Early Stage Protein Misfolding and Amyloid Aggregation | Buch | 978-0-12-812251-8 | sack.de

Buch, Englisch, 320 Seiten, Format (B × H): 152 mm x 229 mm, Gewicht: 700 g

Early Stage Protein Misfolding and Amyloid Aggregation


Erscheinungsjahr 2017
ISBN: 978-0-12-812251-8
Verlag: William Andrew Publishing

Buch, Englisch, 320 Seiten, Format (B × H): 152 mm x 229 mm, Gewicht: 700 g

ISBN: 978-0-12-812251-8
Verlag: William Andrew Publishing


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.
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Zielgruppe


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

Weitere Infos & Material


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


Sandal, Massimo
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.


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