{"id":91,"date":"2021-07-15T15:20:00","date_gmt":"2021-07-15T06:20:00","guid":{"rendered":"https:\/\/www.ls.toyaku.ac.jp\/~cellsig\/wp\/?page_id=91"},"modified":"2026-04-08T14:10:04","modified_gmt":"2026-04-08T05:10:04","slug":"review","status":"publish","type":"page","link":"https:\/\/www.ls.toyaku.ac.jp\/~cellsig\/wp\/?page_id=91","title":{"rendered":"\u696d\u7e3e"},"content":{"rendered":"\n
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Badran MM, Beyri B, Tateishi H, Shimagaki K, Nakata A, Ito A, Nishimura N, Abbas SH, Abdel-Aziz M, Otsuka M, Yoshida M, Fujita M, Br\u00e4se S, Radwan MO. Harnessing Substituted 4-Chlorothieno[2,3- b]pyridine as a New Cap for Potent and Selective Antiproliferative HDAC Inhibitors.\u00a0Pharmaceuticals<\/strong>\u00a019, 442, 2026<\/p>\n\n\n\n

Kawamoto Y, Takase S, Ashutosh K, Maruo H, Maemoto Y, Zhang KYJ, Ito H, Ito A. Discovery of novel 4-aminobenzamide derivatives as small molecule CBX2 inhibitors.\u00a0Bioorg Med. Chem. Lett.<\/strong>\u00a0133, 130526, 2026<\/p>\n\n\n\n

Mukherjee A, Yamashita Y, Maeda R, Akiyama T, Endo K, Takada Y, Tsumoto H, Moriyama Y, Ito A, Shirai F, Tachibana M, Itoh Y, Suzuki T. A Novel PROTAC G9a\/GLP Degrader that Inhibits, Similar to G9a siRNA, the Migration of MCF-7 Breast-Cancer Cells without Affecting Proliferation.\u00a0J. Med. Chem.<\/strong>\u00a068, 18258-18271, 2025<\/p>\n\n\n\n

Takase S, Kumar A, Yokoyama S, Maemoto Y, Aoki K, Arata M, Maruo H, Dohi S, Yun YS, Inoue H, Hamamoto M, Yoshida M, Zhang KYJ, Ito A. Identification of substituted acetanilide compounds as small molecule CBX2 inhibitors via in silico screening. Biochem. Biophys. Res. Commun.<\/strong> 767, 151882, 2025.<\/p>\n\n\n\n

Nishigaya Y, Takase S, Sumiya T, Kikuzato K, Hiroyama T, Maemoto Y, Aoki K, Sato T, Niwa H, Sato S, Ihara K, Nakata A, Matsuoka S, Hashimoto N, Namie R, Honma T, Umehara T, Shirouzu M, Koyama H, Nakamura Y, Yoshida M, Ito A, Shirai F. Discovery of potent substrate-type lysine methyltransferase G9a inhibitors for the treatment of sickle cell disease. Eur. J. Med. Chem.<\/strong> 293, 117721, 2025.<\/p>\n\n\n\n

Mukherjee A, Yamashita Y, Maeda R, Akiyama T, Endo K, Takada Y, Tsumoto H, Moriyama Y, Ito A, Shirai F, Tachibana M, Itoh Y, Suzuki T. A Novel PROTAC G9a\/GLP Degrader that Inhibits, Similar to G9a siRNA, the Migration of MCF-7 Breast-Cancer Cells without Affecting Proliferation. J. Med. Chem.<\/strong> 68, 18258-18271, 2025.<\/p>\n\n\n\n

Dileep KV, Sakai N, Ihara K, Nakata A, Ito A, Sivaraman DM, Yip CW, Shin JW, Yoshida M, Shirouzu M, Zhang KYJ. Identification of benzimidazole-6-carboxamide based inhibitors of secretory glutaminyl cyclase for the treatment of Alzheimer's disease. Int. J. Biol. Macromol.<\/strong> 293, 139320, 2025.<\/p>\n\n\n\n

Tsuchida T, Kubota S, Kamiuezono S, Takasugi N, Ito A, Kumagai Y, Uehara T. Epigenetic regulation of CXC chemokine expression by environmental electrophiles through DNA methyltransferase inhibition. Int. J. Mol. Sci.<\/strong> 25, 11592, 2024.<\/p>\n\n\n\n

Nishigaya Y, Takase S, Sumiya T, Sato T, Niwa H, Sato S, Nakata A, Matsuoka S, Maemoto Y, Hashimoto N, Namie R, Honma T, Umehara T, Shirouzu M, Koyama H, Yoshida M, Ito A, Shirai F. Structure-based development of novel substrate-type G9a inhibitors as epigenetic modulators for sickle cell disease treatment. Bioorg. Med. Chem. Lett.<\/strong> 110, 129856, 2024.<\/p>\n\n\n\n

Matoba S, Shikata D, Shirai F, Tatebe T, Hirose M, Nakata A, Watanabe N, Hasegawa A, Ito A, Yoshida M, Ogura A. Reduction of H3K9 methylation by G9a inhibitors improves the development of mouse SCNT embryos. Stem Cell Reports<\/strong> 19, 906-921, 2024.<\/p>\n\n\n\n

Badran MF, Abbas SH, Tateishi H, Maemoto Y, Toma T, Ito A, Fujita M, Otsuka M, Abdel-Aziz M, Radwan MO. Ligand-based design and synthesis of new trityl Histamine and trityl cysteamine derivatives as SIRT2 Inhibitors for cancer therapy. Eur. J. Med. Chem.<\/strong> 269, 116302, 2024.<\/p>\n\n\n\n

Kikuchi M, Takase S, Konuma T, Noritsugu K, Sekine S, Ikegami T, Ito A, Umehara T. GAS41 promotes H2A.Z deposition through recognition of the N terminus of histone H3 by the YEATS domain. Proc. Natl. Acad. Sci. U S A.<\/strong> 120, e2304103120, 2023.<\/p>\n\n\n\n

Noritsugu K, Suzuki T, Dodo K, Ohgane K, Ichikawa Y, Koike K, Morita S, Umehara T, Ogawa K, Sodeoka M, Dohmae N, Yoshida M, Ito A. Lysine long-chain fatty acylation regulates the TEAD transcription factor. Cell Rep.<\/strong> 42, 112388, 2023.<\/p>\n\n\n\n

Nishigaya Y, Takase S, Sumiya T, Kikuzato K, Sato T, Niwa H, Sato S, Nakata A, Sonoda T, Hashimoto N, Namie R, Honma T, Umehara T, Shirouzu M, Koyama H, Minoru Yoshida M, Ito A, Shirai F. Discovery of Novel Substrate-competitive Lysine Methyltransferase G9a Inhibitors as Anti-cancer Agents. J. Med. Chem.<\/strong> 14, 23, 2023.<\/p>\n\n\n\n

Sekine S, Takase S, Hayase R, Noritsugu K, Maemoto Y, Ichikawa Y, Ogawa K, Kondoh Y, Osada H, Yoshida M, Ito A. Identification of a derivative of the alkaloid emetine as an inhibitor of the YAP-TEAD interaction and its potential as an anticancer agent. Biosci. Biotechnol. Biochem.<\/strong> 87, 501-510, 2023.<\/p>\n\n\n\n

#<\/sup>Okuda K, #<\/sup>Nakahara K, #<\/sup>Ito A, Kumar A, Nomura R, Iijima Y, Takasugi N, Adachi K, Shimada Y, Fujio S, Onuma K, Osaki M, Okada F, Ukegawa T, Takeuchi Y, Yasui N, Yamashita A, Marusawa H, Katagiri T, Shibata T, Uchida K, Nakamura T, Zhang KYZ, Lipton SA, Uehara T. Pivotal role for S-nitrosylation of DNA methyltransferase in epigenetic regulation. Nat. Commun.<\/strong> 14, 621, 2023.<\/p>\n\n\n\n

Takase S, Hiroyama T, Shirai F, Maemoto Y, Nakata A, Arata M, Matsuoka S, Sonoda T, Niwa H, Sato S, Umehara T, Shirouzu M, Nishigaya Y, Sumiya T, Hashimoto N, Namie R, Usui M, Ohishi T, Ohba S, Kawada M, Hayashi Y, Harada H, Yamaguchi T, Shinkai Y, Nakamura Y, *Yoshida M, *Ito A. A specific G9a inhibitor unveils BGLT3 lncRNA as a universal mediator of chemically induced fetal globin gene expression. Nat. Commun.<\/strong> 14, 23, 2023.<\/p>\n\n\n\n

Fujikawa Y, Terakado K, Nezu S, Noritsugu K, Maemoto Y, Ito A, Inoue H. Improving reactivity of naphthalimide-based GST probe by imparting TPP cation: Development and application for live cell imaging. Bioorg. Med. Chem. Lett.<\/strong> 80, 129109, 2023.<\/p>\n\n\n\n

Takase S, Yun YS, Moriya F, Sekine S, Yotsumoto S, Miyake K, Yahagi T, Ito A, Inoue H. 17\u03b2-neriifolin from unripe fruits of Cerbera manghas suppressed cell proliferation via the inhibition of HOXA9-dependent transcription and the induction of apoptosis in the human AML cell line THP-1. J. Nat. Med.<\/strong> 77, 180-187, 2023.<\/p>\n\n\n

Hashimoto K, Ide S, Arata M, Nakata A, Ito A, Ito TK, Kudo N, Lin B, Nunomura K, Tsuganezawa K, Yoshida M, Nagaoka Y, Sumiyoshi T.
Discovery of Benzylpiperazine Derivatives as CNS-Penetrant and Selective Histone Deacetylase 6 Inhibitors.
ACS Med. Chem. Lett.<\/strong> 13, 1077-1082, 2022<\/p>\n

Sasaki K, Suzuki M, Sonoda T, Schneider-Poetsch T, Ito A, Takagi M, Fujishiro S, Sohtome Y, Dodo K, Shin-ya K, Nakao Y, Sodeoka M, Yoshida M.
A novel FRET probe visualizes the dynamic interaction between nucleosomal histone H3K9 tri-methylation and the HP1\u03b1 chromodomain in living cells.
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Yun YS, Nakano T, Fukaya H, Hitotsuyanagi Y, Nakamura M, Umetsu M, Matsushita N, Miyake K, Fuchino H, Kawahara N, Moriya F, Ito A, Takahashi Y, Inoue H. Retusone A, a Guaiane-Type Sesquiterpene Dimer from Wikstroemia retusa and its Inhibitory Effects on Histone Acetyltransferase HBO1 Expression. Molecules<\/strong> 27, 2909, 2022<\/p>\n

Aoyagi Y, Hayashi Y, Harada Y, Choi K, Matsunuma N, Sadato D, Maemoto Y, Ito A, Yanagi S, Starczynowski DT, Harada H. Mitochondrial Fragmentation Triggers Ineffective Hematopoiesis in Myelodysplastic Syndromes. Cancer Discov.<\/strong> 2021. 12, 250-269, 2022<\/p>\n

Kamimura S, Inoue K, Mizutani E, Kim JM, Inoue H, Ogonuki N, Miyamoto K, Ihashi S, Itami N, Wakayama T, Ito A, Nishino N, Yoshida M, Ogura A. Improved development of mouse SCNT embryos by chlamydocin analogues, class I and IIa histone deacetylase inhibitors. Biol Reprod.<\/strong> 105, 543-553, 2021<\/p>\n

Ikeda M, Watanabe T, Ito A, Fujimuro M. Herpes simplex virus 1 infection induces ubiquitination of UBE1a. Biochem. J.<\/strong> 478, 261-279, 2021<\/p>\n

Dileep KV, Sakai N, Ihara K, Kato-Murayama M, Nakata A, Ito A, Sivaraman DM, Shin JW, Yoshida M, Shirouzu M, Zhang KYJ. Piperidine-4-carboxamide as a new scaffold for designing secretory glutaminyl cyclase inhibitors. Int. J. Biol. Macromol.<\/strong> 170, 415-423, 2021<\/p>\n

Ikeda M, Ito A, Sekine Y, Fujimuro M. UBE1a Suppresses Herpes Simplex Virus-1 Replication. Viruses<\/strong> 12, 1391, 2020<\/p>\n

Shiroma Y, Fujita G, Yamamoto T, Takahashi RU, Kumar A, Zhang KYJ, Ito A, Osada H, Yoshida M, Tahara H. Identification of a Selective RelA Inhibitor Based on DSE-FRET Screening Methods. Int. J. Mol. Sci.<\/strong> 21, 9150, 2020<\/p>\n

Maemoto Y, Maruyama T, Nemoto K, Baba T, Motohashi M, Ito A, Tagaya M, Tani K. DDHD1, but Not DDHD2, Suppresses neurite outgrowth in SH-SY5Y and PC12 cells by regulating protein transport from recycling endosomes. Front. Cell Dev. Biol.<\/strong> 8, 670, 2020.<\/p>\n

Radwan MO, Ciftci HI, Ali TFS, Koga R, Tateishi H, Nakata A, Ito A, Yoshida M, Fujita M, Otsuka M. Structure activity study of S-trityl-cysteamine dimethylaminopyridine derivatives as SIRT2 inhibitors: Improvement of SIRT2 binding and inhibition. Bioorg. Med. Chem. Lett.<\/strong> 30, 127458, 2020<\/p>\n

Matsumoto N, Miyamoto Y, Hattori K, Ito A, Harada H, Oizumi H, Ohbuchi K, Mizoguchi K, Yamauchi J. PP1C and PP2A are p70S6K Phosphatases Whose Inhibition Ameliorates HLD12-Associated Inhibition of Oligodendroglial Cell Morphological Differentiation. Biomedicines<\/strong> 8, 89, 2020<\/p>\n

Fujikawa K, Nakahara K, Takasugi N, Nishiya T, Ito A, Uchida K, Uehara T. S-Nitrosylation at the active site decreases the ubiquitin-conjugating activity of ubiquitin-conjugating enzyme E2 D1 (UBE2D1), an ERAD-associated protein. Biochem. Biophys. Res. Commun.<\/strong> 524, 910-915, 2020.<\/p>\n

Nagata A, I Fumiko, Sasho A, Sugita K, Suzuki R, Hinata H, Shimoda Y, Suzuki E, Maemoto Y, Inagawa T, Fujikawa Y, Ikeda E, Fujii C, Inoue H. The evolutionarily conserved deubiquitinase UBH1\/UCH-L1 augments DAF7\/TGF-\u03b2 signaling, inhibits dauer larva formation, and enhances lung tumorigenesis. J Biol Chem.<\/strong> 295, 9105-9120 2020<\/p>\n

Nakahara, K., Fujikawa, K., Hiraoka H., Miyazaki, I., Asanuma, M., Ito, A., Takasugi, N., Uehara, T. Attenuation of macrophage migration inhibitory factor-stimulated signaling via S-nitrosylation. Biol. Pharm. Bull.<\/strong> 42, 1044\u20131047, 2019<\/p>\n

Radwan MO, Ciftci HI, Ali TFS, Ellakwa DE, Koga, R., Tateishi, H., Nakata, A., Ito, A., Yoshida, M., Okamoto, Y., Fujita, M., Otsuka, M. Antiproliferative S-Trityl-l-Cysteine -Derived Compounds as SIRT2 Inhibitors: Repurposing and Solubility Enhancement. Molecules<\/strong> 24, pii: E3295, 2019<\/p>\n

Nomura, Y., Thuaud F., Sekine, D., Ito, A., Maeda, S., Koshino, H., Hashizume, D., Muranaka, A., Cruchter T., Uchiyama, M., Ichikawa, S., Matsuda, A., Yoshida, M., Hirai, G., Sodeoka, M. Synthesis of All Stereoisomers of Monomeric Spectomycin A1\/A2 and Evaluation of Their Protein SUMOylation-Inhibitory Activity. Chemistry<\/strong> 25, 8387-8392, 2019<\/p>\n

Mitsui, E., Yoshida, S., Shinoda, Y., Matsumori, Y., Tsujii, H., Tsuchida, M., Wada, S., Hasegawa, M, Ito, A., Mino, K., Onuki, T., Yoshida, M., Sasaki, R., Mizukami, T. Identification of ryuvidine as a KDM5A inhibitor. Sci Rep.<\/strong> 9, 9952, 2019<\/p>\n

Ali TFS, Ciftci HI, Radwan MO, Koga, R., Ohsugi, T., Okiyama, Y., Honma, T., Nakata, A., Ito, A., Yoshida, M., Fujita, M., Otsuka, M. New SIRT2 inhibitors: Histidine-based bleomycin spin-off. Bioorg. Med. Chem.<\/strong> 27, 1767-1775, 2019<\/p>\n

Hayashi, Y., Harada, Y., Kagiyama, Y., Nishikawa, S., Ding, Y., Imagawa, J., Shingai, N., Kato, N., Kitaura, J., Hokaiwado, S., Maemoto, Y., Ito, A., Matsui, H., Kitabayashi, I., Iwama, A., Komatsu, N., Kitamura, T., Harada, H. NUP98-HBO1-fusion generates phenotypically and genetically relevant chronic myelomonocytic leukemia pathogenesis. Blood Adv.<\/strong> 3, 1047-1060, 2019<\/p>\n

Hiranaka S, Tega Y, Higuchi K, Kurosawa T, Deguchi Y, Arata M, Ito A, Yoshida M, Nagaoka Y, Sumiyoshi T. Design, Synthesis, and Blood\u2212Brain Barrier Transport Study of Pyrilamine Derivatives as Histone Deacetylase Inhibitors. ACS Med. Chem. Lett.<\/strong> 54, 9202-9205, 2018<\/p>\n

Sohtome Y, Shimazu T, Barjau J, Fujishiro S, Akakabe M, Terayama N, Dodo K, Ito A, Yoshida M, Shinkai Y, Sodeoka M. Unveiling epidithiodiketopiperazine as a non-histone arginine methyltransferase inhibitor by chemical protein methylome analyses. Chem. Commun.<\/strong> 54, 9202-9205, 2018<\/p>\n

Maruyama T, Baba T, Maemoto Y, Hara-Miyauchi C, Hasegawa-Ogawa M, Okano HJ, Enda Y, Matsumoto K, Arimitsu N, Nakao K, Hamamoto H6, Sekimizu K, Ohto-Nakanishi T, Nakanishi H, Tokuyama T, Yanagi S, Tagaya M, Tani K. Loss of DDHD2, whose mutation causes spastic paraplegia, promotes reactive oxygen speciesgeneration and apoptosis. Cell Death Dis.<\/strong> 9(8):797. 2018<\/p>\n

Hirano T, Fujiwara T, Niwa H, Hirano M, Ohira K, Okazaki Y, Sato S, Umehara T, Maemoto Y, Ito A, Yoshida M, Kagechika H. Development of Novel Inhibitors for Histone Methyltransferase SET7\/9 based on Cyproheptadine. ChemMedChem.<\/strong> 13(15):1530-1540. 2018<\/p>\n

Nakamura F, Kudo K, Tomachi Y, Nakata A, Takemoto M, Ito A, Tabei H, Arai D, de Voogd N, Yoshida M, Nakao Y, Fusetani N, Halistanol Sulfates I and J, New SIRT1-3 Inhibitory Steroid Sulfates from a Marine Sponge of the Genus Halichondria. J. Antibiot. J Antibiot (Tokyo)<\/strong>, 71(4):483 2018<\/p>\n

Kuroki S, Baba S, Okashita N, Yano M, Yamaguchi M, Kitano S, Miyachi H, Ito A, Yoshida M, Tachibana M. Rescuing the aberrant sex development of H3K9 demethylase Jmjd1a-deficient mice by modulating H3K9 methylation balance. PLoS Genet.<\/strong> 13(9):e1007034, 2017<\/p>\n

#Kudo N, #Ito A, Arata M, Nakata A, Yoshida M. Identification of a novel small molecule that inhibits deacetylase but not defattyacylase reaction catalyzed by SIRT2. Philos. Trans. B. Philos Trans R Soc Lond B Biol Sci.<\/strong> 373(1748), 2018<\/p>\n

Ueda M, Matsui A, Tanaka M, Nakamura T, Abe T, Sako K, Sasaki T, Kim JM, Ito A, Nishino N, Shimada H, Yoshida M, Seki M. The Distinct Roles of Class I and II RPD3-Like Histone Deacetylases in Salinity Stress Response. Plant Physiol.<\/strong> 175(4):1760-1773, 2017<\/p>\n

Okochi-Takada E, Hattori N, Ito A, Niwa T, Wakabayashi M, Kimura K, Yoshida M, Ushijima T. Establishment of a high-throughput detection system for DNA demethylating agents. Epigenetics.<\/strong> 13(2):147-155, 2018<\/p>\n

Noritsugu K, *Ito A, Nakao Y, Yoshida M. Identification of zinc finger transcription factor EGR2 as a novel acetylated protein. Biochem. Biophys. Res. Commun.<\/strong> 489, 455-459, 2017<\/p>\n

Kurita K, Sakamoto T, Yagi N, Sakamoto Y, Ito A, Nishino N, Sako K, Yoshida M, Kimura H, Seki M, Matsunaga S. Live imaging of H3K9 acetylation in plant cells. Sci. Rep.<\/strong> 7, 45894, 2017<\/p>\n

Sunami Y, Araki M, Kan S, Ito A, Hironaka Y, Imai M, Morishita S, Ohsaka A, Komatsu N. Histone acetyltransferase p300\/CREB-binding protein-associated factor (PCAF) is required for all-trans-retinoic acid-induced granulocytic differentiation inleukemia cells. J. Biol. Chem.<\/strong> 292, 2815-2829, 2017<\/p>\n

Narita K, Katoh Y, Ojima K, Dan S, Yamori T, Ito A, Yoshida M, Katoh T. Total Synthesis of the Depsipeptide FR901375 and Preliminary Evaluation of Its Biological Activity. Eur. J. Org. Chem.<\/strong> 121, 5667\u20135677, 2016<\/p>\n

Ueoka R, Hitora Y, Ito A, Yoshida M, Okada S, Takada K, Matsunaga S. Curacin E from the Brittle Star Ophiocoma scolopendrina. J. Nat. Prod.<\/strong> 79, 2754-2757, 2016<\/p>\n

Fukuda I, Hirohama M, *Ito A, Tariq M, Igarashi Y, Saitoh H, Yoshida M. Inhibition of protein SUMOylation by natural quinones. J. Antibiot.<\/strong> 269, 776-779, 2016<\/p>\n

Shah AA, *Ito A, Nakata A, Yoshida M. Identification of a selective SIRT2 inhibitor and its anti-breast cancer activity. Biol. Pharm. Bull.<\/strong> 39, 1739-1742, 2016<\/p>\n

Takada K, Imae Y, Ise Y, Ohtsuka S, Ito A, Okada S, Yoshida M, Matsunaga S. Yakushinamides, Polyoxygenated Fatty Acid Amides That Inhibit HDACs and SIRTs, from the Marine Sponge Theonella swinhoei. J. Nat. Prod.<\/strong> 79, 2384-2390, 2016<\/p>\n

Fujiwara T, Ohira K, Urushibara K, Ito A, Yoshida M, Kanai M, Tanatani A, Kagechika H, Hirano T. Steric structure-activity relationship of cyproheptadine derivatives as inhibitors of histone methyltransferase Set7\/9. Bioorg. Med. Chem.<\/strong> 24, 4318-4323, 2016<\/p>\n

Matsumoto Y, Ito A, Uesugi M, Kittaka A. Efficient N-Acyldopamine Synthesis. Chem. Pharm. Bull.<\/strong> 64, 935-940, 2016<\/p>\n

Narita K, Matsuhara K, Itoh J, Akiyama Y, Dan S, Yamori T, Ito A, Yoshida M, Katoh T. Synthesis and biological evaluation of novel FK228 analogues as potential isoform selective HDAC inhibitors. Eur. J. Med. Chem.<\/strong> 121, 592-609, 2016<\/p>\n

Takemoto Y, *Ito A, Niwa H, Okamura M, Fujiwara T, Hirano T, Handa N, Umehara T, Sonoda T, Ogawa K, Tariq M, Nishino N, Dan S, Kagechika H, Yamori T, Yokoyama S, Yoshida M. Identification of Cyproheptadine as an Inhibitor of SET Domain Containing Lysine Methyltransferase 7\/9 (Set7\/9) That Regulates Estrogen-Dependent Transcription. J. Med. Chem.<\/strong> 59, 3650-3660, 2016<\/p>\n

Nakata S, Watanabe T, Nakagawa K, Takeda H, Ito A, Fujimuro M. The dynamics of histone H2A ubiquitination in HeLa cells exposed to rapamycin, ethanol, hydroxyurea, ER stress, heat shock and DNA damage. Biochem. Biophys. Res. Commun.<\/strong> 472, 46-52, 2016<\/p>\n

Kumar A, Ito A, Hirohama M, Yoshida M, Zhang KY. Identification of new SUMO activating enzyme 1 inhibitors using virtual screening and scaffold hopping. Bioorg. Med. Chem. Lett.<\/strong> 26, 1218-1223, 2016<\/p>\n

Tariq M, *Ito A, Ishfaq M, Bradshaw E, Yoshida M. Eukaryotic translation initiation factor 5A (eIF5A) is essential for HIF-1\u03b1 activation in hypoxia. Biochem. Biophys. Res. Commun.<\/strong> 470, 417-424, 2016<\/p>\n

Nakaoka S, Sasaki K, Ito A, Nakao Y, Yoshida M. A Genetically Encoded FRET Probe to Detect Intranucleosomal Histone H3K9 or H3K14 Acetylation Using BRD4, a BET Family Member. ACS Chem. Biol.<\/strong> 11, 729-733, 2016<\/p>\n

Ito A, Shimazu T, Maeda S, Shah AA, Tsunoda T, Iemura S, Natsume T, Suzuki T, Motohashi H, Yamamoto M, Yoshida M. The subcellular localization and activity of cortactin is regulated by acetylation and interaction with Keap1. Sci. Signal.<\/strong> 8, ra120, 2015<\/p>\n

Okuda K, Ito A, Uehara T. Regulation of Histone Deacetylase 6 Activity via S-Nitrosylation. Biol. Pharm. Bull.<\/strong> 38, 1434-1437, 2015<\/p>\n

Feldman JL, Dittenhafer-Reed KE, Kudo N, Thelen JN, Ito A, Yoshida M, Denu JM. Kinetic and Structural Basis for Acyl-Group Selectivity and NAD(+) Dependence in Sirtuin-Catalyzed Deacylation. Biochemistry.<\/strong> 54, 3037-3050, 2015<\/p>\n

Islam MS, Islam MN, Hoque MA, Nishino N, Kato T, Kim HJ, Ito A, Yoshida M. An efficient synthesis of SK-658 and its analogs as potent histone deacetylase inhibitors. Bioorg. Chem.<\/strong> 59, 145-150, 2015<\/p>\n

Bai D, Nakao R, Ito A, Uematsu H, Senpuku H. Immunoreactive antigens recognized in serum samples from mice intranasally immunized with Porphyromonas gingivalis outer membrane vesicles. Pathog. Dis.<\/strong> 73, pii: ftu006., 2015<\/p>\n

Le Bescont A, Vitte AL, Debernardi A, Curtet S, Buchou T, Vayr J, de Reyni\u00e8s A, Ito A, Guardiola P, Brambilla C, Yoshida M, Brambilla E, Rousseaux S, Khochbin S. Receptor-Independent Ectopic Activity of Prolactin Predicts Aggressive Lung Tumors and Indicates HDACi-Based Therapeutic Strategies. Antioxid. Redox Signal.<\/strong> 23, 1-14, 2015<\/p>\n

Maemoto Y, Ono Y, Kiso S, Shibata H, Takahara T, Sorimachi H, Maki M. Involvement of calpain-7 in epidermal growth factor receptor degradation via the endosomal sorting pathway. FEBS Journal.<\/strong> 281, 3642-3655, 2014<\/p>\n

#Voet A, #Ito A, Hirohama M, Matsuoka S, Tochio N, Kigawa T, Yoshida M, Zhang KY. Discovery of Small Molecule Inhibitors Targeting the SUMO\u2013SIM Interaction Using a Protein Interface Consensus Approach. MedChemComm.<\/strong> 5, 783-786, 2014 #These authors contributed equally<\/p>\n

Islam MN, Islam MS, Hoque MA, Kato T, Nishino N, Ito A, Yoshida M. Bicyclic tetrapeptide histone deacetylase inhibitors with methoxymethyl ketone and boronic acid zinc-binding groups. Bioorg. Chem.<\/strong> 57, 121-126, 2014<\/p>\n

#Kumar A, #Ito A, Hirohama M, Yoshida M, Zhang KY. Identification of sumoylation inhibitors targeting a predicted pocket in ubc9. J. Chem. Inf. Model.<\/strong> 54, 784-793, 2014 #These authors contributed equally<\/p>\n

Hoque MA, Islam MS, Islam MN, Kato T, Nishino N, Ito A, Yoshida M. Design and synthesis of mono and bicyclic tetrapeptides thioester as potent inhibitor of histone deacetylases. Amino Acids.<\/strong> 46, 2435-2444, 2014<\/p>\n

Islam MN, Islam MS, Hoque MA, Kato T, Nishino N, Ito A, Yoshida M. Bicyclic tetrapeptides as potent HDAC inhibitors: Effect of aliphatic loop position and hydrophobicity on inhibitory activity. Bioorg. Med. Chem.<\/strong> 22, 3862-3870, 2014<\/p>\n

Fukui Y, Narita K, Dan S, Yamori T, Ito A, Yoshida M, Katoh T. Total synthesis of burkholdacs A and B and 5,6,20-tri-epi-burkholdac A: HDAC inhibition and antiproliferative activity. Eur. J. Med. Chem.<\/strong> 76, 301-313, 2014<\/p>\n

Khan K, Schneider-Poetsch T, Ishfaq M, Ito A, Yoshimoto R, Mukaida N, Yoshida M. Splicing inhibition induces gene expression through canonical NF-\u03baB pathway and extracellular signal-related kinase activation. FEBS Lett.<\/strong> 588, 1053-1057, 2014<\/p>\n

#Kumar A, #Ito A, Takemoto M, Yoshida M, Zhang KY. Identification of 1,2,5-oxadiazoles as a new class of SENP2 inhibitors using structure based virtual screening. J. Chem. Inf. Model.<\/strong> 54, 870-880, 2014 #These authors contributed equally<\/p>\n

Chi H, Takemoto Y, Nsiama TK, Kato T, Nishino N, Ito A, Yoshida M. Design and synthesis of peptide-MCA substrates for a novel assay of histone methyltransferases and their inhibitors. Bioorg. Med. Chem.<\/strong> 22, 268-275, 2014<\/p>\n

Takemoto M, Kawamura Y, Hirohama M, Yamaguchi Y, Handa H, Saitoh H, Nakao Y, Kawada M, Khalid K, Koshino H, Kimura K, *Ito A, Yoshida M. Inhibition of protein SUMOylation by davidiin, an ellagitannin from Davidia involucrata. J. Antibiot.<\/strong> 67, 335-338, 2014<\/p>\n

Hirohama M, Voet AR, Ozawa T, Saitoh H, Nakao Y, Zhang KY, *Ito A, Yoshida M. Assay methods for small ubiquitin-like modifier (SUMO)-SUMO-interacting motif (SIM) interactions in vivo and in vitro using a split-luciferase complementation system. Anal. Biochem.<\/strong> 448, 92-94, 2014<\/p>\n

Maemoto Y, Kiso S, Shibata H, Maki M. Analysis of limited proteolytic activity of calpain-7 using non-physiological substrates in mammalian cells. FEBS Journal.<\/strong> 280, 2594-2607, 2013<\/p>\n

Maemoto Y, Shibata H, Maki M. Determination of Phosphorylation Site in CHMP1A. Bioscience, Biotechnology, and Biochemistry<\/strong>, 77, 1317-1319, 2013<\/p>\n

Hirohama M, Kumar A, Fukuda I, Matsuoka S, Igarashi Y, Saitoh H, Takagi M, Shin-ya K, Honda K, Kondoh Y, Saito T, Nakao Y, Osada H, Zhang KY, Yoshida M, *Ito A. Spectomycin B1 as a novel SUMOylation inhibitor that directly binds to SUMO E2. ACS Chem. Biol.<\/strong> 8, 2635-2642, 2013<\/p>\n

Hao R, Nanduri P, Rao Y, Panichelli RS, Ito A, Yoshida M, Yao TP. Proteasomes activate aggresome disassembly and clearance by producing unanchored ubiquitin chains. Mol. Cell<\/strong> 51, 819-828, 2013<\/p>\n

Kumar A, Ito A, Hirohama M, Yoshida M, Zhang KY. Identification of quinazolinyloxy biaryl urea as a new class of SUMO activating enzyme 1 inhibitors. Bioorg. Med. Chem. Lett.<\/strong> 23, 5145-5149, 2013<\/p>\n

Arai T, Ashraful Hoque M, Nishino N, Kim HJ, Ito A, Yoshida M. Cyclic tetrapeptides with -SS- bridging between amino acid side chains for potent histone deacetylases\u2019 inhibition. Amino Acids.<\/strong> 45, 835-843, 2013<\/p>\n

Matsubara K, Lee AR, Kishigami S, Ito A, Matsumoto K, Chi H, Nishino N, Yoshida M, Hosoi Y. Dynamics and regulation of lysine-acetylation during one-cell stage mouse embryos. Biochem. Biophys. Res. Commun.<\/strong> 434, 1-7, 2013<\/p>\n

Kumar A, Ito A, Hirohama M, Yoshida M, Zhang KY. Identification of sumoylation activating enzyme 1 inhibitors by structure-based virtual screening. J. Chem. Inf. Model.<\/strong> 53, 809-820, 2013<\/p>\n

Fujishiro S, Dodo K, Iwasa E, Teng Y, Sohtome Y, Hamashima Y, Ito A, Yoshida M, Sodeoka M. Epidithiodiketopiperazine as a pharmacophore for protein lysine methyltransferase G9a inhibitors: Reducing cytotoxicity by structural simplification. Bioorg. Med. Chem. Lett.<\/strong> 23, 733-736, 2013<\/p>\n

Narita K, Fukui Y, Sano Y, Yamori T, Ito A, Yoshida M, Katoh T. Total synthesis of bicyclic depsipeptides spiruchostatins C and D and investigation of their histone deacetylase inhibitory and antiproliferative activities. Eur. J. Med. Chem.<\/strong> 60, 295-304, 2012<\/p>\n

Ishfaq M, Maeta K, Maeda S, Natsume T, *Ito A, Yoshida M. The Role of Acetylation in the Subcellular Localization of an Oncogenic Isoform of Translation Factor eIF5A. Biosci. Biotechnol. Biochem.<\/strong> 76, 2165-2167, 2012<\/p>\n

Hoque MA, Arai T, Nishino N, Kim HJ, Ito A, Yoshida M. Cyclic tetrapeptides with thioacetate tails or intramolecular disulfide bridge as potent inhibitors of histone deacetylases. Bioorg. Med. Chem. Lett.<\/strong> 22, 6770-6772, 2012<\/p>\n

Cho HS, Shimazu T, Toyokawa G, Daigo Y, Maehara Y, Hayami S, Ito A, Masuda K, Ikawa N, Field HI, Tsuchiya E, Ohnuma S, Ponder BA, Yoshida M, Nakamura Y, Hamamoto R. Enhanced HSP70 lysine methylation promotes proliferation of cancer cells through activation of Aurora kinase B. Nat. Commun.<\/strong> 3, 1072, 2012<\/p>\n

Ishfaq M, Maeta K, Maeda S, Natsume T, *Ito A, Yoshida M. Acetylation regulates subcellular localization of eukaryotic translation initiation factor 5A (eIF5A). FEBS Lett.<\/strong> 586, 3236-3241, 2012<\/p>\n

Yoshihara H, Fukushima T, Hakuno F, Saeki Y, Tanaka K, Ito A, Yoshida M, Iemura S, Natsume T, Asano T, Chida K, Girnita L, Takahashi S. Insulin\/insulin-like growth factor (IGF) stimulation abrogates an association between a deubiquitinating enzyme USP7 and insulin receptor substrates (IRSs) followed by proteasomal degradation of IRSs. Biochem. Biophys. Res. Commun.<\/strong> 423, 122-127, 2012<\/p>\n

Kamemura K, Ogawa M, Ohkubo S, Ohtsuka Y, Shitara Y, Komiya T, Maeda S, Ito A, Yoshida M. Depression of mitochondrial metabolism by downregulation of cytoplasmic deacetylase, HDAC6. FEBS Lett.<\/strong> 586, 1379-1383, 2012<\/p>\n

Matsushita K, Kajiwara T, Tamura M, Satoh M, Tanaka N, Tomonaga T, Matsubara H, Shimada H, Yoshimoto R, Ito A, Kubo S, Natsume T, Levens D, Yoshida M, Nomura F. SAP155-mediated splicing of FUSE-binding protein-interacting repressor (FIR) serves as a molecular switch for c-myc gene expression. Mol. Cancer Res.<\/strong> 10, 787-799, 2012<\/p>\n

Kobayashi H, Harada H, Nakamura M, Futamura Y, Ito A, Yoshida M, Iemura SI, Shin-Ya K, Doi T, Takahashi T, Natsume T, Imoto M, Sakakibara Y. Comprehensive predictions of target proteins based on protein-chemical interaction using virtual screening and experimental verifications. BMC Chem. Biol.<\/strong> 12, 2, 2012<\/p>\n

Takahashi M, Takemoto Y, Shimazu T, Kawasaki H, Tachibana M, Shinkai Y, Takagi M, Shin-Ya K, Igarashi Y, *Ito A, Yoshida M. Inhibition of histone H3K9 methyltransferases by gliotoxin and related epipolythiodioxopiperazines. J. Antibiot.<\/strong> 65, 263-265, 2012<\/p>\n

Maemoto Y, Osako Y, Goto E, Nozawa E, Shibata H, Maki M. Calpain-7 binds to CHMP1B at its second \u03b1-helical region and forms a ternary complex with IST1. Journal of Biochemistry<\/strong>, 150, 411-421, 2011<\/p>\n

Fukushima T, Okajima H, Yamanaka D, Ariga M, Nagata S, Ito A, Yoshida M, Asano T, Chida K, Hakuno F, Takahashi S. HSP90 interacting with IRS-2 is involved in cAMP-dependent potentiation of IGF-I signals in FRTL-5 cells. Mol. Cell Endocrinol.<\/strong> 344, 81-89, 2011<\/p>\n

Islam MS, Bhuiyan MP, Islam MN, Nsiama TK, Oishi N, Kato T, Nishino N, Ito A, Yoshida M. Evaluation of functional groups on amino acids in cyclic tetrapeptides in histone deacetylase inhibition. Amino Acids<\/strong> 42, 2103-2120, 2011<\/p>\n

Ito T, Umehara T, Sasaki K, Nakamura Y, Nishino N, Terada T, Shirouzu M, Padmanabhan B, Yokoyama S, *Ito A, *Yoshida M. Real-Time Imaging of Histone H4K12-Specific Acetylation Determines the Modes of Action of Histone Deacetylase and Bromodomain Inhibitors. Chem. Biol.<\/strong> 18, 495-507, 2011<\/p>\n

Furumai R, Ito A, Ogawa K, Maeda S, SaIto A., Nishino N, Horinouchi S, Yoshida M. Histone deacetylase inhibitors block nuclear factor-\u03baB-dependent transcription by interfering with RNA polymerase II recruitment. Cancer Sci.<\/strong> 102, 1081-1087, 2011<\/p>\n

Oiso H, Furukawa N, Suefuji M, Shimoda S, Ito A, Furumai R, Nakagawa J, Yoshida M, Nishino N, Araki E. The role of class I histone deacetylase (HDAC) on gluconeogenesis in liver. Biochem. Biophys. Res. Commun.<\/strong> 404, 166-172, 2011<\/p>\n

Osako Y, Maemoto Y, TanakaR, Suzuki H, Shibata H, Maki M. Autolytic activity of human calpain-7 is enhanced by ESCRT-III-related protein IST1 through MIT-MIM interaction. FEBS Journal<\/strong>, 227, 4412-4426, 2010<\/p>\n

Iwasa E, Hamashima Y, Fujishiro S, Higuchi E, Ito A, Yoshida M, Sodeoka M. Total synthesis of (+)-chaetocin and its analogues: their histone methyltransferase G9a inhibitory activity. J. Am. Chem. Soc.<\/strong> 132, 4078-4079, 2010<\/p>\n

Islam NM, Kato T, Nishino N, Kim HJ, Ito A, Yoshida M. Bicyclic peptides as potent inhibitors of histone deacetylases: optimization of alkyl loop length. Bioorg. Med. Chem. Lett.<\/strong> 20, 997-999, 2010<\/p>\n

Fukuda I, *Ito A, Uramoto M, Saitoh H, Kawasaki H, Osad, H, *Yoshida M. Kerriamycin B inhibits protein SUMOylation. J. Antibiot.<\/strong> 62, 221-224, 2009<\/p>\n

Fukuda I, *Ito A, Hirai G, Nishimura S, Kawasaki H, Saitoh H, Kimura K, Sodeoka M, Yoshida M. Ginkgolic acid inhibits protein SUMOylation by blocking formation of the E1-SUMO intermediate. Chem. Biol.<\/strong> 16, 133-140, 2009<\/p>\n

Ueoka R, Ito A, Izumikawa M, Maeda S, Takagi M, Shin-ya K, Yoshida M, van Soest RW, Matsunaga S. Isolation of azaspiracid-2 from a marine sponge Echinoclathria sp. as a potent cytotoxin. Toxicon<\/strong> 53, 680-684, 2009<\/p>\n

Dohi Y, Ikura T, Hoshikawa Y, Katoh Y, Ota K, Nakanome A, Muto A, Omura S, Ohta T, Ito A, Yoshida M, Noda T, Igarashi K. Bach1 inhibits oxidative stress-induced cellular senescence by impeding p53 function on chromatin. Nat. Struct. Mol. Biol.<\/strong> 15, 1246-1254, 2008<\/p>\n

Kamemura K, *Ito A, Shimazu T, Matsuyama A, Maeda S, Yao TP, Horinouchi S, Khochbin S, Yoshida M. Effects of downregulated HDAC6 expression on the proliferation of lung cancer cells. Biochem. Biophys. Res. Commun.<\/strong> 374, 84-89, 2008<\/p>\n

Kawaguchi Y, Ito A, Appella E, Yao TP. Charge modification at multiple C-terminal lysine residues regulates p53 oligomerization and its nucleus-cytoplasm trafficking. J. Biol. Chem.<\/strong> 281, 1394-1400, 2006<\/p>\n

Saji S, Kawakami M, Hayashi S, Yoshida N, Hirose M, Horiguchi S, Itoh A, Funata N, Schreiber SL, Yoshida M, Toi M. Significance of HDAC6 regulation via estrogen signaling for cell motility and prognosis in estrogen receptor-positive breast cancer. Oncogene<\/strong>, 24, 4531-4539, 2005<\/p>\n

Kawaguchi Y, Kovacs JJ, McLaurin A, Vance JM, Ito A, Yao TP. The Deacetylase HDAC6 Regulates Aggresome Formation and Cell Viability in Response to Misfolded Protein Stress. Cell<\/strong> 115, 727-738, 2003<\/p>\n

Ito A, Kawaguchi Y, Lai CH, Kovacs JJ, Higashimoto Y, Appella E, Yao TP. MDM2-HDAC1-mediated deacetylation of p53 is required for its degradation. EMBO J.<\/strong> 21, 6236-6345, 2002<\/p>\n

Hubbert C, Guardiola A, Shao R, Kawaguchi Y, Ito A, Nixon A, Yoshida, M, Wang XF, Yao TP. HDAC6 is a microtubule-associated deacetylase. Nature<\/strong> 417, 455-458, 2002<\/p>\n

Zhao X, Ito A, Kane CD, Liao TS, Bolger TA, Lemrow SM, Means AR, Yao TP. The Modular Nature of Histone Deacetylase HDAC4 Confers Phosphorylation-dependent Intracellular Trafficking. J. Biol. Chem.<\/strong> 276, 35042-35048, 2001<\/p>\n

Ito A, Lai CH, Zhao X, Saito S, Hamilton MH, Appella E, Yao TP. p300\/CBP-mediated p53 acetylation is commonly induced by p53 activating agents and inhibited by MDM2. EMBO J.<\/strong> 20, 1331-1340, 2001<\/p>\n

Ito A, Uehara T, Nomura Y. Isolation of Ich-1S (caspase-2S)-binding protein that partially inhibits caspase activity. FEBS Lett.<\/strong> 470, 360-364, 2000<\/p>\n

Ito A, Uehara T, Tokumitsu A, Okuma Y, Nomura Y. Possible involvement of cytochrome c release and sequential activation of caspases in ceramide-induced apoptosis in SK-N-MC cells. Biochim. Biophys. Acta.<\/strong> 1452, 263-274, 1999<\/p>\n

Itano Y, Ito A, Uehara T, Nomura Y. Regulation of Bcl-2 protein expression in human neuroblastoma SH-SY5Y cells: positive and negative effects of protein kinases C and A, respectively. J. Neurochem.<\/strong> 67, 131-137, 1996<\/p>\n

Okada F, Ito A, Hirokawa T, Tokumitsu Y Nomura Y. Long-term neuroleptic treatments counteract dopamine D2 agonist inhibition of adenylate cyclase but do not affect pertussis toxin ADP-ribosylation in the rat brain. Neurochem. Int.<\/strong> 28, 161-168, 1996<\/p>\n

Okada F, Takahasi N, Ito A, Tokumitsu Y, Nomura Y. Acceleration of desipramine-induced changes on the dopamine receptor-coupled adenylate cyclase system by pertussis toxin. J. Neural Transm. Gen. Sect.<\/strong> 98, 133-142, 1994<\/p>\n

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Minoru Yoshida and Akihiro Ito, Epigenetic modulators as potential therapeutics for the treatment of genetic diseases, Pacifichem 2025, 2025\/12\/17, Honolulu, Hawaii, USA\uff08\u62db\u5f85\u8b1b\u6f14\uff09<\/span><\/div>\n
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Akihiro Ito and Yoshito Kumagai, Epigenetic regulation by food-derived carboxylic acids: The role of HDAC1\/2 in histone sorbylation, Pacifichem 2025, 2025\/12\/15, Honolulu, Hawaii, USA\uff08\u62db\u5f85\u8b1b\u6f14\uff09<\/span><\/div>\n
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Akihiro Ito, Development of RK-701, a Selective G9a Inhibitor, as a Chemical Tool for \u03b3-Globin Regulation and Its Therapeutic Potential in SCD, 2025\/12\/2, Cheongju, Korea\uff08\u62db\u5f85\u8b1b\u6f14\uff09<\/span><\/div>\n
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Komei Aoki, Kota Noritsugu, Takehiro Suzuki, Yoshito Kumagai, Naoshi Dohmae, Akihiro Ito, Discovery of Novel Histone Acylation Induced by Food-Derived Carboxylic Acids Using a Histone\u2013Reader Protein Interaction Assay. The11th Japan-Korea Chemical Biology Symposium, 2025\/12\/2, Cheongju, Korea<\/span><\/div>\n
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\u00a0<\/div>\n<\/div>\n\n\n

<\/p>\n\n\n\n

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Akihiro Ito, Kota Noritsugu, Takehiro Suzuki, Naoshi Dohmae, Minoru Yoshida. Regulation of the TEAD transcriptional factor by lysine long-chain fatty acylation. FASEB Science Research Conference: Biology of Acetylation in Health and Disease, 2024\/8\/8, Rome, Italy<\/p>

Kota Noritsugu, Takehiro Suzuki, Naoshi Dohmae, Yoshito Kumagai, Akihiro Ito. Novel histone lysine acylation derived from sorbic acid. FASEB Science Research Conference: Biology of Acetylation in Health and Disease, 2024\/8\/6, Rome, Italy<\/p>

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Komei Aoki, Kota Noritsugu, Shohei Takase, Yuki Shimizu, Ai Katsuma, Takehiro Suzuki, Naoshi Dohmae, Akihiro Ito, Exploration of novel histone lysine acyl modifications induced by carboxylic acids from the living environment
The 10th International Congress of Asian Society of Toxicology
2023\/7\/17-20, Taipei, Taiwan<\/p>

\u4f0a\u85e4\u662d\u535a\u3001\u5409\u7530\u7a14\u3001\u6297\u304c\u3093\u5264\u5275\u88fd\u3092\u76ee\u6307\u3057\u305f\u30d2\u30b9\u30c8\u30f3\u30e1\u30c1\u30eb\u5316\u9175\u7d20G9a\u963b\u5bb3\u5264\u306e\u958b\u767a\u3001\u7b2c27\u56de\u65e5\u672c\u304c\u3093\u5206\u5b50\u6a19\u7684\u6cbb\u7642\u5b66\u4f1a\u5b66\u8853\u96c6\u4f1a\u30012023\/6\/21-23\u3001\u4f50\u8cc0\uff08\u62db\u5f85\u8b1b\u6f14\uff09<\/p>

\u4f0a\u85e4\u662d\u535a\u3001\u74b0\u5883\u5316\u5b66\u7269\u8cea\u306b\u3088\u308b\u30d2\u30b9\u30c8\u30f3\u4fee\u98fe\u3092\u4ecb\u3057\u305f\u907a\u4f1d\u5b50\u767a\u73fe\u8abf\u7bc0
\u7b2c50\u56de\u65e5\u672c\u6bd2\u6027\u5b66\u4f1a\u5b66\u8853\u5e74\u4f1a\u30012023\/6\/19-21\u3001\u6a2a\u6d5c\uff08\u62db\u5f85\u8b1b\u6f14\uff09<\/p>

\u9ad9\u702c\u7fd4\u5e73\u3001\u5bdb\u5c71\u9686\u3001\u767d\u4e95\u6587\u5e78\u3001\u5712\u7530\u5065\u3001\u4e2d\u7530\u660e\u5b50\u3001\u4e39\u7fbd\u82f1\u660e\u3001\u6885\u539f\u5d07\u53f2\u3001\u4e2d\u6751\u5e78\u592b\u3001\u5409\u7530\u7a14\u3001\u4f0a\u85e4\u662d\u535a\u3001\u30d2\u30b9\u30c8\u30f3\u30e1\u30c1\u30eb\u5316\u9175\u7d20G9a\u306b\u3088\u308b\u30b0\u30ed\u30d3\u30f3\u30b9\u30a4\u30c3\u30c1\u30f3\u30b0\u8abf\u7bc0\u6a5f\u69cb\u306e\u89e3\u660e\u3001\u7b2c16\u56de\u65e5\u672c\u30a8\u30d4\u30b8\u30a7\u30cd\u30c6\u30a3\u30af\u30b9\u7814\u7a76\u4f1a\u5e74\u4f1a\u30012023\/6\/19-20\u3001\u6771\u4eac<\/p>

\u9752\u6728\u5eb7\u660e\u3001\u5247\u6b21\u6052\u592a\u3001\u9ad8\u702c\u7fd4\u5e73\u3001\u6e05\u6c34\u52c7\u5e0c\u3001\u9234\u6728\u5065\u88d5\u3001\u5802\u524d\u76f4\u3001\u4f0a\u85e4\u662d\u535a\u3001\u5916\u6765\u6027\u30ab\u30eb\u30dc\u30f3\u9178\u7531\u6765\u65b0\u898f\u30d2\u30b9\u30c8\u30f3\u30ea\u30b8\u30f3\u30a2\u30b7\u30eb\u5316\u4fee\u98fe\u306e\u63a2\u7d22\u3001\u65e5\u672c\u30b1\u30df\u30ab\u30eb\u30d0\u30a4\u30aa\u30ed\u30b8\u30fc\u5b66\u4f1a\u7b2c17\u56de\u5e74\u4f1a\u30012023\/5\/29-31\u3001\u5927\u962a<\/p>

\u4f0a\u85e4\u662d\u535a\u3001\u30b1\u30df\u30ab\u30eb\u30d0\u30a4\u30aa\u30ed\u30b8\u30fc\u7684\u30a2\u30d7\u30ed\u30fc\u30c1\u306b\u3088\u308a\u89e3\u304d\u660e\u304b\u3059\u30d2\u30b9\u30c8\u30f3\u30e1\u30c1\u30eb\u5316\u9175\u7d20G9a\u306b\u3088\u308b\u30b0\u30ed\u30d3\u30f3\u30b9\u30a4\u30c3\u30c1\u30f3\u30b0\u6a5f\u69cb\u3001\u8d64\u8840\u7403\u7814\u7a76\u30b7\u30f3\u30dd\u30b8\u30a6\u30e0\u30012023\/5\/26\u3001\u6771\u4eac\uff08\u62db\u5f85\u8b1b\u6f14\uff09<\/p>

\u571f\u80a5\u6c99\u5f25\u9999\u3001\u9ad8\u702c\u7fd4\u5e73\u3001\u5c39\u6c38\u6dd1\u3001\u4e09\u5b85\u514b\u5178\u3001\u77e2\u4f5c\u5fe0\u5f18\u3001\u4f0a\u85e4\u662d\u535a\u3001\u4e95\u4e0a\u82f1\u53f2\u3001\u4e00\u6801\u5e78\u751f\u3001CBX2\u3068\u30d2\u30b9\u30c8\u30f3H3\u306e\u30bf\u30f3\u30d1\u30af\u8cea\u9593\u76f8\u4e92\u4f5c\u7528\u3092\u6a19\u7684\u3068\u3057\u305f\u5929\u7136\u7269\u306e\u63a2\u7d22\u3001\u65e5\u672c\u85ac\u5b66\u4f1a\u7b2c143\u5e74\u4f1a\u30012023\/3\/25-28\u3001\u672d\u5e4c<\/p>

Hakuno F, Isogai M, Yanano R, Nishi H, Fukushima S, Matsumoto E, Kawakami T, Nakura T, Ito A, Kataoka N, Takahashi S. Alternative splicing regulation of insulin receptor (IR) in response to amino acid. Gordon Research Conference, 2023\/3\/12-17, Ventura, USA<\/p>

Kota Noritsugu, Takehiro Suzuki, Yasue Ichikawa, Kenji Ohgane, Naoshi Dohmae, Minoru Yoshida, Akihiro Ito, Lysine long-chain fatty acylation regulates the TEAD transcription factor in Hippo signaling pathway. ChemBioNara2023, 2023\/2\/21-22, Nara, Japan<\/p>

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\u5929\u91ce\u65e5\u83dc\u5b50\u3001\u5e73\u4e2d\u8aa0\u5f25\u3001\u5f0f\u7530\u4eae\u53f2\u3001\u4e2d\u7530\u660e\u5b50\u3001\u65b0\u771f\u7531\u7f8e\u3001\u5de5\u85e4\u7d00\u96c4\u3001\u4f0a\u85e4\u5b5d\u3001\u4f0a\u85e4\u662d\u535a\u3001\u5409\u7530\u7a14\u3001\u5e03\u6751\u4e00\u4eba\u3001\u9577\u5ca1\u5eb7\u592b\u3001\u4f4f\u5409\u5b5d\u660e\u3001\u7b2c39\u56de\u30e1\u30c7\u30a3\u30b7\u30ca\u30eb\u30b1\u30df\u30b9\u30c8\u30ea\u30fc\u30b7\u30f3\u30dd\u30b8\u30a6\u30e0\u30012022\/11\/23-25\u3001\u540d\u53e4\u5c4b<\/p>

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Akihiro Ito, Uncovering functions of novel lysine acyl modifications, RIKEN Chemical Biology Luncheon Seminar, 2021\/11\/30, Online\uff08\u62db\u5f85\u8b1b\u6f14\uff09<\/p>

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\u677e\u672c\u5065\u3001\u9ed2\u5ddd\u7559\u7f8e\u3001Mohammad Tariq\u3001Tilman Schneider-Poetsch\u3001\u51cc\u6953\u3001\u5ba4\u4e95\u8aa0\u3001\u9234\u6728\u5065\u88d5\u3001\u5802\u524d\u76f4\u3001\u4f0a\u85e4\u662d\u535a\u3001\u9577\u7530\u88d5\u4e4b\u3001\u5409\u7530\u7a14\u3001\u30cf\u30a4\u30d7\u30b7\u30f3\u5316\u963b\u5bb3\u5264GC7\u306e\u30df\u30c8\u30b3\u30f3\u30c9\u30ea\u30a2\u3078\u306e\u5f71\u97ff\u3001\u65e5\u672c\u85ac\u5b66\u4f1a\u7b2c140\u5e74\u4f1a\u30012020\/3\u3001\u4eac\u90fd<\/p>

\u9ad8\u702c\u7fd4\u5e73\u3001\u6797\u702c\u7460\u5948\u3001\u5247\u6b21\u6052\u592a\u3001\u5e02\u5ddd\u4fdd\u6075\u3001\u5c0f\u5ddd\u5065\u53f8\u3001\u5409\u7530\u7a14\u3001\u4f0a\u85e4\u662d\u535a\u3001TEAD-YAP\u76f8\u4e92\u4f5c\u7528\u3092\u6a19\u7684\u3068\u3057\u305f\u5316\u5408\u7269\u306e\u63a2\u7d22\u3001\u65e5\u672c\u8fb2\u82b8\u5316\u5b66\u4f1a2020\u5e74\u5ea6\u5927\u4f1a\u30012020\/3\u3001\u798f\u5ca1<\/p>

Taha F.S. Ali, Mohamed O. Radwan, Halil I. Ciftci, Koga, R., Doha E. Ellakwa, Tateishi, H., Nakata, A., Ito, A., Yoshida, M., Otsuka, M., Fujita, M., Novel bleomycin spin-off as potent and selective SIRT2 inhibitors, The 37th Medicinal Chemistry Symposium, 2019\/11, Hachioji<\/p>

\u77f3\u5009\u83dc\u6458\u3001\u524d\u672c\u4f51\u6a39\u3001\u9752\u6728\u5143\u79c0\u3001\u6a58\u9ad8\u6566\u53f2\u3001\u4e0a\u6749\u5fd7\u6210\u3001\u5409\u7530\u7a14\u3001\u4f0a\u85e4\u662d\u535a\u3001\u5185\u56e0\u6027\u8102\u8cea\u4ee3\u8b1d\u7269N-<\/em>\u30a2\u30b7\u30eb\u30c9\u30fc\u30d1\u30df\u30f3\u306b\u3088\u308bHIF-1\u03b1\u6d3b\u6027\u5316\u6a5f\u69cb\u3001\u7b2c24\u56de\u5316\u5b66\u751f\u7269\u5b66\u7814\u7a76\u4f1a\u30012019\/11\u3001\u6771\u4eac<\/p>

\u52a0\u85e4\u7adc\u3001\u5247\u6b21\u6052\u592a\u3001\u9234\u6728\u5065\u88d5\u3001\u5802\u524d\u76f4\u3001\u5409\u7530\u7a14\u3001\u4f0a\u85e4\u662d\u535a\u3001\u30ea\u30b8\u30f3\u9577\u9396\u30a2\u30b7\u30eb\u5316\u30bf\u30f3\u30d1\u30af\u8cea\u306e\u7db2\u7f85\u7684\u63a2\u67fb\u6cd5\u306e\u958b\u767a\u3001\u7b2c24\u56de\u5316\u5b66\u751f\u7269\u5b66\u7814\u7a76\u4f1a\u30012019\/11\u3001\u6771\u4eac<\/p>

\u4f0a\u85e4\u662d\u535a\u3001\u5275\u85ac\u7814\u7a76\u304b\u3089\u898b\u51fa\u3055\u308c\u305f\u30ea\u30b8\u30f3\u9577\u9396\u30a2\u30b7\u30eb\u5316\u4fee\u98fe\u306e\u65b0\u898f\u6a5f\u80fd\u3068\u65b0\u305f\u306a\u5275\u85ac\u7814\u7a76\u3078\u306e\u5c55\u958b\u3001BioJapan2019\u30012019\/10\u3001\u6a2a\u6d5c<\/p>

Sasaki, K., Suzuki, M., Ito, A., Nakao, Y., Yoshida, M., Development of fluorescent probes for visualizing an interaction between intra-nucleosomal histone H3 K9 tri-methylation and HP1\u03b1 chromodomain and live-cell imaging, CSH Asia 2019 Conference Chemical Biology and Drug Discovery, 2019\/10, Suzhou, China<\/p>

\u4f0a\u85e4\u662d\u535a\u3001\u963b\u5bb3\u5264\u958b\u767a\u7814\u7a76\u304b\u3089\u898b\u51fa\u3055\u308c\u305f\u30ea\u30b8\u30f3\u9577\u9396\u30a2\u30b7\u30eb\u5316\u4fee\u98fe\u306b\u3088\u308b\u8ee2\u5199\u8abf\u7bc0\u6a5f\u69cb\u3001Pioneering Project: Chemical Probe\uff08\u751f\u547d\u73fe\u8c61\u63a2\u7d22\u5206\u5b50\uff09\u7b2c\u4e8c\u56de\u5408\u540c\u5408\u5bbf\u30bb\u30df\u30ca\u30fc\u30012019\/10\u3001\u57fc\u7389\uff08\u62db\u5f85\u8b1b\u6f14\uff09<\/p>

Hiranaka, S., Tega, Y., Higuchi, K., Kurosawa, T., Deguchi, Y., Arata, M., Tanaka, A., Hashizume, Y., Kudo, N., Ito, A., Yoshida, M., Nagaoka, Y., Sumiyoshi, T., Drug Discovery of Pyrilamine Derivatives as Blood-Brain Barrier Permeable Histone Deacetylase Inhibitors, 27th International Society of Heterocyclic Chemistry (ISHC) Congress, 2019\/9, Kyoto<\/p>

\u4f0a\u85e4\u662d\u535a\u3001\u4f4e\u5206\u5b50\u5316\u5408\u7269\u306b\u3088\u308b\u89e3\u6790\u304b\u3089\u898b\u3048\u3066\u304d\u305fSIRT2\u306e\u4e8c\u91cd\u7279\u7570\u6027\u9175\u7d20\u6d3b\u6027\u306e\u8abf\u7bc0\u6a5f\u69cb\u3001\u7b2c92\u56de\u65e5\u672c\u751f\u5316\u5b66\u5b66\u4f1a\u5927\u4f1a\u30012019\/9\u3001\u6a2a\u6d5c\uff08\u62db\u5f85\u8b1b\u6f14\uff09<\/p>

\u4f0a\u85e4\u662d\u535a\u3001\u963b\u5bb3\u5264\u958b\u767a\u7814\u7a76\u304b\u3089\u898b\u51fa\u3055\u308c\u305f\u30ea\u30b8\u30f3\u9577\u9396\u30a2\u30b7\u30eb\u5316\u4fee\u98fe\u306e\u65b0\u898f\u6a5f\u80fd\u3001\u6771\u4eac\u5927\u5b66\u30bb\u30df\u30ca\u30fc\u30012019\/8\u3001\u6771\u4eac\uff08\u62db\u5f85\u8b1b\u6f14\uff09<\/p>

Ito, A., Kato, R., Noritsugu, K., Suzuki, T., Dohmae, N., Yoshida, M., Comprehensive screening for lysine long-chain fatty acyl proteins, FASEB Science Research Conference: Reversible Protein Acetylation in Health and Disease, 2019\/8, Lisbon, Portugal<\/p>

Noritsugu, K., Ogawa, K., Suzuki, T., Dohmae, N., Yoshida, M., Ito, A., The role of lysine long-chain fatty acylation of TEAD transcription factors for transcriptional output of Hippo signaling pathway, FASEB Science Research Conference: Reversible Protein Acetylation in Health and Disease, 2019\/8, Lisbon, Portugal<\/p>

\u9ad8\u702c\u7fd4\u5e73\u3001\u5802\u524d\u76f4\u3001\u65b0\u5bb6\u4e00\u7537\u3001\u9577\u7530\u88d5\u4e4b\u3001\u4f0a\u85e4\u662d\u535a\u3001\u5409\u7530\u7a14\u3001E1A\u767a\u73fe\u7d30\u80de\u9078\u629e\u7684\u7d30\u80de\u6b7b\u3092\u8a98\u5c0e\u3059\u308bJBIR-140\u306e\u4f5c\u7528\u6a5f\u69cb\u89e3\u6790\u3001\u7b2c23\u56de\u65e5\u672c\u304c\u3093\u5206\u5b50\u6a19\u7684\u6cbb\u7642\u5b66\u4f1a\u5b66\u8853\u96c6\u4f1a\u30012019\/6\u3001\u5927\u962a<\/p>

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Takase, S., Tomori, M., Hayashi, H., Maemoto, Y., Hiroyama, T., Nakamura, Y., Shirai, F., Yoshida, M., Ito A. Development of G9a inhibitors as therapeutic agents against sickle cell disease. RIKEN Epigenetics in Wako 2019, 2019\/2, Wako<\/p>

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Ito, A., Regulation of a dual specificity deacylase activity of SIRT2. The 9th Japan-Korea Chemical Biology Symposium, The Central Park Hotel, 2018\/5, Incheon, Korea\uff08\u62db\u5f85\u8b1b\u6f14\uff09<\/p>

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\u5247\u6b21\u6052\u592a\u3001\u4f0a\u85e4\u662d\u535a\u3001\u5c0f\u5ddd\u5065\u53f8\u3001\u9234\u6728\u5065\u88d5\u3001\u5802\u524d\u76f4\u3001\u5409\u7530\u7a14\u3001\u30ea\u30b8\u30f3\u9577\u9396\u30a2\u30b7\u30eb\u5316\u4fee\u98fe\u306b\u3088\u308b\u8ee2\u5199\u56e0\u5b50TEAD\u306e\u6d3b\u6027\u5236\u5fa1\u6a5f\u69cb\u306e\u89e3\u6790\u3001\u65e5\u672c\u8fb2\u82b8\u5316\u5b66\u4f1a2018\u5e74\u5ea6\u5927\u4f1a\u30012018\u5e743\u6708\u3001\u540d\u53e4\u5c4b<\/p>

\u68ee\u53e3\u7f8e\u91cc\u3001\u4f0a\u85e4\u662d\u535a\u3001\u6e21\u90e8\u5321\u53f2\u3001\u85e4\u5ba4\u96c5\u5f18\u3001\u30aa\u30eb\u30ac\u30cd\u30e9\u30b9\u30c8\u30ec\u30b9\u306b\u3088\u308b\u7d30\u80de\u5185\u30e6\u30d3\u30ad\u30c1\u30f3\u5316\u4fee\u98fe\u306e\u5909\u52d5\u30012017\u5e74\u5ea6\u751f\u547d\u79d1\u5b66\u7cfb\u5b66\u4f1a\u5408\u540c\u5e74\u6b21\u5927\u4f1a\uff08ConBio2017\uff09\u30012017\u5e7412\u6708\u3001\u795e\u6238<\/p>

\u5247\u6b21\u6052\u592a\u3001\u4f0a\u85e4\u662d\u535a\u3001\u5c0f\u5ddd\u5065\u53f8\u3001\u9234\u6728\u5065\u88d5\u3001\u5802\u524d\u76f4\u3001\u5409\u7530\u7a14\u3001\u8ee2\u5199\u56e0\u5b50TEAD\u306e\u30ea\u30b8\u30f3\u9577\u9396\u30a2\u30b7\u30eb\u5316\u4fee\u98fe\u5236\u5fa1\u6a5f\u69cb\u3068\u305d\u306e\u6a5f\u80fd\u306e\u89e3\u6790\u30012017\u5e74\u5ea6\u751f\u547d\u79d1\u5b66\u7cfb\u5b66\u4f1a\u5408\u540c\u5e74\u6b21\u5927\u4f1a\uff08ConBio2017\uff09\u30012017\u5e7412\u6708\u3001\u795e\u6238<\/p>

\u524d\u672c\u4f51\u6a39\u3001\u6839\u672c\u548c\u5f70\u3001\u672c\u6a4b\u611b\u4f9d\u3001\u99ac\u5834\u5d07\u3001\u4f0a\u85e4\u662d\u535a\u3001\u8c37\u4f73\u6d25\u5b50\u3001\u795e\u7d4c\u7a81\u8d77\u4f38\u9577\u306b\u304a\u3051\u308b\u30ea\u30f3\u8102\u8cea\u5206\u89e3\u9175\u7d20PA-PLA1\u306e\u5f79\u5272\u30012017\u5e74\u5ea6\u751f\u547d\u79d1\u5b66\u7cfb\u5b66\u4f1a\u5408\u540c\u5e74\u6b21\u5927\u4f1a\uff08ConBio2017\uff09\u30012017\u5e7412\u6708\u3001\u795e\u6238<\/p>

\u5e73\u91ce\u667a\u4e5f\u3001\u5e73\u91ce\u9053\u4e08\u3001\u85e4\u539f\u656c\u58eb\u3001\u6885\u539f\u5d07\u53f2\u3001\u4f0a\u85e4\u662d\u535a\u3001\u5409\u7530\u7a14\u3001\u5f71\u8fd1\u5f18\u4e4b\u3001\u7279\u7570\u306a\u69cb\u9020\u3092\u6709\u3059\u308bCyproheptadine\u8a98\u5c0e\u4f53\u306eSet7\/9\u963b\u5bb3\u5264\u3068\u3057\u3066\u306e\u69cb\u9020\u5c55\u958b\u3001\u7b2c35\u56de\u30e1\u30c7\u30a3\u30b7\u30ca\u30eb\u30b1\u30df\u30b9\u30c8\u30ea\u30fc\u30b7\u30f3\u30dd\u30b8\u30a6\u30e0\u30012017\u5e7410\u6708\u3001\u540d\u53e4\u5c4b<\/p>

\u624b\u8cc0\u60a0\u771f\u3001\u5e73\u4e2d\u8aa0\u5f25\u3001\u6a0b\u53e3\u6167\u3001\u51fa\u53e3\u82b3\u6625\u3001\u4f0a\u85e4\u662d\u535a\u3001\u5409\u7530\u7a14\u3001\u9577\u5ca1\u5eb7\u592b\u3001\u4f4f\u5409\u5b5d\u660e\u3001H+<\/sup>\/\u6709\u6a5f\u30ab\u30c1\u30aa\u30f3\u4ea4\u63db\u8f38\u9001\u4f53\u3092\u6a19\u7684\u3068\u3057\u305fHDAC\u963b\u5bb3\u5264\u306e\u8133\u3078\u306e\u30c7\u30ea\u30d0\u30ea\u30fc\u3001\u7b2c39\u56de\u751f\u4f53\u819c\u3068\u85ac\u7269\u306e\u76f8\u4e92\u4f5c\u7528\u30b7\u30f3\u30dd\u30b8\u30a6\u30e0\u30012017\u5e7410\u6708\u3001\u91d1\u6ca2\uff08\u62db\u5f85\u8b1b\u6f14\uff09<\/p>

\u4f0a\u85e4\u662d\u535a\u3001\u300cNAD\u4f9d\u5b58\u7684\u8131\u30a2\u30bb\u30c1\u30eb\u5316\u9175\u7d20SIRT2\u3092\u6a19\u7684\u3068\u3057\u305f\u5275\u85ac\u7814\u7a76\u304b\u3089\u898b\u51fa\u3055\u308c\u305f\u8102\u8cea\u4ee3\u8b1d\u7269\u306e\u65b0\u3057\u3044\u6a5f\u80fd\u306e\u767a\u898b\u300d\u3001\u751f\u4f53\u6a5f\u80fd\u3068\u5275\u85ac\u30b7\u30f3\u30dd\u30b8\u30a6\u30e02017\u30012017\u5e748\u6708\u3001\u4eac\u90fd<\/p>

Akihiro Ito, Kota Noritsugu, Takehiro Suzuki, Naoshi Dohmae, Minoru Yoshida, Long chain fatty acyl lysine modification of TEAD transcription factors, FASEB Science Research Conference, Reversible Acetylation on Health and Disease (HDACs), August 7, 2017, Big Sky, MT, USA<\/p>

Yoshida M and Ito A, \u201cChemical biology on deacetylation and deacylation by sirtuins\u201d, FASEB Science Research Conferences \u201cReversible acetylation in health and disease\u201d, August 2017, Big Sky, USA<\/p><\/p>\n\n\n\n

\u8457\u66f8\u30fb\u7279\u8a31<\/h3>\n\n\n\n

\u8457\u66f8<\/h4>\n\n\n\n

\u524d\u672c \u4f51\u6a39\u3001\u4f0a\u85e4 \u662d\u535a \u3001 \u300c\u30ea\u30b7\u30f3\u9577\u9396\u30a2\u30b7\u30eb\u5316\uff1a\u53ef\u9006\u7684\u8102\u80aa\u9178\u4fee\u98fe\u306e\u65b0\u5c55\u958b\u300d\u30d5\u30a1\u30eb\u30de\u30b7\u30a2 2026 \u5e7462 \u5dfb2 \u53f7 p. 132-136 \u30002026\u5e742\u67081\u65e5<\/p>\n\n\n\n

\u9ad8\u702c\u7fd4\u5e73\u3001\u4f0a\u85e4\u662d\u535a\u3001\u5409\u7530\u7a14\u3001\u300c\u963b\u5bb3\u5264\u306b\u3088\u308b\u30d2\u30b9\u30c8\u30f3\u30a2\u30bb\u30c1\u30eb\u5316\u306e\u8abf\u7bc0\u300d\u3001\u533b\u5b66\u306e\u3042\u3086\u307f 272(1), 115-122, 2020<\/p>\n\n\n\n

\u57fa\u790e\u8b1b\u7fa9\u5206\u5b50\u751f\u7269\u5b66\u3000\u6771\u4eac\u5316\u5b66\u540c\u4eba\u30002020\u5e749\u670816\u65e5<\/p>\n\n\n\n

\u57fa\u790e\u8b1b\u7fa9\u751f\u7269\u5b66\u3000\u6771\u4eac\u5316\u5b66\u540c\u4eba\u30002020\u5e743\u670823\u65e5<\/p>\n\n\n\n

\u4f4f\u5409\u5b5d\u660e\u3001\u5e73\u4e2d\u8aa0\u5f25\u3001\u51fa\u53e3\u82b3\u6625\u3001\u4f0a\u85e4\u662d\u535a\u3001\u5409\u7530\u7a14\u3001\u300c\u8840\u6db2\u8133\u95a2\u9580\u900f\u904e\u6027\u3092\u6709\u3059\u308b\u30d2\u30b9\u30c8\u30f3\u8131\u30a2\u30bb\u30c1\u30eb\u5316\u9175\u7d20\u963b\u5bb3\u5264\u306e\u63a2\u7d22\u300dMEDCHEM NEWS 30(1), 43-46, 2020<\/p>\n\n\n\n

\u7279\u8a31<\/h4>\n\n\n\n

\u56fd\u7acb\u7814\u7a76\u958b\u767a\u6cd5\u4eba\u7406\u5316\u5b66\u7814\u7a76\u6240\u3001\u5b66\u6821\u6cd5\u4eba\u6771\u4eac\u85ac\u79d1\u5927\u5b66. G9a\u963b\u5bb3\u5264. \u5409\u7530\u7a14\u3001\u767d\u4e95\u6587\u5e78\u3001\u4f0a\u85e4\u662d\u535a\u3001\u9ad8\u702c\u7fd4\u5e73. PCT\/JP2022\/022270. 2022-6-02.<\/p>\n\n\n\n

\u674f\u6797\u88fd\u85ac\u682a\u5f0f\u4f1a\u793e\u3001\u56fd\u7acb\u7814\u7a76\u958b\u767a\u6cd5\u4eba\u7406\u5316\u5b66\u7814\u7a76\u6240\u3001\u5b66\u6821\u6cd5\u4eba\u6771\u4eac\u85ac\u79d1\u5927\u5b66\u3001\u516c\u76ca\u8ca1\u56e3\u6cd5\u4eba\u5fae\u751f\u7269\u5b66\u7814\u7a76\u4f1a. G9a\u963b\u5bb3\u5264. \u89d2\u8c37\u9f8d\u5c55\u3001\u897f\u30f6\u8c37\u6d0b\u8f14\u3001\u6d6a\u6c5f\u4eae\u4ecb\u3001\u6a4b\u672c\u61b2\u660e\u3001\u4f0a\u85e4\u662d\u535a\u3001\u767d\u4e95\u6587\u5e78\u3001\u559c\u4e45\u91cc\u8ca2\u3001\u5409\u7530\u7a14. PCT\/JP2020\/43966. 2020-11-26.<\/p>\n\n\n\n

\u516c\u958b\u756a\u53f7\uff1aWO2021\/106988A1\uff3b2022\u5e745\u6708\u306b\u5404\u56fd\u79fb\u884c\uff1a\u65e5\u672c\u3001\u7c73\u56fd\u3001\u6b27\u5dde\u3001\u30ab\u30ca\u30c0\u3001\u30a4\u30f3\u30c9\uff3d\u3001\u674f\u6797\u88fd\u85ac\u682a\u5f0f\u4f1a\u793e\u3001\u56fd\u7acb\u7814\u7a76\u958b\u767a\u6cd5\u4eba\u7406\u5316\u5b66\u7814\u7a76\u6240\u3001\u5b66\u6821\u6cd5\u4eba\u6771\u4eac\u85ac\u79d1\u5927\u5b66\u3001\u516c\u76ca\u8ca1\u56e3\u6cd5\u4eba\u5fae\u751f\u7269\u5b66\u7814\u7a76\u4f1a. G9a\u963b\u5bb3\u5264. \u89d2\u8c37\u9f8d\u5c55\u3001\u897f\u30f6\u8c37\u6d0b\u8f14\u3001\u6d6a\u6c5f\u4eae\u4ecb\u3001\u6a4b\u672c\u61b2\u660e\u3001\u4f0a\u85e4\u662d\u535a\u3001\u767d\u4e95\u6587\u5e78\u3001\u559c\u4e45\u91cc\u8ca2\u3001\u5409\u7530\u7a14. \u7279\u98582019-213990. 2019-11-27.<\/p>\n\n\n\n

\u56fd\u7acb\u5927\u5b66\u6cd5\u4eba\u5ca1\u5c71\u5927\u5b66\u3001\u56fd\u7acb\u7814\u7a76\u958b\u767a\u6cd5\u4eba\u7406\u5316\u5b66\u7814\u7a76\u6240\u3001\u56fd\u7acb\u5927\u5b66\u6cd5\u4eba\u9ce5\u53d6\u5927\u5b66. DNMT\u306eS-\u30cb\u30c8\u30ed\u30b7\u30eb\u5316\u963b\u5bb3\u5264\u3001\u304c\u3093\u6cbb\u7642\u85ac\u53ca\u3073\u305d\u306e\u30b9\u30af\u30ea\u30fc\u30cb\u30f3\u30b0\u65b9\u6cd5. \u4e0a\u539f\u5b5d\u3001\u4f0a\u85e4\u662d\u535a\u3001\u30ab\u30e0 \u30ef\u30a4 \u30b8\u30a7\u30a4 \u30b6\u30f3\u3001\u30af\u30de\u30fc\u30eb \u30a2\u30b7\u30e5\u30c8\u30b7\u30e5\u3001\u5ca1\u7530\u592a. \u7279\u98582017-056367. 2017-3-22.<\/p>\n\n\n\n

\u56fd\u7acb\u7814\u7a76\u958b\u767a\u6cd5\u4eba\u7406\u5316\u5b66\u7814\u7a76\u6240. \u95a2\u539f\u660e\u3001\u5409\u7530\u7a14\u3001\u4e0a\u7530\u5b9f\u3001\u4f50\u53e4\u9999\u7e54\u3001\u91d1\u9418\u660e\u3001\u4f50\u3005\u6728\u5353\u3001\u4f0a\u85e4\u662d\u535a. \u690d\u7269\u306e\u8010\u5869\u6027\u5411\u4e0a\u5264. \u7279\u98582014-198624. 2014-9-29.<\/p>\n\n\n\n

\u56fd\u7acb\u5927\u5b66\u6cd5\u4eba\u4e5d\u5dde\u5de5\u696d\u5927\u5b66\u3001\u8ca1\u56e3\u6cd5\u4eba\u764c\u7814\u7a76\u4f1a. \u897f\u91ce\u61b2\u548c\u3001\u7af9\u672c\u9756\u3001\u4f0a\u85e4\u662d\u535a\u3001\u5409\u7530\u7a14\u3001\u77e2\u5b88\u9686\u592b. \u30bf\u30f3\u30d1\u30af\u8cea\u30ea\u30b7\u30f3\u30e1\u30c1\u30eb\u5316\u9175\u7d20Set7\/9\u306e\u963b\u5bb3\u7269\u8cea\u3092\u542b\u6709\u3059\u308b\u75be\u60a3\u306e\u4e88\u9632\u30fb\u6cbb\u7642\u5264. \u7279\u98582010-230916. 2010-10-13.<\/p>\n\n\n\n

\u56fd\u7acb\u5927\u5b66\u6cd5\u4eba\u4e5d\u5dde\u5de5\u696d\u5927\u5b66. \u897f\u91ce\u61b2\u548c\u3001\u7af9\u672c\u9756\u3001\u4f0a\u85e4\u662d\u535a\u3001\u5409\u7530\u7a14. \u30d2\u30b9\u30c8\u30f3\u30e1\u30c1\u30eb\u5316\u9175\u7d20\u6d3b\u6027\u306e\u6e2c\u5b9a\u6cd5. \u7279\u98582010-202484. 2010-09-09.<\/p>\n\n\n

<\/p>","protected":false},"excerpt":{"rendered":"

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