| Chapter title |
Analyzing Tau Aggregation with Electron Microscopy.
|
|---|---|
| Chapter number | 7 |
| Book title |
Protein Amyloid Aggregation
|
| Published in |
Methods in molecular biology, January 2016
|
| DOI | 10.1007/978-1-4939-2978-8_7 |
| Pubmed ID | |
| Book ISBNs |
978-1-4939-2977-1, 978-1-4939-2978-8
|
| Authors |
Huseby, Carol J, Kuret, Jeff, Carol J. Huseby, Jeff Kuret |
| Abstract |
Conversion of monomeric tau protein into filamentous aggregates is a defining event in the pathogenesis of Alzheimer's disease. To gain insight into disease pathogenesis, the mechanisms that trigger and mediate tau aggregation are under intense investigation. Characterization efforts have relied primarily on recombinant tau protein preparations and high-throughput solution-based detection methods such as thioflavin-dye fluorescence and laser-light-scattering spectroscopies. Transmission electron microscopy (TEM) is a static imaging tool that complements these approaches by detecting individual tau filaments at nanometer resolution. In doing so, it can provide unique insight into the quality, quantity, and composition of synthetic tau filament populations. Here we describe protocols for analysis of tau filament populations by TEM for purposes of dissecting aggregation mechanism. |
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