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Related Concept Videos

Channel Rhodopsins01:11

Channel Rhodopsins

Most organisms use photoreceptors to sense and respond to light. Examples of photoreceptors include bacteriorhodopsins and bacteriophytochromes in some bacteria, phytochromes in plants, and rhodopsins in the photoreceptor cells of the vertebral retina. The light-sensitive property of these receptors is because of the bound chromophores, such as bilin in the phytochromes and retinal in the rhodopsins.
Rhodopsins belong to the family of cell surface proteins called G-protein coupled receptors,...
Transducer Mechanism: Enzyme-Linked Receptors01:27

Transducer Mechanism: Enzyme-Linked Receptors

Enzyme-linked receptors are cell-surface receptors acting as an enzyme or associating with an enzyme intracellularly. They make excellent drug targets. Drugs can bind to the extracellular ligand-binding domain or directly affect their enzymatic domain and alter their activity.
Major types that are helpful drug targets include:
Transducer Mechanism: Nuclear Receptors01:31

Transducer Mechanism: Nuclear Receptors

Nuclear receptors, or NRs, are unique transcription factors that regulate gene transcription and affect the cellular pathways involved in reproduction, development, or metabolism. Their ability to be stimulated by small lipophilic ligands and control vital cellular processes makes them ideal drug targets. Nearly 10-15% of currently prescribed drugs target these receptors.
About 48 different soluble family members of nuclear receptors are identified that can be divided into two main classes:
G Protein-coupled Receptors01:15

G Protein-coupled Receptors

G Protein-Coupled Receptors or GPCRs are membrane-bound receptors that transiently associate with heterotrimeric G proteins and induce an appropriate response to sensory stimuli such as light, odors, hormones, cytokines, or neurotransmitters.
GPCRs are also called heptahelical, 7TM, or serpentine receptors, and consist of seven (H1-H7) transmembrane alpha-helices that span the bilayer to form a cylindrical core. The transmembrane helices are connected by three extracellular loops and three...
Drug-Receptor Bonds01:25

Drug-Receptor Bonds

Drug-receptor bonds are formed through various chemical forces when drugs interact with target cells. Covalent bonds, strong and irreversible, are exemplified by DNA-alkylating anticancer agents that inhibit cell division. However, such irreversible drug binding lacks selectivity and can modify the DNA of the surrounding healthy cells. Covalent binding often contributes to tissue toxicity, as seen with chloroform and paracetamol metabolites binding to the liver, causing hepatotoxicity.
In...
The Two-State Receptor Model01:29

The Two-State Receptor Model

The two-state receptor model explains a drug's interaction with receptors, such as G protein-coupled receptors and ligand-gated ion channels, to induce or inhibit a biological response. When no natural ligands are present, a receptor exists in an equilibrium of inactive (Ri) and active (Ra) conformations. The inactive form does not produce a response, while the active form generates a basal effect known as constitutive activity.
The binding affinity of a drug determines its interaction with one...

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Related Experiment Video

Updated: May 17, 2026

Crystal Structure of the N-terminal Domain of Ryanodine Receptor from Plutella xylostella
11:31

Crystal Structure of the N-terminal Domain of Ryanodine Receptor from Plutella xylostella

Published on: November 30, 2018

Ryanodine receptor patents.

Alexander Kushnir1, Andrew R Marks

  • 1Department of Medicine, Jacobi Medical Center, Albert Einstein College of Medicine, 1400 Pelham ParkwaySouth, New York, NY 10461, USA.

Recent Patents on Biotechnology
|October 25, 2012
PubMed
Summary
This summary is machine-generated.

Dysfunctional ryanodine receptors (RyR) are linked to muscle diseases. Patents reveal RyR

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High-throughput Screening for Small-molecule Modulators of Inward Rectifier Potassium Channels
10:07

High-throughput Screening for Small-molecule Modulators of Inward Rectifier Potassium Channels

Published on: January 27, 2013

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Last Updated: May 17, 2026

Crystal Structure of the N-terminal Domain of Ryanodine Receptor from Plutella xylostella
11:31

Crystal Structure of the N-terminal Domain of Ryanodine Receptor from Plutella xylostella

Published on: November 30, 2018

High-throughput Screening for Small-molecule Modulators of Inward Rectifier Potassium Channels
10:07

High-throughput Screening for Small-molecule Modulators of Inward Rectifier Potassium Channels

Published on: January 27, 2013

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Pharmacology

Background:

  • Ryanodine receptors (RyR) are critical Ca(2+) release channels in muscle excitation-contraction (EC) coupling.
  • Dysfunction of RyR is implicated in the pathogenesis of cardiac and skeletal myopathies.

Purpose of the Study:

  • To review the patent landscape surrounding ryanodine receptor research.
  • To highlight the evolution of RyR as a drug target for muscle diseases.

Main Methods:

  • Patent analysis of RyR-related research and drug development.
  • Review of scientific literature on RyR function and dysfunction.

Main Results:

  • Patents trace RyR discovery from plant alkaloid targets to their role in EC coupling.
  • Ongoing clinical trials investigate RycalsTM for inhibiting pathological Ca(2+) leak.
  • Patents reflect evolving understanding and future research directions.

Conclusions:

  • RyR research has advanced significantly, leading to potential therapeutic strategies.
  • The patent literature provides a historical and forward-looking perspective on RyR-targeted therapies for myopathies.