ArticleScience (New York, N.Y.)2010
Structure of the human BK channel Ca2+-activation apparatus at 3.0 A resolution.
Article in Science (New York, N.Y.), 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 191 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
191 citing papers in PubMed, 300 citations in OpenAlex.
- Mechanism of Kch activation by ZnPNAS nexus · 2026Article
- Potassium channels in vascular smooth muscle cells.Physiological reviews · 2026Review
- From venom peptides to neurotherapeutics: BmK defensins and short-chain peptides as modulators of ion channels.Frontiers in pharmacology · 2026Review
- Cytochrome C-like Domain Within the Human BK Channel.International journal of molecular sciences · 2025Article
- Structural basis of voltage-dependent gating in BK channels.Nature communications · 2025Article
- Calcium channels as pharmacological targets for cancer therapy.Clinical and experimental medicine · 2025Review
- Identification ofMolecules (Basel, Switzerland) · 2025Article
- Review
- Ethanol alters mechanosensory habituation in C. elegans by way of the BK potassium channel through a novel mechanism.PloS one · 2025Article
- Activation mechanism and novel binding sites of the BKLife science alliance · 2024Article
- Transmembrane determinants of voltage-gating differences between BK (Slo1) and Slo3 channels.Biophysical journal · 2024Article
- Redox-dependent CdBiophysical journal · 2024Article
- Article
- Unusual Voltage-Gated Sodium and Potassium Channelopathies Related to Epilepsy.Journal of clinical neurology (Seoul, Korea) · 2024Article
- Calcium-gated potassium channel blockade via membrane-facing fenestrations.Nature chemical biology · 2024Article
- SLO3: A Conserved Regulator of Sperm Membrane Potential.International journal of molecular sciences · 2023Review
- Regulation of Neurotransmitter Release by KAdvances in neurobiology · 2023Article
- Cholesterol and PIPAdvances in experimental medicine and biology · 2023Article
- KCurrent neuropharmacology · 2023Review
- Refractory Hypokalemia in Secretory Diarrhea Phenotype of Colonic Pseudo-Obstruction (Ogilvie's Syndrome).Cureus · 2022Article
131 more citing papers are in PubMed but not listed here.
Corrections and comments
- Commented on by
Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
High-conductance voltage- and Ca2+-activated K+ (BK) channels encode negative feedback regulation of membrane voltage and Ca2+ signaling, playing a central role in numerous physiological processes. We determined the x-ray structure of the human BK Ca2+ gating apparatus at a resolution of 3.0 angstroms and deduced its tetrameric assembly by solving a 6 angstrom resolution structure of a Na+-activated homolog. Two tandem C-terminal regulator of K+ conductance (RCK) domains from each of four channel subunits form a 350-kilodalton gating ring at the intracellular membrane surface. A sequence of aspartic amino acids that is known as the Ca2+ bowl, and is located within the second of the tandem RCK domains, creates four Ca2+ binding sites on the outer perimeter of the gating ring at the "assembly interface" between RCK domains. Functionally important mutations cluster near the Ca2+ bowl, near the "flexible interface" between RCK domains, and on the surface of the gating ring that faces the voltage sensors. The structure suggests that the Ca2+ gating ring, in addition to regulating the pore directly, may also modulate the voltage sensor.
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.