Zobrazeno 1 - 10
of 11
pro vyhledávání: '"Keisuke Chosa"'
Autor:
Ryoko Sasaki, Mary Ann Suico, Keisuke Chosa, Yuriko Teranishi, Takashi Sato, Asuka Kagami, Shunsuke Kotani, Hikaru Kato, Yuki Hitora, Sachiko Tsukamoto, Tomohiro Yamashita, Takeshi Yokoyama, Mineyuki Mizuguchi, Hirofumi Kai, Tsuyoshi Shuto
Publikováno v:
Journal of Pharmacological Sciences, Vol 151, Iss 1, Pp 54-62 (2023)
Hereditary ATTR amyloidosis is caused by the point mutation in serum protein transthyretin (TTR) that destabilizes its tetrameric structure to dissociate into monomer. The monomers form amyloid fibrils, which are deposited in peripheral nerves and or
Externí odkaz:
https://doaj.org/article/73aa628980de4100b6bdb344612c5194
Autor:
Shingo Suzuki, Keisuke Chosa, Cristina Barillà, Michael Yao, Orsetta Zuffardi, Hirofumi Kai, Tsuyoshi Shuto, Mary Ann Suico, Yuet W. Kan, R. Geoffrey Sargent, Dieter C. Gruenert
Publikováno v:
Frontiers in Genome Editing, Vol 4 (2022)
Background: Gene correction via homology directed repair (HDR) in patient-derived induced pluripotent stem (iPS) cells for regenerative medicine are becoming a more realistic approach to develop personalized and mutation-specific therapeutic strategi
Externí odkaz:
https://doaj.org/article/98771079d2134f55b64cdc7d8d0cd6f4
Autor:
Takeshi Yokoyama, Shun Takaki, Keisuke Chosa, Takashi Sato, Mary Ann Suico, Yuriko Teranishi, Tsuyoshi Shuto, Mineyuki Mizuguchi, Hirofumi Kai
Publikováno v:
Journal of Pharmacological Sciences, Vol 129, Iss 4, Pp 240-243 (2015)
Familial amyloid polyneuropathy (FAP) is a genetic, adult-onset, neurodegenerative disorder caused by amyloid formation of transthyretin (TTR), a thyroxine-binding protein. Mutation in TTR causes a propensity of TTR tetramer to dissociate to monomer,
Externí odkaz:
https://doaj.org/article/4cbd743c7ee9416aab2b4f630f72e43b
Autor:
Ryoko Sasaki, Mary Ann Suico, Keisuke Chosa, Yuriko Teranishi, Takashi Sato, Asuka Kagami, Shunsuke Kotani, Hikaru Kato, Yuki Hitora, Sachiko Tsukamoto, Tomohiro Yamashita, Takeshi Yokoyama, Mineyuki Mizuguchi, Hirofumi Kai, Tsuyoshi Shuto
Publikováno v:
Journal of pharmacological sciences. 151(1)
Hereditary ATTR amyloidosis is caused by the point mutation in serum protein transthyretin (TTR) that destabilizes its tetrameric structure to dissociate into monomer. The monomers form amyloid fibrils, which are deposited in peripheral nerves and or
Autor:
Punnajit Lim, Chih-Hong Lou, Yusuke Higuchi, Jia-Ling Teo, Xiaohui Hu, Nyam-Osor Chimge, Patrick T. Fueger, Keisuke Chosa, Elizabeth Melendez, Keane K. Y. Lai, Masaya Ono, Michael G. Kahn, John Termini, Cu Nguyen
Publikováno v:
Cancers, Vol 13, Iss 5884, p 5884 (2021)
Cancers; Volume 13; Issue 23; Pages: 5884
Cancers
Cancers; Volume 13; Issue 23; Pages: 5884
Cancers
Simple Summary The coupling of metabolism with cellular status is critically important and highly evolutionarily conserved. However, how cells coordinate metabolism with transcription as they change their status is not clear. Utilizing multiomic and
p300 Serine 89: A Critical Signaling Integrator and Its Effects on Intestinal Homeostasis and Repair
Autor:
Patrick T. Fueger, Michael Kahn, Nobuo Kato, Sarah K. Highlander, Masaya Ono, Nyam Osor Chimge, Yusuke Higuchi, Andre J. Ouellette, Cu Nguyen, Keisuke Chosa, Elizabeth Melendez, David P. Lin, Yoshihiro Eriguchi, Xiaohui Hu, Keith Lai, Keane K Y Lai
Publikováno v:
Cancers, Vol 13, Iss 1288, p 1288 (2021)
Cancers
Volume 13
Issue 6
Cancers
Volume 13
Issue 6
Simple Summary Given their high degree of identity and even greater similarity at the amino acid level, Kat3 coactivators, CBP (Kat3A) and p300 (Kat3B), have long been considered redundant. We describe the generation of novel p300 S89A knock-in mice
Autor:
Mary Ann Suico, Keisuke Chosa, Tsuyoshi Shuto, Yuriko Wakita, Nami Hashimoto, Shingo Kawano, Hiroshi Morioka, Ryoko Sasaki, Yoshiki Imai, Yuriko Teranishi, Hirofumi Kai, Takashi Sato
Publikováno v:
Biological and Pharmaceutical Bulletin. 41:628-636
Transthyretin (TTR) is a tetrameric beta-sheet-rich protein that is important in the plasma transport of thyroxine and retinol. Mutations in the TTR gene cause TTR tetramer protein to dissociate to monomer, which is the rate-limiting step in familial
Autor:
Takashi Sato, Takeshi Yokoyama, Keisuke Chosa, Tsuyoshi Shuto, Hirofumi Kai, Mineyuki Mizuguchi, Yuriko Teranishi, Mary Ann Suico, Shun Takaki
Publikováno v:
Journal of Pharmacological Sciences, Vol 129, Iss 4, Pp 240-243 (2015)
Familial amyloid polyneuropathy (FAP) is a genetic, adult-onset, neurodegenerative disorder caused by amyloid formation of transthyretin (TTR), a thyroxine-binding protein. Mutation in TTR causes a propensity of TTR tetramer to dissociate to monomer,
Autor:
Masayuki Kaneko, Ikuo Wada, Tomoaki Koga, Saori Morino-Koga, Koichi Kokame, Misato Sho, Takashi Sato, Hideki Nishitoh, Tsukasa Okiyoneda, Yasuhiro Sako, Mary Ann Suico, Tsuyoshi Shuto, Manabu Taura, Mamiko Momohara, Keisuke Chosa, Hirofumi Kai, Masanori Miyata
Publikováno v:
Molecular Cell. 47(1):99-110
Summary Nascent secretory proteins are extensively scrutinized at the endoplasmic reticulum (ER). Various signatures of client proteins, including exposure of hydrophobic patches or unpaired sulfhydryls, are coordinately utilized to reduce nonnative
Publikováno v:
Molecular Therapy. 24:S51
Development of effective gene modification via Homology Directed Repair (HDR) as well as induced pluripotent stem cells (iPSCs) have been significant advances in development of gene- and cell-based therapies for inherited diseases. Patient-specific i