Reviewing the role of protein misfolding and aggregation in neurodegenerative diseases
Date of Issue2016-05-16
School of Biological Sciences
Over the past decades, numerous studies have revealed a presence of misfolded protein aggregates in neurodegenerative diseases. It is now widely accepted that these aggregates are involved in pathogenesis of neurodegeneration. Each neurodegenerative disease is associated with a disease protein that folds wrongly and form large aggregates. In this review, I summarize several key findings on how protein aggregates form and how they relate to neurotoxicity. In particular, I highlight a central role of the oligomeric and protofibrillar intermediates, which are precursors of the large aggregates.
DRNTU::Science::Biological sciences::Human anatomy and physiology::Neurobiology
Final Year Project (FYP)
Nanyang Technological University