Early Stage Protein Misfolding and Amyloid Aggregation /

Bibliographic Details
Call Number:Libro Electrónico
Other Authors: Sandal, Massimo (Editor)
Format: Electronic eBook
Language:Inglés
Published: Cambridge, MA : Academic Press is an imprint of Elsevier, 2017.
Series:International review of cell and molecular biology ; v. 329.
Subjects:
Prions.
Amyloid.
Protein folding.
Amyloid
Prions (Virologie)
Amylo�ide.
Prot�eines > Repliement.
SCIENCE > Life Sciences > Biochemistry.
Online Access:Texto completo
Table of Contents:
  • From the evolution of protein sequences able to resist self-assembly to the prediction of aggregation propensity
  • Protein aggregation and molecular crowding: perspectives from multiscale simulations
  • Structural characteristiscs of [alpha]-synuclein oligomers
  • Effects of intrinsic and extrinsic factors on aggregation of physiologically important intrinsically disordered proteins
  • The nucleantion of protein aggregates : from crystals to amyloids fibrils
  • What makes a prion: infectious proteins from animals to yeast
  • The structure of mammalian prions and their aggregates.

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