Monica Bucciantini

TL;DR: This finding provides added evidence that avoidance of protein aggregation is crucial for the preservation of biological function and suggests common features in the origins of this family of protein deposition diseases.

TL;DR: The results suggest that misfolded proteinaceous aggregates stimulate generic cellular responses as a result of the exposure of regions of the structure that are buried in the normally folded proteins and support the idea that a higher number of degenerative pathologies than previously known might be considered as protein deposition diseases.

TL;DR: Comparison of the rates of folding of AcP and four other proteins with the same topology, including ADA2h, supports the concept that the average distance in sequence between interacting residues (that is, the contact order) is an important determinant of the rate of protein folding.

TL;DR: The hypothesis that neurodegenerative disorders result primarily from a generic cell dysfunction caused by early misfolded species in the aggregation process is supported.

TL;DR: The results show that the aggregation process that leads to amyloid deposition takes place from an ensemble of denatured conformations under conditions in which non‐covalent interactions are still favoured, and support the hypothesis that the stability of the native state of globular proteins is a major factor preventing the in vivo conversion of natural proteins into amyloids fibrils under non‐pathological conditions.