title: Protein aggregation in the brain: the molecular basis for Alzheimer's and Parkinson's diseases.
abstract: Developing effective treatments for neurodegenerative diseases is one of the greatest medical challenges of the 21st century. Although many of these clinical entities have been recognized for more than a hundred years, it is only during the past twenty years that the molecular events that precipitate disease have begun to be understood. Protein aggregation is a common feature of many neurodegenerative diseases, and it is assumed that the aggregation process plays a central role in pathogenesis. In this process, one molecule (monomer) of a soluble protein interacts with other monomers of the same protein to form dimers, oligomers, and polymers. Conformation changes in three-dimensional structure of the protein, especially the formation of beta-strands, often accompany the process. Eventually, as the size of the aggregates increases, they may precipitate as insoluble amyloid fibrils, in which the structure is stabilized by the beta-strands interacting within a beta-sheet. In this review, we discuss this theme as it relates to the two most common neurodegenerative conditions-Alzheimer's and Parkinson's diseases.
authors: School of Medicine and Dentistry, The Queen's University of Belfast, Belfast, Northern Ireland. b.irvine@qub.ac.uk
authors: G Brent
authors: GB
authors: Irvine
authors: Omar M
authors: OM
authors: El-Agnaf
authors: Ganesh M
authors: GM
authors: Shankar
authors: Dominic M
authors: DM
authors: Walsh
mesh_terms: D000544:Alzheimer Disease / Q000175:diagnosis / Q000453:epidemiology / Q000209:etiology* / Q000378:metabolism; D016229:Amyloid beta-Peptides / Q000378:metabolism* / Q000502:physiology / Q000633:toxicity; D001921:Brain / Q000378:metabolism* / Q000473:pathology; D006801:Humans; D015994:Incidence; D008954:Models, Biological; D010300:Parkinson Disease / Q000175:diagnosis / Q000453:epidemiology / Q000209:etiology* / Q000378:metabolism; D058225:Plaque, Amyloid / Q000378:metabolism*; D051844:alpha-Synuclein / Q000378:metabolism / Q000502:physiology
chemical_list: D016229:Amyloid beta-Peptides; D051844:alpha-Synuclein