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Current Medicinal Chemistry
ISSN (Print): 0929-8673
ISSN (Online): 1875-533X
DOI: 10.2174/0929867023369123      Price:  $58

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

Author(s): Andrew J. Thompson and Colin J. Barrow
Pages 1751-1762 (12)
The accumulation of proteinaceous deposits has been recognised to occur in several neurodegenerative conditions including Prion diseases, Alzheimers disease, Parkinsons disease, and Huntingtons 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.
Amyloid Formation, Prion Diseases, Fibrillogenesis, Oxidative Stress
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