Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Antiepileptic Drugs: Potassium Channel Activators01:20

Antiepileptic Drugs: Potassium Channel Activators

485
Ezocgabine or retigabine, an antiepileptic drug of remarkable efficacy, has revolutionized the management of seizures. It is a potassium channel activator, explicitly targeting the family of Q subtype potassium channels. It enhances the transmembrane potassium currents, regulating neuronal excitability. This action stabilizes the resting membrane potential, a pivotal factor in mitigating the hyperexcitability that characterizes epilepsy.
Ezogabine has gained approval as an adjunctive treatment...
485
Voltage-gated Ion Channels01:26

Voltage-gated Ion Channels

9.8K
Voltage-gated ion channels are transmembrane proteins that open and close in response to changes in the membrane potential. They are present on the membranes of all electrically excitable cells such as neurons, heart, and muscle cells.
Generally, all voltage-gated ion channels have a 'voltage-sensing domain' that spans the lipid bilayer. The charged residues in the sensor move in response to the membrane potential changes that open the channel allowing ions movement. There are several...
9.8K
Non-gated Ion Channels01:24

Non-gated Ion Channels

7.8K
Ion channels are specialized proteins on the plasma membrane that allow charged ions to pass down their electrochemical gradient. Their main function is to maintain the membrane potential which is critical for cell viability. These channels are either gated or non-gated and can transport more than a thousand ions within milliseconds for the cellular event to occur.
Compared to the gated ion channels, the non-gated channels, also known as leakage or passive channels, have no gating mechanism....
7.8K
Mechanically-gated Ion Channels01:12

Mechanically-gated Ion Channels

7.4K
Mechanically-gated ion channels are proteins found in eukaryotic and prokaryotic cell membranes that open in response to mechanical stress. Tension, compression, swelling, and shear stress can alter the conformation of the protein, opening a transmembrane channel that allows the passage of ions for signal transmission. In eukaryotes, mechanically-gated channels are distributed in several regions like the neurons, lungs, skin, bladder, and heart, where they play critical roles in numerous...
7.4K
Antiarrhythmic Drugs: Class III Agents as Potassium Channel Blockers01:12

Antiarrhythmic Drugs: Class III Agents as Potassium Channel Blockers

1.6K
Class III antiarrhythmic drugs are a group of medications that can prolong action potentials in the heart. They achieve this by blocking potassium channels or enhancing inward currents from sodium channels. However, these drugs have a unique property of "reverse use-dependence," which is most pronounced at slower heart rates and can lead to torsades de pointes—a specific type of arrhythmia. However, it is essential to note that excessive QT interval prolongation—a measure of...
1.6K
Regulation of Sodium and Potassium01:26

Regulation of Sodium and Potassium

1.7K
The regulation of sodium and potassium ion concentrations in the human body is a complex process governed primarily by hormones such as aldosterone, antidiuretic hormone (ADH), and atrial natriuretic peptide (ANP).
Sodium Regulation
Sodium ions make up approximately 90% of extracellular cations, with a normal blood plasma concentration of 136–148 mEq/L. A decrease in blood volume and pressure triggers the release of renin from granular cells in the juxtaglomerular complex (JGC), primarily...
1.7K

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Improving AlphaFold2 Performance in Virtual Screens Targeting GPCRs by Enhancing Binding-Site Conformational Sampling.

Journal of chemical information and modeling·2026
Same author

The N-Myc MB0-MBI region interacts specifically and dynamically with the N-lobe of Aurora kinase A.

Nature communications·2026
Same author

Autoimmunity-associated DIORA1 binds the MRCK family of serine/threonine kinases and controls cell motility.

Proceedings of the National Academy of Sciences of the United States of America·2025
Same author

A rich conformational palette underlies human Ca<sub>V</sub>2.1-channel availability.

Nature communications·2025
Same author

Protein-Peptide Docking with ESMFold Language Model.

Journal of chemical theory and computation·2025
Same author

AFsample2 predicts multiple conformations and ensembles with AlphaFold2.

Communications biology·2025

Related Experiment Video

Updated: Dec 6, 2025

Patch Clamp and Perfusion Techniques for Studying Ion Channels Expressed in Xenopus oocytes
10:19

Patch Clamp and Perfusion Techniques for Studying Ion Channels Expressed in Xenopus oocytes

Published on: January 10, 2011

21.5K

Coupling stabilizers open KV1-type potassium channels.

Malin Silverå Ejneby1, Björn Wallner2, Fredrik Elinder3

  • 1Department of Biomedical and Clinical Sciences, Linköping University, SE-581 85 Linköping, Sweden.

Proceedings of the National Academy of Sciences of the United States of America
|October 14, 2020
PubMed
Summary

Researchers discovered novel warfarin-like compounds that specifically open voltage-gated type 1 potassium (KV1) channels. This finding offers a new strategy for developing drugs that modulate ion channel activity.

Keywords:
Kv1 channelVSD-to-pore couplingpotassium-channel openers

More Related Videos

Voltage-Dependent Potassium Current Recording on H9c2 Cardiomyocytes via the Whole-Cell Patch-Clamp Technique
08:11

Voltage-Dependent Potassium Current Recording on H9c2 Cardiomyocytes via the Whole-Cell Patch-Clamp Technique

Published on: November 11, 2022

3.3K
Reconstitution of a Transmembrane Protein, the Voltage-gated Ion Channel, KvAP, into Giant Unilamellar Vesicles for Microscopy and Patch Clamp Studies
11:42

Reconstitution of a Transmembrane Protein, the Voltage-gated Ion Channel, KvAP, into Giant Unilamellar Vesicles for Microscopy and Patch Clamp Studies

Published on: January 22, 2015

19.6K

Related Experiment Videos

Last Updated: Dec 6, 2025

Patch Clamp and Perfusion Techniques for Studying Ion Channels Expressed in Xenopus oocytes
10:19

Patch Clamp and Perfusion Techniques for Studying Ion Channels Expressed in Xenopus oocytes

Published on: January 10, 2011

21.5K
Voltage-Dependent Potassium Current Recording on H9c2 Cardiomyocytes via the Whole-Cell Patch-Clamp Technique
08:11

Voltage-Dependent Potassium Current Recording on H9c2 Cardiomyocytes via the Whole-Cell Patch-Clamp Technique

Published on: November 11, 2022

3.3K
Reconstitution of a Transmembrane Protein, the Voltage-gated Ion Channel, KvAP, into Giant Unilamellar Vesicles for Microscopy and Patch Clamp Studies
11:42

Reconstitution of a Transmembrane Protein, the Voltage-gated Ion Channel, KvAP, into Giant Unilamellar Vesicles for Microscopy and Patch Clamp Studies

Published on: January 22, 2015

19.6K

Area of Science:

  • Molecular pharmacology
  • Ion channel biophysics

Background:

  • Voltage-gated ion channels control ion flux across cell membranes, and their gating is crucial for cellular function.
  • Modulating ion channel gating presents a significant opportunity for pharmacological interventions.

Purpose of the Study:

  • To identify novel compounds that can modulate the function of voltage-gated ion channels.
  • To investigate the mechanism of action for newly discovered channel modulators.

Main Methods:

  • Screening of warfarin-like compounds for activity on voltage-gated potassium channels.
  • Electrophysiological characterization of compound effects on specific KV1 channel subtypes (KV1.5 and Shaker).
  • Structural analysis to determine the binding site and mechanism of action.

Main Results:

  • A novel class of warfarin-derived compounds was identified that selectively opens KV1.5 and Shaker channels.
  • These compounds do not affect other potassium channel subtypes, including KV2, KV4, and KV7.
  • The compounds bind to positively charged residues within the intracellular region connecting voltage-sensor and pore domains in the open channel state.

Conclusions:

  • Warfarin-like compounds represent a new class of pharmacological agents targeting KV1 channels.
  • The identified binding mechanism provides a basis for the rational design of novel ion channel modulators.
  • This discovery opens new therapeutic avenues for conditions involving KV1 channel dysfunction.