{"id":{"repo_id":"buffalo","oai_identifier":"oai:ubir.buffalo.edu:10477/79319"},"canonical_url":"https://search.dev.ndltd.org/etd/buffalo/oai:ubir.buffalo.edu:10477/79319","repository":{"repo_id":"buffalo","name":"Buffalo","base_url":"https://ubir.buffalo.edu/oai/request"},"display":{"title":"Novel Anti-Cancer Agents Targeting Epidermal Growth Factor (EGF) Protein-Protein Interactions","abstract":"Ph.D.","abstract_html":"Ph.D.","abstract_has_math":false,"creators":["Yawson, Emmanuel"],"institution":"State University of New York at Buffalo","degree_name":null,"degree_level":null,"degree_discipline":null,"degree_department":null,"school":null,"contributors":["Dubocovich, Margarita","Pharmacology and Toxicology"],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2019,"date_issued":"2019-04-04T18:34:55Z","date_published":"2019-04-04T18:34:55Z","updated_at":"2026-07-27T19:05:14Z","subjects":["pharmacology"],"languages":["eng"],"rights":["Users of works found in University at Buffalo Institutional Repository (UBIR) are responsible for identifying and contacting the copyright owner for permission to reuse. University at Buffalo Libraries do not manage rights for copyright-protected works and cannot assist with permissions.","Copyright retained by author."],"rights_urls":[],"identifier_entries":[]},"links":{"outbound_url":"http://hdl.handle.net/10477/79319","outbound_label":"Handle","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor","label":"Contributor","values":["Dubocovich, Margarita","Pharmacology and Toxicology"]},{"key":"dc:creator","label":"Author","values":["Yawson, Emmanuel"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date","label":"Dc Date","values":["2019-04-04T18:34:55Z","2019","2019-01-14 14:51:22"]},{"key":"dc:publisher","label":"Institution","values":["State University of New York at Buffalo"]},{"key":"dc:type","label":"Dc Type","values":["Text","Dissertation"]}]},{"id":"subjects_keywords","label":"Subjects and Keywords","entries":[{"key":"dc:subject","label":"Dc Subject","values":["pharmacology"]}]},{"id":"language_rights","label":"Language and Rights","entries":[{"key":"dc:language","label":"Dc Language","values":["eng"]},{"key":"dc:rights","label":"Dc Rights","values":["Users of works found in University at Buffalo Institutional Repository (UBIR) are responsible for identifying and contacting the copyright owner for permission to reuse. University at Buffalo Libraries do not manage rights for copyright-protected works and cannot assist with permissions.","Copyright retained by author."]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier","label":"Identifier","values":["http://hdl.handle.net/10477/79319"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description","label":"Description","values":["Ph.D.","Epidermal growth factor (EGF) mediates several cellular functions and processes such as survival, motility, differentiation, proliferation and death. When it is released by epidermal tissues, EGF binds to cell surface receptors such as the epidermal growth factor receptor (EGFR) causing a conformational change which facilitates dimerization. Receptor dimerization activates the tyrosine kinase activity of the cytoplasmic domain of the receptor which then causes a signal transduction leading to DNA synthesis and cell proliferation. Growth factors are upregulated in various cancers. In breast cancer the upregulation of EGF activity correlates with endocrine resistance. A possible mechanism is interaction with estrogen receptor alpha (ERα). This provides a significant bottleneck for endocrine therapy targeting ERα. EGF is reported to bind to ERα. (Stoica et al. 2000). However EGF does not contain any known ER binding motif. Using proteomics, we have identified regions of EGF with potential to serve as interaction sites with the coactivator binding domain of ERα. This includes two novel ER binding motif in EGF. Epidermal growth factor receptor (EGFR) is a viable target for triple negative breast cancer. Hence, peptides derived from EGF hold potential to function as dual inhibitors of ERα and EGFR. Studying the molecular interaction of these peptides with ERα and EGFR will provide structural and mechanistic clues towards novel therapeutics to combat breast cancer."]},{"key":"dc:format","label":"Dc Format","values":["application/pdf"]},{"key":"dc:title","label":"Title","values":["Novel Anti-Cancer Agents Targeting Epidermal Growth Factor (EGF) Protein-Protein Interactions"]}]}],"canonical_facts":{"dc:contributor":["Dubocovich, Margarita","Pharmacology and Toxicology"],"dc:creator":["Yawson, Emmanuel"],"dc:date":["2019-04-04T18:34:55Z","2019","2019-01-14 14:51:22"],"dc:description":["Ph.D.","Epidermal growth factor (EGF) mediates several cellular functions and processes such as survival, motility, differentiation, proliferation and death. When it is released by epidermal tissues, EGF binds to cell surface receptors such as the epidermal growth factor receptor (EGFR) causing a conformational change which facilitates dimerization. Receptor dimerization activates the tyrosine kinase activity of the cytoplasmic domain of the receptor which then causes a signal transduction leading to DNA synthesis and cell proliferation. Growth factors are upregulated in various cancers. In breast cancer the upregulation of EGF activity correlates with endocrine resistance. A possible mechanism is interaction with estrogen receptor alpha (ERα). This provides a significant bottleneck for endocrine therapy targeting ERα. EGF is reported to bind to ERα. (Stoica et al. 2000). However EGF does not contain any known ER binding motif. Using proteomics, we have identified regions of EGF with potential to serve as interaction sites with the coactivator binding domain of ERα. This includes two novel ER binding motif in EGF. Epidermal growth factor receptor (EGFR) is a viable target for triple negative breast cancer. Hence, peptides derived from EGF hold potential to function as dual inhibitors of ERα and EGFR. Studying the molecular interaction of these peptides with ERα and EGFR will provide structural and mechanistic clues towards novel therapeutics to combat breast cancer."],"dc:format":["application/pdf"],"dc:identifier":["http://hdl.handle.net/10477/79319"],"dc:language":["eng"],"dc:publisher":["State University of New York at Buffalo"],"dc:rights":["Users of works found in University at Buffalo Institutional Repository (UBIR) are responsible for identifying and contacting the copyright owner for permission to reuse. University at Buffalo Libraries do not manage rights for copyright-protected works and cannot assist with permissions.","Copyright retained by author."],"dc:subject":["pharmacology"],"dc:title":["Novel Anti-Cancer Agents Targeting Epidermal Growth Factor (EGF) Protein-Protein Interactions"],"dc:type":["Text","Dissertation"]},"updated_at":"2026-07-27T19:05:14Z"}