Structural investigation of cholesterol homeostasis and bacterial toxins
dc.contributor.advisor | Raunser, Stefan | |
dc.contributor.author | Günther, Patrick | |
dc.contributor.referee | Summerer, Daniel | |
dc.date.accepted | 2023-08-22 | |
dc.date.accessioned | 2023-09-26T08:44:22Z | |
dc.date.available | 2023-09-26T08:44:22Z | |
dc.date.issued | 2023 | |
dc.description.abstract | Membrane proteins regulate a variety of processes that are critical for living organisms. They participate in cell-cell communication, catalyze reactions in or at the membrane, are involved in transmitting signals from the environment into the cell, and can transport molecules across membranes. Approximately 60% of all clinically approved drugs target membrane proteins, underscoring their importance. In order to understand the function of membrane proteins and to design more targeted drugs, determining their precise three-dimensional structures is required. In this PhD project, I aimed to structurally characterize two membrane protein complexes involved in the regulation of cholesterol homeostasis – the Scap-Insig and HMGCR-UBIAD1 complexes – and the type VI secretion system (T6SS) effector RhsA. My PhD work showcases that biochemical studies combined with structural determination by cryo-EM provides valuable insights into molecular processes that occur in or at the membrane and is of utmost pharmacological interest. | en |
dc.identifier.uri | http://hdl.handle.net/2003/42108 | |
dc.identifier.uri | http://dx.doi.org/10.17877/DE290R-23941 | |
dc.language.iso | en | de |
dc.subject | Cryo-EM | en |
dc.subject | Single particle analysis | en |
dc.subject | Membrane proteins | en |
dc.subject | Bacterial toxins | en |
dc.subject | Type VI secretion system | en |
dc.subject | Cholesterol | en |
dc.subject.ddc | 570 | |
dc.subject.ddc | 540 | |
dc.subject.rswk | Elektronenmikroskopie | de |
dc.subject.rswk | Membranproteine | de |
dc.title | Structural investigation of cholesterol homeostasis and bacterial toxins | en |
dc.type | Text | de |
dc.type.publicationtype | PhDThesis | de |
dcterms.accessRights | open access | |
eldorado.secondarypublication | false | de |