Overproduction or poor clearance of amyloids lead to amyloid aggregation and even amyloidosis development. Different amyloids may interact synergistically to promote their aggregation and accelerate pathology in amyloidoses. Amyloid oligomers assembled from different amyloids share common structures and epitopes, and are considered the most toxic species in the pathologic processes of amyloidos...

The amyloidoses are a group of protein-misfolding disorders characterized by the accumulation of amyloid fibrils formed from a variety of proteins. Currently, twentyeight different kinds of human and animal proteins, in intact or fragmented forms, have been found to be associated with pathological disorders such as Alzheimer’s disease, type II diabetes, prion diseases, dialysis-related amyloido...

PURPOSE OF REVIEW This review aims to summarize recent developments in the area of systemic amyloidoses with emphasis on pathologic diagnosis. RECENT FINDINGS In recent years, management of amyloidosis has shifted from a purely supportive approach to quite diverse, radical and aggressive treatments. The central issue is the understanding that treatment of systemic amyloidoses depends on the m...

Transthyretin (TTR) is a plasma homotetrameric protein implicated in fatal systemic amyloidoses. TTR tetramer dissociation precedes pathological TTR aggregation. Native state stabilizers are promising drugs to treat TTR amyloidoses. Here we repurpose tolcapone, an FDA-approved molecule for Parkinson's disease, as a potent TTR aggregation inhibitor. Tolcapone binds specifically to TTR in human p...