Transmissible spongiform encephalopathies (TSEs or prion diseases) are a rare group of
invariably fatal neurodegenerative disorders that affect humans and other mammals. TSEs …

Mutual conformational selection and population shift followed by minor induced-fit
optimization is the key mechanism in biomolecular recognition, and monomers and small …

Background Amyloid fibrils associated with neurodegenerative diseases can be considered
biologically relevant failures of cellular quality control mechanisms. It is known that in vivo …

Aggregation of misfolded proteins or peptides is a common feature of neurodegenerative
diseases including Alzheimer's, Parkinson's, Huntington's, prion and other diseases. Recent …

The cellular prion protein, PrP C, is a small, cell surface glycoprotein with a function that is
currently somewhat ill defined. It is also the key molecule involved in the family of …

It has been well established that a single amino acid sequence can give rise to several
conformationally distinct amyloid states. The extent to which amyloid structures formed …

In several recent studies transmissible prion disease was induced in animals by inoculation
with recombinant prion protein amyloid fibrils produced in vitro. Serial transmission of …

A key structural component of amyloid fibrils is a highly ordered, crystalline-like cross-β-
sheet core. Conformationally different amyloid structures can be formed within the same …

We consider a model for the polymerization (fragmentation) process involved in infectious
prion self-replication and study both its dynamics and non-zero steady state. We address …

Background According to the prevailing view, soluble oligomers or small fibrillar fragments
are considered to be the most toxic species in prion diseases. To test this hypothesis, two …