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dc.contributor.authorSzyszka, Taylor Nicole
dc.date.accessioned2019-03-29
dc.date.available2019-03-29
dc.date.issued2019-03-29
dc.identifier.urihttp://hdl.handle.net/2123/20221
dc.description.abstractThe work presented in this Thesis examines aspects of the molecular mechanisms underlying gene regulation, focusing on the bromodomain and extra-terminal domain (BET) protein family. BET proteins use their tandem bromodomains to bind acetylated lysines, such as those present on histones or transcription factors, while the extra-terminal (ET) domain has been described as a putative protein:protein interaction domain. This Thesis aims to connect these two functions, one in the recognition of post-translational modifications relevant to transcriptional activity and the other the recruitment of transcriptional machinery to specific sites in the genome. What emerges is a model wherein the bromodomains and ET domain work in synchrony to carry out various BET protein functions, both in normal and disease pathways. Additionally, the potential of the BET proteins to associate with themselves, each other, and other potential partners is addressed. Overall, this work provides another component to the emerging story of the complex molecular choreography underlying gene regulation.en_AU
dc.publisherUniversity of Sydneyen_AU
dc.publisherFaculty of Scienceen_AU
dc.publisherLife and Environmental Sciencesen_AU
dc.rightsThe author retains copyright of this thesis. It may only be used for the purposes of research and study. It must not be used for any other purposes and may not be transmitted or shared with others without prior permission.en_AU
dc.subjectNMRen_AU
dc.subjectProteinen_AU
dc.subjectStructureen_AU
dc.subjectGene Regulationen_AU
dc.titleStructural Studies of Bromodomain and Extra-Terminal Domain Protein BRD3en_AU
dc.typePhD Doctorateen_AU
dc.type.pubtypeDoctor of Philosophy Ph.D.en_AU
dc.description.disclaimerAccess is restricted to staff and students of the University of Sydney . UniKey credentials are required. Non university access may be obtained by visiting the University of Sydney Library.en_AU


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