The aggregation of a polypeptide chain into amyloid fibrils and their accumulation and
deposition into insoluble plaques and intracellular inclusions is the hallmark of several …

In most cases, protein aggregation stems from the establishment of non-native
intermolecular contacts. The formation of insoluble protein aggregates is associated with …

Protein aggregation is a topic of immense interest to the scientific community due to its role
in several neurodegenerative diseases/disorders and industrial importance. Several in silico …

Aggregation can be thought of as a form of protein folding in which intermolecular
associations lead to the formation of large, insoluble assemblies. Various types of …

Nonnative protein aggregation is the process by which otherwise folded, monomeric
proteins are converted to stable aggregates composed of protein chains that have …

Intracellular synthesis, folding, trafficking and degradation of proteins are controlled and
integrated by proteostasis. The frequency of protein misfolding disorders in the human …

Background Amyloids are proteins capable of forming fibrils whose intramolecular contact
sites assume densely packed zipper pattern. Their oligomers can underlie serious diseases …

Highlights•Computational methods identify aggregation-prone regions in protein sequences
as a guide for protein engineering.•Rational methods can reveal genotype-phenotype …

Protein aggregation is a widespread phenomenon implicated in debilitating diseases like
Alzheimer's, Parkinson's, and cataracts, presenting complex hurdles for the field of …

Prions are self-propagating infectious protein isoforms. A growing number of prions have
been identified in yeast, each resulting from the conversion of soluble proteins into an …