It is now generally accepted that macromolecules do not act in isolation but “live” in a
crowded environment, that is, an environment populated by numerous different molecules …

Protein misfolding and aggregation is observed in many amyloidogenic diseases affecting
either the central nervous system or a variety of peripheral tissues. Structural and dynamic …

The conversion of native peptides and proteins into amyloid aggregates is a hallmark of over
50 human disorders, including Alzheimer's and Parkinson's diseases. Increasing evidence …

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 …

Most neurodegenerative diseases are characterized by the intracellular or extracellular
aggregation of misfolded proteins such as amyloid-β and tau in Alzheimer disease, α …

Post-translational modifications (PTMs) on tau have long been recognized as affecting
protein function and contributing to neurodegeneration. The explosion of information on …

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 …

The phenomenon of protein aggregation and amyloid formation has become the subject of
rapidly increasing research activities across a wide range of scientific disciplines. Such …

It is important to have sustainable and edible scaffolds to produce cultivated meat. In this
research, three-dimensional (3D) porous scaffolds were developed by soy protein amyloid …

Proteinaceous materials based on the amyloid core structure have recently been discovered
at the origin of biological functionality in a remarkably diverse set of roles, and attention is …