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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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Study of amyloids using yeast.

Reed B Wickner1, Dmitry Kryndushkin, Frank Shewmaker

  • 1Laboratory of Biochemistry and Genetics, National Institute of Diabetes Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD, USA. wickner@helix.nih.gov

Methods in Molecular Biology (Clifton, N.J.)
|April 25, 2012
PubMed
Summary
This summary is machine-generated.

This study outlines key genetic, biochemical, and physical techniques for investigating yeast amyloids and prions. These methods enable detailed analysis of prion propagation and amyloid filament structures in yeast models.

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Area of Science:

  • Molecular biology
  • Biochemistry
  • Genetics

Background:

  • Amyloids are protein aggregates implicated in various diseases.
  • Yeast prions are protein-based genetic elements formed by amyloid structures.
  • Understanding yeast prions provides insights into amyloid biology.

Purpose of the Study:

  • To present a comprehensive overview of methods for studying yeast amyloids.
  • To detail techniques for analyzing yeast prions and their underlying amyloid structures.

Main Methods:

  • Cytoduction for cytoplasmic mixing and prion transmission studies.
  • Infection of yeast cells with pre-formed prion amyloids.
  • Green fluorescent protein (GFP) fusions for visualizing amyloid formation in vivo.
  • Protein purification and in vitro amyloid formation assays.
  • Electron microscopy for analyzing amyloid filament morphology.

Main Results:

  • Established protocols for genetic, biochemical, and physical characterization of yeast amyloids.
  • Demonstrated utility of various techniques for prion research.
  • Provided a toolkit for researchers studying amyloid formation and propagation.

Conclusions:

  • The presented methods are essential for advancing research on yeast prions.
  • These techniques facilitate a deeper understanding of amyloidogenesis and its implications.
  • This work serves as a valuable resource for the scientific community studying protein misfolding.