When RNA translation has completed and the proteins have been properly folded, most proteins are subject to a diverse range of post-translational modifications that affect their function. It is an important cellular strategy that enables the cell to react dynamically to intracellular or environmental changes caused by exposure to stress factors, growth stimuli or differentiation signals. Proteins are modified by methylation, acetylation, hydroxylation, phosphorylation or conjugated to ubiquitin (Ub) and ubiquitin-like (Ubl) proteins. The posttranslational modification with Ub of proteins has emerged to play an essential role in the regulation of virtually all aspects of cell biology.

DNA repair, cell biology, protease
T.K. Sixma (Titia)
Erasmus University Rotterdam
This research was financially supported by Rubicon Network of Excellence (EU), KWF (Koningin Wilhelmina Fonds) and NWO-CW (Nederlandse organisatie voor de wetenschappelijk onderzoek - chemische wetenschappen, CBG (Centre for Biomedical Genetics) and Antoni van Leeuwenhoek Hospital
978-90-8570-690-8
hdl.handle.net/1765/26844
Erasmus MC: University Medical Center Rotterdam

Vargas, M.P.A. (2011, November 9). Structural and Functional Studies on the Ubiquitin-Specific Protease Family. Erasmus University Rotterdam. Retrieved from http://hdl.handle.net/1765/26844