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dc.contributor.author | Takada, Kenta | en |
dc.contributor.author | Amano, Ryo | en |
dc.contributor.author | Nomura, Yusuke | en |
dc.contributor.author | Tanaka, Yoichiro | en |
dc.contributor.author | Sugiyama, Shigeru | en |
dc.contributor.author | Nagata, Takashi | en |
dc.contributor.author | Katahira, Masato | en |
dc.contributor.author | Nakamura, Yoshikazu | en |
dc.contributor.author | Kozu, Tomoko | en |
dc.contributor.author | Sakamoto, Traiichi | en |
dc.contributor.alternative | 永田, 祟 | ja |
dc.contributor.alternative | 片平, 正人 | ja |
dc.date.accessioned | 2018-04-16T05:30:05Z | - |
dc.date.available | 2018-04-16T05:30:05Z | - |
dc.date.issued | 2018-02 | - |
dc.identifier.issn | 2211-5463 | - |
dc.identifier.uri | http://hdl.handle.net/2433/230576 | - |
dc.description.abstract | Since the invention of systematic evolution of ligands by exponential enrichment, many short oligonucleotides (or aptamers) have been reported that can bind to a wide range of target molecules with high affinity and specificity. Previously, we reported an RNA aptamer that shows high affinity to the Runt domain (RD) of the AML1 protein, a transcription factor with roles in haematopoiesis and immune function. From kinetic and thermodynamic studies, it was suggested that the aptamer recognises a large surface area of the RD, using numerous weak interactions. In this study, we identified the secondary structure by nuclear magnetic resonance spectroscopy and performed a mutational study to reveal the residue critical for binding to the RD. It was suggested that the large contact area was formed by a DNA‐mimicking motif and a multibranched loop, which confers the high affinity and specificity of binding. | en |
dc.format.mimetype | application/pdf | - |
dc.language.iso | eng | - |
dc.publisher | Wiley-Blackwell | en |
dc.rights | © 2017 The Authors. Published by FEBS Press and John Wiley & Sons Ltd. This is an open access article under the terms of the Creative Commons Attribution License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited. | en |
dc.subject | AML1 | en |
dc.subject | aptamer | en |
dc.subject | Mutation | en |
dc.subject | NMR | en |
dc.title | Characterisation of an aptamer against the Runt domain of AML1 (RUNX1) by NMR and mutational analyses | en |
dc.type | journal article | - |
dc.type.niitype | Journal Article | - |
dc.identifier.jtitle | FEBS Open Bio | en |
dc.identifier.volume | 8 | - |
dc.identifier.issue | 2 | - |
dc.identifier.spage | 264 | - |
dc.identifier.epage | 270 | - |
dc.relation.doi | 10.1002/2211-5463.12368 | - |
dc.textversion | publisher | - |
dc.address | Department of Life and Environmental Sciences, Faculty of Engineering, Chiba Institute of Technology | en |
dc.address | Department of Life and Environmental Sciences, Faculty of Engineering, Chiba Institute of Technology | en |
dc.address | Division of Medical Devices, National Institute of Health Sciences | en |
dc.address | Facility for RI Research and Education, Instrumental Analysis Center, Yokohama National University | en |
dc.address | Faculty of Science and Technology, Kochi University | en |
dc.address | Institute of Advanced Energy, Kyoto University | en |
dc.address | Institute of Advanced Energy, Kyoto University | en |
dc.address | Department of Basic Medical Sciences, Institute of Medical Science, University of Tokyo | en |
dc.address | Research Institute for Clinical Oncology, Saitama Cancer Center | en |
dc.address | Department of Life and Environmental Sciences, Faculty of Engineering, Chiba Institute of Technology | en |
dc.identifier.pmid | 29435416 | - |
dcterms.accessRights | open access | - |
出現コレクション: | 学術雑誌掲載論文等 |
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