Abstract
Modification of proteins by ubiquitin plays a fundamental role in maintaining a functional proteome. Proteins can be modified by single ubiquitin moieties or by various types of ubiquitin chains differing in linkage type and topology. Different ubiquitin chains are assumed to signal target proteins for different fates, but how this is achieved is only partially understood. We developed an easy-to-use strategy to generate large amounts of linkage-defined, non-hydrolyzable ubiquitin chains and show their potential to dissect ubiquitin signalling.
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