. Kir7.1 disease mutant T153I within the inner pore affects KAmerican journal of physiology. Cell physiology · 2022
    Article
  16. Review
  17. Retinal Development and Pathophysiology in Kcnj13 Knockout Mice.Frontiers in cell and developmental biology · 2021
    Article
  18. Comparison of KHandbook of experimental pharmacology · 2021
    Article
  19. Sensing through Non-Sensing Ocular Ion Channels.International journal of molecular sciences · 2020
    Review
  20. Article

13 more citing papers are in PubMed but not listed here.

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

7 authors at 2 institutions in 1 country.

F DöringMolecular Neurobiology of Signal Transduction, Max-Planck-Institute for Biophysical Chemistry, D-37070 Göttingen, Germany.
C Derst
E Wischmeyer
C Karschin
R Schneggenburger
J Daut
A Karschin
Philipps University of Marburg · DEMax Planck Institute for Biophysical Chemistry · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Rat and human cDNAs were isolated that both encoded a 360 amino acid polypeptide with a tertiary structure typical of inwardly rectifying K+ channel (Kir) subunits. The new proteins, termed Kir7.1, were <37% identical to other Kir subunits and showed various unique residues at conserved sites, particularly near the pore region. High levels of Kir7.1 transcripts were detected in rat brain, lung, kidney, and testis. In situ hybridization of rat brain sections demonstrated that Kir7.1 mRNA was absent from neurons and glia but strongly expressed in the secretory epithelial cells of the choroid plexus (as confirmed by in situ patch-clamp measurements). In cRNA-injected Xenopus oocytes Kir7.1 generated macroscopic Kir currents that showed a very shallow dependence on external K+ ([K+]e), which is in marked contrast to all other Kir channels. At a holding potential of -100 mV, the inward current through Kir7.1 averaged -3.8 +/- 1.04 microA with 2 mM [K+]e and -4.82 +/- 1.87 microA with 96 mM [K+]e. Kir7.1 has a methionine at position 125 in the pore region where other Kir channels have an arginine. When this residue was replaced by the conserved arginine in mutant Kir7.1 channels, the pronounced dependence of K+ permeability on [K+]e, characteristic for other Kir channels, was restored and the Ba2+ sensitivity was increased by a factor of approximately 25 (Ki = 27 microM). These findings support the important role of this site in the regulation of K+ permeability in Kir channels by extracellular cations.

Indexed as

Potassium Channels, Inwardly RectifyingAmino Acid SequenceAmino Acid SubstitutionAnimalsAnimals, NewbornBlotting, NorthernBrainChoroid PlexusCloning, MolecularEpithelial CellsHumansIn Situ HybridizationMolecular Sequence DataPotassiumPotassium ChannelsRatsPotassiumPotassium ChannelsPotassium Channels, Inwardly Rectifying

Identifiers

PMID9786970
PMCPMC6793533
OpenAlexW1900482019

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.