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 possible link between hIAPP accumulation and β-cell death in diabetic patients has
inspired numerous studies focusing on amyloid structures and aggregation pathways of this …

An increasing number of human diseases has been shown to be linked to aggregation and
amyloid formation by intrinsically disordered proteins (IDPs). Amylin, amyloid-β, and α …

The toxicity of amyloid‐forming proteins is correlated with their interactions with cell
membranes. Binding events between amyloidogenic proteins and membranes result in …

The hormone islet amyloid polypeptide (IAPP, or amylin) plays a role in glucose
homeostasis but aggregates to form islet amyloid in type‐2 diabetes. Islet amyloid formation …

Biological membranes and membrane proteins, responsible for numerous exciting
biological processes, present one of the paramount challenges in biophysics today …

The aggregation of proteins is tightly controlled in living systems, and misfolded proteins are
normally removed before aggregation of the misfolded protein can occur. But for reasons not …

This tutorial review presents descriptions of two amyloidogenic proteins, amyloid-β (Aβ)
peptides and islet amyloid polypeptide (IAPP), whose misfolding propensities are implicated …

Several diseases share misfolding of different peptides and proteins as a key feature for
their development. This is the case of important neurodegenerative diseases such as …

Mechanistic understanding of nucleation dependent polymerization by α-synuclein (α-Syn)
into toxic oligomers and amyloids is important for the drug development against Parkinson's …