Chapter title |
Yeast as a platform to explore polyglutamine toxicity and aggregation.
|
---|---|
Chapter number | 11 |
Book title |
Tandem Repeats in Genes, Proteins, and Disease
|
Published in |
Methods in molecular biology, January 2013
|
DOI | 10.1007/978-1-62703-438-8-11 |
Pubmed ID | |
Book ISBNs |
978-1-62703-437-1, 978-1-62703-438-8
|
Authors |
Duennwald, Martin L, Martin L. Duennwald |
Abstract |
Protein misfolding is associated with many neurodegenerative diseases, including neurodegenerative diseases caused by polyglutamine expansion proteins, such as Huntington's disease. The model organism baker's yeast (Saccharomyces cerevisiae) has provided important general insights into the basic cellular mechanisms underlying protein misfolding. Furthermore, experiments in yeast have identified cellular factors that modulate the toxicity and the aggregation associated with polyglutamine expansion proteins. Notably, many features discovered in yeast have been proven to be highly relevant in other model organisms and in human pathology. The experimental protocols depicted here serve to reliably determine polyglutamine toxicity and polyglutamine aggregation in yeast. |
Mendeley readers
Geographical breakdown
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Demographic breakdown
Readers by professional status | Count | As % |
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Researcher | 5 | 167% |
Student > Bachelor | 4 | 133% |
Student > Doctoral Student | 1 | 33% |
Student > Ph. D. Student | 1 | 33% |
Professor | 1 | 33% |
Other | 2 | 67% |
Readers by discipline | Count | As % |
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Biochemistry, Genetics and Molecular Biology | 3 | 100% |
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Nursing and Health Professions | 1 | 33% |
Other | 2 | 67% |