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 β-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 β-strands interacting within a β-sheet. In this review, we discuss this theme as it relates to the two most common neurodegenerative conditions - Alzheimer's and Parkinson's diseases.
CITATION STYLE
Irvine, G. B., El-Agnaf, O. M., Shankar, G. M., & Walsh, D. M. (2008, July). Protein aggregation in the brain: The molecular basis for Alzheimer’s and Parkinson’s diseases. Molecular Medicine. https://doi.org/10.2119/2007-00100.Irvine
Mendeley helps you to discover research relevant for your work.