Zobrazeno 1 - 10
of 19
pro vyhledávání: '"Fangjia, Luo"'
Autor:
Basudev Maity, Mitsuo Shoji, Fangjia Luo, Takanori Nakane, Satoshi Abe, Shigeki Owada, Jungmin Kang, Kensuke Tono, Rie Tanaka, Thuc Toan Pham, Mariko Kojima, Yuki Hishikawa, Junko Tanaka, Jiaxin Tian, Misaki Nagama, Taiga Suzuki, Hiroki Noya, Yuto Nakasuji, Asuka Asanuma, Xinchen Yao, So Iwata, Yasuteru Shigeta, Eriko Nango, Takafumi Ueno
Publikováno v:
Nature Communications, Vol 15, Iss 1, Pp 1-12 (2024)
Abstract Determining short-lived intermediate structures in chemical reactions is challenging. Although ultrafast spectroscopic methods can detect the formation of transient intermediates, real-space structures cannot be determined directly from such
Externí odkaz:
https://doaj.org/article/3cfd85e7dc894b0b8e4ff072dfe8dad1
Publikováno v:
Clinical and Experimental Obstetrics & Gynecology, Vol 50, Iss 10, p 204 (2023)
Background: Uterine corpus endometrial carcinoma (UCEC) is a prevalent gynaecologic malignancy. It has been demonstrated that the immune cell infiltration (ICI) pattern plays a critical role in the tumour progression of UCEC. Methods: To further inve
Externí odkaz:
https://doaj.org/article/96971d97b25441c280c5534c47c9b40f
Autor:
Carrillo, Melissa, Pandey, Suraj, Sanchez, Juan, Noda, Moraima, Poudyal, Ishwor, Aldama, Luis, Malla, Tek Narsingh, Claesson, Elin, Wahlgren, Weixiao Yuan, Feliz, Denisse, Šrajer, Vukica, Maj, Michał, Castillon, Leticia, Iwata, So, Nango, Eriko, Tanaka, Rie, Tanaka, Tomoyuki, Fangjia, Luo, Tono, Kensuke, Owada, Shigeki, Westenhoff, Sebastian, Stojković, Emina A., Schmidt, Marius
Publikováno v:
In Structure 1 July 2021 29(7):743-754
Lipidic cubic phase serial femtosecond crystallography structure of a photosynthetic reaction centre
Autor:
Petra Båth, Analia Banacore, Per Börjesson, Robert Bosman, Cecilia Wickstrand, Cecilia Safari, Robert Dods, Swagatha Ghosh, Peter Dahl, Giorgia Ortolani, Tinna Björg Ulfarsdottir, Greger Hammarin, María-José García Bonete, Adams Vallejos, Lucija Ostojić, Petra Edlund, Johanna-Barbara Linse, Rebecka Andersson, Eriko Nango, Shigeki Owada, Rie Tanaka, Kensuke Tono, Yasumasa Joti, Osamu Nureki, Fangjia Luo, Daniel James, Karol Nass, Philip J. M. Johnson, Gregor Knopp, Dmitry Ozerov, Claudio Cirelli, Christopher Milne, So Iwata, Gisela Brändén, Richard Neutze
Publikováno v:
Acta Crystallographica Section D Structural Biology. 78:698-708
Serial crystallography is a rapidly growing method that can yield structural insights from microcrystals that were previously considered to be too small to be useful in conventional X-ray crystallography. Here, conditions for growing microcrystals of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bb1f5a91eac8f35496a07f4ecfc7a445
https://doi.org/10.1107/s2059798322004144
https://doi.org/10.1107/s2059798322004144
Autor:
Manuel Maestre-Reyna, Cheng-Han Yang, Eriko Nango, Wei-Cheng Huang, Eka Putra Gusti Ngurah Putu, Wen-Jin Wu, Po-Hsun Wang, Sophie Franz-Badur, Martin Saft, Hans-Joachim Emmerich, Hsiang-Yi Wu, Cheng-Chung Lee, Kai-Fa Huang, Yao-Kai Chang, Jiahn-Haur Liao, Jui-Hung Weng, Wael Gad, Chiung-Wen Chang, Allan H. Pang, Michihiro Sugahara, Shigeki Owada, Yuhei Hosokawa, Yasumasa Joti, Ayumi Yamashita, Rie Tanaka, Tomoyuki Tanaka, Fangjia Luo, Kensuke Tono, Kai-Cheng Hsu, Stephan Kiontke, Igor Schapiro, Roberta Spadaccini, Antoine Royant, Junpei Yamamoto, So Iwata, Lars-Oliver Essen, Yoshitaka Bessho, Ming-Daw Tsai
Publikováno v:
Nature Chemistry
Nature Chemistry, 2022, 14 (6), pp.677-685. ⟨10.1038/s41557-022-00922-3⟩
Nature Chemistry, 2022, 14 (6), pp.677-685. ⟨10.1038/s41557-022-00922-3⟩
International audience; Flavin coenzymes are universally found in biological redox reactions. DNA photolyases, with their flavin chromophore (FAD), utilize blue light for DNA repair and photoreduction. The latter process involves two single-electron
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2ab1ccc473a4c1aff447bbd9403e54d0
https://hal.science/hal-03716098
https://hal.science/hal-03716098
Autor:
Xiaohong Liu, Pengcheng Liu, Hongjie Li, Zhen Xu, Lu Jia, Yan Xia, Minling Yu, Wenqin Tang, Xiaolei Zhu, Chao Chen, Yuanlin Zhang, Eriko Nango, Rie Tanaka, Fangjia Luo, Koji Kato, Yoshiki Nakajima, Shunpei Kishi, Huaxin Yu, Naoki Matsubara, Shigeki Owada, Kensuke Tono, So Iwata, Long-Jiang Yu, Jian-Ren Shen, Jiangyun Wang
Publikováno v:
Nature chemistry. 14(9)
One of the primary objectives in chemistry research is to observe atomic motions during reactions in real time. Although X-ray free-electron lasers (XFELs) have facilitated the capture of reaction intermediates using time-resolved serial femtosecond
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bdf7ee0d66ce59311b2e76cc189d14bb
https://pubmed.ncbi.nlm.nih.gov/35851837
https://pubmed.ncbi.nlm.nih.gov/35851837
Autor:
Junken Aoki, Masatoshi Hagiwara, Asuka Inoue, Kunio Hirata, Yuki Shiimura, Shintaro Maeda, Eriko Nango, Masayasu Toyomoto, Nobuo Tanaka, Hidetsugu Asada, Fangjia Luo, So Iwata
Publikováno v:
Science Advances
Active S1PR3 structure reveals the unique ligand-binding mode and signaling selectivity switching mechanism.
Sphingosine-1-phosphate (S1P) regulates numerous important physiological functions, including immune response and vascular integrity, vi
Sphingosine-1-phosphate (S1P) regulates numerous important physiological functions, including immune response and vascular integrity, vi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e7488e5c612954f6b3f1e3ab9ceb9c31
https://pubmed.ncbi.nlm.nih.gov/34108205
https://pubmed.ncbi.nlm.nih.gov/34108205
Akademický článek
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Autor:
Fangjia Luo, Kyoko Shinzawa-Itoh, Satoru Shimada, Shinya Yoshikawa, Kaede Hagimoto, Eiki Yamashita, Atsuhiro Shimada, Tomitake Tsukihara
Publikováno v:
Acta Crystallographica. Section F, Structural Biology Communications
Although the enzymatic activity of cytochrome c oxidase (CcO) depends sensitively on pH over a wide range, X-ray structure analyses of bovine CcO have been conducted using crystals prepared at pH 5.7 owing to difficulty in crystallizing this protein.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::73f8866ac5a60f8c0e2ad2058e1a6458
https://doi.org/10.1107/s2053230x17008834
https://doi.org/10.1107/s2053230x17008834
Akademický článek
Tento výsledek nelze pro nepřihlášené uživatele zobrazit.
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