Reviewing the role of protein misfolding and aggregation in neurodegenerative diseases

• Main Author: Ren, Qunfang
• Other Authors: Mu Yuguang
• Format: Final Year Project
• Language: English
• Published: 2016
• Subjects: DRNTU::Science::Biological sciences::Human anatomy and physiology::Neurobiology
• Online Access: http://hdl.handle.net/10356/67383
• Institution: Nanyang Technological University

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.