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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. 
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Lysosomes are the site for the degradation of macromolecules and biological polymers released during membrane trafficking events such as secretory, endocytic, autophagic, and phagocytic pathways. The membrane-enclosed area of the lysosome, called the lumen, contains hydrolytic enzymes active in an acidic environment. These acid hydrolases are functional at a pH between 4.5 and 5 and are involved in cellular processes such as cell signaling, energy metabolism, restoration of the plasma membrane,...
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Local Anesthetics: Mechanism of Action01:23

Local Anesthetics: Mechanism of Action

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Updated: May 23, 2026

Isolation of Soluble and Insoluble PrP Oligomers in the Normal Human Brain
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Published on: October 3, 2012

Lichens: unexpected anti-prion agents?

Cynthia M Rodriguez1, James P Bennett, Christopher J Johnson

  • 1USGS National Wildlife Health Center; Department of Bacteriology, University of Wisconsin, Madison, WI, USA.

Prion
|March 29, 2012
PubMed
Summary
This summary is machine-generated.

Certain lichens degrade disease-causing prion protein (PrP) using a serine protease. This discovery offers potential new strategies for managing environmental prion contamination in diseases like chronic wasting disease.

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Protein Misfolding Cyclic Amplification of Prions
10:12

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Published on: November 7, 2012

Area of Science:

  • Environmental microbiology
  • Prion biology
  • Biochemistry

Background:

  • Prion diseases, such as sheep scrapie and chronic wasting disease (CWD), spread through environmental reservoirs.
  • Prions persist in the environment, posing a long-term transmission risk.
  • Inactivating environmental prions is crucial for disease control.

Purpose of the Study:

  • To identify environmental factors capable of prion inactivation.
  • To investigate the potential of lichens to degrade prion protein (PrP).

Main Methods:

  • Tested over twenty lichen species for their ability to degrade abnormal prion protein (PrP).
  • Assessed the efficacy of a lichen-derived serine protease against various prion strains and hosts.
  • Quantified PrP reduction levels.

Main Results:

  • Approximately half of the tested lichen species demonstrated PrP degradation capabilities.
  • A lichen-derived serine protease effectively degraded PrP from multiple hosts and prion strains.
  • PrP levels were reduced by at least two logs.

Conclusions:

  • Lichens possess a serine protease with the capacity to degrade abnormal prion protein (PrP).
  • Further research is needed to assess the impact of lichens on prion infectivity and environmental prion levels.
  • Lichens may play a role in mitigating environmental prion contamination and warrant consideration in dietary studies.