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Elsevier Science
Early Stage Protein Misfolding and Amyloid Aggregation

Early Stage Protein Misfolding and Amyloid Aggregation

by Elsevier ScienceElsevier Science
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Early Stage Protein Misfolding and Amyloid Aggregation, Volume 329, the latest in the International Review of Cell and Molecular Biology series presents comprehensive reviews and current advances in cell and molecular biology, including articles that address the structure and control of gene expression, nucleocytoplasmic interactions, control of cell development and differentiation, and cell transformation and growth.

The series has a worldwide readership and maintains a high standard by publishing invited articles on important and timely topics as authored by prominent cell and molecular biologists.

  • Provides comprehensive reviews and current advances
  • Presents a wide range of perspectives on specific subjects
  • Includes valuable reference material for advanced undergraduates, graduate students, and professional scientists

Product Details

ISBN-13: 9780128122518
Publisher: Elsevier Science
Publication date: 02/13/2017
Series: International Review of Cell and Molecular Biology , #329
Pages: 320
Product dimensions: 6.10(w) x 9.10(h) x 0.90(d)

About the Author

MMassimo Sandal received his doctorate qualification from the University of Bologna in 2008 for his research on active conformers of proteins. He has gone on to conduct research on proteins in departements of Biochemistry and Biotechnology across Europe. Following on from the University of Bologna, he was a post-doctoral FEBS Fellow at the University of Cambridge and a post-doctoral associate at the University of Verona in 2012. From 2013 to 2016 he was associated to the German Research School for Simulation Sciences in Jülich, Germany.

Table of Contents

1. From the Evolution of Protein Sequences Able to Resist Self-Assembly to the Prediction of Aggregation Propensity 2. Protein Aggregation and Molecular Crowding: Perspectives from Multiscale Simulations 3. Structural Characteristics of a -Synuclein Oligomers 4. Effects of Intrinsic and Extrinsic Factors on Aggregation of Physiologically Important Intrinsically Disordered Proteins 5. The Nucleation of Protein Aggregates - from Crystals to Amyloid Fibrils 6. What Makes a Prion: Infectious Proteins From Animals to Yeast 7. The Structure of Mammalian Prions and their Aggregates

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