Structure and function of the human Poly(ADP-ribose) polymerase enzyme family
Thesis (Ph. D.)--Massachusetts Institute of Technology, Dept. of Biology, 2013.
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| Format: | Thesis |
| Language: | eng |
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Massachusetts Institute of Technology
2013
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| Online Access: | http://hdl.handle.net/1721.1/81033 |
| _version_ | 1826208812467486720 |
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| author | Rood, Jennifer E. (Jennifer Evelyn) |
| author2 | Paul Chang. |
| author_facet | Paul Chang. Rood, Jennifer E. (Jennifer Evelyn) |
| author_sort | Rood, Jennifer E. (Jennifer Evelyn) |
| collection | MIT |
| description | Thesis (Ph. D.)--Massachusetts Institute of Technology, Dept. of Biology, 2013. |
| first_indexed | 2024-09-23T14:13:01Z |
| format | Thesis |
| id | mit-1721.1/81033 |
| institution | Massachusetts Institute of Technology |
| language | eng |
| last_indexed | 2024-09-23T14:13:01Z |
| publishDate | 2013 |
| publisher | Massachusetts Institute of Technology |
| record_format | dspace |
| spelling | mit-1721.1/810332019-04-12T12:19:42Z Structure and function of the human Poly(ADP-ribose) polymerase enzyme family Rood, Jennifer E. (Jennifer Evelyn) Paul Chang. Massachusetts Institute of Technology. Department of Biology. Massachusetts Institute of Technology. Department of Biology. Biology. Thesis (Ph. D.)--Massachusetts Institute of Technology, Dept. of Biology, 2013. Cataloged from PDF version of thesis. Includes bibliographical references. The poly(ADP-ribose) polymerase (PARP) family of enzymes in humans is comprised of 17 proteins. PARP-1, the first member of the family, synthesizes a large, complex post-translational modification, poly(ADP-ribose). While PARP-1 and some other PARPs have been extensively functionally characterized, the enzymatic and cellular functions of many PARPs are unknown. This thesis presents work that seeks to characterize the enzymatic functions of the PARP family. First, experimental demonstration of the automodification capacity of each PARP is presented. We find that PARP enzymatic activity largely conforms to bioinformatic predictions of PARP activity. Then, we seek to provide a structural rationale for these enzymatic capabilities based on the analysis of extant and modeled crystal structures of each PARP. We present a structural hypothesis for catalytic differences among PARPs. Finally, we examine methods for the identification of cellular targets of PARP activity and functional interaction partners of PARPs. Together, these elements of PARP characterization will aid in the discovery of physiologically relevant targets and a mechanistic understanding of PARP enzymatic activity in the cellular context. by Jennifer E. Rood. Ph.D. 2013-09-24T19:38:21Z 2013-09-24T19:38:21Z 2013 2013 Thesis http://hdl.handle.net/1721.1/81033 857791165 eng M.I.T. theses are protected by copyright. They may be viewed from this source for any purpose, but reproduction or distribution in any format is prohibited without written permission. See provided URL for inquiries about permission. http://dspace.mit.edu/handle/1721.1/7582 226 p. application/pdf Massachusetts Institute of Technology |
| spellingShingle | Biology. Rood, Jennifer E. (Jennifer Evelyn) Structure and function of the human Poly(ADP-ribose) polymerase enzyme family |
| title | Structure and function of the human Poly(ADP-ribose) polymerase enzyme family |
| title_full | Structure and function of the human Poly(ADP-ribose) polymerase enzyme family |
| title_fullStr | Structure and function of the human Poly(ADP-ribose) polymerase enzyme family |
| title_full_unstemmed | Structure and function of the human Poly(ADP-ribose) polymerase enzyme family |
| title_short | Structure and function of the human Poly(ADP-ribose) polymerase enzyme family |
| title_sort | structure and function of the human poly adp ribose polymerase enzyme family |
| topic | Biology. |
| url | http://hdl.handle.net/1721.1/81033 |
| work_keys_str_mv | AT roodjenniferejenniferevelyn structureandfunctionofthehumanpolyadpribosepolymeraseenzymefamily |