Evidence map›Paper›PMID 12554641›Full record

ArticleThe EMBO journal2003

C-terminal domains implicated in the functional surface expression of potassium channels.

Marc Jenke, Araceli Sánchez, Francisco Monje, Walter Stühmer, Rüdiger M Weseloh, Luis A Pardo

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.

0numbers the graph read from it
0cells of the map it votes in
57citing papers in PubMed
4.0field-weighted citation impact, top 6% 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

57 citing papers in PubMed, 146 citations in OpenAlex.

  1. Article
  2. Identification and functional assessment of a KCNH2 compound heterozygosity in a patient with presumed idiopathic ventricular fibrillation ascertains the diagnosis of long QT syndrome type 2.Europace : European pacing, arrhythmias, and cardiac electrophysiology : journal of the working groups on cardiac pacing, arrhythmias, and cardiac cellular electrophysiology of the European Society of Cardiology · 2026
    Article
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  4. Sudden Death-AssociatedbioRxiv : the preprint server for biology · 2025
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  5. Article
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  7. Article
  8. Therapeutic Antibodies Targeting Potassium Ion Channels.Handbook of experimental pharmacology · 2021
    Article
  9. Atomistic Insights of Calmodulin Gating of Complete Ion Channels.International journal of molecular sciences · 2020
    Review
  10. Review
  11. Article
  12. Article
  13. Global versus local mechanisms of temperature sensing in ion channels.Pflugers Archiv : European journal of physiology · 2018
    Review
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Kv10.1 K(+) channel: from physiology to cancer.Pflugers Archiv : European journal of physiology · 2016
    Review
  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

6 authors at 1 institution in 1 country.

Marc JenkeMax Planck Institute for Experimental Medicine, Hermann-Rein-Strasse 3, 37075 Göttingen, Germany.
Araceli Sánchez
Francisco Monje
Walter Stühmer
Rüdiger M Weseloh
Luis A Pardo
Max Planck Institute of Experimental Medicine · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A short C-terminal domain is required for correct tetrameric assembly in some potassium channels. Here, we show that this domain forms a coiled coil that determines not only the stability but also the selectivity of the multimerization. Synthetic peptides comprising the sequence of this domain in Eag1 and other channels are able to form highly stable tetrameric coiled coils and display selective heteromultimeric interactions. We show that loss of function caused by disruption of this domain in Herg1 can be rescued by introducing the equivalent domain from Eag1, and that this chimeric protein can form heteromultimers with Eag1 while wild-type Erg1 cannot. Additionally, a short endoplasmic reticulum retention sequence closely preceding the coiled coil plays a crucial role for surface expression. Both domains appear to co-operate to form fully functional channels on the cell surface and are a frequent finding in ion channels. Many pathological phenotypes may be attributed to mutations affecting one or both domains.

Indexed as

Protein ConformationAmino Acid SequenceAnimalsCircular DichroismElectrophysiologyHumansMolecular Sequence DataMutagenesis, Site-DirectedOocytesPeptidesPotassium ChannelsProtein SubunitsRecombinant Fusion ProteinsSequence AlignmentSurface Plasmon ResonanceTemperaturePeptidesPotassium ChannelsProtein SubunitsRecombinant Fusion Proteins

Identifiers

PMID12554641
PMCPMC140720
OpenAlexW2012739573

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.