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 …

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

Prions are proteins that can self-propagate, leading to the misfolding of proteins. In addition
to the previously demonstrated pathogenic roles of prions during the development of …

Abstract Changes in the abundance of protein and RNA molecules can impair the formation
of complexes in the cell leading to toxicity and death. Here we exploit the information …

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 …

Age-related neurodegenerative diseases involving amyloid aggregation remain one of the
biggest challenges of modern medicine. Alterations in the gastrointestinal microbiome play …

The problems associated with the drugs currently used to treat leishmaniasis, including
resistance, toxicity, and the high cost of some formulations, call for the urgent identification of …

The misfolding and aggregation of proteins is the neuropathological hallmark for numerous
diseases including Alzheimer's disease, Parkinson's disease, and prion diseases. It is …

The presence of insoluble protein deposits in tissues and organs is a hallmark of many
human pathologies. In addition, the formation of protein aggregates is considered one of the …