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

Drug-Receptor Interaction: Agonist01:25

Drug-Receptor Interaction: Agonist

3.3K
Agonists are drugs that interact with specific receptors in the body to produce a biological response. When an agonist binds to a receptor, it activates or enhances the receptor's function, leading to physiological effects. The interaction between agonist drugs and receptors is crucial for their therapeutic action in various medical treatments.
Agonists can bind to receptors in different ways. Some agonists bind directly to the receptor's active site, mimicking the endogenous...
3.3K
Adrenergic Agonists: Chemistry and Structure-Activity Relationship01:16

Adrenergic Agonists: Chemistry and Structure-Activity Relationship

3.6K
Adrenergic agonists' structure-activity relationship (SAR) determines their selectivity and efficacy. These agonists comprise a phenylethylamine moiety with an aromatic ring and an ethylamine side chain.
Aromatic ring substitutions: Substituting the aromatic ring with –OH groups at positions 3 and 4 yields catecholamines (e.g., epinephrine), which have a high affinity for adrenoceptors. Hydrogen bonding between –OH groups and receptors enhances adrenergic activity.
Separation of...
3.6K
Opioid Receptors: Overview01:22

Opioid Receptors: Overview

2.9K
Opioid receptors, including the mu (μ, MOR), delta (δ, DOR), and kappa (κ, KOR) types, belong to the rhodopsin family of G protein-coupled receptors. These receptors are located throughout the central and peripheral nervous systems and in non-neuronal tissues such as macrophages and astrocytes. Opioid receptor ligands can be categorized into agonists or antagonists. Highly selective agonists include [d-Ala2, MePhe4, Gly(ol)5]-enkephalin or DAMGO for MOR, [D-Pen2,...
2.9K
Direct-Acting Cholinergic Agonists: Chemistry and Structure-Activity Relationship01:22

Direct-Acting Cholinergic Agonists: Chemistry and Structure-Activity Relationship

1.6K
Cholinergic agonists or cholinomimetics mimic the action of acetylcholine to stimulate the parasympathetic nervous system. They are categorized into direct-acting and indirect-acting agents. The direct-acting cholinergic drugs induce the parasympathetic response by directly binding to the muscarinic or nicotine receptors. In comparison, the indirect-acting cholinergic drugs prevent acetylcholine hydrolysis, indirectly contributing to the extended parasympathetic response.
The direct-acting...
1.6K
Adrenergic Agonists: Direct-Acting Agents01:30

Adrenergic Agonists: Direct-Acting Agents

2.1K
Drugs that mimic the action of endogenous catecholamines like noradrenaline and adrenaline are called adrenergic agonists or sympathomimetics. Based on their mechanism of action, sympathomimetics can be classified as direct-, indirect-, or mixed-acting sympathomimetics. Direct-acting adrenergic agonists activate adrenoceptors without affecting presynaptic neurons, making them independent of neuronal catecholamine-depleting agents like reserpine and guanethidine.
These agents can be classified...
2.1K
Adrenergic Agonists: Indirect-Acting Agents01:25

Adrenergic Agonists: Indirect-Acting Agents

2.2K
Indirect-acting adrenergic agonists potentiate the effects of endogenous catecholamines through different mechanisms without directly binding to adrenoceptors.
One mechanism involves depleting stored catecholamines by displacing them from synaptic vesicles. These agents, known as "displacers," are transported into vesicles at the expense of noradrenaline. Examples include amphetamine and tyramine, which lack a catechol moiety, resulting in prolonged action, improved oral...
2.2K

You might also read

Related Articles

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

Sort by
Same author

The gating properties of Drosophila NMJ glutamate receptors and their dependence on Neto.

The Journal of physiology·2024
Same author

Expression and Functional Analysis of Ctenophore Glutamate Receptor Genes.

Methods in molecular biology (Clifton, N.J.)·2024
Same author

Jeffrey Watkins (1929-2023).

Neuron·2023
Same author

Structural biology of kainate receptors.

Neuropharmacology·2021
Same author

Glutamate receptors from diverse animal species exhibit unexpected structural and functional diversity.

The Journal of physiology·2020
Same author

Structural biology of glutamate receptor ion channels: towards an understanding of mechanism.

Current opinion in structural biology·2019

Related Experiment Video

Updated: Nov 6, 2025

Methods for the Discovery of Novel Compounds Modulating a Gamma-Aminobutyric Acid Receptor Type A Neurotransmission
07:16

Methods for the Discovery of Novel Compounds Modulating a Gamma-Aminobutyric Acid Receptor Type A Neurotransmission

Published on: August 16, 2018

13.8K

Partial agonists go molecular.

Mark L Mayer1

  • 1Porter Neuroscience Research Center, National Institute of Neurological Disorders and Stroke (NINDS), National Institutes of Health (NIH), Bethesda, MD 20892, USA.

Trends in Pharmacological Sciences
|May 9, 2021
PubMed
Summary
This summary is machine-generated.

Glycine receptor activation involves a surprising, long-lived intermediate state. This partially activated, agonist-bound closed state differs from the previously identified short-lived

Keywords:
cryo-electron microscopyglycine receptorsligand-gated ion channelssingle-channel recording

More Related Videos

The Sciatic Nerve Cuffing Model of Neuropathic Pain in Mice
07:09

The Sciatic Nerve Cuffing Model of Neuropathic Pain in Mice

Published on: July 16, 2014

48.7K
A Kinetic Fluorescence-based Ca2+ Mobilization Assay to Identify G Protein-coupled Receptor Agonists, Antagonists, and Allosteric Modulators
07:41

A Kinetic Fluorescence-based Ca2+ Mobilization Assay to Identify G Protein-coupled Receptor Agonists, Antagonists, and Allosteric Modulators

Published on: February 20, 2018

9.1K

Related Experiment Videos

Last Updated: Nov 6, 2025

Methods for the Discovery of Novel Compounds Modulating a Gamma-Aminobutyric Acid Receptor Type A Neurotransmission
07:16

Methods for the Discovery of Novel Compounds Modulating a Gamma-Aminobutyric Acid Receptor Type A Neurotransmission

Published on: August 16, 2018

13.8K
The Sciatic Nerve Cuffing Model of Neuropathic Pain in Mice
07:09

The Sciatic Nerve Cuffing Model of Neuropathic Pain in Mice

Published on: July 16, 2014

48.7K
A Kinetic Fluorescence-based Ca2+ Mobilization Assay to Identify G Protein-coupled Receptor Agonists, Antagonists, and Allosteric Modulators
07:41

A Kinetic Fluorescence-based Ca2+ Mobilization Assay to Identify G Protein-coupled Receptor Agonists, Antagonists, and Allosteric Modulators

Published on: February 20, 2018

9.1K

Area of Science:

  • Neuroscience
  • Molecular Biology
  • Structural Biology

Background:

  • Single-channel analysis indicated a transient "flipped" state in glycine receptor activation by partial agonists.
  • Understanding receptor activation mechanisms is crucial for drug development.

Purpose of the Study:

  • To elucidate the structural basis of glycine receptor activation by partial agonists.
  • To investigate the nature and kinetics of intermediate states during receptor gating.

Main Methods:

  • X-ray crystallography was employed to determine the structures of the glycine receptor.
  • Structural analysis focused on agonist-bound states and comparison with previous kinetic data.

Main Results:

  • Novel structures reveal a stable, partially activated agonist-bound closed state.
  • This state is significantly longer-lived than the previously proposed transient "flipped" state.
  • The findings challenge existing models of glycine receptor activation.

Conclusions:

  • Glycine receptor activation by partial agonists proceeds through a surprisingly stable intermediate.
  • This stable, partially activated state represents a distinct mechanistic step previously uncharacterized.
  • Structural insights provide a new framework for understanding receptor function and allosteric modulation.