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

Voltage-gated Ion Channels01:26

Voltage-gated Ion Channels

10.0K
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...
10.0K
The Role of Ion Channels in Neuronal Computation01:19

The Role of Ion Channels in Neuronal Computation

3.5K
A postsynaptic neuron usually receives numerous impulses from several other presynaptic neurons. The axon hillock of the postsynaptic neuron integrates all these signals and determines the likelihood of firing an action potential.
Sometimes a single EPSP is strong enough to induce an action potential in the postsynaptic neuron. However, multiple presynaptic inputs must often create EPSPs around the same time for the postsynaptic neuron to be sufficiently depolarized to fire an action potential....
3.5K
Calmodulin-dependent Signaling01:16

Calmodulin-dependent Signaling

5.9K
Calmodulin (CaM) is a calcium-binding protein in eukaryotes that controls various calcium-regulated cellular processes. It has four calcium-binding sites that bind calcium to form the calcium-calmodulin ( Ca2+-CaM) complex. GPCR stimulation increases the calcium levels in the cells that bind to CaM and induces a conformational change.
The Ca2+-CaM complex does not have enzymatic activity by itself. Instead, the complex binds downstream target proteins, including membrane proteins or enzymes,...
5.9K
Ligand-Gated Ion Channel Receptor: Gating Mechanism01:30

Ligand-Gated Ion Channel Receptor: Gating Mechanism

3.6K
Ligand-gated ion channels are transmembrane proteins that play a vital role in intercellular communication and functions of the nervous system. They allow the influx of ions across the membrane once the neurotransmitter binds, allowing the subsequent transmission of electrical excitation across the neurons. Other ligand-gated ion channels, like the γ-aminobutyric acid (GABA) receptor, permit anions like chloride into the cells on the binding of the GABA molecule. Their entry into the cell...
3.6K
Mechanically-gated Ion Channels01:12

Mechanically-gated Ion Channels

7.5K
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...
7.5K

You might also read

Related Articles

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

Sort by
Same author

SARgate: a structure-bioactivity analyser for navigating chemical space and mining SAR trends.

European journal of medicinal chemistry·2026
Same author

From Genome Inspection to Precision Agrochemicals: A Structure-Based Antivirulence Roadmap for Sustainable Crop Protection against <i>Xylella fastidiosa</i>.

Journal of agricultural and food chemistry·2026
Same author

Streamlined Synthesis and Structure-Activity Relationship Analysis of 2-Amidothiophene-3-Carboxamides Targeting Influenza Polymerase PA-PB1 Heterodimerization.

ChemMedChem·2026
Same author

KCa3.1 mediates radioresistance of silver nanoparticles in human glioblastoma cells.

Pflugers Archiv : European journal of physiology·2026
Same author

Modulation of L-Type Calcium Currents by Resveratrol-Induced Myogenesis in C2C12 Cells.

Cells·2026
Same author

2-Phenylquinolines Exhibit Anti-Severe Acute Respiratory Syndrome Coronavirus-2 Activity Through the Nonstructural Protein 13 Helicase Inhibition.

ChemMedChem·2026

Related Experiment Video

Updated: Dec 26, 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

21.6K

New Insights on KCa3.1 Channel Modulation.

Giuseppe Manfroni1, Francesco Ragonese2,3, Lorenzo Monarca2,3

  • 1Department of Pharmaceutical Sciences, University of Perugia, Via del Liceo, 1-06123-Perugia (PG), Italy.

Current Pharmaceutical Design
|March 17, 2020
PubMed
Summary
This summary is machine-generated.

Researchers modeled how potassium channel openers (KCOs) modulate the KCa3.1 channel, identifying 1,4-benzothiazin-3-one as a potential scaffold for new KCa3.1 modulators.

Keywords:
1-4 benzothiazine-3-oneIntermediate conductance calcium activated potassium channelKCa3.1benzoimidazolonesdrug discoverygating model.

More Related Videos

Recapitulation of an Ion Channel IV Curve Using Frequency Components
10:14

Recapitulation of an Ion Channel IV Curve Using Frequency Components

Published on: February 8, 2011

13.8K
Isolation and Kv Channel Recordings in Murine Atrial and Ventricular Cardiomyocytes
11:33

Isolation and Kv Channel Recordings in Murine Atrial and Ventricular Cardiomyocytes

Published on: March 12, 2013

13.7K

Related Experiment Videos

Last Updated: Dec 26, 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

21.6K
Recapitulation of an Ion Channel IV Curve Using Frequency Components
10:14

Recapitulation of an Ion Channel IV Curve Using Frequency Components

Published on: February 8, 2011

13.8K
Isolation and Kv Channel Recordings in Murine Atrial and Ventricular Cardiomyocytes
11:33

Isolation and Kv Channel Recordings in Murine Atrial and Ventricular Cardiomyocytes

Published on: March 12, 2013

13.7K

Area of Science:

  • Biophysics
  • Pharmacology
  • Molecular Biology

Background:

  • The KCa3.1 channel is crucial for cellular functions like secretion and calcium signaling.
  • Its activity is modulated by various endogenous and pharmacological agents.
  • Understanding KCa3.1 modulation is key for addressing related pathophysiological conditions.

Purpose of the Study:

  • To propose a model for potassium channel opener (KCO) action on KCa3.1 channel activity.
  • To identify novel chemical scaffolds for KCa3.1 channel modulation.
  • To explore the pharmacological potential of KCa3.1 channel modulators.

Main Methods:

  • Computational modeling techniques were employed.
  • Analysis of existing cryo-electron microscopy (cryo-EM) data.
  • Structure-activity relationship analysis of benzimidazolone derivatives.

Main Results:

  • A model for KCOs action on KCa3.1 channel modulation was proposed.
  • Benzimidazolones were confirmed as KCa3.1 channel openers (e.g., 1-EBIO) or blockers (e.g., NS1619).
  • 1,4-benzothiazin-3-one emerged as a promising scaffold for developing new KCa3.1 modulators.

Conclusions:

  • The study provides insights into KCa3.1 channel modulation mechanisms.
  • 1,4-benzothiazin-3-one derivatives warrant further investigation for therapeutic applications.
  • Targeting KCa3.1 channels with novel modulators holds potential for treating various diseases.