The manner in which a newly synthesized chain of amino acids transforms itself into a
perfectly folded protein depends both on the intrinsic properties of the amino-acid sequence …

This review summarises our current understanding of the underlying and universal
mechanism by which newly synthesised proteins achieve their biologically functional states …

In many branches of materials science it is now routine to generate data sets of such large
size and dimensionality that conventional methods of analysis fail. Paradigms and tools from …

Increasing evidence indicates that many peptides and proteins can be converted in vitro into
highly organised amyloid structures, provided that the appropriate experimental conditions …

Increasing evidence in recent years indicates that protein misfolding and aggregation,
leading to ER stress, are central factors of pathogenicity in neurodegenerative diseases …

Interfaces can strongly accelerate or inhibit protein aggregation, destabilizing proteins that
are stable in solution or, conversely, stabilizing proteins that are aggregation-prone …

Folding and unfolding are essential ways for a protein to regulate its biological activity. The
misfolding of proteins usually reduces or completely compromises their biological functions …

Amyloidogenic proteins and polypeptides can be divided into two structural classes, namely
those which are flexible and are intrinsically disordered in their unaggregated state and …

An increasing number of cases where amyloids of different proteins are found in the same
patient are being reported. This observation complicates diagnosis and clinical intervention …

Amyloid formation and aberrant protein aggregation have been implicated in more than 15
different human diseases and an even wider range of proteins form amyloid in vitro. From a …