Protein conformational misfolding and amyloid formation: characteristics of a new class of disorders that include Alzheimer's and Prion diseases.
The accumulation of proteinaceous deposits has been recognised to occur in several neurodegenerative conditions including Prion diseases, Alzheimer's disease, Parkinson's disease, and Huntington's disease. Over the last two decades interest in these conditions has increased markedly, fueled partially by an increasing prevalence of these diseases in the Western world. Evidence indicates that anomalous protein misfolding and aggregation, with an accompanying "toxic gain of function" is central to the neuropathogenesis of these diseases. An increased understanding of the similarities and differences in the production, aggregation and accumulation of the respective proteins involved in these diseases, and the associated mechanisms of neurodegeneration, should aid in the development of new therapeutic agents to treat this group of related disorders.
D000544:Alzheimer Disease / Q000209:etiology; D000682:Amyloid / Q000737:chemistry* / Q000378:metabolism; D000686:Amyloidosis / Q000209:etiology*; D000818:Animals; D006801:Humans; D006816:Huntington Disease / Q000209:etiology; D010300:Parkinson Disease / Q000209:etiology; D017096:Prion Diseases / Q000209:etiology; D011487:Protein Conformation; D017510:Protein Folding
D000682:Amyloid