The presence of neuritic plaques and amyloid fibrils arising from the misfolding of certain
proteins is the principal molecular indicator of neurodegenerative diseases such as …

The phenomenon of protein misfolding and aggregation is one of the most important topics
in current biomedical research.[1] The failure of proteins to fold correctly, or to remain …

Highly ordered protein aggregates, termed amyloid fibrils, are associated with a broad range
of diseases, many of which are neurodegenerative, for example, Alzheimer's and …

To date, approximately 50 proteins have been identified that can misfold and aggregate to
form amyloid fibrils and cause neurodegenerative diseases such as Alzheimer disease …

The aggregation of proteins into amyloid fibrils has been implicated in the pathogenesis of a
variety of neurodegenerative diseases, including Alzheimer's disease and Parkinson's …

In this chapter we review novel imaging modalities that permit the investigation of protein
self-assembly reactions in situ. First, we review a class of techniques we collectively refer to …

The misfolding and aggregation of polypeptide chains into β-sheet-rich amyloid fibrils is
associated with a wide range of neurodegenerative diseases. Growing evidence indicates …

The investigation of amyloid fibril formation is paramount for advancing our understanding of
neurodegenerative diseases and for exploring potential correlated therapeutic strategies …

Amyloids are a broad class of proteins and peptides that can misfold and assemble into long
unbranched fibrils with a cross-β conformation. These misfolding and aggregation events …

Oligomeric species of amyloidogenic peptides or proteins are often considered as the most
toxic species in several amyloid disorders, like Alzheimer or Parkinson's diseases, and …