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

Repressible Operon: trp Operon01:21

Repressible Operon: trp Operon

2.5K
The trp operon in Escherichia coli exemplifies a repressible operon. It regulates the synthesis of tryptophan through repressor-mediated transcriptional control and attenuation. This dual regulatory mechanism ensures tryptophan biosynthesis occurs only when needed, conserving cellular resources.Structure of the trp OperonThe trp operon consists of five structural genes (trpE, trpD, trpC, trpB, and trpA) that encode enzymes for tryptophan biosynthesis. These genes are transcribed as a single...
2.5K
Thermosensation01:43

Thermosensation

35.5K
Peripheral thermosensation is the perception of external temperature. A change in temperature (on the surface of the skin and other tissues) is detected by a family of temperature-sensitive ion channels called Transient Receptor Potential, or TRP, receptors. These receptors are located on free nerve endings. Those detecting cold temperatures are closer to the surface of the skin than the nerve endings detecting warmth. These thermoTRP channels, while temperature selective, have relatively...
35.5K
Mechanically-gated Ion Channels01:12

Mechanically-gated Ion Channels

8.1K
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...
8.1K

You might also read

Related Articles

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

Sort by
Same author

Structural physiology of distinctive water channels elucidated by cryo-EM.

IUCrJ·2026
Same author

Search for Inhibitors against Inflammatory Responses of Microglia in a Meroterpenoid Library Constructed by Synthetic-Biological Manipulation of Biosynthetic Pathways.

ACS omega·2026
Same author

Cryo-EM structure of human AQP11 reveals a trimeric architecture with a large pore.

Science advances·2026
Same author

N-[3-(4-(2-methoxyphenyl) piperazine-1-yl) propyl]-heteroaromatic carboxamide as selective α<sub>1A/1D</sub>-adrenoceptor antagonists: SAR study and metabolic stability evaluation.

Bioorganic & medicinal chemistry letters·2025
Same author

A fungi-derived cyclic peptide enhances Th9-mediated antitumor immunity by targeting ZAP70 and SREBP1.

The Journal of clinical investigation·2025
Same author

Selective agonism of GPR34 stimulates microglial uptake and clearance of amyloid β fibrils.

Alzheimer's research & therapy·2025

Related Experiment Video

Updated: Apr 2, 2026

Use of Label-free Optical Biosensors to Detect Modulation of Potassium Channels by G-protein Coupled Receptors
10:59

Use of Label-free Optical Biosensors to Detect Modulation of Potassium Channels by G-protein Coupled Receptors

Published on: February 10, 2014

10.7K

Deciphering Subtype-Selective Modulations in TRPA1 Biosensor Channels.

Daisuke Kozai, Reiko Sakaguchi, Tomohiko Ohwada

  • 1Laboratory of Molecular Biology, Department of Synthetic Chemistry and Biological Chemistry, Graduate School of Engineering, Kyoto University, Katsura Campus, Nishikyoku, Kyoto 615-8510, Japan. mori@sbchem.kyoto-u.ac.jp.

Current Neuropharmacology
|September 29, 2015
PubMed
Summary

Transient receptor potential ankyrin 1 (TRPA1) channels are key sensors. Novel N-nitrosamine compounds selectively activate TRPA1 via S-nitrosylation, offering a new therapeutic avenue.

More Related Videos

Yeast Luminometric and Xenopus Oocyte Electrophysiological Examinations of the Molecular Mechanosensitivity of TRPV4
12:09

Yeast Luminometric and Xenopus Oocyte Electrophysiological Examinations of the Molecular Mechanosensitivity of TRPV4

Published on: December 31, 2013

10.7K
Monitoring Leucine-Rich Repeat Containing 8 Channel (LRRC8/VRAC) Activity Using Sensitized-Emission F&#246;rster Resonance Energy Transfer (SE-FRET)
08:54

Monitoring Leucine-Rich Repeat Containing 8 Channel (LRRC8/VRAC) Activity Using Sensitized-Emission Förster Resonance Energy Transfer (SE-FRET)

Published on: August 9, 2024

991

Related Experiment Videos

Last Updated: Apr 2, 2026

Use of Label-free Optical Biosensors to Detect Modulation of Potassium Channels by G-protein Coupled Receptors
10:59

Use of Label-free Optical Biosensors to Detect Modulation of Potassium Channels by G-protein Coupled Receptors

Published on: February 10, 2014

10.7K
Yeast Luminometric and Xenopus Oocyte Electrophysiological Examinations of the Molecular Mechanosensitivity of TRPV4
12:09

Yeast Luminometric and Xenopus Oocyte Electrophysiological Examinations of the Molecular Mechanosensitivity of TRPV4

Published on: December 31, 2013

10.7K
Monitoring Leucine-Rich Repeat Containing 8 Channel (LRRC8/VRAC) Activity Using Sensitized-Emission F&#246;rster Resonance Energy Transfer (SE-FRET)
08:54

Monitoring Leucine-Rich Repeat Containing 8 Channel (LRRC8/VRAC) Activity Using Sensitized-Emission Förster Resonance Energy Transfer (SE-FRET)

Published on: August 9, 2024

991

Area of Science:

  • Ion channel biology
  • Molecular pharmacology
  • Pain research

Background:

  • Transient receptor potential (TRP) proteins function as cellular sensors.
  • TRPA1 channels are implicated in neuropathic pain and physiological functions.
  • TRPA1 is sensitive to oxidative stress and electrophilic compounds.

Purpose of the Study:

  • To review molecular pharmacology of TRPA1 modulators.
  • To discuss mechanisms of TRPA1 modulation.
  • To highlight novel selective TRPA1 activators.

Main Methods:

  • Literature review of TRPA1 modulators.
  • Analysis of oxidative modification of cysteine residues.
  • Investigation of S-nitrosylation mechanisms.

Main Results:

  • TRPA1 is activated by oxidative stress and electrophiles via cysteine modification.
  • Non-electrophilic compounds also modulate TRPA1, potentially at non-cysteine sites.
  • Novel N-nitrosamine compounds selectively activate TRPA1 through S-nitrosylation.

Conclusions:

  • Selective TRPA1 modulation by small molecules remains a challenge.
  • N-nitrosamine compounds offer subtype selectivity via synergistic mechanisms.
  • Understanding TRPA1 modulation is crucial for therapeutic development.