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Nominated as an outstanding Ph.D. thesis by the Technische Universität München, Germany
Detailed analysis of the X-ray structures of the murine immune- and constitutive proteasome
Yeast mutagenesis study to explore the differences between the constitutive proteasome, the immunoproteasome and the thymoproteasome
Inhibition studies on the immunoproteasome-selective compound ONX 0914
In this acclaimed thesis, Eva Maria Huber reveals ground-breaking results by elucidating the crystal structure of the murine immunoproteasome in complex with a selective inhibitor. Huber does this by performing multidisciplinary methodologies including X-ray crystallography, fluorescence spectroscopy and mutagenesis experiments. Her exceptional results explore the immunoproteasome complex structures and are of outstanding importance for future scientific research especially in the pharmaceutical industry. These results will enable the functional analysis of individual proteasome subunits and support the development of novel drugs for autoimmune diseases such as multiple sclerosis or rheumatoid arthritis.
Content Level »Research
Keywords »Antigen Generation - Drugs for Cancers and Autoimmune Diseases - Immunoproteasome X-ray Structure - Proteasome Inhibition - Protein Crystallography - Proteolytic Degradation - Structure-based Drug Design - Ubiquitin-proteasome System