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Protein Misfolding Cyclic Amplification of Prions
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Protein Misfolding Cyclic Amplification of Prions

Published on: November 7, 2012

Interactions between non-identical prion proteins.

Aaron C Gonzalez Nelson1, Eric D Ross

  • 1Department of Biochemistry and Molecular Biology, Colorado State University, Fort Collins, CO 80523, USA.

Seminars in Cell & Developmental Biology
|March 1, 2011
PubMed
Summary
This summary is machine-generated.

Prion formation involves specific protein conversion. Heterologous prion interactions, including across species or between unrelated proteins in yeast, can influence prion propagation and disease transmission.

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Last Updated: Jun 4, 2026

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Monitoring Cell-to-cell Transmission of Prion-like Protein Aggregates in Drosophila Melanogaster
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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 formation converts soluble proteins into infectious amyloids.
  • Prion aggregation is typically templated by identical proteins.
  • Interactions between non-identical prions can modulate prion formation and propagation.

Purpose of the Study:

  • To examine heterologous prion interactions.
  • To investigate cross-species prion transmission (species barrier).
  • To analyze interactions between unrelated prion proteins within a single species.

Main Methods:

  • Analysis of prion formation and propagation mechanisms.
  • Studies on protein sequence effects on cross-species transmission.
  • Investigating yeast prion interactions in Saccharomyces cerevisiae.

Main Results:

  • Subtle protein sequence changes can significantly impact cross-species prion transmission.
  • In Saccharomyces cerevisiae, unrelated prion proteins can interact to affect prion formation and propagation.
  • Heterologous prion interactions influence prion disease transmission efficiency and yeast physiology.

Conclusions:

  • Prion interactions are complex, extending beyond identical protein templating.
  • Understanding these interactions is crucial for prion disease transmission and yeast prion biology.
  • Yeast models offer insights into diverse prion interaction mechanisms.