Date of Award
January 2016
Degree Type
Dissertation
Degree Name
Doctor of Philosophy (PhD)
Department
Biological Science
First Advisor
Andrew Mescar
Committee Member 1
Humaira Gowher
Committee Member 2
Jeffrey Bolin
Committee Member 3
Timothy Ratliff
Abstract
Ubiquitination is an important post-translational modification involved in maintaining cellular homeostasis by regulating many delicate cellular processes, including the cell-cycle, membrane protein trafficking, endocytosis and apoptosis. Ubiquitin Specific Proteases (USPs) remove ubiquitin modifications from protein substrates to reverse the signal imposed by the ubiquitination. Perturbations in the expression levels of USPs has been implicated in many types of cancers where patients show significant elevation in cellular levels of specific USPs. This suggests that targeting specific upregulated members of the USP family in specific disease states would be ideal for the development of personalized anti-cancer therapeutics.
Recommended Citation
Hjortland, Nicole M., "Defining the regulatory determinants in substrate catalysis by biochemical, biophysical, and kinetic studies for the development of specific small-molecule inhibitors of ubiquitin specific proteases 7 and 17" (2016). Open Access Dissertations. 1461.
https://docs.lib.purdue.edu/open_access_dissertations/1461