Early Stage Protein Misfolding and Amyloid Aggregation
- 1st Edition, Volume 329 - January 30, 2017
- Latest edition
- Editor: Massimo Sandal
- Language: English
- Hardback ISBN:9 7 8 - 0 - 1 2 - 8 1 2 2 5 1 - 8
- eBook ISBN:9 7 8 - 0 - 1 2 - 8 1 2 2 5 2 - 5
Early Stage Protein Misfolding and Amyloid Aggregation, Volume 329, the latest in the International Review of Cell and Molecular Biology series presents comprehensive reviews… Read more
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
Cell biologists, molecular biologists, developmental biologists, and physiologists (organ level); biomedical scientists and biochemists studying cell-cell interactions and cell variation; and evolution students and researchers
- Chapter One: From the Evolution of Protein Sequences Able to Resist Self-Assembly to the Prediction of Aggregation Propensity
- Abstract
- 1 Introduction
- 2 Evolution of Protein Sequences: Need to be Functional vs Risk of Aggregation
- 3 Evolutionary Strategies to Inhibit Aggregation at the Primary Sequence Level
- 4 Evolutionary Strategies to Inhibit Aggregation at the Structural Level
- 5 Evolutionary Strategies to Inhibit Aggregation at the Cellular Level
- 6 Development of the Algorithms Able to Identify Amyloid Hot Spots and Amyloid Propensity
- 7 Conclusions and Future Perspectives
- Chapter Two: Protein Aggregation and Molecular Crowding: Perspectives From Multiscale Simulations
- Abstract
- 1 Introduction
- 2 Computational Techniques
- 3 Perspectives
- Chapter Three: Structural Characteristics of α-Synuclein Oligomers
- Abstract
- 1 Introduction
- 2 Amyloid Formation
- 3 α-Synuclein
- 4 Oligomeric States of αS
- 5 Relationships Between Different Types of Amyloid Species
- Chapter Four: Effects of Intrinsic and Extrinsic Factors on Aggregation of Physiologically Important Intrinsically Disordered Proteins
- Abstract
- 1 Aggregation of Intrinsically Disordered Proteins
- 2 Factors Influencing Aggregation of IDPs
- 3 Conclusions
- Acknowledgments
- Chapter Five: The Nucleation of Protein Aggregates - From Crystals to Amyloid Fibrils
- Abstract
- 1 Protein Condensation
- 2 Nucleation - The Emergence of A New Phase
- 3 Heterogeneous Nucleation at Interfaces
- 4 Secondary Nucleation As a Special Case of Heterogeneous Nucleation
- 5 Experimental Methods to Study Nucleation of Condensed Protein Phases
- 6 Amyloid Oligomers And (Critical) Amyloid Nuclei
- 7 Outlook
- 8 Conclusions
- Acknowledgments
- Chapter Six: What Makes a Prion: Infectious Proteins From Animals to Yeast
- Abstract
- 1 Introduction
- 2 Pathogens and the Emergence of the Prion Hypothesis
- 3 Evidence Found: Identification of Animal, Yeast, and Other Prions
- 4 What Makes a Prion: Features That Define Prions
- 5 The Enlarging Prion Concept in Disease and Beyond
- 6 Concluding Remarks
- Chapter Seven: The Structure of Mammalian Prions and Their Aggregates
- Abstract
- 1 Introduction
- 2 Amorphous Aggregates and Oligomers
- 3 Two-Dimensional Crystals
- 4 Amyloid Fibrils
- 5 Outlook on the Future Structural Biology of Prions
- 6 Concluding Remarks
- Acknowledgments
- Index
- Edition: 1
- Latest edition
- Volume: 329
- Published: January 30, 2017
- Language: English
MS
Massimo Sandal
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.
Affiliations and expertise
German Research School for Simulation Sciences, Aachen, GermanyRead Early Stage Protein Misfolding and Amyloid Aggregation on ScienceDirect