Quantitative approaches to probe the acetylproteome
Thesis (Ph. D.)--Massachusetts Institute of Technology, Dept. of Biological Engineering, 2013.
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| Other Authors: | |
| Format: | Thesis |
| Language: | eng |
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Massachusetts Institute of Technology
2013
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| Online Access: | http://hdl.handle.net/1721.1/81664 |
| _version_ | 1811097865552920576 |
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| author | Bryson, Bryan David |
| author2 | Forest M. White. |
| author_facet | Forest M. White. Bryson, Bryan David |
| author_sort | Bryson, Bryan David |
| collection | MIT |
| description | Thesis (Ph. D.)--Massachusetts Institute of Technology, Dept. of Biological Engineering, 2013. |
| first_indexed | 2024-09-23T17:06:12Z |
| format | Thesis |
| id | mit-1721.1/81664 |
| institution | Massachusetts Institute of Technology |
| language | eng |
| last_indexed | 2024-09-23T17:06:12Z |
| publishDate | 2013 |
| publisher | Massachusetts Institute of Technology |
| record_format | dspace |
| spelling | mit-1721.1/816642019-04-11T04:57:55Z Quantitative approaches to probe the acetylproteome Bryson, Bryan David Forest M. White. Massachusetts Institute of Technology. Department of Biological Engineering. Massachusetts Institute of Technology. Department of Biological Engineering. Biological Engineering. Thesis (Ph. D.)--Massachusetts Institute of Technology, Dept. of Biological Engineering, 2013. Cataloged from PDF version of thesis. Includes bibliographical references (p. 173-175). Lysine acetylation is a prevalent post-translational modification whose multi-varied biological roles have recently emerged. While having all the necessary components of a signaling network, lysine acetylation studies have been limited to a small subset of proteins and pathways. Using a quantitative unbiased mass spectrometry approach, we explored the role of growth factor stimulation on lysine acetylation. Although the growth factors bind receptor tyrosine kinases, growth factor stimulation resulted in rapid and dynamic changes in lysine acetylation. Furthermore, we demonstrated that short-term HDAC inhibition alters phosphotyrosine-signaling networks. To better understand this behavior, a suite of biochemical and computational methods were developed. Bromodomains were engineered to explore binding preferences using degenerate peptide arrays as well as develop acetyllysine affinity reagents as an alternative to anti-acetyllysine antibodies. Additionally, bioorthogonal proteomics were employed to identify acetyltransferase substrates. Taken together, the knowledge generated and the methods developed provide a toolkit for the analysis of lysine acetylation networks in the context of many biological processes as well as diseases. by Bryan David Bryson. Ph.D. 2013-10-24T17:41:15Z 2013-10-24T17:41:15Z 2013 2013 Thesis http://hdl.handle.net/1721.1/81664 859883403 eng MIT theses are protected by copyright. They may be viewed, downloaded, or printed from this source but further reproduction or distribution in any format is prohibited without written permission. http://dspace.mit.edu/handle/1721.1/7582 175 p. application/pdf Massachusetts Institute of Technology |
| spellingShingle | Biological Engineering. Bryson, Bryan David Quantitative approaches to probe the acetylproteome |
| title | Quantitative approaches to probe the acetylproteome |
| title_full | Quantitative approaches to probe the acetylproteome |
| title_fullStr | Quantitative approaches to probe the acetylproteome |
| title_full_unstemmed | Quantitative approaches to probe the acetylproteome |
| title_short | Quantitative approaches to probe the acetylproteome |
| title_sort | quantitative approaches to probe the acetylproteome |
| topic | Biological Engineering. |
| url | http://hdl.handle.net/1721.1/81664 |
| work_keys_str_mv | AT brysonbryandavid quantitativeapproachestoprobetheacetylproteome |