{"id":{"repo_id":"vu-aus","oai_identifier":"oai:eprints.vu.edu.au:15673"},"canonical_url":"https://search.dev.ndltd.org/etd/vu-aus/oai:eprints.vu.edu.au:15673","repository":{"repo_id":"vu-aus","name":"Victoria University (Australia)","base_url":"https://vuir.vu.edu.au/cgi/oai2"},"display":{"title":"Molecular basis of Fce receptor: IgE interactions","abstract":"Allergic diseases such as asthma and hay fever cause distress to numerous individuals throughout the world, sometimes with fatal consequences. Many associated costs - physical absences, psychological corollaries or medication - are borne by the community via health agencies or the government. The symptoms of these diseases, such as inflammation of the airways, are initially caused by the apposite allergen crosslinking at least two molecules of IgE bound to their high-affinity cell surface receptor FceRI. This interaction initiates intracellular signalling starting a cascade of events resulting in cellular degranulation and the release of inflammatory mediators. Many present treatments for these conditions act at this stage to inhibit the activity of these chemical intermediaries, after inflammation has been initiated. This thesis specifically addresses the high-affinity receptor for IgE (a chain) - FceRI-a, chimeric receptors of FceRI-a and FcyRIIa, with FceRI-a point mutants, and their interaction with IgE.","abstract_html":"Allergic diseases such as asthma and hay fever cause distress to numerous individuals throughout the world, sometimes with fatal consequences. Many associated costs - physical absences, psychological corollaries or medication - are borne by the community via health agencies or the government. The symptoms of these diseases, such as inflammation of the airways, are initially caused by the apposite allergen crosslinking at least two molecules of IgE bound to their high-affinity cell surface receptor FceRI. This interaction initiates intracellular signalling starting a cascade of events resulting in cellular degranulation and the release of inflammatory mediators. Many present treatments for these conditions act at this stage to inhibit the activity of these chemical intermediaries, after inflammation has been initiated. This thesis specifically addresses the high-affinity receptor for IgE (a chain) - FceRI-a, chimeric receptors of FceRI-a and FcyRIIa, with FceRI-a point mutants, and their interaction with IgE.","abstract_has_math":false,"creators":["Rigby, Aveline Joan"],"institution":"Victoria University of Technology","degree_name":"phd","degree_level":"doctoral","degree_discipline":null,"degree_department":null,"school":null,"contributors":[],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2001,"date_issued":"2001","date_published":"2001","updated_at":"2026-07-24T06:33:17Z","subjects":["1107 Immunology","School of Engineering and Science","0304 Medicinal and Bimolecular Chemistry"],"languages":["en"],"rights":[],"rights_urls":[],"identifier_entries":[]},"links":{"outbound_url":null,"outbound_label":null,"outbound_source":null},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:creator","label":"Author","values":["Rigby, Aveline Joan"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date","label":"Dc Date","values":["2001"]},{"key":"dc:date.issued","label":"Date","values":["2001"]},{"key":"dc:publisher.department","label":"Dc Publisher Department","values":["Centre for Bioprocessing and Food Technology"]},{"key":"dc:publisher.institution","label":"Dc Publisher Institution","values":["Victoria University of Technology"]},{"key":"dc:relation.isreferencedby","label":"Dc Relation Isreferencedby","values":["https://vuir.vu.edu.au/15673/"]},{"key":"dc:type","label":"Dc Type","values":["Thesis"]},{"key":"dc:type.qualificationlevel","label":"Dc Type Qualificationlevel","values":["doctoral"]},{"key":"dc:type.qualificationname","label":"Dc Type Qualificationname","values":["phd"]}]},{"id":"subjects_keywords","label":"Subjects and Keywords","entries":[{"key":"dc:subject","label":"Dc Subject","values":["1107 Immunology","School of Engineering and Science","0304 Medicinal and Bimolecular Chemistry"]}]},{"id":"language_rights","label":"Language and Rights","entries":[{"key":"dc:language","label":"Dc Language","values":["en"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier.uri","label":"Identifier URI","values":["https://vuir.vu.edu.au/15673/3/RIGBY%20Aveline-thesis_nosignature.pdf"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description.abstract","label":"Abstract","values":["Allergic diseases such as asthma and hay fever cause distress to numerous individuals throughout the world, sometimes with fatal consequences. Many associated costs - physical absences, psychological corollaries or medication - are borne by the community via health agencies or the government. The symptoms of these diseases, such as inflammation of the airways, are initially caused by the apposite allergen crosslinking at least two molecules of IgE bound to their high-affinity cell surface receptor FceRI. This interaction initiates intracellular signalling starting a cascade of events resulting in cellular degranulation and the release of inflammatory mediators. Many present treatments for these conditions act at this stage to inhibit the activity of these chemical intermediaries, after inflammation has been initiated. This thesis specifically addresses the high-affinity receptor for IgE (a chain) - FceRI-a, chimeric receptors of FceRI-a and FcyRIIa, with FceRI-a point mutants, and their interaction with IgE."]},{"key":"dc:format","label":"Dc Format","values":["text"]},{"key":"dc:title","label":"Title","values":["Molecular basis of Fce receptor: IgE interactions"]}]}],"canonical_facts":{"dc:creator":["Rigby, Aveline Joan"],"dc:date":["2001"],"dc:date.issued":["2001"],"dc:description.abstract":["Allergic diseases such as asthma and hay fever cause distress to numerous individuals throughout the world, sometimes with fatal consequences. Many associated costs - physical absences, psychological corollaries or medication - are borne by the community via health agencies or the government. The symptoms of these diseases, such as inflammation of the airways, are initially caused by the apposite allergen crosslinking at least two molecules of IgE bound to their high-affinity cell surface receptor FceRI. This interaction initiates intracellular signalling starting a cascade of events resulting in cellular degranulation and the release of inflammatory mediators. Many present treatments for these conditions act at this stage to inhibit the activity of these chemical intermediaries, after inflammation has been initiated. This thesis specifically addresses the high-affinity receptor for IgE (a chain) - FceRI-a, chimeric receptors of FceRI-a and FcyRIIa, with FceRI-a point mutants, and their interaction with IgE."],"dc:format":["text"],"dc:identifier.uri":["https://vuir.vu.edu.au/15673/3/RIGBY%20Aveline-thesis_nosignature.pdf"],"dc:language":["en"],"dc:publisher.department":["Centre for Bioprocessing and Food Technology"],"dc:publisher.institution":["Victoria University of Technology"],"dc:relation.isreferencedby":["https://vuir.vu.edu.au/15673/"],"dc:subject":["1107 Immunology","School of Engineering and Science","0304 Medicinal and Bimolecular Chemistry"],"dc:title":["Molecular basis of Fce receptor: IgE interactions"],"dc:type":["Thesis"],"dc:type.qualificationlevel":["doctoral"],"dc:type.qualificationname":["phd"]},"updated_at":"2026-07-24T06:33:17Z"}