The hidden world of amyloid biology has suddenly snapped into atomic-level focus,
revealing over 80 amyloid protein fibrils, both pathogenic and functional. Unlike globular …

Amyloid diseases are global epidemics with profound health, social and economic
implications and yet remain without a cure. This dire situation calls for research into the …

Water solubility and structural stability are key merits for proteins defined by the primary
sequence and 3D-conformation. Their manipulation represents important aspects of the …

The formation of amyloid fibrils is a general class of protein self-assembly behaviour, which
is associated with both functional biology and the development of a number of disorders …

Mammalian prions propagate as distinct strains and are composed of multichain assemblies
of misfolded host-encoded prion protein (PrP). Here, we present a near-atomic resolution …

Amyloid fibrils have traditionally been considered only as pathological aggregates in human
neurodegenerative diseases, but it is increasingly becoming clear that the propensity to form …

Amyloids are implicated in neurodegenerative diseases. Fibrillar aggregates of the amyloid-
β protein (Aβ) are the main component of the senile plaques found in brains of Alzheimer's …

Subcellular membraneless assemblies are a reinvigorated area of study in biology, with
spirited scientific discussions on the forces between the low-complexity protein domains …

When protein/peptides aggregate, they usually form the amyloid state consisting of cross β-
sheet structure built by repetitively stacked β-strands forming long fibrils. Amyloids are …

The majority of protein molecules must fold into defined three-dimensional structures to
acquire functional activity. However, protein chains can adopt a multitude of conformational …