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Related Experiment Video

Updated: Feb 9, 2026

Interactions with and Membrane Permeabilization of Brain Mitochondria by Amyloid Fibrils

Interactions with and Membrane Permeabilization of Brain Mitochondria by Amyloid Fibrils

Published on: September 28, 2019

Study of Amyloids Using Yeast.

Reed B Wickner¹, Dmitry Kryndushkin^2,3, Frank Shewmaker³

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.)

|June 11, 2018

Summary

This summary is machine-generated.

This study outlines genetic and biochemical techniques for yeast prion research. Key methods include cytoduction, prion infection, and fluorescent protein tagging for studying amyloid filaments.

Keywords:

Cytoduction Electron diffraction Mass per length Protein transformation

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Last Updated: Feb 9, 2026

Interactions with and Membrane Permeabilization of Brain Mitochondria by Amyloid Fibrils

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Published on: September 28, 2019

Yeast As a Chassis for Developing Functional Assays to Study Human P53

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Genetic Studies of Human DNA Repair Proteins Using Yeast as a Model System

Genetic Studies of Human DNA Repair Proteins Using Yeast as a Model System

Published on: March 18, 2010

Area of Science:

Molecular biology
Biochemistry
Yeast genetics

Background:

Amyloids are protein aggregates implicated in various diseases.
Yeast prions are protein-based genetic elements that form amyloid structures.
Understanding yeast prions provides insights into amyloid formation and propagation.

Purpose of the Study:

To present a comprehensive overview of methods for studying yeast amyloids and prions.
To provide researchers with practical techniques for amyloid research in yeast models.

Main Methods:

Cytoduction for cytoplasmic mixing and genetic analysis.
Infection of yeast cells with pre-formed prion amyloids.
Green fluorescent protein (GFP) fusions for visualizing amyloid protein localization.
In vitro protein purification and amyloid formation assays.
Electron microscopy for analyzing amyloid filament ultrastructure.

Main Results:

Detailed descriptions of established and novel techniques are provided.
The presented methods enable genetic, biochemical, and physical characterization of yeast prions.
Successful application of these methods allows for the study of amyloid formation and propagation.

Conclusions:

A robust set of tools is available for yeast prion research.
These methods facilitate the investigation of amyloid structures and their biological roles.
Further research into yeast amyloids can inform our understanding of related human diseases.