{"id":{"repo_id":"purdue-thes","oai_identifier":"oai:docs.lib.purdue.edu:open_access_dissertations-2677"},"canonical_url":"https://search.dev.ndltd.org/etd/purdue-thes/oai:docs.lib.purdue.edu:open_access_dissertations-2677","repository":{"repo_id":"purdue-thes","name":"Purdue University","base_url":"https://docs.lib.purdue.edu/do/oai/"},"display":{"title":"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","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.","abstract_html":"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.","abstract_has_math":false,"creators":["Hjortland, Nicole M."],"institution":null,"degree_name":"Doctor of Philosophy (PhD)","degree_level":"Dissertation","degree_discipline":"Biological Science","degree_department":null,"school":null,"contributors":["Andrew Mescar","Humaira Gowher","Jeffrey Bolin","Timothy Ratliff"],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2016,"date_issued":"2016-01-01T08:00:00Z","date_published":"2016-01-01T08:00:00Z","updated_at":"2026-07-24T03:54:44Z","subjects":["Enzyme Kinetics","Intramolecular Activation","Ubiquitin","Ubiquitin Specific Protease"],"languages":[],"rights":[],"rights_urls":[],"identifier_entries":[]},"links":{"outbound_url":"https://docs.lib.purdue.edu/open_access_dissertations/1461","outbound_label":"Repository record","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor","label":"Contributor","values":["Andrew Mescar","Humaira Gowher","Jeffrey Bolin","Timothy Ratliff"]},{"key":"dc:creator","label":"Author","values":["Hjortland, Nicole M."]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"thesis:degree_discipline","label":"Discipline","values":["Biological Science"]},{"key":"thesis:degree_level","label":"Degree Level","values":["Dissertation"]},{"key":"thesis:degree_name","label":"Degree Name","values":["Doctor of Philosophy (PhD)"]}]},{"id":"subjects_keywords","label":"Subjects and Keywords","entries":[{"key":"dc:subject","label":"Dc Subject","values":["Enzyme Kinetics","Intramolecular Activation","Ubiquitin","Ubiquitin Specific Protease"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier","label":"Identifier","values":["https://docs.lib.purdue.edu/open_access_dissertations/1461"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description.abstract","label":"Abstract","values":["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."]},{"key":"dc:title","label":"Title","values":["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"]}]}],"canonical_facts":{"dc:contributor":["Andrew Mescar","Humaira Gowher","Jeffrey Bolin","Timothy Ratliff"],"dc:creator":["Hjortland, Nicole M."],"dc:description.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. 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