Evidence map›Paper›PMID 42424558›Full record

ArticleArchiv der Pharmazie2026

Aberrant TMPRSS6-Protease Regulation of Disease Mutant HCN4-KCNE1 Channel Complex Depends on the KCNE1-G38S Polymorphism.

David Linhoff, Minay Mertens, Ricarda Zimmermann, Stefan Peischard, Christoph Brenker, Thomas Budde, Sven Meuth, Christos Gatsogiannis, Annika Lüttjohann, Liudmila Sosulina and 3 more

Abstract read
In one paragraph

Article in Archiv der Pharmazie, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. 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

13 authors.

David LinhoffGRK 2515, Chemical Biology of Ion Channels (Chembion), Universität Münster, Münster, Germany.
Minay MertensGRK 2515, Chemical Biology of Ion Channels (Chembion), Universität Münster, Münster, Germany.
Ricarda ZimmermannGRK 2515, Chemical Biology of Ion Channels (Chembion), Universität Münster, Münster, Germany.
Stefan PeischardDepartment of Cardiovascular Medicine, Institute for Genetics of Heart Diseases (IfGH), University Hospital Münster, Münster, Germany.
Christoph BrenkerGRK 2515, Chemical Biology of Ion Channels (Chembion), Universität Münster, Münster, Germany.
Thomas BuddeGRK 2515, Chemical Biology of Ion Channels (Chembion), Universität Münster, Münster, Germany.ORCID https://orcid.org/0000-0002-5263-8183
Sven MeuthKlinik für Neurologie mit Institut für Translationale Neurologie, ICB, Münster, Germany.
Christos GatsogiannisInstitute for Medical Physics and Biophysics and Center for Soft Nanoscience, Universität Münster, Münster, Germany.
Annika LüttjohannGRK 2515, Chemical Biology of Ion Channels (Chembion), Universität Münster, Münster, Germany.
Liudmila SosulinaLeibniz Institute for Neurobiology, Magdeburg, Germany.
Jürgen HeschelerDr. Neher's Biophysics Laboratory for Innovative Drug Discovery, State Key Laboratory of Mechanism and Quality of Chinese Medicine, Faculty of Chinese Medicine, Macau University of Science and Technology, Macau SAR, China.
Nathalie Strutz-SeebohmDepartment of Cardiovascular Medicine, Institute for Genetics of Heart Diseases (IfGH), University Hospital Münster, Münster, Germany.
Guiscard SeebohmGRK 2515, Chemical Biology of Ion Channels (Chembion), Universität Münster, Münster, Germany.ORCID https://orcid.org/0000-0001-9303-5373

Funding

Deutsche Forschungsgemeinschaft (DFG, German Research Foundation), Projektnummer 567500531
6 · The paper itself

Abstract

The sinoatrial node pacemaker channel HCN4 plays a central role in cardiac automaticity, and disease-associated variants can predispose to atrial arrhythmias. Here, we investigated the functional interplay between the HCN4 variant P883R and the potassium channel β-subunit KCNE1, focusing on the common atrial fibrillation-associated KCNE1 variant G38S and its regulation by the iron-induced serine protease TMPRSS6. Electrophysiological analyses revealed that HCN4-P883R decreases net HCN4 currents I

Indexed as

Atrial FibrillationHyperpolarization-Activated Cyclic Nucleotide-Gated ChannelsMembrane ProteinsPotassium ChannelsPotassium Channels, Voltage-GatedSerine EndopeptidasesAnimalsHEK293 CellsHumansMuscle ProteinsMutationPolymorphism, GeneticHCN4 protein, humanHyperpolarization-Activated Cyclic Nucleotide-Gated ChannelsKCNE1 protein, humanMembrane ProteinsMuscle ProteinsPotassium ChannelsPotassium Channels, Voltage-GatedSerine Endopeptidasesenvironmentgeneticion channelmodifierproteolysis

Identifiers

PMID42424558
PMCPMC13349338

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.