Protein Conformational Misfolding and Amyloid Formation: Characteristics of a New Class of Disorders that Include Alzheimer's and Prion Diseases

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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, fuelled 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.

Keywords: Amyloid Formation; Fibrillogenesis; Oxidative Stress; Prion Diseases

Document Type: Review Article


Publication date: October 1, 2002

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  • Current Medicinal Chemistry covers all the latest and outstanding developments in medicinal chemistry and rational drug design. Each issue contains a series of timely in-depth reviews written by leaders in the field covering a range of the current topics in medicinal chemistry. Current Medicinal Chemistry is an essential journal for every medicinal chemist who wishes to be kept informed and up-to-date with the latest and most important developments.
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