Protein Amyloid Aggregation

Methods and Protocols

  • David Eliezer

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

Table of contents

  1. Front Matter
    Pages i-xiv
  2. Labeling Strategies

    1. Front Matter
      Pages 1-1
    2. Tianqi O. Zhang, Maksim Grechko, Sean D. Moran, Martin T. Zanni
      Pages 21-41
  3. Kinetics/Mechanism

  4. Oligomers

    1. Front Matter
      Pages 113-113
    2. Wojciech Paslawski, Nikolai Lorenzen, Daniel E. Otzen
      Pages 133-150
    3. Niels Zijlstra, Nathalie Schilderink, Vinod Subramaniam
      Pages 151-169
  5. Fibrils

    1. Front Matter
      Pages 171-171
    2. Marcus D. Tuttle, Joseph M. Courtney, Alexander M. Barclay, Chad M. Rienstra
      Pages 173-183
    3. Asher Moshe, Meytal Landau, David Eisenberg
      Pages 201-210
    4. Andrei T. Alexandrescu
      Pages 211-222
  6. Computational Approaches

    1. Front Matter
      Pages 223-223

About this book

Introduction

This detailed volume focuses on methods for the characterization of aggregation processes that lead to the formation of amyloid fibrils and amyloid oligomers which feature in the etiology of a variety of human disorders collectively known as amyloidoses. The scope of the collection includes techniques for visualizing early steps on the amyloid formation pathway, methods for capturing and characterizing oligomeric, potentially toxic, intermediates, strategies for preparing and characterizing mature amyloid fibrils, and approaches for understanding templating and transmission of amyloid aggregates. Written in the highly successful Methods in Molecular Biology series format, the chapters include introductions to their respective topics, lists of the necessary materials and reagents, step-by-step, readily reproducible laboratory protocols, and tips on troubleshooting and avoiding known pitfalls.

 

Authoritative and practical, Protein Amyloid Aggregation: Methods and Protocols serves as an ideal guide for biochemists and biophysicists with an interest in elucidating the mechanisms of protein amyloid formation, as well as chemists, pharmacologists, and clinicians with an interest in leveraging an understanding of such mechanisms for the purpose of therapeutic development.

Keywords

Aggregation processes Amyloid fibrils Amyloid formation pathway Amyloidoses Human disease Pharmacology Therapeutic development Toxicity

Editors and affiliations

  • David Eliezer
    • 1
  1. 1.Weill Cornell Medical CollegeNew YorkUSA

Bibliographic information

  • DOI https://doi.org/10.1007/978-1-4939-2978-8
  • Copyright Information Springer Science+Business Media New York 2016
  • Publisher Name Humana Press, New York, NY
  • eBook Packages Springer Protocols
  • Print ISBN 978-1-4939-2977-1
  • Online ISBN 978-1-4939-2978-8
  • Series Print ISSN 1064-3745
  • Series Online ISSN 1940-6029
  • About this book
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