Zobrazeno 1 - 2
of 2
pro vyhledávání: '"Kawori Kihara"'
Autor:
Ryutaro Kanada, Yoshiko Kagoshima, Takashi Suzuki, Akifumi Nakamura, Hideaki Funami, Jun Watanabe, Masayoshi Asano, Mizuki Takahashi, Osamu Ubukata, Kanae Suzuki, Tomoya Aikawa, Kazumi Sato, Megumi Goto, Genzui Setsu, Kentaro Ito, Kawori Kihara, Mutsumi Kuroha, Takashi Kohno, Hideaki Ogiwara, Takeshi Isoyama, Yuichi Tominaga, Saito Higuchi, Hiroyuki Naito
Publikováno v:
Journal of medicinal chemistry.
Histone acetylation is a post-translational modification of histones that is catalyzed by histone acetyltransferases (HATs) and plays an essential role in cellular processes. The HAT domain of EP300/CBP has recently emerged as a potential drug target
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1b85052fce6ba975a5f0b046a0c345b1
https://pubmed.ncbi.nlm.nih.gov/36572866
https://pubmed.ncbi.nlm.nih.gov/36572866
Autor:
Ryutaro Kanada, Yoshiko Kagoshima, Masayoshi Asano, Takashi Suzuki, Takeshi Murata, Makoto Haruta, Mizuki Takahashi, Osamu Ubukata, Kazuyuki Hashimoto, Kenichi Obata, Kawori Kihara, Mutsumi Kuroha, Toshihiro Banjo, Noriko Togashi, Kazumi Sato, Yuka Yamamoto, Kanae Suzuki, Takeshi Isoyama, Yuichi Tominaga, Saito Higuchi, Hiroyuki Naito
Publikováno v:
Bioorganic & Medicinal Chemistry Letters. 66:128726
EP300 and its paralog CBP play an important role in post-translational modification as histone acetyltransferases (HATs). EP300/CBP inhibition has been gaining attention as an anticancer treatment target in recent years. Herein, we describe the ident
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ff918b04f7e52785501cd868f56b66a7
https://doi.org/10.1016/j.bmcl.2022.128726
https://doi.org/10.1016/j.bmcl.2022.128726