Výsledky vyhledávání - "Hideyuki Oki"

Discovery of Brain-Penetrant Glucosylceramide Synthase Inhibitors with a Novel Pharmacophore

Publikováno v: Journal of Medicinal Chemistry. 65:4270-4290

Inhibition of glucosylceramide synthase (GCS) is a major therapeutic strategy for Gaucher's disease and has been suggested as a potential target for treating Parkinson's disease. Herein, we report the discovery of novel brain-penetrant GCS inhibitors

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a407ff68d50cb206d4c182ef36b2c1cf
https://doi.org/10.1021/acs.jmedchem.1c02078

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Design, synthesis, and structure-activity relationship of TAK-418 and its derivatives as a novel series of LSD1 inhibitors with lowered risk of hematological side effects

Autor: Yasushi Hattori, Shigemitsu Matsumoto, Shinji Morimoto, Masaki Daini, Masashi Toyofuku, Satoru Matsuda, Rina Baba, Koji Murakami, Misa Iwatani, Hideyuki Oki, Shinji Iwasaki, Kouta Matsumiya, Yusuke Tominari, Haruhide Kimura, Mitsuhiro Ito

Publikováno v: European journal of medicinal chemistry. 239

Lysine-specific demethylase 1 (LSD1) is an enzyme that demethylates methylated histone H3 lysine 4 (H3K4). Inhibition of LSD1 enzyme activity could increase H3K4 methylation levels and treat diseases associated with epigenetic dysregulation. However,

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e1799e4688154809d1d4f50bf466e86b
https://pubmed.ncbi.nlm.nih.gov/35749987

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T-448, a specific inhibitor of LSD1 enzyme activity, improves learning function without causing thrombocytopenia in mice

Autor: Shigeru Igaki, Ryosuke Hibino, Ken Tsuchida, Shinji Iwasaki, Satoru Matsuda, Ryujiro Hara, Hiroko Kamada, Masashi Toyofuku, Haruhide Kimura, Misa Iwatani, Rina Baba, Mitsuhiro Ito, Kota Matsumiya, Hideyuki Oki, Yusuke Kamada, Takeshi Hirakawa, Shinji Morimoto

Publikováno v: Neuropsychopharmacology

Dysregulation of histone H3 lysine 4 (H3K4) methylation has been implicated in the pathogenesis of several neurodevelopmental disorders. Targeting lysine-specific demethylase 1 (LSD1), an H3K4 demethylase, is therefore a promising approach to treat t

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c6a412d79e9c823a65878035790b06f0
https://doi.org/10.1038/s41386-018-0300-9

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LSD1 enzyme inhibitor TAK-418 unlocks aberrant epigenetic machinery and improves autism symptoms in neurodevelopmental disorder models

Autor: Ryuji Yamada, Mitsuhiro Ito, Hideyuki Oki, Yasushi Hattori, Yuuichi Arakawa, Matsumoto Shigemitsu, Satoru Matsuda, Atsushi Nakatani, Masaki Daini, Shigeru Igaki, Noriko Suzuki, Haruhide Kimura, Tatsuya Ando, Rina Baba

Publikováno v: Science Advances

LSD1 inhibitor TAK-418 could be a therapeutic option for neurodevelopmental disorders via normalization of gene expression.
Persistent epigenetic dysregulation may underlie the pathophysiology of neurodevelopmental disorders, such as autism spec

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::226b60276736066095731de4a03ae505
https://doi.org/10.1126/sciadv.aba1187

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Cryo-EM Structure of K

Autor: Tatsuki, Asai, Naruhiko, Adachi, Toshio, Moriya, Hideyuki, Oki, Takamitsu, Maru, Masato, Kawasaki, Kano, Suzuki, Sisi, Chen, Ryohei, Ishii, Kazuko, Yonemori, Shigeru, Igaki, Satoshi, Yasuda, Satoshi, Ogasawara, Toshiya, Senda, Takeshi, Murata

Publikováno v: Structure (London, England : 1993). 29(3)

The hERG channel is a voltage-gated potassium channel involved in cardiac repolarization. Off-target hERG inhibition by drugs has become a critical issue in the pharmaceutical industry. The three-dimensional structure of the hERG channel was recently

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::0c5c71ba40770276671cc88c93110a4e
https://pubmed.ncbi.nlm.nih.gov/33450182

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Identification of cytidine-5-triphosphate synthase1-selective inhibitory peptide from random peptide library displayed on T7 phage

Autor: Shin-ichi Matsumoto, Yumi Zama, Hideyuki Oki, Kotaro Sakamoto, Yoshihiro Ishibashi, Satoshi Sogabe, Junichi Sakamoto, Akiyoshi Tani, Yusuke Kamada, Ryutaro Adachi

Publikováno v: Peptides. 94:56-63

Cytidine triphosphate synthase 1 (CTPS1) is an enzyme expressed in activated lymphocytes that catalyzes the conversion of uridine triphosphate (UTP) to cytidine triphosphate (CTP) with ATP-dependent amination, using either L-glutamine or ammonia as t

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f88d111b68cab3eede6a22501e4bc2a4
https://doi.org/10.1016/j.peptides.2017.06.007

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Discovery and Characterization of a Eukaryotic Initiation Factor 4A-3-Selective Inhibitor That Suppresses Nonsense-Mediated mRNA Decay

Autor: Samuel Aparicio, Tomohiro Kawamoto, Yoshihiro Ishibashi, Atsushi Nakanishi, Hiromichi Kimura, Daisuke Morishita, Misa Iwatani-Yoshihara, Takashi Ito, Hideyuki Oki, Yasuhiro Imaeda, Toshio Tanaka, Masahiro Ito

Publikováno v: ACS Chemical Biology. 12:1760-1768

Eukaryotic initiation factor 4A-3 (eIF4A3) is an Asp-Glu-Ala-Asp (DEAD) box-family adenosine triphosphate (ATP)-dependent RNA helicase. Subtypes eIF4A1 and eIF4A2 are required for translation initiation, but eIF4A3 participates in the exon junction c

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ed64391b881c548a1b4fda32aaa18a7d
https://doi.org/10.1021/acschembio.7b00041

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Discovery of Novel, Highly Potent, and Selective Matrix Metalloproteinase (MMP)-13 Inhibitors with a 1,2,4-Triazol-3-yl Moiety as a Zinc Binding Group Using a Structure-Based Design Approach

Autor: Takashi Santou, Masakuni Kori, Jun Terauchi, Kenjiro Sato, Akira Kaieda, Yoshio Yamamoto, Hideyuki Oki, Hiroshi Nara, Haruhiko Kuno, Naoyuki Kanzaki, Osamu Uchikawa, Hideyuki Mototani, Takako Naito

Publikováno v: Journal of Medicinal Chemistry. 60:608-626

On the basis of a superposition study of X-ray crystal structures of complexes of quinazoline derivative 1 and triazole derivative 2 with matrix metalloproteinase (MMP)-13 catalytic domain, a novel series of fused pyrimidine compounds which possess a

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f1606a72172cce8cef2bce74e9bffbdb
https://doi.org/10.1021/acs.jmedchem.6b01007

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