Reviewing the role of protein misfolding and aggregation in neurodegenerative diseases
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...
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Format: | Final Year Project |
Language: | English |
Published: |
2016
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Online Access: | http://hdl.handle.net/10356/67383 |
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Institution: | Nanyang Technological University |
Language: | English |
Summary: | 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. |
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