Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

G-Protein Gated Ion Channels

G-Protein Gated Ion Channels

GPCRs are primarily responsible for our sense of smell, taste, and vision. The binding of a sensory stimulus activates GPCR to stimulate effector proteins, many of which are ion channels in the sensory organs. GPCRs modulate the opening and closing of the target ion channels either directly by binding them, or by releasing second messengers that activate these channels. As ions move across the membrane, the membrane potential is altered, which induces an appropriate response.
Sensory organs,...

You might also read

Related Articles

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

Sort by

Same author

Control of Gemcitabine Activity With Blue and Red Light.

Chemistry (Weinheim an der Bergstrasse, Germany)·2026

Same author

Dissecting the Chemical and Thermal Stabilities of Tetrads in G-Quadruplexes to Derive a Structure-Activity Relation for a Thrombin-Binding DNA G-Quadruplex Aptamer.

Chembiochem : a European journal of chemical biology·2026

Same author

Phospholipid-driven conformational switching of HCV NS5A links protein folding to replication membrane remodeling.

Science advances·2026

Same author

Single-molecule dynamics reveal ATP binding alone powers substrate translocation by an ABC transporter.

Nature communications·2026

Same author

Investigations into linker effects of DNA-VHL ligand conjugates by multiplexed affinity measurements using focal molography.

RSC chemical biology·2026

Same author

Wash-Free Multi-Target Super-Resolution Microscopy With Photocaged DNA Labels.

Angewandte Chemie (International ed. in English)·2026

Same journal

Incorporation of Engineered Cu<sup>0</sup>/Cu<sup>+</sup> Interfaces in Metal-Organic Frameworks for Boosting CO<sub>2</sub> Hydrogenation to Methanol.

Angewandte Chemie (International ed. in English)·2026

Same journal

Planar Chiral Carbazole-Naphthalene Bisimide Hetero-Cyclophane for Circularly Polarized Delayed Fluorescence.

Angewandte Chemie (International ed. in English)·2026

Same journal

Charge-Transfer Exciton Flows: Red Luminescent Zn<sub>8</sub>D<sub>14</sub>A<sub>4</sub> Nanotubes.

Angewandte Chemie (International ed. in English)·2026

Same journal

Au(III) Complexes as Pyroptosis Inducers by Targeting Mitochondrial DNA for Tumor Immunity.

Angewandte Chemie (International ed. in English)·2026

Same journal

Suppressing Interfacial-Accelerated Degradation in Perovskite Solar Cells via Supramolecular Co-Assembly.

Angewandte Chemie (International ed. in English)·2026

Same journal

Isolation and Reactivity of a Stannabismuthene.

Angewandte Chemie (International ed. in English)·2026

See all related articles

Search research articles

Related Experiment Video

Updated: May 24, 2026

Live Imaging of the Mitochondrial Glutathione Redox State in Primary Neurons using a Ratiometric Indicator

Live Imaging of the Mitochondrial Glutathione Redox State in Primary Neurons using a Ratiometric Indicator

Published on: October 20, 2021

Caged glutathione - triggering protein interaction by light.

Volker Gatterdam¹, Tatjana Stoess, Clara Menge

¹Institute of Biochemistry, Biocenter, Cluster of Excellence Frankfurt, Goethe University Frankfurt, Frankfurt am Main, Germany.

Angewandte Chemie (International Ed. in English)

|March 7, 2012

Summary

This summary is machine-generated.

Researchers developed a photoactivatable glutathione (GSH) to control the GSH-GST network with light. This breakthrough enables light-triggered assembly of glutathione S-transferase (GST) fusion proteins in situ.

More Related Videos

Studies of Chaperone-Cochaperone Interactions using Homogenous Bead-Based Assay

Studies of Chaperone-Cochaperone Interactions using Homogenous Bead-Based Assay

Published on: July 21, 2021

Bioluminescent Optogenetics 2.0: Harnessing Bioluminescence to Activate Photosensory Proteins In Vitro and In Vivo

Bioluminescent Optogenetics 2.0: Harnessing Bioluminescence to Activate Photosensory Proteins In Vitro and In Vivo

Published on: August 4, 2021

Related Experiment Videos

Last Updated: May 24, 2026

Live Imaging of the Mitochondrial Glutathione Redox State in Primary Neurons using a Ratiometric Indicator

Live Imaging of the Mitochondrial Glutathione Redox State in Primary Neurons using a Ratiometric Indicator

Published on: October 20, 2021

Studies of Chaperone-Cochaperone Interactions using Homogenous Bead-Based Assay

Studies of Chaperone-Cochaperone Interactions using Homogenous Bead-Based Assay

Published on: July 21, 2021

Bioluminescent Optogenetics 2.0: Harnessing Bioluminescence to Activate Photosensory Proteins In Vitro and In Vivo

Bioluminescent Optogenetics 2.0: Harnessing Bioluminescence to Activate Photosensory Proteins In Vitro and In Vivo

Published on: August 4, 2021

Area of Science:

Biochemistry
Molecular Biology
Biotechnology

Background:

Glutathione (GSH) is a crucial endogenous antioxidant and cofactor.
Glutathione S-transferase (GST) enzymes utilize GSH for detoxification and other cellular processes.
Controlling cellular redox and enzymatic activity with external stimuli is a significant challenge.

Purpose of the Study:

To develop a photoactivatable glutathione (GSH) system.
To enable light-inducible control over the GSH-GST network.
To demonstrate the spatial and structural assembly of GST fusion proteins using light.

Main Methods:

Synthesis of a photoactivatable glutathione analog.
Utilizing laser-scanning activation to trigger GSH-GST interactions.
Engineering GST fusion proteins for light-controlled assembly.

Main Results:

Successful photoactivation of the GSH-GST network using light.
Demonstrated in situ assembly of GST fusion proteins at variable densities.
Showcased precise spatial control over protein assembly via laser scanning.

Conclusions:

Photoactivatable GSH provides a novel tool for spatiotemporal control of biological processes.
Light-triggered assembly of GST fusion proteins offers new possibilities in synthetic biology and biomaterials.
This approach enhances our ability to manipulate cellular redox and enzymatic functions with high precision.