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Related Concept Videos

Transducer Mechanism: G Protein–Coupled Receptors01:30

Transducer Mechanism: G Protein–Coupled Receptors

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G Protein–Coupled Receptors (GPCRs) are membrane-bound receptors that transiently associate with heterotrimeric G proteins and induce an appropriate response to various stimuli. GPCRs regulate critical physiological pathways and are excellent drug targets for treating diseases such as diabetes, cancer, obesity, depression, or Alzheimer's. Nearly 35% of approved drugs implement their therapeutic effects by selectively interacting with specific GPCRs.
GPCRs are also called heptahelical,...
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G Protein-coupled Receptors01:15

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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.
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Plant cells communicate to coordinate their cycle of growth, flowering and fruiting, and activities in roots, shoots, and leaves in response to the changing environmental conditions. Plant signaling is distinct from animal signaling. Plants primarily utilize enzyme-linked receptors, whereas the largest class of cell-surface receptors in animals are G-protein coupled receptors (GPCRs). Unlike animals, receptor tyrosine kinases are rare in plants. Instead, plants have a diverse class of...
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Transducer Mechanism: Enzyme-Linked Receptors01:27

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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:
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G-protein Coupled Receptors01:21

G-protein Coupled Receptors

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G-protein coupled receptors are ligand binding receptors that indirectly affect changes in the cell. The actual receptor is a single polypeptide that transverses the cell membrane seven times creating intracellular and extracellular loops. The extracellular loops create a ligand specific pocket which binds to neurotransmitters or hormones. The intracellular loops holds onto the G-protein.
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Related Experiment Video

Updated: Mar 20, 2026

Monitoring Activation of the Antiviral Pattern Recognition Receptors RIG-I And PKR By Limited Protease Digestion and Native PAGE
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RIG-I-Like Receptors: One STrEP Forward.

Charlotte Lässig1, Karl-Peter Hopfner2

  • 1Gene Center, Ludwig-Maximilians-Universität München, Munich, Germany; Department of Biochemistry, Ludwig-Maximilians-Universität München, Munich, Germany.

Trends in Microbiology
|May 30, 2016
PubMed
Summary
This summary is machine-generated.

RIG-I-like receptors (RLRs) detect viral RNA to trigger innate immunity. New research used STrEP-purification and sequencing to reveal how RLRs bind viral RNA, showing specialization and collaboration in antiviral defense.

Keywords:
LGP2MDA5RIG-IRNAaffinity purificationinnate immune systemnext generation sequencing

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Genetically-encoded Molecular Probes to Study G Protein-coupled Receptors
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Area of Science:

  • Immunology
  • Virology
  • Molecular Biology

Background:

  • RIG-I-like receptors (RLRs) are crucial sensors of viral RNA in the cytosol.
  • RLRs initiate the innate immune response against viral infections.
  • Understanding RLR-RNA interactions is key to antiviral immunity.

Purpose of the Study:

  • To characterize the physiological viral RNA ligands bound by RLRs in infected cells.
  • To investigate the binding mechanisms and interactions of all three RLRs with viral RNA.

Main Methods:

  • Utilized the one STrEP-purification technique.
  • Employed next-generation sequencing (NGS) for comprehensive analysis.
  • Studied RLRs within the context of an infected cell.

Main Results:

  • Identified specific viral RNA structures bound by RLRs.
  • Revealed distinct binding preferences and sites for each RLR.
  • Demonstrated collaborative binding patterns among different RLRs.

Conclusions:

  • RLRs exhibit specialized roles in viral RNA recognition.
  • Collaboration between RLRs enhances the antiviral response.
  • New insights into RLR-RNA binding provide a foundation for therapeutic strategies.