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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...

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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

Recent progress in prion and prion-like protein aggregation.

Chuan-Wei Yi1, Wen-Chang Xu, Jie Chen

  • 1State Key Laboratory of Virology, College of Life Sciences, Wuhan University, Wuhan 430072, China.

Acta Biochimica Et Biophysica Sinica
|May 28, 2013
PubMed
Summary

Prion diseases and similar protein misfolding conditions arise from abnormal protein aggregates, like Tau, causing neurodegeneration. Understanding protein conformations and cellular environments is key to studying these fatal diseases.

Keywords:
macromolecular crowdingphysiological environmentprion proteinprion-like proteinprotein misfolding

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Area of Science:

  • Neuroscience
  • Biochemistry
  • Pathology

Background:

  • Prion diseases and prion-like disorders involve abnormal protein aggregation (e.g., prion protein, Tau protein) in neurons.
  • These misfolded proteins exhibit self-duplication and transmissibility, leading to fatal neurodegenerative diseases.
  • Prion diseases affect both animals and humans, with varying phenotypes linked to protein conformations.

Purpose of the Study:

  • To review structural information of prion and prion-like proteins.
  • To discuss post-translational modifications and infectious properties of prions.
  • To explore prion-like protein aggregation in cellular environments.

Main Methods:

  • Literature review of existing structural data for prion and prion-like proteins.
  • Analysis of factors contributing to prion infectivity and strain diversity.
  • In vitro studies mimicking crowded physiological environments to study protein misfolding.

Main Results:

  • Misfolded protein conformations are central to aggregation and disease pathogenesis.
  • Prion-like protein aggregation (e.g., Tau, SOD1) occurs in crowded cellular environments.
  • Distinct protein conformations correlate with different prion strains.

Conclusions:

  • Understanding protein structure and cellular environment is crucial for prion disease research.
  • Misfolded proteins, not conventional pathogens, drive these neurodegenerative conditions.
  • Further research into prion-like protein aggregation mechanisms is warranted.