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

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.

Name thesis:degree_name

Doctor of Philosophy (PhD)

Level thesis:degree_level

Dissertation

Discipline thesis:degree_discipline

Biological Science

Year

2016

Author dc:creator

• Hjortland, Nicole M.

Contributors dc:contributor

• Andrew Mescar
• Humaira Gowher
• Jeffrey Bolin
• Timothy Ratliff

• Enzyme Kinetics
• Intramolecular Activation
• Ubiquitin
• Ubiquitin Specific Protease

Repository record dc:identifier

https://docs.lib.purdue.edu/open_access_dissertations/1461

OAI identifier oai:identifier

oai:docs.lib.purdue.edu:open_access_dissertations-2677