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

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...
Biodeterioration01:28

Biodeterioration

Biodeterioration refers to the unwanted alteration of materials caused by microorganisms—especially fungi—which damage both organic substrates (paper, wood, textiles) and inorganic ones (stone, plaster, glass). Unlike abiotic decay, biodeterioration results from biological activity that produces physical disruption and chemical degradation.Physical deterioration occurs as fungal hyphae penetrate pores, cracks, and surface irregularities. Hyphal turgor pressure, thigmotropic growth along...
Regulated Protein Degradation02:58

Regulated Protein Degradation

It is vital to regulate the activity of enzymatic as well as non-enzymatic proteins inside the cell. This can be achieved either through creating a balance between their rate of synthesis and degradation or regulating the intrinsic activity of the protein. Both these regulation mechanisms play an essential role in the normal functioning of cells.
Protein degradation plays two important roles in the cells. It helps to protect cells from misfolded or damaged proteins before they lead to a...
Parkinson Disease ll: Pathophysiology01:24

Parkinson Disease ll: Pathophysiology

Parkinson disease (PD) is a progressive neurodegenerative disorder primarily affecting movement, with additional non-motor features. Its pathophysiology involves complex interactions among genetic susceptibility, environmental exposures, and cellular dysfunction, including dopaminergic neuron loss, protein aggregation, and mitochondrial impairment.Selective NeurodegenerationA key feature is the degeneration of dopaminergic neurons in the substantia nigra pars compacta, leading to reduced...

You might also read

Related Articles

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

Sort by
Same author

Gpnmb defines a phagocytic state of microglia linked to cell death in prion disease mouse model.

Nature communications·2026
Same author

Altered crosstalk of bacterial lipopolysaccharide with immune cells in colorectal cancer compared to paired adjacent intestinal tissue.

Gut microbes·2026
Same author

Prion propagation is controlled by a hierarchical network involving the nuclear Tfap2c and hnRNP K factors and the cytosolic mTORC1 complex.

PLoS pathogens·2026
Same author

Large-scale bidirectional arrayed genetic screens identify OXR1 and EMC4 as modifiers of αSynuclein aggregation.

FEBS open bio·2026
Same author

Structure-function relationship of alpha-synuclein fibrillar polymorphs derived from distinct synucleinopathies.

Molecular systems biology·2026
Same author

Lysosomal escape and TMEM106B fibrillar core determine TDP-43 seeding outcomes.

bioRxiv : the preprint server for biology·2026

Related Experiment Video

Updated: May 21, 2026

Protein Misfolding Cyclic Amplification of Prions
10:12

Protein Misfolding Cyclic Amplification of Prions

Published on: November 7, 2012

Prion propagation, toxicity and degradation.

Adriano Aguzzi1, Jeppe Falsig

  • 1Institute of Neuropathology, University Hospital Zürich, Zürich, Switzerland. adriano.aguzzi@usz.ch

Nature Neuroscience
|June 28, 2012
PubMed
Summary

Prion diseases like mad cow disease can spread between individuals. This review explores how prions harm hosts and the body's defense mechanisms against these infections.

Area of Science:

  • Neuroscience
  • Infectious Diseases
  • Molecular Biology

Background:

  • Prion diseases, such as bovine spongiform encephalopathy (BSE), caused significant public concern due to human transmission via contaminated food and blood transfusions.
  • Interest in prion science has declined following the decrease in BSE cases.
  • Recent findings reveal that various diseases share prion-like characteristics, including cell-to-cell spread.

Purpose of the Study:

  • To review recent advancements in prion biology.
  • To highlight key unanswered questions regarding prion pathogenesis and host defense mechanisms.

Main Methods:

  • Literature review of prion science developments.
  • Synthesis of current understanding of prion-host interactions.

More Related Videos

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

Prion Safety Laboratory Swipe Test
06:01

Prion Safety Laboratory Swipe Test

Published on: February 14, 2025

Related Experiment Videos

Last Updated: May 21, 2026

Protein Misfolding Cyclic Amplification of Prions
10:12

Protein Misfolding Cyclic Amplification of Prions

Published on: November 7, 2012

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

Prion Safety Laboratory Swipe Test
06:01

Prion Safety Laboratory Swipe Test

Published on: February 14, 2025

Main Results:

  • Prion diseases exhibit complex transmission dynamics, including zoonotic and iatrogenic routes.
  • Emerging evidence links other diseases to prion-like mechanisms of propagation.
  • Fundamental questions remain about the molecular mechanisms of prion-induced neurotoxicity.
  • The host's innate and adaptive immune responses to prion invasion are not fully elucidated.

Conclusions:

  • Prion science continues to evolve, with new insights into disease mechanisms and potential therapeutic targets.
  • Understanding prion pathogenesis and host responses is crucial for addressing both prion and prion-like diseases.
  • Further research is needed to unravel the complexities of prion interactions within the host.