Evidence map›Paper›PMID 36815709›Full record

ArticleBiophysical journal2022

The voltage-sensing domain of a hERG1 mutant is a cation-selective channel.

Meruyert Kudaibergenova, Jiqing Guo, Hanif M Khan, James Lees-Miller, Mahdi Mousaei, Williams Miranda, Van A Ngo, Sergei Yu Noskov, D Peter Tieleman, Henry J Duff

Open access · greenAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Biophysical journal, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
1.0field-weighted citation impact, top 25% 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

3 citing papers in PubMed, 13 citations in OpenAlex.

  1. Voltage sensors.Molecular pharmacology · 2025
    Review
  2. Review
  3. 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

10 authors at 2 institutions in 1 country.

Meruyert KudaibergenovaCentre for Molecular Simulation and Department of Biological Sciences, University of Calgary, Calgary, AB, Canada.
Jiqing GuoDepartment of Cardiac Sciences, Libin Cardiovascular Institute of Alberta, University of Calgary, Calgary, AB, Canada.
Hanif M KhanCentre for Molecular Simulation and Department of Biological Sciences, University of Calgary, Calgary, AB, Canada.
James Lees-MillerDepartment of Cardiac Sciences, Libin Cardiovascular Institute of Alberta, University of Calgary, Calgary, AB, Canada.
Mahdi MousaeiCentre for Molecular Simulation and Department of Biological Sciences, University of Calgary, Calgary, AB, Canada.
Williams MirandaCentre for Molecular Simulation and Department of Biological Sciences, University of Calgary, Calgary, AB, Canada.
Van A NgoCentre for Molecular Simulation and Department of Biological Sciences, University of Calgary, Calgary, AB, Canada.
Sergei Yu NoskovCentre for Molecular Simulation and Department of Biological Sciences, University of Calgary, Calgary, AB, Canada.
D Peter TielemanCentre for Molecular Simulation and Department of Biological Sciences, University of Calgary, Calgary, AB, Canada. Electronic address: tieleman@ucalgary.ca.
Henry J DuffDepartment of Cardiac Sciences, Libin Cardiovascular Institute of Alberta, University of Calgary, Calgary, AB, Canada. Electronic address: hduff@ucalgary.ca.
University of Calgary · CALibin Cardiovascular Institute of Alberta · CA

Funding

Breakthrough Molecular Dynamics Research via an Anton2 SupercomputerR01GM116961 · NIGMS · CARNEGIE-MELLON UNIVERSITY · PI BLOOD, PHILIP D. · 2016 to 2023
$3.0M
NIGMS NIH HHS R01 GM116961
6 · The paper itself

Abstract

A cationic leak current known as an "omega current" may arise from mutations of the first charged residue in the S4 of the voltage sensor domains of sodium and potassium voltage-gated channels. The voltage-sensing domains (VSDs) in these mutated channels act as pores allowing nonspecific passage of cations, such as Li

Indexed as

ERG1 Potassium ChannelCationsHumansMolecular Dynamics SimulationMutationCationsERG1 Potassium ChannelKCNH2 protein, human

Identifiers

PMID36815709
PMCPMC9748372
OpenAlexW4307818875

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.