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 amyloid-β oligomer (AβO) hypothesis was introduced in 1998. It proposed that the brain
damage leading to Alzheimer's disease (AD) was instigated by soluble, ligand-like AβOs …

The amyloid-β (Aβ) peptide is associated with the development of Alzheimer's disease and
is known to form highly neurotoxic prefibrillar oligomeric aggregates, which are difficult to …

The cascade of amyloid formation relates to multiple complex events at the molecular level.
Previous research has established amyloid plaque deposition as the leading cause of …

One of the grand challenges of biophysical chemistry is to understand the principles that
govern protein misfolding and aggregation, which is a highly complex process that is …

Amyloids, fibrillar assembly of (poly) peptide chains, are associated with neurodegenerative
illnesses such as Alzheimer's and Parkinson's diseases, for which there are no cures. The …

Aggregation refers to the assembly of proteins into nonphysiological higher order structures.
While amyloid has been studied extensively, much less is known about amorphous …

Metal ions play a key role in aggregation of amyloid β protein by interfering with their proper
folding, altering protein homeostasis and cell viability, and ultimately leading to …

Intrinsically disordered proteins (IDPs) play many biological roles in the human proteome
ranging from vesicular transport, signal transduction to neurodegenerative diseases. The Aβ …

Mounting evidence suggests that the neuronal cell membrane is the main site of oligomer-
mediated neuronal toxicity of amyloid-β peptides in Alzheimer's disease. To gain a detailed …