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Biological and Physicochemical Functions of Ubiquitylation Revealed by Synthetic Chemistry Approaches

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Department of Molecular Engineering, Graduate School of Engineering, Kyoto University, Kyoto-Daigaku Katsura, Nishikyo-ku, Kyoto 615-8510, Japan
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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
Int. J. Mol. Sci. 2017, 18(6), 1145; https://doi.org/10.3390/ijms18061145
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)
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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MDPI and ACS Style

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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Int. J. Mol. Sci., EISSN 1422-0067, Published by MDPI AG
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