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タイトル: Biological and physicochemical functions of ubiquitylation revealed by synthetic chemistry approaches
著者: Morimoto, Daichi  kyouindb  KAKEN_id  orcid https://orcid.org/0000-0002-7672-2136 (unconfirmed)
Walinda, Erik  kyouindb  KAKEN_id  orcid https://orcid.org/0000-0003-1882-6401 (unconfirmed)
Sugase, Kenji  kyouindb  KAKEN_id  orcid https://orcid.org/0000-0001-8623-7743 (unconfirmed)
Shirakawa, Masahiro  kyouindb  KAKEN_id
著者名の別形: 森本, 大智
菅瀬, 謙治
キーワード: ubiquitin
post-translational modification
chemical ubiquitylation
site-directed conjugation
発行日: 27-May-2017
出版者: MDPI AG
誌名: International Journal of Molecular Sciences
巻: 18
号: 6
論文番号: 1145
抄録: 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.
著作権等: © 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).
URI: http://hdl.handle.net/2433/226315
DOI(出版社版): 10.3390/ijms18061145
PubMed ID: 28555012
出現コレクション:学術雑誌掲載論文等

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