Abstract
Intracellular proteolysis is an essential process (1). The ubiquitin—proteasome pathway represents a strictly controlled complex enzymatic machinery for nonlysosomal protein degradation in eukaryotic cells. Thus, it is particularly important for the turnover of many critical proteins controlling a vast array of biologic pathways, including proliferation, differentiation, and inflammation (2–4). The system functions in two steps: first, a protein substrate is marked by covalent addition of a poly-ubiquitin chain; second, the poly-ubiquitinated substrate is degraded by a 2500-kDa proteolytic complex called the 26S proteasome.
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Groll, M., Huber, R. (2004). Structures of the Yeast Proteasome Core Particle in Complex with Inhibitors. In: Adams, J. (eds) Proteasome Inhibitors in Cancer Therapy. Cancer Drug Discovery and Development. Humana Press, Totowa, NJ. https://doi.org/10.1007/978-1-59259-794-9_3
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DOI: https://doi.org/10.1007/978-1-59259-794-9_3
Publisher Name: Humana Press, Totowa, NJ
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Online ISBN: 978-1-59259-794-9
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