Zobrazeno 1 - 10
of 76
pro vyhledávání: '"Hideo AGO"'
Autor:
Takao Hirano, Akemi Koyanagi, Hideo Ago, Masaki Yamamoto, Jiro Kitaura, Masataka Kasai, Ko Okumura
Publikováno v:
Communications Biology, Vol 7, Iss 1, Pp 1-11 (2024)
Abstract Immunoglobulin E (IgE) plays pivotal roles in allergic diseases through interaction with a high-affinity receptor (FcεRI). We established that Fab fragments of anti-IgE antibodies (HMK-12 Fab) rapidly dissociate preformed IgE-FcεRI complex
Externí odkaz:
https://doaj.org/article/992f8009b99f4b3aa52e8e87b3b51b9f
Autor:
Erika Tsutsumi, Satomi Niwa, Ryota Takeda, Natsuki Sakamoto, Kei Okatsu, Shuya Fukai, Hideo Ago, Satoshi Nagao, Hiroshi Sekiguchi, Kazuki Takeda
Publikováno v:
Communications Chemistry, Vol 6, Iss 1, Pp 1-10 (2023)
Abstract Iron-sulfur clusters are prosthetic groups of proteins involved in various biological processes. However, details of the immature state of the iron-sulfur cluster into proteins have not yet been elucidated. We report here the first structura
Externí odkaz:
https://doaj.org/article/30b12ec1b8914a4389fcc2ab513e3b95
Autor:
Thomas P. Halsted, Keitaro Yamashita, Chai C. Gopalasingam, Rajesh T. Shenoy, Kunio Hirata, Hideo Ago, Go Ueno, Matthew P. Blakeley, Robert R. Eady, Svetlana V. Antonyuk, Masaki Yamamoto, S. Samar Hasnain
Publikováno v:
IUCrJ, Vol 6, Iss 4, Pp 761-772 (2019)
Copper-containing nitrite reductases (CuNiRs) that convert NO2− to NO via a CuCAT–His–Cys–CuET proton-coupled redox system are of central importance in nitrogen-based energy metabolism. These metalloenzymes, like all redox enzymes, are very s
Externí odkaz:
https://doaj.org/article/75b697a700aa49f6a796474d45d8a635
Autor:
Thomas P. Halsted, Keitaro Yamashita, Kunio Hirata, Hideo Ago, Go Ueno, Takehiko Tosha, Robert R. Eady, Svetlana V. Antonyuk, Masaki Yamamoto, S. Samar Hasnain
Publikováno v:
IUCrJ, Vol 5, Iss 1, Pp 22-31 (2018)
Synchrotron-based X-ray structural studies of ligand-bound enzymes are powerful tools to further our understanding of reaction mechanisms. For redox enzymes, it is necessary to study both the oxidized and reduced active sites to fully elucidate the r
Externí odkaz:
https://doaj.org/article/87c9109de0cd4a60a6e1fd9c06147529
Autor:
Takehiko Tosha, Takashi Nomura, Takuma Nishida, Naoya Saeki, Kouta Okubayashi, Raika Yamagiwa, Michihiro Sugahara, Takanori Nakane, Keitaro Yamashita, Kunio Hirata, Go Ueno, Tetsunari Kimura, Tamao Hisano, Kazumasa Muramoto, Hitomi Sawai, Hanae Takeda, Eiichi Mizohata, Ayumi Yamashita, Yusuke Kanematsu, Yu Takano, Eriko Nango, Rie Tanaka, Osamu Nureki, Osami Shoji, Yuka Ikemoto, Hironori Murakami, Shigeki Owada, Kensuke Tono, Makina Yabashi, Masaki Yamamoto, Hideo Ago, So Iwata, Hiroshi Sugimoto, Yoshitsugu Shiro, Minoru Kubo
Publikováno v:
Nature Communications, Vol 8, Iss 1, Pp 1-9 (2017)
Using photosensitive caged-compound for femtosecond crystallography at X-ray free electron lasers would allow the structure determination of reaction intermediates. Here the authors demonstrate the feasibility of this approach with a caged NO-compoun
Externí odkaz:
https://doaj.org/article/09d185f659f54420bd7260a89d764ebf
Autor:
Keitaro Yamashita, Naoyuki Kuwabara, Takanori Nakane, Tomohiro Murai, Eiichi Mizohata, Michihiro Sugahara, Dongqing Pan, Tetsuya Masuda, Mamoru Suzuki, Tomomi Sato, Atsushi Kodan, Tomohiro Yamaguchi, Eriko Nango, Tomoyuki Tanaka, Kensuke Tono, Yasumasa Joti, Takashi Kameshima, Takaki Hatsui, Makina Yabashi, Hiroshi Manya, Tamao Endo, Ryuichi Kato, Toshiya Senda, Hiroaki Kato, So Iwata, Hideo Ago, Masaki Yamamoto, Fumiaki Yumoto, Toru Nakatsu
Publikováno v:
IUCrJ, Vol 4, Iss 5, Pp 639-647 (2017)
Serial femtosecond crystallography (SFX) using X-ray free-electron lasers (XFELs) holds enormous potential for the structure determination of proteins for which it is difficult to produce large and high-quality crystals. SFX has been applied to vario
Externí odkaz:
https://doaj.org/article/6801e2bc89df4536aa7bf825ab1a4cbf
Autor:
Masaki Yamamoto, Kunio Hirata, Keitaro Yamashita, Kazuya Hasegawa, Go Ueno, Hideo Ago, Takashi Kumasaka
Publikováno v:
IUCrJ, Vol 4, Iss 5, Pp 529-539 (2017)
The progress in X-ray microbeam applications using synchrotron radiation is beneficial to structure determination from macromolecular microcrystals such as small in meso crystals. However, the high intensity of microbeams causes severe radiation dama
Externí odkaz:
https://doaj.org/article/2c24ce98426e46549bb5e3ba3edca214
Autor:
Ryoko Ando, Satoshi Shimozono, Hideo Ago, Masatoshi Takagi, Mayu Sugiyama, Hiroshi Kurokawa, Masahiko Hirano, Go Ueno, Fumiyoshi Ishidate, Takahiro Fujiwara, Yasushi Okada, Masaki Yamamoto, Atsushi Miyawaki
Although StayGold is a bright and highly photostable fluorescent protein (FP), its obligate dimer formation may prevent its application in molecular fusion and membrane targeting. With the objective of attaining monovalent as well as bright and photo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::b61460d9f41142f9dea16a0ea4561768
https://doi.org/10.21203/rs.3.rs-2941917/v1
https://doi.org/10.21203/rs.3.rs-2941917/v1
Publikováno v:
Nihon Kessho Gakkaishi. 65:2-2
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ef59deadc2804134357f6a95a5228ffd
https://doi.org/10.5940/jcrsj.65.2
https://doi.org/10.5940/jcrsj.65.2
Autor:
Keitaro Yamashita, C.C. Gopalasingam, Masaki Yamamoto, Kunio Hirata, S. Samar Hasnain, Rajesh T. Shenoy, T.P. Halsted, Hideo Ago, Robert R. Eady, Svetlana V. Antonyuk, Go Ueno, Matthew P. Blakeley
Publikováno v:
'IUCrJ ', vol: 6, pages: 761-772 (2019)
IUCRJ
IUCrJ, Vol 6, Iss 4, Pp 761-772 (2019)
IUCrJ
IUCRJ
IUCrJ, Vol 6, Iss 4, Pp 761-772 (2019)
IUCrJ
Damage-free structures of the resting state of one of the most studied copper nitrite reductases were obtained independently by X-ray free-electron laser (XFEL) and neutron crystallography, representing the first direct comparison of neutron and XFEL
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1ec7e97f0aaa219bbb07ef0b4943ef80
https://epn-library.esrf.fr/flora/jsp/index_view_direct_anonymous.jsp?record=doc:PUB_ILL:28739
https://epn-library.esrf.fr/flora/jsp/index_view_direct_anonymous.jsp?record=doc:PUB_ILL:28739