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|Title:||Reviewing the role of protein misfolding and aggregation in neurodegenerative diseases||Authors:||Ren, Qunfang||Keywords:||DRNTU::Science::Biological sciences::Human anatomy and physiology::Neurobiology||Issue Date:||2016||Abstract:||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.||URI:||http://hdl.handle.net/10356/67383||Rights:||Nanyang Technological University||Fulltext Permission:||restricted||Fulltext Availability:||With Fulltext|
|Appears in Collections:||SBS Student Reports (FYP/IA/PA/PI)|
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