{"id":{"repo_id":"uiuc","oai_identifier":"oai:www.ideals.illinois.edu:2142/84280"},"canonical_url":"https://search.dev.ndltd.org/etd/uiuc/oai:www.ideals.illinois.edu:2142/84280","repository":{"repo_id":"uiuc","name":"University of Illinois - Urbana-Champaign","base_url":"https://www.ideals.illinois.edu/oai-pmh"},"display":{"title":"Novel Applications of Top Down MS/MS for Interrogating the Human Proteome","abstract":"Top Down MS analysis of proteins from human cervical carcinoma cell lines and primary human leukocytes harvested from leukoreduction filters provided identification of 261 protein forms, with &sim;12% overlap between the two proteomes. The protein forms were produced by 162 unique genes (&sim;22% overlap). The above information demonstrates the dynamic expression patterns of proteins in various human cell types. Among the above identifications, 89 proteolysis events, 16 methylation events, 10 phosphorylation sites, 7 acetylations (non-N-terminal), and 9 other modifications were observed. These data indicate the significant post-translational complexity present in the human proteome and validate the application of Top Down in complex proteomes, with the most precise molecular characterization of human proteins demonstrated to date.","abstract_html":"Top Down MS analysis of proteins from human cervical carcinoma cell lines and primary human leukocytes harvested from leukoreduction filters provided identification of 261 protein forms, with &amp;sim;12% overlap between the two proteomes. The protein forms were produced by 162 unique genes (&amp;sim;22% overlap). The above information demonstrates the dynamic expression patterns of proteins in various human cell types. Among the above identifications, 89 proteolysis events, 16 methylation events, 10 phosphorylation sites, 7 acetylations (non-N-terminal), and 9 other modifications were observed. These data indicate the significant post-translational complexity present in the human proteome and validate the application of Top Down in complex proteomes, with the most precise molecular characterization of human proteins demonstrated to date.","abstract_has_math":false,"creators":["Roth, Michael"],"institution":"University of Illinois at Urbana-Champaign","degree_name":"Ph.D.","degree_level":"Dissertation","degree_discipline":"Chemistry","degree_department":null,"school":null,"contributors":["Kelleher, Neil L."],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2015,"date_issued":"2015-09-25T22:13:46Z","date_published":"2015-09-25T22:13:46Z","updated_at":"2026-07-22T22:26:22Z","subjects":["Chemistry, Analytical"],"languages":["eng"],"rights":[],"rights_urls":[],"identifier_entries":[{"key":"dc:identifier","label":"Identifier","values":["(MiAaPQ)AAI3290364"],"render_values":[{"text":"(MiAaPQ)AAI3290364","href":null,"code":true}]}]},"links":{"outbound_url":"http://hdl.handle.net/2142/84280","outbound_label":"Handle","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor","label":"Contributor","values":["Kelleher, Neil L."]},{"key":"dc:creator","label":"Author","values":["Roth, Michael"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date","label":"Dc Date","values":["2015-09-25T22:13:46Z","10000-01-01","2007"]},{"key":"dc:type","label":"Dc Type","values":["text"]},{"key":"thesis:degree_discipline","label":"Discipline","values":["Chemistry"]},{"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":["Chemistry, Analytical"]}]},{"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/2142/84280","(MiAaPQ)AAI3290364"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description","label":"Description","values":["Top Down MS analysis of proteins from human cervical carcinoma cell lines and primary human leukocytes harvested from leukoreduction filters provided identification of 261 protein forms, with &sim;12% overlap between the two proteomes. 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