Evidence map›Paper›PMID 37965565›Full record

ArticlePNAS nexus2023

Arrhythmia-associated calmodulin variants interact with KCNQ1 to confer aberrant membrane trafficking and function.

Po Wei Kang, Lucy Woodbury, Paweorn Angsutararux, Namit Sambare, Jingyi Shi, Martina Marras, Carlota Abella, Anish Bedi, DeShawn Zinn, Jianmin Cui and 1 more

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

Article in PNAS nexus, 2023. 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
1.1field-weighted citation impact, top 20% 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, 5 citations in OpenAlex.

  1. Calcium interaction with Nav1.5 via FGF12A and CaM binding.bioRxiv : the preprint server for biology · 2026
    Article
  2. Article
  3. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

11 authors at 1 institution in 1 country.

Po Wei KangDepartment of Biomedical Engineering, Washington University in St.Louis, St. Louis, MO 63130, USA.ORCID https://orcid.org/0000-0002-5933-545X
Lucy WoodburyDepartment of Biomedical Engineering, Washington University in St.Louis, St. Louis, MO 63130, USA.
Paweorn AngsutararuxDepartment of Biomedical Engineering, Washington University in St.Louis, St. Louis, MO 63130, USA.
Namit SambareDepartment of Biomedical Engineering, Washington University in St.Louis, St. Louis, MO 63130, USA.
Jingyi ShiDepartment of Biomedical Engineering, Washington University in St.Louis, St. Louis, MO 63130, USA.
Martina MarrasDepartment of Biomedical Engineering, Washington University in St.Louis, St. Louis, MO 63130, USA.ORCID https://orcid.org/0000-0001-6740-3806
Carlota AbellaDepartment of Biomedical Engineering, Washington University in St.Louis, St. Louis, MO 63130, USA.
Anish BediDepartment of Biomedical Engineering, Washington University in St.Louis, St. Louis, MO 63130, USA.
DeShawn ZinnDepartment of Biomedical Engineering, Washington University in St.Louis, St. Louis, MO 63130, USA.
Jianmin CuiDepartment of Biomedical Engineering, Washington University in St.Louis, St. Louis, MO 63130, USA.ORCID https://orcid.org/0000-0002-9198-6332
Jonathan R SilvaDepartment of Biomedical Engineering, Washington University in St.Louis, St. Louis, MO 63130, USA.ORCID https://orcid.org/0000-0002-3696-3955
Washington University in St. Louis · US

Funding

Gating Mechanisms of KCNQ1/IKS ChannelsR01HL155398 · NHLBI · WASHINGTON UNIVERSITY · PI CUI, JIANMIN · 2021 to 2024
$2.5M
MODULATION OF CARDIAC NAV CHANNEL FUNCTION AND ELECTROPHYSIOLOGY BY INTERACTING MOLECULESR01HL136553 · NHLBI · WASHINGTON UNIVERSITY · PI SILVA, JONATHAN R · 2017 to 2021
$1.9M
KCNQ CHANNELS: GATING AND SUBUNITS MODULATIONR01NS092570 · NINDS · WASHINGTON UNIVERSITY · PI SILVA, JONATHAN R · 2015 to 2020
$1.7M
Calmodulin Regulation of KCNQ1 Potassium ChannelsF30HL151042 · NHLBI · WASHINGTON UNIVERSITY · PI KANG, PO WEI · 2020 to 2022
$136k
NHLBI NIH HHS F30 HL151042NHLBI NIH HHS R01 HL136553NHLBI NIH HHS R01 HL155398NINDS NIH HHS R01 NS092570
6 · The paper itself

Abstract

Missense variants in calmodulin (CaM) predispose patients to arrhythmias associated with high mortality rates ("calmodulinopathy"). As CaM regulates many key cardiac ion channels, an understanding of disease mechanism associated with CaM variant arrhythmias requires elucidating individual CaM variant effects on distinct channels. One key CaM regulatory target is the KCNQ1 (K

Indexed as

arrhythmiacalmodulincalmodulinopathyion channelsKCNQ1KV7.1

Identifiers

PMID37965565
PMCPMC10642763
OpenAlexW4387640094

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.