Zobrazeno 1 - 10
of 106
pro vyhledávání: '"Takumi Ueda"'
Autor:
Yuki Hosono, Satoshi Uchida, Moe Shinkai, Chad E. Townsend, Colin N. Kelly, Matthew R. Naylor, Hsiau-Wei Lee, Kayoko Kanamitsu, Mayumi Ishii, Ryosuke Ueki, Takumi Ueda, Koh Takeuchi, Masatake Sugita, Yutaka Akiyama, Scott R. Lokey, Jumpei Morimoto, Shinsuke Sando
Publikováno v:
Nature Communications, Vol 14, Iss 1, Pp 1-14 (2023)
Naturally occurring peptides with high membrane permeability often have backbone ester bonds. Here, the authors investigated the effect of an amide-to-ester substitution on membrane permeability of peptides and found the substitution is useful for im
Externí odkaz:
https://doaj.org/article/a59489e908164722a8c86ea5023eb75f
Autor:
Yutaro Shiraishi, Yutaka Kofuku, Takumi Ueda, Shubhi Pandey, Hemlata Dwivedi-Agnihotri, Arun K. Shukla, Ichio Shimada
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-11 (2021)
β-arrestins commonly bind to two distinct elements in GPCRs: the phosphorylated carboxyl terminal tail (C tail) and the cytoplasmic face of the transmembrane region (TM core). Here, the authors use methyl-TROSY NMR measurements to characterise the i
Externí odkaz:
https://doaj.org/article/c2744b4652694e1eb22b0a1f83faea09
Autor:
Yutaro Shiraishi, Mei Natsume, Yutaka Kofuku, Shunsuke Imai, Kunio Nakata, Toshimi Mizukoshi, Takumi Ueda, Hideo Iwaï, Ichio Shimada
Publikováno v:
Nature Communications, Vol 9, Iss 1, Pp 1-10 (2018)
Upon stimulation by agonist binding, the C-terminal regions of G-protein-coupled receptors (GPCRs) become phosphorylated by GPCR kinases, and phosphorylated GPCRs bind arrestin. Here the authors give structural insights into the phosphorylation induc
Externí odkaz:
https://doaj.org/article/11dca4d48ec6418dbf505466ac65a7b4
Autor:
Koh Takeuchi, Yutaka Kofuku, Shunsuke Imai, Takumi Ueda, Yuji Tokunaga, Yuki Toyama, Yutaro Shiraishi, Ichio Shimada
Publikováno v:
Membranes, Vol 11, Iss 8, p 604 (2021)
A primary biological function of multi-spanning membrane proteins is to transfer information and/or materials through a membrane by changing their conformations. Therefore, particular dynamics of the membrane proteins are tightly associated with thei
Externí odkaz:
https://doaj.org/article/399a52ea34974dbb844af3cc8f0e5f6e
Publikováno v:
Nihon Kessho Gakkaishi. 64:279-284
Autor:
Jumpei Morimoto, Yota Shiratori, Marin Yokomine, Takumi Ueda, Takayuki Nakamuro, Kiyofumi Takaba, Saori Maki-Yonekura, Koji Umezawa, Koichiro Miyanishi, Yasuhiro Fukuda, Takumu Watanabe, Wataru Mizukami, Koh Takeuchi, Koji Yonekura, Eiichi Nakamura, Shinsuke Sando
De novo design of peptide nanoshapes is of great interest in biomolecular science since the local peptide nanoshapes formed by a short peptide chain in the proteins are often key to the biological activities. Here, we show that the de novo design of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::9d14148d76aabbed2275c4cd011d12a9
https://doi.org/10.26434/chemrxiv-2023-c4mw6
https://doi.org/10.26434/chemrxiv-2023-c4mw6
Autor:
Wenchao Zhu, Shiori Takeuchi, Shosei Imai, Tohru Terada, Takumi Ueda, Yusuke Nasu, Takuya Terai, Robert E. Campbell
Publikováno v:
Nature Chemical Biology.
Autor:
Yoshimitsu Itoh, Shuo Chen, Ryota Hirahara, Takeshi Konda, Tsubasa Aoki, Takumi Ueda, Ichio Shimada, James J. Cannon, Cheng Shao, Junichiro Shiomi, Kazuhito V. Tabata, Hiroyuki Noji, Kohei Sato, Takuzo Aida
Publikováno v:
Science. 376:738-743
Ultrafast water permeation in aquaporins is promoted by their hydrophobic interior surface. Polytetrafluoroethylene has a dense fluorine surface, leading to its strong water repellence. We report a series of fluorous oligoamide nanorings with interio
Autor:
Jungyeon Kim, Hiroka Kobayashi, Marin Yokomine, Yota Shiratori, Takumi Ueda, Koh Takeuchi, Koji Umezawa, Daisuke Kuroda, Kouhei Tsumoto, Jumpei Morimoto, Shinsuke Sando
Publikováno v:
Organic & Biomolecular Chemistry. 20:6994-7000
The first design strategy for a preorganized β-peptoid monomer is described. A cyclopentane constraint realized the preorganized monomer and led to a β-peptoid with a stable twisted strand shape.
Publikováno v:
BUTSURI-TANSA(Geophysical Exploration). 75:38-55