Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Hajime Kamoshida"'
Autor:
Miwa Fujisaki, Yuji Tokunaga, Ichio Shimada, Hajime Kamoshida, Hiroyuki Hanzawa, Takeshi Takizawa, Koh Takeuchi, Imai Misaki
Publikováno v:
Angewandte Chemie International Edition. 60:6567-6572
Cyclorasins 9A5 and 9A54 are 11-mer cyclic peptides that inhibit the Ras-Raf protein interaction. The peptides share a cell-penetrating peptide (CPP)-like motif; however, only cyclorasin 9A5 can permeabilize cells to exhibit strong cell-based activit
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b9a734ff9aed4852c9eb27187ac5522a
https://doi.org/10.1002/anie.202016647
https://doi.org/10.1002/anie.202016647
Autor:
Takashi Tanaka, Teppei Ikeya, Hajime Kamoshida, Yusuke Suemoto, Masaki Mishima, Masahiro Shirakawa, Peter Güntert, Yutaka Ito
Publikováno v:
Angewandte Chemie. 131:7362-7366
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::32f7170f81860ac878aa480a9176fedd
https://doi.org/10.1002/ange.201900840
https://doi.org/10.1002/ange.201900840
Autor:
Hajime Kamoshida, Ichio Shimada, Misaki Imai, Miwa Fujisaki, Takeshi Takizawa, Yumiko Mizukoshi, Yuji Tokunaga, Koh Takeuchi, Hitomi Matsuo, Hiroyuki Hanzawa
Publikováno v:
Science Advances
An NMR-based strategy was established to improve protein druggability by stabilizing cryptic binding sites in an equilibrium.
Cryptic ligand binding sites, which are not evident in the unligated structures, are beneficial in tackling with diffic
Cryptic ligand binding sites, which are not evident in the unligated structures, are beneficial in tackling with diffic
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6e854b2554c181c517439d63c5e7dcaa
https://doi.org/10.1126/sciadv.abd0480
https://doi.org/10.1126/sciadv.abd0480
Autor:
Yutaka Ito, Takashi Tanaka, Teppei Ikeya, Masaki Mishima, Masahiro Shirakawa, Peter Güntert, Hajime Kamoshida, Yusuke Suemoto
Publikováno v:
Angewandte Chemie (International ed. in English). 58(22)
Proteins in living cells interact specifically or nonspecifically with an enormous number of biomolecules. To understand the behavior of proteins under intracellular crowding conditions, it is indispensable to observe their three-dimensional (3D) str
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::906d5812ffa4084310d4724a98ef54f4
https://pubmed.ncbi.nlm.nih.gov/30938016
https://pubmed.ncbi.nlm.nih.gov/30938016
Publikováno v:
Chemical communications (Cambridge, England). 53(81)
By using in-cell NMR experiments, we have demonstrated that the protein folding state in cells is significantly influenced by the cellular health conditions. hAK1 was denatured in cells under stressful culture conditions, while it remained functional
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9232ce7b9cecd4db9867e8e42f8ed63b
https://pubmed.ncbi.nlm.nih.gov/28960222
https://pubmed.ncbi.nlm.nih.gov/28960222
Autor:
Jin Inoue, Masahiro Shirakawa, Hajime Kamoshida, Teppei Ikeya, Tsutomu Mikawa, Jumpei Hamatsu, Takahiro Haremaki, Masaki Mishima, Nobuhiro Hayashi, D.S.S. Hembram, Yutaka Ito
Publikováno v:
Biochemical and Biophysical Research Communications. 438:653-659
Recent developments in in-cell NMR techniques have allowed us to study proteins in detail inside living eukaryotic cells. The lifetime of in-cell NMR samples is however much shorter than that in culture media, presumably because of various stresses a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6a035fdd0083ce5108a4caf1abbc3587
https://doi.org/10.1016/j.bbrc.2013.07.127
https://doi.org/10.1016/j.bbrc.2013.07.127
Autor:
Yumiko Mizukoshi1, Koh Takeuchi2 koh-takeuchi@aist.go.jp, Yuji Tokunaga2, Hitomi Matsuo1, Misaki Imai1, Miwa Fujisaki1, Hajime Kamoshida1, Takeshi Takizawa3, Hiroyuki Hanzawa3, Ichio Shimada4,5 ichio.shimada@riken.jp
Publikováno v:
Science Advances. 9/30/2020, Vol. 6 Issue 40, p1-8. 8p.