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Int. J. Mol. Sci. 2017, 18(6), 1145;

Biological and Physicochemical Functions of Ubiquitylation Revealed by Synthetic Chemistry Approaches

Department of Molecular Engineering, Graduate School of Engineering, Kyoto University, Kyoto-Daigaku Katsura, Nishikyo-ku, Kyoto 615-8510, Japan
Department of Molecular and Cellular Physiology, Graduate School of Medicine, Kyoto University, Yoshida Konoe-cho, Sakyo-ku, Kyoto 606-8501, Japan
Author to whom correspondence should be addressed.
Academic Editor: Nobuhiro Nakamura
Received: 30 April 2017 / Revised: 23 May 2017 / Accepted: 24 May 2017 / Published: 27 May 2017
(This article belongs to the Special Issue Ubiquitin System)
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Most intracellular proteins are subjected to post-translational modification by ubiquitin. Accordingly, it is of fundamental importance to investigate the biological and physicochemical effects of ubiquitylation on substrate proteins. However, preparation of ubiquitylated proteins by an enzymatic synthesis bears limitations in terms of yield and site-specificity. Recently established chemical ubiquitylation methodologies can overcome these problems and provide a new understanding of ubiquitylation. Herein we describe the recent chemical ubiquitylation procedures with a focus on the effects of ubiquitylation on target proteins revealed by the synthetic approach. View Full-Text
Keywords: ubiquitin; post-translational modification; chemical ubiquitylation; site-directed conjugation ubiquitin; post-translational modification; chemical ubiquitylation; site-directed conjugation

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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

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Morimoto, D.; Walinda, E.; Sugase, K.; Shirakawa, M. Biological and Physicochemical Functions of Ubiquitylation Revealed by Synthetic Chemistry Approaches. Int. J. Mol. Sci. 2017, 18, 1145.

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