Evidence map›Paper›PMID 31825788›Full record

ReviewBiochimica et biophysica acta. Biomembranes2020

The membrane protein KCNQ1 potassium ion channel: Functional diversity and current structural insights.

Gunjan Dixit, Carole Dabney-Smith, Gary A Lorigan

Open access · greenAbstract readReview
In one paragraph

Review in Biochimica et biophysica acta. Biomembranes, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
2.1field-weighted citation impact, top 11% 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

19 citing papers in PubMed, 41 citations in OpenAlex.

  1. Article
  2. A potential drug target in epilepsy and its role in other neurological disorders.Naunyn-Schmiedeberg's archives of pharmacology · 2026
    Article
  3. Chemical tuning reveals a cation-π gating bridge between the voltage-sensor and pore domains in the KProceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  4. Article
  5. Article
  6. Article
  7. A novel link betweenBiomedical reports · 2025
    Article
  8. Andrology · 2025
    Review
  9. Voltage sensors.Molecular pharmacology · 2025
    Review
  10. Article
  11. A versatile functional interaction between electrically silent KCellular and molecular life sciences : CMLS · 2024
    Article
  12. Article
  13. Genetic Background of Epilepsy and Antiepileptic Treatments.International journal of molecular sciences · 2023
    Review
  14. The role of native cysteine residues in the oligomerization of KCNQ1 channels.Biochemical and biophysical research communications · 2023
    Article
  15. Review
  16. Recurrent Pregnancy Loss and Concealed Long-QT Syndrome.Journal of the American Heart Association · 2021
    Article
  17. Article
  18. Article
  19. 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

3 authors at 1 institution in 1 country.

Gunjan DixitCell, Molecular, and Structural Biology Program, Department of Chemistry & Biochemistry, Miami University, Oxford, OH 45056, USA; Department of Chemistry and Biochemistry, Miami University, Oxford, OH 45056, USA.
Carole Dabney-SmithCell, Molecular, and Structural Biology Program, Department of Chemistry & Biochemistry, Miami University, Oxford, OH 45056, USA; Department of Chemistry and Biochemistry, Miami University, Oxford, OH 45056, USA.
Gary A LoriganCell, Molecular, and Structural Biology Program, Department of Chemistry & Biochemistry, Miami University, Oxford, OH 45056, USA; Department of Chemistry and Biochemistry, Miami University, Oxford, OH 45056, USA. Electronic address: gary.lorigan@miamioh.edu.
Miami University · US

Funding

EPR Spectroscopic Studies of Membrane Proteins-Diversity SupplementR35GM126935 · NIGMS · MIAMI UNIVERSITY OXFORD · PI GARY A LORIGAN · 2018 to 2026
$3.3M
NIGMS NIH HHS R35 GM126935
6 · The paper itself

Abstract

backgroundIon channels play crucial roles in cellular biology, physiology, and communication including sensory perception. Voltage-gated potassium (Kv) channels execute their function by sensor activation, pore-coupling, and pore opening leading to K SCOPE OF REVIEW: This review focuses on a voltage-gated K MAJOR

conclusionsKCNQ1 executes its important physiological functions via interacting with KCNE1 and non-KCNE1 proteins/molecules: calmodulin, PIP GENERAL SIGNIFICANCE: KCNQ1 mutations can result in channel defects and lead to several diseases including atrial fibrillation and long QT syndrome. Therefore, a thorough structure-function understanding of this channel complex is essential to understand its role in both normal and disease biology. Moreover, unraveling the molecular mechanisms underlying the regulation of this channel complex will help to find therapeutic strategies for several diseases.

Indexed as

HumansIon Channel GatingIon ChannelsIon TransportKCNQ1 Potassium ChannelLong QT SyndromeMembranesPotassiumPotassium ChannelsPotassium Channels, Voltage-GatedIon ChannelsKCNE1 protein, humanKCNQ1 Potassium ChannelPotassiumPotassium ChannelsPotassium Channels, Voltage-GatedChannelopathyChanomeKCNE1KCNQ1Long QT syndromePotassium ion channel

Identifiers

PMID31825788
PMCPMC7050432
OpenAlexW2993976820

What OpenQuestion holds

Textmetadata
LicenceTDM
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.