ArticleeLife2020
Structure and physiological function of the human KCNQ1 channel voltage sensor intermediate state.
Article in eLife, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
What it found
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Who cites it
35 citing papers in PubMed, 54 citations in OpenAlex.
- Article
- Barium senses subtle pore changes in a voltage-gated KScience advances · 2026Article
- PIPNature communications · 2026Article
- Discovery of Small-Molecule Inhibitors of the KCNQ1/Kv7.1 Potassium Channel with Virtual Screening and Functional Validation in Electrophysiological Assays and KCNQ1-Knockout Neural Stem Cells.ACS chemical neuroscience · 2026Article
- Secondary structure transitions and dual PIP2 binding define cardiac KCNQ1-KCNE1 channel gating.Cell research · 2025Article
- PIPResearch square · 2025Article
- A physiologically-relevant intermediate state structure of a voltage-gated potassium channel.Nature communications · 2025Article
- Electrosome assembly: Structural insights from high voltage-activated calcium channel (CaV)-chaperone interactions.Biochemical Society transactions · 2025Review
- Voltage sensors.Molecular pharmacology · 2025Review
- Ion channel traffic jams: the significance of trafficking deficiency in long QT syndrome.Cell discovery · 2025Review
- Identification of KCNE6, a new member of the KCNE family of potassium channel auxiliary subunits.Communications biology · 2024Article
- The fully activated open state of KCNQ1 controls the cardiac "fight-or-flight" response.PNAS nexus · 2024Article
- Targeting the ICirculation research · 2024Article
- A small-molecule activation mechanism that directly opens the KCNQ2 channel.Nature chemical biology · 2024Article
- Optimizing NMR fragment-based drug screening for membrane protein targets.Journal of structural biology: X · 2024Article
- Modulation of potassium channels by transmembrane auxiliary subunits via voltage-sensing domains.Physiological reports · 2024Review
- Arrhythmia-associated calmodulin variants interact with KCNQ1 to confer aberrant membrane trafficking and function.PNAS nexus · 2023Article
- Conformational rearrangements in the second voltage sensor domain switch PIPProceedings of the National Academy of Sciences of the United States of America · 2023Article
- Structural mechanisms for the activation of human cardiac KCNQ1 channel by electro-mechanical coupling enhancers.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Article
Corrections and comments
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Authors and funding
15 authors at 4 institutions in 1 country.
Funding
Abstract
Voltage-gated ion channels feature voltage sensor domains (VSDs) that exist in three distinct conformations during activation: resting, intermediate, and activated. Experimental determination of the structure of a potassium channel VSD in the intermediate state has previously proven elusive. Here, we report and validate the experimental three-dimensional structure of the human KCNQ1 voltage-gated potassium channel VSD in the intermediate state. We also used mutagenesis and electrophysiology in
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Registered trials
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.