Kasumi Ohira
Current Organizations / Institutes
The organizations/institutes from the scholar's latest article
Research Subjects
Research Interests
Kasumi Ohira has a total of 11 co-authors. Here are the top co-authors by number of shared publications:
- Akihiro Ito
Tokyo University of Pharmacy and Life Sciences
1 shared publication - Hideaki Niwa
Laboratory for Epigenetics Drug Discovery, RIKEN Center for Biosystems Dynamics Research, 1-7-22 Suehiro-cho, Tsurumi, Yokohama 230-0045, Japan
1 shared publication - Hiroyuki Kagechika
Laboratory for Biomaterials and Bioengineering, Institute of Integrated Research, Institute of Science Tokyo
1 shared publication - Michitake Hirano
Institute of Biomaterials and Bioengineering, Tokyo Medical and Dental University (TMDU), 2-3-10 Kanda-Surugadai, Chiyoda-ku, Tokyo, 101-0062, Japan
1 shared publication - Minoru Yoshida
Graduate School of Agricultural and Life Sciences, The University of Tokyo
1 shared publication - Shin Sato
Epigenetics Drug Discovery Unit, RIKEN Center for Life Science Technologies (CLST), 1-7-22 Suehiro-cho, Tsurumi-ku, Yokohama, 230-0045, Japan
1 shared publication
Latest Publications
- 6 July 2018
- Published by Wiley in ChemMedChem
- Vol. 13 (15) , 1530-1540
Development of Novel Inhibitors for Histone Methyltransferase SET7/9 based on Cyproheptadine
The histone methyltransferase SET7/9 methylates not only histone but also non‐histone proteins as substrates, and therefore, SET7/9 inhibitors are considered candidates for the treatment of diseases. Previously, our group identified cyproheptadine, used clinically as a serotonin receptor antagonist and histamine receptor (H1) antagonist, as a novel scaffold of the SET7/9 inhibitor. In this work, we focused on dibenzosuberene as a substructure of cyproheptadine and synthesized derivatives with various functional groups. Among them, the compound bearing a 2‐hydroxy group showed the most potent activity. On the other hand, a 3‐hydroxy group or another hydrophilic functional group such as acetamide decreased the activity. Structural analysis clarified a rationale for the improved potency only by tightly restricted location and type of the hydrophilic group. In addition, a SET7/9 loop, which was only partially visible in the complex with cyproheptadine, became more clearly visible in the complex with 2‐hydroxycyproheptadine. These results are expected to be helpful for further structure‐based development of SET7/9 inhibitors.
- 6 July 2018
- Published by Wiley in ChemMedChem
- Vol. 13 (15) , 1530-1540
Development of Novel Inhibitors for Histone Methyltransferase SET7/9 based on Cyproheptadine
The histone methyltransferase SET7/9 methylates not only histone but also non‐histone proteins as substrates, and therefore, SET7/9 inhibitors are considered candidates for the treatment of diseases. Previously, our group identified cyproheptadine, used clinically as a serotonin receptor antagonist and histamine receptor (H1) antagonist, as a novel scaffold of the SET7/9 inhibitor. In this work, we focused on dibenzosuberene as a substructure of cyproheptadine and synthesized derivatives with various functional groups. Among them, the compound bearing a 2‐hydroxy group showed the most potent activity. On the other hand, a 3‐hydroxy group or another hydrophilic functional group such as acetamide decreased the activity. Structural analysis clarified a rationale for the improved potency only by tightly restricted location and type of the hydrophilic group. In addition, a SET7/9 loop, which was only partially visible in the complex with cyproheptadine, became more clearly visible in the complex with 2‐hydroxycyproheptadine. These results are expected to be helpful for further structure‐based development of SET7/9 inhibitors.