Amyloid fibrils are β-sheet-rich linear protein polymers that can be formed by a large variety
of different proteins. These assemblies have received much interest in recent decades, due …

Cells ensure their protein quality control through the proteostasis network. Aging and age-
related diseases, such as neurodegenerative and cardiovascular diseases, have been …

In prion diseases, fibrillar assemblies of misfolded prion protein (PrP) self-propagate by
incorporating PrP monomers. These assemblies can evolve to adapt to changing …

Prion diseases are associated with the structural conversion of prion protein (PrP) to a β-
sheet-rich aggregate, PrP Sc. Previous studies have indicated that a reduction of the …

The middle disordered hydrophobic region of the prion protein plays a critical role in
conformational conversion of the protein, with pathogenic as well as protective mutations …

Transmissible spongiform encephalopathy is associated with misfolding of prion protein
(PrP) into an amyloid β‐rich aggregate. Previous studies have indicated that PrP interacts …

Prions replicate via the autocatalytic conversion of cellular prion protein (PrP C) into fibrillar
assemblies of misfolded PrP. While this process has been extensively studied in vivo and in …

We present a model to describe the concentration-dependent growth of protein filaments.
Our model contains two states, a low entropy/high affinity ordered state and a high …

Prion diseases are fatal neurodegenerative diseases associated with structural conversion
of α-helical prion protein (PrP) into its β-sheet rich isoform (PrP Sc). Previous genetic …

Protein misfolding diseases are a group of devastating disorders characterized by structural
conversion of a soluble protein into an amyloid-like aggregate. Typically, the structural …