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Related Concept Videos

Amyloid Fibrils03:03

Amyloid Fibrils

Amyloid fibrils are aggregates of misfolded proteins.  Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils. 
Amyloid deposits were observed as early as 1639 in the liver and the spleen.   In 1854, Rudolph Virchow performed iodine staining, normally used to...
Amyloid Fibrils03:03

Amyloid Fibrils

Amyloid fibrils are aggregates of misfolded proteins.  Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils. 
Amyloid deposits were observed as early as 1639 in the liver and the spleen.   In 1854, Rudolph Virchow performed iodine staining, normally used to...
Subviral Agents01:29

Subviral Agents

Subviral agents are infectious entities that resemble viruses but lack one or more viral components, such as a capsid or essential replication machinery. These agents include viroids, prions, and satellites, each possessing distinct structural and functional characteristics that influence their mode of infection and replication.Viroids are the simplest subviral agents, consisting of circular, single-stranded RNA molecules without a protein coat. They exclusively infect plants, relying entirely...
Fungal Phylum Microsporidia01:28

Fungal Phylum Microsporidia

Microsporidia are a group of obligate intracellular fungi that were initially classified as protists but were later reclassified based on phylogenetic, molecular, and structural evidence linking them to the Chytridiomycota. These unicellular, non-motile organisms are highly specialized parasites that infect a wide range of animal hosts, including humans. They have evolved extensive genomic and metabolic reductions, making them highly dependent on their hosts for survival.Morphology and Genomic...
Rabies01:28

Rabies

Rabies is a lethal zoonotic disease caused by a single-stranded, negative-sense RNA virus of the Lyssavirus genus, within the family Rhabdoviridae. Its primary mode of transmission to humans is through bites or saliva-contaminated scratches from infected mammals such as dogs, bats, raccoons, or foxes. Transmission can also occur if infectious saliva contacts abraded skin or intact mucous membranes, including the conjunctiva.Viral Entry and Early ReplicationOnce introduced at the bite or scratch...
Infection01:20

Infection

When a pathogen enters the body and reproduces, it can cause an infection, damage body cells, and cause illness symptoms that eventually lead to disease. Therefore, its prevention requires breaking the chain of infection.
The chain begins with pathogens: bacteria, viruses, fungi, prions, or parasites such as protozoa helminths. These can be present on the skin as transient or resident flora, or they can be acquired from the environment. Identifying and treating the type of infection and...

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Related Experiment Video

Updated: Jun 27, 2026

Investigating the Spreading and Toxicity of Prion-like Proteins Using the Metazoan Model Organism C. elegans
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Investigating the Spreading and Toxicity of Prion-like Proteins Using the Metazoan Model Organism C. elegans

Published on: January 8, 2015

Prion infection: seeded fibrillization or more?

Eva Birkmann1, Detlev Riesner

  • 1Institut für Physikalische Biologie, Heinrich-Heine-Universitaet Duesseldorf & Institut für Biophysik und Neurowissenschaften, Forschungszentrum Juelich, Duesseldorf, Germany.

Prion
|December 23, 2008
PubMed
Summary

Prion protein (PrP) conversion from cellular PrP(C) to infectious PrP(Sc) was studied in vitro. Mechanistic models reveal intermediates, kinetics of fibril formation, and membrane effects on prion disease.

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Related Experiment Videos

Last Updated: Jun 27, 2026

Investigating the Spreading and Toxicity of Prion-like Proteins Using the Metazoan Model Organism C. elegans
12:57

Investigating the Spreading and Toxicity of Prion-like Proteins Using the Metazoan Model Organism C. elegans

Published on: January 8, 2015

Protein Misfolding Cyclic Amplification of Prions
10:12

Protein Misfolding Cyclic Amplification of Prions

Published on: November 7, 2012

Monitoring Cell-to-cell Transmission of Prion-like Protein Aggregates in Drosophila Melanogaster
10:26

Monitoring Cell-to-cell Transmission of Prion-like Protein Aggregates in Drosophila Melanogaster

Published on: March 12, 2018

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Neuroscience

Background:

  • Prion diseases involve the misfolding of cellular prion protein (PrP(C)) into infectious PrP(Sc) isoforms.
  • Understanding the in vitro conversion mechanism is crucial for developing therapeutic strategies.

Purpose of the Study:

  • To investigate the in vitro conversion process of prion protein.
  • To develop mechanistic models of prion protein conversion and fibrillogenesis.

Main Methods:

  • In vitro conversion assays using recombinant and cellular PrP.
  • Characterization of intermediates and precursor states.
  • Kinetic studies of spontaneous and seeded fibrillogenesis.
  • Analysis of the impact of the membrane environment.

Main Results:

  • Detailed characterization of intermediate and precursor states during PrP conversion.
  • Kinetic analysis of both spontaneous and seeded fibrillogenesis.
  • Demonstration of the influence of membrane environments on prion conversion.

Conclusions:

  • The study provides insights into the molecular mechanisms of prion protein conversion.
  • Mechanistic models derived from in vitro studies can explain key aspects of prion pathogenesis.
  • Further research into membrane interactions may offer new avenues for therapeutic intervention.