{"id":{"repo_id":"uiuc","oai_identifier":"oai:www.ideals.illinois.edu:2142/84845"},"canonical_url":"https://search.dev.ndltd.org/etd/uiuc/oai:www.ideals.illinois.edu:2142/84845","repository":{"repo_id":"uiuc","name":"University of Illinois - Urbana-Champaign","base_url":"https://www.ideals.illinois.edu/oai-pmh"},"display":{"title":"Engineering T Cell Receptors for Potential Therapeutic Applications","abstract":"The overall goal of developing new engineering strategies to allow for the isolation of high affinity mutants of many different TCRs was extended to methods for affinity maturation in Chapter 4. Previous affinity-based selections have involved incubating yeast cells with fluorescently labeled recombinant pepMHC ligand. Many pepMHC ligands are difficult to express and purify, so an alternative affinity selection strategy that obviates the need for this material would likewise facilitate affinity maturation. The new method described in Chapter 4 selects for yeast-displayed high-affinity TCR mutants by virtue of their binding to antigen-presenting cells. The concepts and strategies described herein not only provide insight into the folding of TCR domains, but also expand the repertoire of methods for TCR engineering by yeast display.","abstract_html":"The overall goal of developing new engineering strategies to allow for the isolation of high affinity mutants of many different TCRs was extended to methods for affinity maturation in Chapter 4. Previous affinity-based selections have involved incubating yeast cells with fluorescently labeled recombinant pepMHC ligand. Many pepMHC ligands are difficult to express and purify, so an alternative affinity selection strategy that obviates the need for this material would likewise facilitate affinity maturation. The new method described in Chapter 4 selects for yeast-displayed high-affinity TCR mutants by virtue of their binding to antigen-presenting cells. The concepts and strategies described herein not only provide insight into the folding of TCR domains, but also expand the repertoire of methods for TCR engineering by yeast display.","abstract_has_math":false,"creators":["Richman, Sarah A."],"institution":"University of Illinois at Urbana-Champaign","degree_name":"Ph.D.","degree_level":"Dissertation","degree_discipline":"Biochemistry","degree_department":null,"school":null,"contributors":["Kranz, David M."],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2015,"date_issued":"2015-09-25T22:28:10Z","date_published":"2015-09-25T22:28:10Z","updated_at":"2026-07-22T22:26:24Z","subjects":["Biology, Molecular"],"languages":["eng"],"rights":[],"rights_urls":[],"identifier_entries":[{"key":"dc:identifier","label":"Identifier","values":["(MiAaPQ)AAI3290358"],"render_values":[{"text":"(MiAaPQ)AAI3290358","href":null,"code":true}]}]},"links":{"outbound_url":"http://hdl.handle.net/2142/84845","outbound_label":"Handle","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor","label":"Contributor","values":["Kranz, David M."]},{"key":"dc:creator","label":"Author","values":["Richman, Sarah A."]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date","label":"Dc Date","values":["2015-09-25T22:28:10Z","10000-01-01","2007"]},{"key":"dc:type","label":"Dc Type","values":["text"]},{"key":"thesis:degree_discipline","label":"Discipline","values":["Biochemistry"]},{"key":"thesis:degree_level","label":"Degree Level","values":["Dissertation"]},{"key":"thesis:degree_name","label":"Degree Name","values":["Ph.D."]},{"key":"thesis:institution_name","label":"Thesis Institution Name","values":["University of Illinois at Urbana-Champaign"]}]},{"id":"subjects_keywords","label":"Subjects and Keywords","entries":[{"key":"dc:subject","label":"Dc Subject","values":["Biology, Molecular"]}]},{"id":"language_rights","label":"Language and Rights","entries":[{"key":"dc:language","label":"Dc Language","values":["eng"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier","label":"Identifier","values":["http://hdl.handle.net/2142/84845","(MiAaPQ)AAI3290358"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description","label":"Description","values":["The overall goal of developing new engineering strategies to allow for the isolation of high affinity mutants of many different TCRs was extended to methods for affinity maturation in Chapter 4. Previous affinity-based selections have involved incubating yeast cells with fluorescently labeled recombinant pepMHC ligand. Many pepMHC ligands are difficult to express and purify, so an alternative affinity selection strategy that obviates the need for this material would likewise facilitate affinity maturation. The new method described in Chapter 4 selects for yeast-displayed high-affinity TCR mutants by virtue of their binding to antigen-presenting cells. The concepts and strategies described herein not only provide insight into the folding of TCR domains, but also expand the repertoire of methods for TCR engineering by yeast display.","Made available in DSpace on 2015-09-25T22:28:10Z (GMT). No. of bitstreams: 2 license.txt: 4848 bytes, checksum: 96035ab3f5e1c23cc7138a224ce498bd (MD5) 3290358.pdf: 4462631 bytes, checksum: 78bb7d20e23b8596e91d1514bf8008a9 (MD5) Previous issue date: 2007","Embargo set by: Seth Robbins for item 86126 Lift date: Forever Reason: Restricted to the U of I community idenfinitely during batch ingest of legacy ETDs","Restricted to the U of I community idenfinitely during batch ingest of legacy ETDs","U of I Only","125 p.","Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 2007."]},{"key":"dc:title","label":"Title","values":["Engineering T Cell Receptors for Potential Therapeutic Applications"]}]}],"canonical_facts":{"dc:contributor":["Kranz, David M."],"dc:creator":["Richman, Sarah A."],"dc:date":["2015-09-25T22:28:10Z","10000-01-01","2007"],"dc:description":["The overall goal of developing new engineering strategies to allow for the isolation of high affinity mutants of many different TCRs was extended to methods for affinity maturation in Chapter 4. Previous affinity-based selections have involved incubating yeast cells with fluorescently labeled recombinant pepMHC ligand. Many pepMHC ligands are difficult to express and purify, so an alternative affinity selection strategy that obviates the need for this material would likewise facilitate affinity maturation. The new method described in Chapter 4 selects for yeast-displayed high-affinity TCR mutants by virtue of their binding to antigen-presenting cells. The concepts and strategies described herein not only provide insight into the folding of TCR domains, but also expand the repertoire of methods for TCR engineering by yeast display.","Made available in DSpace on 2015-09-25T22:28:10Z (GMT). No. of bitstreams: 2 license.txt: 4848 bytes, checksum: 96035ab3f5e1c23cc7138a224ce498bd (MD5) 3290358.pdf: 4462631 bytes, checksum: 78bb7d20e23b8596e91d1514bf8008a9 (MD5) Previous issue date: 2007","Embargo set by: Seth Robbins for item 86126 Lift date: Forever Reason: Restricted to the U of I community idenfinitely during batch ingest of legacy ETDs","Restricted to the U of I community idenfinitely during batch ingest of legacy ETDs","U of I Only","125 p.","Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 2007."],"dc:identifier":["http://hdl.handle.net/2142/84845","(MiAaPQ)AAI3290358"],"dc:language":["eng"],"dc:subject":["Biology, Molecular"],"dc:title":["Engineering T Cell Receptors for Potential Therapeutic Applications"],"dc:type":["text"],"thesis:degree_discipline":["Biochemistry"],"thesis:degree_level":["Dissertation"],"thesis:degree_name":["Ph.D."],"thesis:institution_name":["University of Illinois at Urbana-Champaign"]},"updated_at":"2026-07-22T22:26:24Z"}