Evidence map›Paper›PMID 36030326›Full record

ArticleScientific reports2022

Intracellular hemin is a potent inhibitor of the voltage-gated potassium channel Kv10.1.

Nirakar Sahoo, Kefan Yang, Ina Coburger, Alisa Bernert, Sandip M Swain, Guido Gessner, Reinhard Kappl, Toni Kühl, Diana Imhof, Toshinori Hoshi and 2 more

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
0.5field-weighted citation impact, top 38% 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

9 citing papers in PubMed, 9 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Review
  6. Cytochrome C-like Domain Within the Human BK Channel.International journal of molecular sciences · 2025
    Article
  7. Review
  8. Review
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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

12 authors at 5 institutions in 2 countries.

Nirakar SahooDepartment of Biophysics, Center for Molecular Biomedicine, Friedrich Schiller University Jena & Jena University Hospital, Hans-Knöll-Str. 2, 07745, Jena, Germany.
Kefan YangDepartment of Biophysics, Center for Molecular Biomedicine, Friedrich Schiller University Jena & Jena University Hospital, Hans-Knöll-Str. 2, 07745, Jena, Germany.
Ina CoburgerDepartment of Biophysics, Center for Molecular Biomedicine, Friedrich Schiller University Jena & Jena University Hospital, Hans-Knöll-Str. 2, 07745, Jena, Germany.
Alisa BernertDepartment of Biophysics, Center for Molecular Biomedicine, Friedrich Schiller University Jena & Jena University Hospital, Hans-Knöll-Str. 2, 07745, Jena, Germany.
Sandip M SwainDepartment of Biophysics, Center for Molecular Biomedicine, Friedrich Schiller University Jena & Jena University Hospital, Hans-Knöll-Str. 2, 07745, Jena, Germany.
Guido GessnerDepartment of Biophysics, Center for Molecular Biomedicine, Friedrich Schiller University Jena & Jena University Hospital, Hans-Knöll-Str. 2, 07745, Jena, Germany.
Reinhard KapplInstitute of Biophysics, Saarland University, 66421, Homburg, Germany.
Toni KühlPharmaceutical Biochemistry and Bioanalytics, Pharmaceutical Institute, University of Bonn, An der Immenburg 4, 53121, Bonn, Germany.
Diana ImhofPharmaceutical Biochemistry and Bioanalytics, Pharmaceutical Institute, University of Bonn, An der Immenburg 4, 53121, Bonn, Germany.
Toshinori HoshiDepartment of Physiology, University of Pennsylvania, Philadelphia, PA, 19104-6085, USA.
Roland SchönherrDepartment of Biophysics, Center for Molecular Biomedicine, Friedrich Schiller University Jena & Jena University Hospital, Hans-Knöll-Str. 2, 07745, Jena, Germany.
Stefan H HeinemannDepartment of Biophysics, Center for Molecular Biomedicine, Friedrich Schiller University Jena & Jena University Hospital, Hans-Knöll-Str. 2, 07745, Jena, Germany. Stefan.H.Heinemann@uni-jena.de.
Friedrich Schiller University Jena · DEJena University Hospital · DEUniversity of Bonn · DESaarland University · DEUniversity of Pennsylvania · US

Funding

Mechanism of blood pressure lowering by fatty acid nutraceuticalsR01GM121375 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI HOSHI, TOSHINORI · 2017 to 2020
$2.3M
Emerging role of heme and heme degradation products in the modulation of cardiac ion channelsSC2GM139715 · NIGMS · UNIVERSITY OF TEXAS RIO GRANDE VALLEY · PI SAHOO, NIRAKAR · 2021 to 2023
$444k
NIGMS NIH HHS R01 GM121375NIGMS NIH HHS SC2 GM139715NIH HHS GM121375NIH HHS GM139715
6 · The paper itself

Abstract

Heme, an iron-protoporphyrin IX complex, is a cofactor bound to various hemoproteins and supports a broad range of functions, such as electron transfer, oxygen transport, signal transduction, and drug metabolism. In recent years, there has been a growing recognition of heme as a non-genomic modulator of ion channel functions. Here, we show that intracellular free heme and hemin modulate human ether à go-go (hEAG1, Kv10.1) voltage-gated potassium channels. Application of hemin to the intracellular side potently inhibits Kv10.1 channels with an IC

Indexed as

Ether-A-Go-Go Potassium ChannelsHeminHumansMembrane PotentialsEther-A-Go-Go Potassium ChannelsHemin

Identifiers

PMID36030326
PMCPMC9420133
OpenAlexW4293367477

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.