This review will focus on the process of amyloid-type protein aggregation. Amyloid fibrils are
an important hallmark of protein misfolding diseases and therefore have been investigated …

In the last two decades, solid-state nuclear magnetic resonance (ssNMR) spectroscopy has
transformed from a spectroscopic technique investigating small molecules and industrial …

Amyloid refers to insoluble protein aggregates that are responsible for amyloid diseases but
are also implicated in important physiological functions (functional amyloids). The …

Most neurodegenerative diseases such as Alzheimer's disease, type 2 diabetes, Parkinson's
disease, etc. are caused by inclusions and plaques containing misfolded protein …

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 …

Current interest in amyloid fibrils stems from their involvement in neurodegenerative and
other diseases and from their role as an alternative structural state for many peptides and …

Many peptides and proteins self-assemble into amyloidfibrils. Examples include mammalian
and fungal prion proteins, polypeptides associated with human amyloid diseases, and …

Studies of proteins' formation of amyloid fibrils have revealed that potentially cytotoxic
oligomers frequently accumulate during fibril formation. An important question in the context …

The amyloid fibrils of beta-amyloid (Aβ) peptides play important roles in the pathology of
Alzheimer's disease. Comprehensive solid-state NMR (SSNMR) structural studies on …

Protein misfolding and amyloid assembly have long been recognized as being responsible
for many devastating human diseases. Recent findings indicate that amyloid assemblies …