ReviewJournal of bioenergetics and biomembranes1996
High-conductance calcium-activated potassium channels; structure, pharmacology, and function.
Review in Journal of bioenergetics and biomembranes, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 99 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
99 citing papers in PubMed, 300 citations in OpenAlex.
- Article
- Ball-and-chain inactivation of a human large conductance calcium-activated potassium channel.Nature communications · 2025Article
- The modes of action of ion-channel-targeting neurotoxic insecticides: lessons from structural biology.Nature structural & molecular biology · 2023Review
- Future targets for migraine treatment beyond CGRP.The journal of headache and pain · 2023Review
- Generation of Alternate Indole Diterpene Architectures in Two Species ofJournal of the American Chemical Society · 2023Article
- Small molecule modulation of the Drosophila Slo channel elucidated by cryo-EM.Nature communications · 2021Article
- Mechanotransduction at the Plasma Membrane-Cytoskeleton Interface.International journal of molecular sciences · 2021Review
- Beta-Cell Ion Channels and Their Role in Regulating Insulin Secretion.Comprehensive Physiology · 2021Review
- The Large-Conductance, Calcium-Activated Potassium Channel: A Big Key Regulator of Cell Physiology.Frontiers in physiology · 2021Review
- Bibliometric analysis of potassium channel research.Channels (Austin, Tex.) · 2020Article
- Molecular mechanism of a potassium channel gating through activation gate-selectivity filter coupling.Nature communications · 2019Article
- Energy imbalance alters CaeLife · 2017Article
- Chloroform Extract ofEvidence-based complementary and alternative medicine : eCAM · 2017Article
- International Union of Basic and Clinical Pharmacology. C. Nomenclature and Properties of Calcium-Activated and Sodium-Activated Potassium Channels.Pharmacological reviews · 2017Review
- Properties and physiological function of Ca2+-dependent K+ currents in uniglomerular olfactory projection neurons.Journal of neurophysiology · 2016Article
- Peptide toxins and small-molecule blockers of BK channels.Acta pharmacologica Sinica · 2016Review
- WNK1 activates large-conductance Ca2+-activated K+ channels through modulation of ERK1/2 signaling.Journal of the American Society of Nephrology : JASN · 2015Article
- KCa1.1 inhibition attenuates fibroblast-like synoviocyte invasiveness and ameliorates disease in rat models of rheumatoid arthritis.Arthritis & rheumatology (Hoboken, N.J.) · 2015Article
- Ability of naringenin, a bioflavonoid, to activate M-type potassium current in motor neuron-like cells and to increase BKCa-channel activity in HEK293T cells transfected with α-hSlo subunit.BMC neuroscience · 2014Article
- Current understanding of iberiotoxin-resistant BK channels in the nervous system.Frontiers in physiology · 2014Review
39 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
High-conductance calcium-activated potassium (maxi-K) channels comprise a specialized family of K+ channels. They are unique in their dual requirement for depolarization and Ca2+ binding for transition to the open, or conducting, state. Ion conduction through maxi-K channels is blocked by a family of venom-derived peptides, such as charybdotoxin and iberiotoxin. These peptides have been used to study function and structure of maxi-K channels, to identify novel channel modulators, and to follow the purification of functional maxi-K channels from smooth muscle. The channel consists of two dissimilar subunits, alpha and beta. The alpha subunit is a member of the slo Ca(2+)-activated K+ channel gene family and forms the ion conduction pore. The beta subunit is a structurally unique, membrane-spanning protein that contributes to channel gating and pharmacology. Potent, selective maxi-K channel effectors (both agonists and blockers) of low molecular weight have been identified from natural product sources. These agents, together with peptidyl inhibitors and site-directed antibodies raised against alpha and beta subunit sequences, can be used to anatomically map maxi-K channel expression, and to study the physiologic role of maxi-K channels in various tissues. One goal of such investigations is to determine whether maxi-K channels represent novel therapeutic targets.
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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.