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Structural and Functional Characterization of the Immunoproteasome [electronic resource] / by Eva Maria Huber.

By: Huber, Eva Maria [author.].
Contributor(s): SpringerLink (Online service).
Material type: materialTypeLabelBookSeries: Springer Theses, Recognizing Outstanding Ph.D. Research: Publisher: Cham : Springer International Publishing : Imprint: Springer, 2013Description: XIX, 82 p. 33 illus., 29 illus. in color. online resource.Content type: text Media type: computer Carrier type: online resourceISBN: 9783319015569.Subject(s): Chemistry | Analytical biochemistry | Biochemistry | Chemistry | Analytical Chemistry | Protein Science | Medicinal ChemistryDDC classification: 543 Online resources: Click here to access online
Contents:
Introduction -- Objective -- Materials and Methods -- Results -- Discussion -- Appendix.
In: Springer eBooksSummary: 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.
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Introduction -- Objective -- Materials and Methods -- Results -- Discussion -- Appendix.

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.

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