The abundance of intrinsic disorder in the protein realm and its role in a variety of
physiological and pathological cellular events have strengthened the interest of the scientific …

Simple Summary This review presents the beginning of the history of toxic properties of
amyloids, especially on Aβ amyloids. We discuss anti-amyloid therapy and its problems and …

Fibrillar protein aggregates are a hallmark of a range of human disorders, from prion
diseases to dementias, but are also encountered in several functional contexts. Yet, the …

Proteins and RNAs assemble in membrane-less organelles that organize intracellular
spaces and regulate biochemical reactions. The ability of proteins and RNAs to form …

Amyloids are proteins associated with several clinical disorders, including Alzheimer's, and
Creutzfeldt-Jakob's. Despite their diversity, all amyloid proteins can undergo aggregation …

Protein aggregates, and in particular amyloids, are generally considered to be inherently
irreversible aberrant clumps, and are often associated with pathologies, such as Alzheimer's …

Correct termination of transcription is essential for gene expression. In bacteria, factor-
dependent termination relies on the Rho factor, that classically has three conserved …

Prions are self‐perpetuating proteins able to switch between a soluble state and an
aggregated‐and‐transmissible conformation. These proteinaceous entities have been …

Protein amyloid nanofibers provide a biocompatible platform for the development of
functional nanomaterials. However, the functionalities generated up to date are still limited …

Prions are a singular subset of proteins able to switch between a soluble conformation and a
self-perpetuating amyloid state. Traditionally associated with neurodegenerative diseases …