Proper protein folding is a delicate balance that is crucial for normal biological function. In mammals, protein misfolding and aggregation leads to loss of function of the original protein while in many cases being associated with neurodegenerative diseases, eventually leading to death of the organism. In yeast however, the aggregated prion state is associated with positive cellular outcomes, and cells can switch between the [PRION+] and [prion-] states. Understanding the factors that lead to changes in prion state conformation in yeast could lead to novel insight into the conditions controlling misfolding by neurodegenerative proteinopathies. We believe that by studying the interface between neurodegeneration, protein misfolding, and epigenetics, we can elucidate the mechanisms leading to disease, and potentially reveal novel targets for therapeutic development. Our results highlight a need for further research into how misfolded protein aggregates disrupt the histone PTM landscape. We hope this work will lead to the discovery of novel targets for neurodegenerative disease therapeutics.
","abstract_html":"<p>Proper protein folding is a delicate balance that is crucial for normal biological function. In mammals, protein misfolding and aggregation leads to loss of function of the original protein while in many cases being associated with neurodegenerative diseases, eventually leading to death of the organism. In yeast however, the aggregated prion state is associated with positive cellular outcomes, and cells can switch between the [PRION+] and [prion-] states. Understanding the factors that lead to changes in prion state conformation in yeast could lead to novel insight into the conditions controlling misfolding by neurodegenerative proteinopathies. We believe that by studying the interface between neurodegeneration, protein misfolding, and epigenetics, we can elucidate the mechanisms leading to disease, and potentially reveal novel targets for therapeutic development. Our results highlight a need for further research into how misfolded protein aggregates disrupt the histone PTM landscape. We hope this work will lead to the discovery of novel targets for neurodegenerative disease therapeutics.</p>","abstract_has_math":false,"creators":["Cobos, Samantha"],"institution":"The Graduate School and University Center of The City University of New York","degree_name":"Doctor of Philosophy","degree_level":"Doctoral","degree_discipline":"Chemistry","degree_department":null,"school":null,"contributors":[],"advisors":["Mariana Torrente"],"committee_chairs":[],"committee_members":["Shana Elbaum-Garfinkle","Lesley Emtage","David Jeruzalmi","Emilio Gallicchio"],"year":2023,"date_issued":"2023-09-01T07:00:00Z","date_published":"2023-09-01T07:00:00Z","updated_at":"2026-07-24T01:59:14Z","subjects":["Chemistry","amyotrophic lateral sclerosis","epigenetics","posttranslational modifications","histones","prion","liquid liquid phase separation"],"languages":[],"rights":[],"rights_urls":[],"identifier_entries":[]},"links":{"outbound_url":"https://academicworks.cuny.edu/gc_etds/5452","outbound_label":"Repository record","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor.advisor","label":"Advisor","values":["Mariana Torrente"]},{"key":"dc:contributor.committeemember","label":"Committee Member","values":["Shana Elbaum-Garfinkle","Lesley Emtage","David Jeruzalmi","Emilio Gallicchio"]},{"key":"dc:creator","label":"Author","values":["Cobos, Samantha"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date.available","label":"Dc Date Available","values":["2023-07-28T07:00:00Z"]},{"key":"thesis:degree_discipline","label":"Discipline","values":["Chemistry"]},{"key":"thesis:degree_level","label":"Degree Level","values":["Doctoral"]},{"key":"thesis:degree_name","label":"Degree Name","values":["Doctor of Philosophy"]},{"key":"thesis:institution_name","label":"Thesis Institution Name","values":["The Graduate School and University Center of The City University of New York"]}]},{"id":"subjects_keywords","label":"Subjects and Keywords","entries":[{"key":"dc:subject","label":"Dc Subject","values":["Chemistry","amyotrophic lateral sclerosis","epigenetics","posttranslational modifications","histones","prion","liquid liquid phase separation"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier","label":"Identifier","values":["https://academicworks.cuny.edu/gc_etds/5452"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description.abstract","label":"Abstract","values":["Proper protein folding is a delicate balance that is crucial for normal biological function. In mammals, protein misfolding and aggregation leads to loss of function of the original protein while in many cases being associated with neurodegenerative diseases, eventually leading to death of the organism. In yeast however, the aggregated prion state is associated with positive cellular outcomes, and cells can switch between the [PRION+] and [prion-] states. Understanding the factors that lead to changes in prion state conformation in yeast could lead to novel insight into the conditions controlling misfolding by neurodegenerative proteinopathies. We believe that by studying the interface between neurodegeneration, protein misfolding, and epigenetics, we can elucidate the mechanisms leading to disease, and potentially reveal novel targets for therapeutic development. Our results highlight a need for further research into how misfolded protein aggregates disrupt the histone PTM landscape. We hope this work will lead to the discovery of novel targets for neurodegenerative disease therapeutics.
"]},{"key":"dc:title","label":"Title","values":["Disordered Protein Aggregates Are Linked to Changes in the Histone Post-Translational Modification Landscape in Disease and Non-Disease Models"]}]}],"canonical_facts":{"dc:contributor.advisor":["Mariana Torrente"],"dc:contributor.committeemember":["Shana Elbaum-Garfinkle","Lesley Emtage","David Jeruzalmi","Emilio Gallicchio"],"dc:creator":["Cobos, Samantha"],"dc:date.available":["2023-07-28T07:00:00Z"],"dc:description.abstract":["Proper protein folding is a delicate balance that is crucial for normal biological function. In mammals, protein misfolding and aggregation leads to loss of function of the original protein while in many cases being associated with neurodegenerative diseases, eventually leading to death of the organism. In yeast however, the aggregated prion state is associated with positive cellular outcomes, and cells can switch between the [PRION+] and [prion-] states. Understanding the factors that lead to changes in prion state conformation in yeast could lead to novel insight into the conditions controlling misfolding by neurodegenerative proteinopathies. We believe that by studying the interface between neurodegeneration, protein misfolding, and epigenetics, we can elucidate the mechanisms leading to disease, and potentially reveal novel targets for therapeutic development. Our results highlight a need for further research into how misfolded protein aggregates disrupt the histone PTM landscape. We hope this work will lead to the discovery of novel targets for neurodegenerative disease therapeutics.
"],"dc:identifier":["https://academicworks.cuny.edu/gc_etds/5452"],"dc:subject":["Chemistry","amyotrophic lateral sclerosis","epigenetics","posttranslational modifications","histones","prion","liquid liquid phase separation"],"dc:title":["Disordered Protein Aggregates Are Linked to Changes in the Histone Post-Translational Modification Landscape in Disease and Non-Disease Models"],"thesis:degree_discipline":["Chemistry"],"thesis:degree_level":["Doctoral"],"thesis:degree_name":["Doctor of Philosophy"],"thesis:institution_name":["The Graduate School and University Center of The City University of New York"]},"updated_at":"2026-07-24T01:59:14Z"}