dc.contributor.authorRen, Qunfang
dc.date.accessioned2016-05-16T06:21:27Z
dc.date.available2016-05-16T06:21:27Z
dc.date.issued2016
dc.identifier.urihttp://hdl.handle.net/10356/67383
dc.description.abstractOver 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.en_US
dc.format.extent19 p.en_US
dc.language.isoenen_US
dc.rightsNanyang Technological University
dc.subjectDRNTU::Science::Biological sciences::Human anatomy and physiology::Neurobiologyen_US
dc.titleReviewing the role of protein misfolding and aggregation in neurodegenerative diseasesen_US
dc.typeFinal Year Project (FYP)en_US
dc.contributor.supervisorMu Yuguangen_US
dc.contributor.schoolSchool of Biological Sciencesen_US
dc.description.degreeBachelor of Science in Biological Sciencesen_US


Files in this item

Thumbnail

This item appears in the following Collection(s)

Show simple item record