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DC Field | Value | Language |
---|---|---|
dc.contributor.author | Jiang, Ping | en |
dc.date.accessioned | 2012-12-26T06:44:26Z | en |
dc.date.available | 2012-12-26T06:44:26Z | en |
dc.date.copyright | 2011 | en |
dc.date.issued | 2011 | en |
dc.identifier.citation | Jiang, P. (2011). In silico folding and aggregation study of human amylin, an amyloidosis protein. Doctoral thesis, Nanyang Technological University, Singapore. | en |
dc.identifier.uri | https://hdl.handle.net/10356/50957 | en |
dc.description.abstract | Abnormal self-assembly of proteins converting their native conformations into β-sheet rich fibrillar structures is the hallmark of several so called "misfolding diseases" including Type 2 Diabetes Mellitus (T2DM), Alzheimer's and Parkinson's diseases, etc. Human islet amyloid polypeptide (hlAPP or amylin) is the major component of amyloid deposits found in the pancreas of 90% T2DM patients. Although extensive studies have been performed in the recent decades, detailed information about hIAPP aggregation and the related pathology remains missing. | en |
dc.format.extent | 142 p. | en |
dc.language.iso | en | en |
dc.subject | DRNTU::Science::Biological sciences | en |
dc.title | In silico folding and aggregation study of human amylin, an amyloidosis protein | en |
dc.type | Thesis | en |
dc.contributor.supervisor | Mu Yuguang | en |
dc.contributor.school | School of Biological Sciences | en |
dc.description.degree | DOCTOR OF PHILOSOPHY (SBS) | en |
dc.identifier.doi | 10.32657/10356/50957 | en |
item.grantfulltext | open | - |
item.fulltext | With Fulltext | - |
Appears in Collections: | SBS Theses |
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JiangPing11.pdf | 4.58 MB | Adobe PDF | ![]() View/Open |
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