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https://hdl.handle.net/10356/44593
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DC Field | Value | Language |
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dc.contributor.author | Xia, Yan | |
dc.date.accessioned | 2011-06-02T07:27:59Z | |
dc.date.available | 2011-06-02T07:27:59Z | |
dc.date.copyright | 2011 | en_US |
dc.date.issued | 2011 | |
dc.identifier.uri | http://hdl.handle.net/10356/44593 | |
dc.description.abstract | Bcl-2 is the central regulator in apoptosis. Structural studies of Bcl-2 reveal a flexible loop flanking the Bcl-2 homology domain 3 (BH3) and BH4. In response to external stimuli, several kinases phosphorylate the loop of Bcl-2. Phosphorylation on Bcl-2 has been thought to affect the protein’s activity in apoptosis as well as autophagy. However, the molecular basis and mechanistic details of Bcl-2 phosphorylation still remains a mystery. To further define and better understand the biological significance and the regulation of Bcl-2 through phosphorylation, we focus on changes in molecular interaction, using a phospho-mimetic Bcl-2 as a model. Our structural analysis indicates phosphorylation would induce conformational change in the flexible loop of Bcl-2. Binding study revealed phospho-mimetic Bcl-2 has decreased affinity to pro-apoptotic protein Bak. Based on our result, we hypothesized the structural-function relationship for Bcl-2 phosphorylation. | en_US |
dc.format.extent | 34 p. | en_US |
dc.language.iso | en | en_US |
dc.rights | Nanyang Technological University | |
dc.subject | DRNTU::Science::Biological sciences::Molecular biology | en_US |
dc.title | Bcl-2 phosphorylation and implications in apoptosis in cancer cells | en_US |
dc.type | Final Year Project (FYP) | en_US |
dc.contributor.supervisor | Yoon Ho Sup | en_US |
dc.contributor.school | School of Biological Sciences | en_US |
dc.description.degree | Bachelor of Science in Biological Sciences | en_US |
item.fulltext | With Fulltext | - |
item.grantfulltext | restricted | - |
Appears in Collections: | SBS Student Reports (FYP/IA/PA/PI) |
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File | Description | Size | Format | |
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FYP report.doc Restricted Access | 7.31 MB | Microsoft Word | View/Open |
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