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- YAMADA Koji
- Department of Biological Sciences, Graduate School of Science and Technology, Kumamoto University Department of Biological Sciences, Graduate School of Science and Technology, Kumamoto University
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- MURAMATSU Miyuki
- Department of Biological Sciences, Graduate School of Science and Technology, Kumamoto University Department of Biological Sciences, Graduate School of Science and Technology, Kumamoto University
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- SAITO Daiki
- Department of Biological Sciences, Graduate School of Science and Technology, Kumamoto University Department of Biological Sciences, Graduate School of Science and Technology, Kumamoto University
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- SATO-OKA Mai
- Department of Biological Sciences, Graduate School of Science and Technology, Kumamoto University Department of Biological Sciences, Graduate School of Science and Technology, Kumamoto University
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- SAITO Masayuki
- Department of Biological Sciences, Graduate School of Science and Technology, Kumamoto University Department of Biological Sciences, Graduate School of Science and Technology, Kumamoto University
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- MORIYAMA Taishi
- Department of Biological Sciences, Graduate School of Science and Technology, Kumamoto University Department of Biological Sciences, Graduate School of Science and Technology, Kumamoto University
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- SAITOH Hisato
- Department of Biological Sciences, Graduate School of Science and Technology, Kumamoto University Department of New Frontier Sciences, Graduate School of Science and Technology, Kumamoto University Global COE (Centers of Excellence) Program, Global Initiative Center for Pulsed Power Engineering, Kumamoto University Department of Biological Sciences, Graduate School of Science and Technology, Kumamoto University Department of New Frontier Sciences, Graduate School of Science and Technology, Kumamoto University Global COE (Centers of Excellence) Program, Global Initiative Center for Pulsed Power Engineering, Kumamoto University
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抄録
A hallmark of small ubiquitin-related modifier (SUMO) is the production of a C-terminal tail containing diglycines (GGs), which are believed to be required for SUMOylation. Whether GGs are required components in SUMOylation remains unanswered experimentally. In this study we found that the SUMO-1/3-AA/-GS/-GN/-GA mutant can form sodium dodecyl sulfate (SDS)-dithiothreitol (DTT)-resistant complexes with cellular proteins, indicating that the GG motif is not strictly required for SUMOylation.
収録刊行物
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- Bioscience, Biotechnology, and Biochemistry
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Bioscience, Biotechnology, and Biochemistry 76 (5), 1035-1037, 2012
公益社団法人 日本農芸化学会
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詳細情報 詳細情報について
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- CRID
- 1390282681455031168
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- NII論文ID
- 10030753299
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- NII書誌ID
- AA10824164
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- COI
- 1:STN:280:DC%2BC38jltlOmug%3D%3D
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- ISSN
- 13476947
- 09168451
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- NDL書誌ID
- 023682087
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- PubMed
- 22738983
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- 本文言語コード
- en
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- データソース種別
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- JaLC
- NDL
- Crossref
- PubMed
- CiNii Articles
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- 抄録ライセンスフラグ
- 使用不可