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ツゲ ヒデアキ
TSUGE HIDEAKI
津下 英明 所属 京都産業大学 生命科学部 先端生命科学科 職種 教授 |
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| 言語種別 | 日本語 |
| 発行・発表の年月 | 2024/07 |
| 形態種別 | 研究論文 |
| 査読 | 査読あり |
| 標題 | General ADP-Ribosylation Mechanism Based on the Structure of ADP-Ribosyltransferase-Substrate Complexes. |
| 執筆形態 | 共著 |
| 掲載誌名 | Toxins |
| 掲載区分 | 国外 |
| 巻・号・頁 | 16(7) |
| 著者・共著者 | Tsuge Hideaki, Habuka Noriyuki, Yoshida Toru |
| 概要 | ADP-ribosylation is a ubiquitous modification of proteins and other targets, such as nucleic acids, that regulates various cellular functions in all kingdoms of life. Furthermore, these ADP-ribosyltransferases (ARTs) modify a variety of substrates and atoms. It has been almost 60 years since ADP-ribosylation was discovered. Various ART structures have been revealed with cofactors (NAD+ or NAD+ analog). However, we still do not know the molecular mechanisms of ART. It needs to be better understood how ART specifies the target amino acids or bases. For this purpose, more information is needed about the tripartite complex structures of ART, the cofactors, and the substrates. The tripartite complex is essential to understand the mechanism of ADP-ribosyltransferase. This review updates the general ADP-ribosylation mechanism based on ART tripartite complex structures. |
| DOI | 10.3390/toxins16070313 |
| ISSN | 2072-6651 |
| PMID | 39057953 |