ArticleNature2020
Ball-and-chain inactivation in a calcium-gated potassium channel.
Article in Nature, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.
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.
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.
Who cites it
46 citing papers in PubMed, 66 citations in OpenAlex.
- Lipid gating of BK channels and activation mechanism by negatively charged lipids.Communications chemistry · 2026Article
- Gating crosstalk in potassium channels.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Mechanism of Kch activation by ZnPNAS nexus · 2026Article
- Atomic structure and plasticity of the CTX-MthK complex investigated by cryo-EM, NMR, and MD simulations.Nature communications · 2026Article
- Lipid trapping slows ball-and-chain inactivation in a calcium-activated potassium channel.Nature communications · 2026Article
- Hydrophobic and lipid-mediated gating mechanism revealed by low-conductance MthK mutants.bioRxiv : the preprint server for biology · 2026Article
- Beyond Small Molecules: Orchestrating Cell Fate with Engineered Water-Soluble Membrane Proteins.Biomolecules · 2026Article
- Atomistic Mechanism of Calcium-Mediated Inward Rectification of the MthK Potassium Channel by Solid-State NMR and MD Simulations.Journal of the American Chemical Society · 2025Article
- PIP2-driven cytoplasmic domain motions are coupled to Kir2 channel gating.The Journal of general physiology · 2025Article
- Lipid-mediated hydrophobic gating in the BK potassium channel.Nature communications · 2025Article
- Gating mechanism of the two-pore-domain potassium channel THIK1.Nature structural & molecular biology · 2025Article
- Article
- Solvent-mediated analgesia via the suppression of water permeation through TRPV1 ion channels.Nature biomedical engineering · 2025Article
- A short intrinsically disordered region at KtrB's N-terminus facilitates allosteric regulation of KNature communications · 2025Article
- Ball-and-chain inactivation of a human large conductance calcium-activated potassium channel.Nature communications · 2025Article
- Exploring the Gating Mechanism of the Human Copper Transporter, hCtr1, Using EPR Spectroscopy.Biomolecules · 2025Article
- Structural biology and molecular pharmacology of voltage-gated ion channels.Nature reviews. Molecular cell biology · 2024Review
- Resurgent current in context: Insights from the structure and function of Na and K channels.Biophysical journal · 2024Review
- Research Progress on Plant Shaker KPlants (Basel, Switzerland) · 2024Review
- Structural mechanism of voltage-gated sodium channel slow inactivation.Nature communications · 2024Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 3 institutions in 3 countries.
Funding
Abstract
Inactivation is the process by which ion channels terminate ion flux through their pores while the opening stimulus is still present
Indexed as
Identifiers
What OpenQuestion holds
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.