2008/03/18 by G. Brent Irvine, Omar M. A. El‐Agnaf, Ganesh M. Shankar +1 · 1 citation
Medicine · Biochemistry, Genetics and Molecular Biology · Chemistry · Neuroscience · #Alzheimer's disease research and treatments #Parkinson's Disease Mechanisms and Treatments #Prion Diseases and Protein Misfolding #Protein aggregation #Fibril #Monomer #Amyloid fibril #Disease #Pathogenesis #Chemistry #Amyloid (mycology) #Neuroscience #Medicine #Biophysics #Amyloid β #Biology #Polymer #Biochemistry #Pathology
paper · pdf · doi:10.2119/2007-00100.irvine
openalex publication_date 2008/03/18 · openalex created_date 2025/10/10 · openalex updated_date 2026/08/03
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.