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Title: Biological and physicochemical functions of ubiquitylation revealed by synthetic chemistry approaches
Authors: Morimoto, Daichi  kyouindb  KAKEN_id  orcid (unconfirmed)
Walinda, Erik
Sugase, Kenji  kyouindb  KAKEN_id  orcid (unconfirmed)
Shirakawa, Masahiro
Author's alias: 森本, 大智
菅瀬, 謙治
Keywords: ubiquitin
post-translational modification
chemical ubiquitylation
site-directed conjugation
Issue Date: 27-May-2017
Publisher: MDPI AG
Journal title: International Journal of Molecular Sciences
Volume: 18
Issue: 6
Thesis number: 1145
Abstract: 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.
Rights: © 2017 by the authors. Licensee MDPI, Basel, Switzerland.
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).
DOI(Published Version): 10.3390/ijms18061145
Appears in Collections:Journal Articles

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