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Analyzing Tau Aggregation with Electron Microscopy

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Protein Amyloid Aggregation

Part of the book series: Methods in Molecular Biology ((MIMB,volume 1345))

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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Acknowledgment

This work was supported by NIH grant AG14452. Images presented in this report were generated using an instrument at the Campus Microscopy and Imaging Facility, The Ohio State University, Columbus, OH.

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Authors and Affiliations

  1. Department of Molecular and Cellular Biochemistry, Interdisciplinary Biophysics Graduate Program, The Ohio State University College of Medicine, Columbus, OH, USA

    Carol J. Huseby

  2. Department of Molecular and Cellular Biochemistry, The Ohio State University College of Medicine, 108 Rightmire Hall, 1060 Carmack Road, Columbus, OH, 43210, USA

    Jeff Kuret Ph.D.

Authors
  1. Carol J. Huseby
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  2. Jeff Kuret Ph.D.
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Corresponding author

Correspondence to Jeff Kuret Ph.D. .

Editor information

Editors and Affiliations

  1. Weill Cornell Medical College, New York, New York, USA

    David Eliezer

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Huseby, C.J., Kuret, J. (2016). Analyzing Tau Aggregation with Electron Microscopy. In: Eliezer, D. (eds) Protein Amyloid Aggregation. Methods in Molecular Biology, vol 1345. Humana Press, New York, NY. https://doi.org/10.1007/978-1-4939-2978-8_7

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  • DOI: https://doi.org/10.1007/978-1-4939-2978-8_7

  • Publisher Name: Humana Press, New York, NY

  • Print ISBN: 978-1-4939-2977-1

  • Online ISBN: 978-1-4939-2978-8

  • eBook Packages: Springer Protocols

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