{"id":{"repo_id":"uiuc","oai_identifier":"oai:www.ideals.illinois.edu:2142/88341"},"canonical_url":"https://search.dev.ndltd.org/etd/uiuc/oai:www.ideals.illinois.edu:2142/88341","repository":{"repo_id":"uiuc","name":"University of Illinois - Urbana-Champaign","base_url":"https://www.ideals.illinois.edu/oai-pmh"},"display":{"title":"Characterization of the Anti-Inflammatory Effects of the Molluscum Contagiosum Virus MC160 Protein","abstract":"Using a series of MC160 deletion mutant proteins, we found that two distinct regions of the MC160 protein independently inhibit TNF-mediated NF-kappaB activation. Specifically, we observed that the second DED of MC160 interacts with procaspase-8 as a means to inhibit NF-kappaB activation, while the C-terminus of MC160 interacts with the chaperone Hsp90. Because both procaspase-8 and Hsp90 associate with the IKK complex, we believe that the MC160 protein binds these proteins as a means to destabilize the IKK complex, resulting in reduced IKK activation, and ultimately, inhibition of NF-kappaB activation.","abstract_html":"Using a series of MC160 deletion mutant proteins, we found that two distinct regions of the MC160 protein independently inhibit TNF-mediated NF-kappaB activation. Specifically, we observed that the second DED of MC160 interacts with procaspase-8 as a means to inhibit NF-kappaB activation, while the C-terminus of MC160 interacts with the chaperone Hsp90. Because both procaspase-8 and Hsp90 associate with the IKK complex, we believe that the MC160 protein binds these proteins as a means to destabilize the IKK complex, resulting in reduced IKK activation, and ultimately, inhibition of NF-kappaB activation.","abstract_has_math":false,"creators":["Nichols, Daniel B."],"institution":"University of Illinois at Urbana-Champaign","degree_name":"Ph.D.","degree_level":"Dissertation","degree_discipline":null,"degree_department":null,"school":null,"contributors":["Joanna Shisler"],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2015,"date_issued":"2015-10-14T19:24:54Z","date_published":"2015-10-14T19:24:54Z","updated_at":"2026-07-22T22:26:32Z","subjects":["Biology, Virology"],"languages":["eng"],"rights":[],"rights_urls":[],"identifier_entries":[{"key":"dc:identifier","label":"Identifier","values":["(MiAaPQ)AAI3347488"],"render_values":[{"text":"(MiAaPQ)AAI3347488","href":null,"code":true}]}]},"links":{"outbound_url":"http://hdl.handle.net/2142/88341","outbound_label":"Handle","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor","label":"Contributor","values":["Joanna Shisler"]},{"key":"dc:creator","label":"Author","values":["Nichols, Daniel B."]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date","label":"Dc Date","values":["2015-10-14T19:24:54Z","10000-01-01","2008"]},{"key":"dc:type","label":"Dc Type","values":["text"]},{"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, Virology"]}]},{"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/2142/88341","(MiAaPQ)AAI3347488"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description","label":"Description","values":["Using a series of MC160 deletion mutant proteins, we found that two distinct regions of the MC160 protein independently inhibit TNF-mediated NF-kappaB activation. Specifically, we observed that the second DED of MC160 interacts with procaspase-8 as a means to inhibit NF-kappaB activation, while the C-terminus of MC160 interacts with the chaperone Hsp90. Because both procaspase-8 and Hsp90 associate with the IKK complex, we believe that the MC160 protein binds these proteins as a means to destabilize the IKK complex, resulting in reduced IKK activation, and ultimately, inhibition of NF-kappaB activation.","Made available in DSpace on 2015-10-14T19:24:54Z (GMT). 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Specifically, we observed that the second DED of MC160 interacts with procaspase-8 as a means to inhibit NF-kappaB activation, while the C-terminus of MC160 interacts with the chaperone Hsp90. Because both procaspase-8 and Hsp90 associate with the IKK complex, we believe that the MC160 protein binds these proteins as a means to destabilize the IKK complex, resulting in reduced IKK activation, and ultimately, inhibition of NF-kappaB activation.","Made available in DSpace on 2015-10-14T19:24:54Z (GMT). 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