Cell biological processes require intense and continuous regulation. This often involves complex systems that, when disturbed, fail to generate the desired outcome and finally result in diseases. Defects in these systems can have different origins. For example, the translation of the genes can be misregulated, leading to altered protein expression levels. Alternatively, genes can encode for mutated, truncated or chimeric fusion proteins, altering the function and activity of that protein. On the other hand, the defects can also originate from the regulation of the activity of otherwise correctly functional proteins. These regulation systems often rely on chemical modifications of the proteins, and these are also frequently perturbed in diseases. The focus of this thesis will be on one such important modification: ubiquitination.

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The research described in this thesis was supported by 3D repertoire (EU), Rubicon Network of excellence (EU), KWF (Koningin Wilhelmina Fonds), NWO-CW (Nederlandse organisatie voor de wetenschappelijk onderzoek – chemische wetenschappen) and Antoni van Leeuwenhoek Ziekenhuis
T.K. Sixma (Titia)
Erasmus University Rotterdam
hdl.handle.net/1765/26843
Erasmus MC: University Medical Center Rotterdam

Faesen, A. (2011, November 9). Activity modulation of Ubiquitin-Specific Proteases. Retrieved from http://hdl.handle.net/1765/26843