| Literature DB >> 20190788 |
Adriano Aguzzi1, Tracy O'Connor.
Abstract
A growing number of diseases seem to be associated with inappropriate deposition of protein aggregates. Some of these diseases--such as Alzheimer's disease and systemic amyloidoses--have been recognized for a long time. However, it is now clear that ordered aggregation of pathogenic proteins does not only occur in the extracellular space, but in the cytoplasm and nucleus as well, indicating that many other diseases may also qualify as amyloidoses. The common structural and pathogenic features of these diverse protein aggregation diseases is only now being fully understood, and may provide novel opportunities for overarching therapeutic approaches such as depleting the monomeric precursor protein, inhibiting aggregation, enhancing aggregate clearance or blocking common aggregation-induced cellular toxicity pathways.Entities:
Mesh:
Substances:
Year: 2010 PMID: 20190788 DOI: 10.1038/nrd3050
Source DB: PubMed Journal: Nat Rev Drug Discov ISSN: 1474-1776 Impact factor: 84.694