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Updated: May 2, 2026

In Vitro Analysis of E3 Ubiquitin Ligase Function
Published on: May 14, 2021
Ubiquitin code assembly and disassembly
Claire Heride1, Sylvie Urbé1, Michael J Clague1
1Cellular and Molecular Physiology, Institute of Translational Medicine, University of Liverpool, L69 3BX, UK.
Abstract:
Ubiquitin, a 76 amino-acid polypeptide, presents a compact three-dimensional structure, utilising a fold that recurs within larger polypeptides and in other protein modifiers, such as NEDD8 and SUMO. Ubiquitylation was initially recognised as a signal for proteasome-mediated degradation. We shall consider here how this view has evolved to appreciate that the dynamic appendage of different types of ubiquitin chains represents a versatile, three-dimensional code, fundamental to the control of many cellular processes.
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