Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/50957
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dc.contributor.authorJiang, Pingen
dc.date.accessioned2012-12-26T06:44:26Zen
dc.date.available2012-12-26T06:44:26Zen
dc.date.copyright2011en
dc.date.issued2011en
dc.identifier.citationJiang, P. (2011). In silico folding and aggregation study of human amylin, an amyloidosis protein. Doctoral thesis, Nanyang Technological University, Singapore.en
dc.identifier.urihttps://hdl.handle.net/10356/50957en
dc.description.abstractAbnormal 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.extent142 p.en
dc.language.isoenen
dc.subjectDRNTU::Science::Biological sciencesen
dc.titleIn silico folding and aggregation study of human amylin, an amyloidosis proteinen
dc.typeThesisen
dc.contributor.supervisorMu Yuguangen
dc.contributor.schoolSchool of Biological Sciencesen
dc.description.degreeDOCTOR OF PHILOSOPHY (SBS)en
dc.identifier.doi10.32657/10356/50957en
item.grantfulltextopen-
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