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Early Stage Protein Misfolding and Amyloid Aggregation International Review of Cell and Molecular Biology Series

Langue : Anglais
Couverture de l’ouvrage Early Stage Protein Misfolding and Amyloid Aggregation

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.

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

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
  • 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

Date de parution :

Ouvrage de 320 p.

15x22.8 cm

Disponible chez l'éditeur (délai d'approvisionnement : 14 jours).

207,58 €

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Thèmes d’Early Stage Protein Misfolding and Amyloid Aggregation :