The predator becomes the prey: regulating the ubiquitin system by ubiquitylation and degradation
Author:
Publisher
Springer Science and Business Media LLC
Subject
Cell Biology,Molecular Biology
Link
http://www.nature.com/articles/nrm3173.pdf
Reference157 articles.
1. Wilkinson, K. D. The discovery of ubiquitin-dependent proteolysis. Proc. Natl Acad. Sci. USA 102, 15280–15282 (2005).
2. Shabek, N., Iwai, K. & Ciechanover, A. Ubiquitin is degraded by the ubiquitin system as a monomer and as part of its conjugated target. Biochem. Biophys. Res. Commun. 363, 425–431 (2007).
3. Hershko, A., Eytan, E., Ciechanover, A. & Haas, A. L. Immunochemical analysis of the turnover of ubiquitin-protein conjugates in intact cells. Relationship to the breakdown of abnormal proteins. J. Biol. Chem. 257, 13964–13970 (1982). The first description of the role of the ubiquitin proteolytic system in the degradation of proteins in intact nucleated cells. All prior studies describing the roles of the system were carried out using reticulocytes and mostly cell-free extracts from these cells, which are terminally differentiating red blood cells.
4. Haas, A. L. & Bright, P. M. The dynamics of ubiquitin pools within cultured human lung fibroblasts. J. Biol. Chem. 262, 345–351 (1987).
5. Patel, M. B. & Majetschak, M. Distribution and interrelationship of ubiquitin proteasome pathway component activities and ubiquitin pools in various porcine tissues. Physiol. Res. 56, 341–350 (2007).
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