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Related Concept Videos

Amyloid Fibrils03:03

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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,...
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Subviral Agents01:29

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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...
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Alzheimer's Disease (AD) is a continually advancing neurodegenerative disorder, distinguished by escalating memory loss, cognitive dysfunction, and dementia. The disease unfolds in three stages: preclinical, mild cognitive impairment (MCI), and dementia. Its onset is insidious, and the progression gradual, with the cause not well explained by other disorders.
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Updated: Mar 23, 2026

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

L O Tjernberg1, A Rising1,2, J Johansson1,2

  • 1Department of Neurobiology Care Sciences and Society, Division of Neurogeriatrics, Center for Alzheimer Research, Karolinska Institutet, Huddinge, Sweden.

Journal of Internal Medicine
|March 23, 2016
PubMed
Summary
This summary is machine-generated.

Protein misfolding causes about 30 lethal human diseases. Research investigates if diseases like Alzheimer's and Parkinson's, and biomaterials like artificial spider silk, could be transmissible like prion diseases.

Keywords:
amyloidfibrilprionspider silktransmission

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Area of Science:

  • Biochemistry
  • Neuroscience
  • Materials Science

Background:

  • Approximately 30 human diseases are linked to protein misfolding and amyloid formation, posing significant societal and health burdens.
  • Prion proteins are established pathogenic agents in transmissible diseases like Creutzfeldt-Jakob disease and bovine spongiform encephalopathy.
  • Emerging research explores the potential transmissibility of other amyloid diseases and the amyloidogenic nature of novel biomaterials.

Purpose of the Study:

  • To introduce amyloid, prions, and related proteins involved in amyloid diseases.
  • To review current evidence regarding the potential transmission of amyloid diseases.
  • To discuss the implications of protein-based biomaterials, such as artificial spider silk, in the context of amyloidosis.

Main Methods:

  • Literature review of scientific articles on protein misfolding diseases.
  • Analysis of research on prion protein and transmissible spongiform encephalopathies.
  • Comparative study of amyloid structures and artificial silk properties.

Main Results:

  • Established role of prions in transmissible neurodegenerative diseases.
  • Ongoing debate and research into the potential transmissibility of Alzheimer's, Parkinson's, and other amyloidoses.
  • Identification of potential amyloidogenic properties in novel biomaterials like artificial spider silk.

Conclusions:

  • Protein misfolding diseases represent a significant health challenge with potential for transmission.
  • Further research is crucial to understand the risks associated with protein-based biomaterials and their potential to form amyloids.
  • Distinguishing between amyloid structures and their disease-causing potential is vital for both medicine and biomaterial development.