Protein aggregation in the brain: the molecular basis for Alzheimer's and Parkinson's diseases.

Brent Irvine, O.M. El-Agnaf, G.M. Shankar, D.M. Walsh

Research output: Contribution to journalArticlepeer-review

371 Citations (Scopus)

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.
Original languageEnglish
Pages (from-to)451-464
Number of pages14
JournalMolecular medicine
Volume14(7-8)
Issue number7-8
DOIs
Publication statusPublished - Jul 2008

ASJC Scopus subject areas

  • Genetics

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