{"id":{"repo_id":"unr","oai_identifier":"oai:scholarwolf.unr.edu:11714/3282"},"canonical_url":"https://search.dev.ndltd.org/etd/unr/oai:scholarwolf.unr.edu:11714/3282","repository":{"repo_id":"unr","name":"University of Nevada - Reno","base_url":"https://scholarwolf.unr.edu/server/oai/request"},"display":{"title":"Exploring the Mitigation of TDP-43 Toxicity by Sis1 in Yeast","abstract":"Amyotrophic Lateral Sclerosis is a progressive neurodegenerative disease with a 100% fatality rate. Most cases have no known cause, with 5-10% of cases having a familial link. Currently there is no cure. Research has revealed that Tar DNA-binding Protein 43 cytoplasmic aggregates are involved in many cases of Amyotrophic Lateral Sclerosis. One possible mechanism for TDP-43 induced toxicity is that these aggregates are titrating away a molecular chaperone protein, Sis1, from the nucleus of the cell. Sis1 is important in the degradation of proteins, and without it, the cell would become non-viable. In order to examine the relationship between the two proteins, they were tagged with fluorescent proteins and examined for colocalization under fluorescent microscopy. However, while TDP-43 does appear to titrate Sis1 out of the nucleus, there was no evidence that the two proteins colocalized.","abstract_html":"Amyotrophic Lateral Sclerosis is a progressive neurodegenerative disease with a 100% fatality rate. Most cases have no known cause, with 5-10% of cases having a familial link. Currently there is no cure. Research has revealed that Tar DNA-binding Protein 43 cytoplasmic aggregates are involved in many cases of Amyotrophic Lateral Sclerosis. One possible mechanism for TDP-43 induced toxicity is that these aggregates are titrating away a molecular chaperone protein, Sis1, from the nucleus of the cell. Sis1 is important in the degradation of proteins, and without it, the cell would become non-viable. In order to examine the relationship between the two proteins, they were tagged with fluorescent proteins and examined for colocalization under fluorescent microscopy. However, while TDP-43 does appear to titrate Sis1 out of the nucleus, there was no evidence that the two proteins colocalized.","abstract_has_math":false,"creators":["Ham, Jacqueline"],"institution":"University of Nevada, Reno","degree_name":"Biochemistry and Molecular Biology","degree_level":"Honors Thesis","degree_discipline":null,"degree_department":null,"school":null,"contributors":[],"advisors":["Park, Sei-Kyoung","Liebman, Susan"],"committee_chairs":[],"committee_members":[],"year":2016,"date_issued":"2016","date_published":"2016","updated_at":"2026-07-27T21:46:41Z","subjects":[],"languages":["en_US","English"],"rights":["In Copyright"],"rights_urls":[],"identifier_entries":[]},"links":{"outbound_url":"http://hdl.handle.net/11714/3282","outbound_label":"Handle","outbound_source":"dc:identifier.uri"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor.advisor","label":"Advisor","values":["Park, Sei-Kyoung","Liebman, Susan"]},{"key":"dc:creator","label":"Author","values":["Ham, Jacqueline"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date.accessioned","label":"Dc Date Accessioned","values":["2018-05-07T17:02:44Z"]},{"key":"dc:date.available","label":"Dc Date Available","values":["2018-05-07T17:02:44Z"]},{"key":"dc:date.issued","label":"Date","values":["2016"]},{"key":"dc:type","label":"Dc Type","values":["Thesis"]},{"key":"thesis:degree_level","label":"Degree Level","values":["Honors Thesis"]},{"key":"thesis:degree_name","label":"Degree Name","values":["Biochemistry and Molecular Biology"]},{"key":"thesis:institution_name","label":"Thesis Institution Name","values":["University of Nevada, Reno"]}]},{"id":"language_rights","label":"Language and Rights","entries":[{"key":"dc:language","label":"Dc Language","values":["English"]},{"key":"dc:language.iso","label":"Language (ISO)","values":["en_US"]},{"key":"dc:rights","label":"Dc Rights","values":["In Copyright"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier.uri","label":"Identifier URI","values":["http://hdl.handle.net/11714/3282"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description","label":"Description","values":["The University of Nevada, Reno Libraries will promptly respond to removal requests related to content that violates intellectual property laws, data protections, or has been uploaded without creator consent. Takedown notices should be directed to our ScholarWolf team (scholarwolf@library.unr.edu) with information about the object, including its full URL and the nature of your complaint."]},{"key":"dc:description.abstract","label":"Abstract","values":["Amyotrophic Lateral Sclerosis is a progressive neurodegenerative disease with a 100% fatality rate. Most cases have no known cause, with 5-10% of cases having a familial link. Currently there is no cure. Research has revealed that Tar DNA-binding Protein 43 cytoplasmic aggregates are involved in many cases of Amyotrophic Lateral Sclerosis. One possible mechanism for TDP-43 induced toxicity is that these aggregates are titrating away a molecular chaperone protein, Sis1, from the nucleus of the cell. Sis1 is important in the degradation of proteins, and without it, the cell would become non-viable. In order to examine the relationship between the two proteins, they were tagged with fluorescent proteins and examined for colocalization under fluorescent microscopy. However, while TDP-43 does appear to titrate Sis1 out of the nucleus, there was no evidence that the two proteins colocalized."]},{"key":"dc:format","label":"Dc Format","values":["PDF"]},{"key":"dc:title","label":"Title","values":["Exploring the Mitigation of TDP-43 Toxicity by Sis1 in Yeast"]}]}],"canonical_facts":{"dc:contributor.advisor":["Park, Sei-Kyoung","Liebman, Susan"],"dc:creator":["Ham, Jacqueline"],"dc:date.accessioned":["2018-05-07T17:02:44Z"],"dc:date.available":["2018-05-07T17:02:44Z"],"dc:date.issued":["2016"],"dc:description":["The University of Nevada, Reno Libraries will promptly respond to removal requests related to content that violates intellectual property laws, data protections, or has been uploaded without creator consent. Takedown notices should be directed to our ScholarWolf team (scholarwolf@library.unr.edu) with information about the object, including its full URL and the nature of your complaint."],"dc:description.abstract":["Amyotrophic Lateral Sclerosis is a progressive neurodegenerative disease with a 100% fatality rate. Most cases have no known cause, with 5-10% of cases having a familial link. Currently there is no cure. Research has revealed that Tar DNA-binding Protein 43 cytoplasmic aggregates are involved in many cases of Amyotrophic Lateral Sclerosis. One possible mechanism for TDP-43 induced toxicity is that these aggregates are titrating away a molecular chaperone protein, Sis1, from the nucleus of the cell. Sis1 is important in the degradation of proteins, and without it, the cell would become non-viable. In order to examine the relationship between the two proteins, they were tagged with fluorescent proteins and examined for colocalization under fluorescent microscopy. However, while TDP-43 does appear to titrate Sis1 out of the nucleus, there was no evidence that the two proteins colocalized."],"dc:format":["PDF"],"dc:identifier.uri":["http://hdl.handle.net/11714/3282"],"dc:language":["English"],"dc:language.iso":["en_US"],"dc:rights":["In Copyright"],"dc:title":["Exploring the Mitigation of TDP-43 Toxicity by Sis1 in Yeast"],"dc:type":["Thesis"],"thesis:degree_level":["Honors Thesis"],"thesis:degree_name":["Biochemistry and Molecular Biology"],"thesis:institution_name":["University of Nevada, Reno"]},"updated_at":"2026-07-27T21:46:41Z"}