Zobrazeno 1 - 10
of 21
pro vyhledávání: '"Ju Yaen Kim"'
Autor:
Ju Yaen Kim1, Masato Nakayama1, Hiroshi Toyota1, Genji Kurisu2 gkurisu@protein.osaka-u.ac.jp, Toshiharu Hase1 enzyme@protein.osaka-u.ac.jp
Publikováno v:
Journal of Biochemistry. Aug2016, Vol. 160 Issue 2, p101-109. 9p.
Autor:
Ryota Mizushima, Ju Yaen Kim, Isao Suetake, Hiroaki Tanaka, Tomoyo Takai, Narutoshi Kamiya, Yu Takano, Yuichi Mishima, Shoji Tajima, Yuji Goto, Kenji Fukui, Young-Ho Lee
Publikováno v:
PLoS ONE, Vol 9, Iss 6, p e98554 (2014)
MutL is a multi-domain protein comprising an N-terminal ATPase domain (NTD) and C-terminal dimerization domain (CTD), connected with flexible linker regions, that plays a key role in DNA mismatch repair. To expand understanding of the regulation mech
Externí odkaz:
https://doaj.org/article/aca89f16ab304fe4bed2c0498c10bed4
Autor:
Takahisa Ikegami, Yuji Goto, Young-Ho Lee, Toshiharu Hase, John E. Ladbury, Chojiro Kojima, Genji Kurisu, Ju Yaen Kim, Toshihiko Sugiki, Misaki Kinoshita, Hanke Gt, Satoshi Kume
Publikováno v:
Europe PubMed Central
Although electrostatic interactions between negatively charged ferredoxin (Fd) and positively charged sulfite reductase (SiR) have been predominantly highlighted to characterize complex formation, the detailed nature of intermolecular forces remains
Autor:
Satoshi Kume, Genji Kurisu, Takahisa Ikegami, Yoko Kimata-Ariga, Chojiro Kojima, Misaki Kinoshita, Toshiharu Hase, Toshihiko Sugiki, Yukiko Sakakibara, Young-Ho Lee, Ju Yaen Kim
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1847:1200-1211
Although acidic residues of ferredoxin (Fd) are known to be essential for activities of various Fd-dependent enzymes, including ferredoxin NADP+ reductase (FNR) and sulfite reductase (SiR), through electrostatic interactions with basic residues of pa
Autor:
Misaki, Kinoshita, Ju Yaen, Kim, Satoshi, Kume, Yuxi, Lin, K Hun, Mok, Yosky, Kataoka, Koichiro, Ishimori, Natalia, Markova, Genji, Kurisu, Toshiharu, Hase, Young-Ho, Lee
Publikováno v:
Biochemical and biophysical research communications. 482(4)
In spite of a number of studies to characterize ferredoxin (Fd):ferredoxin NADP
Publikováno v:
Methods in molecular biology (Clifton, N.J.). 1498
Mutations in proteins often affect interactions with partner molecules, sequentially changing their activities and functions. In order to examine mutagenic effects, we herein describe practical and detailed protocols for enzymatic activity assays usi
Publikováno v:
Methods in Molecular Biology ISBN: 9781493964703
Mutations in proteins often affect interactions with partner molecules, sequentially changing their activities and functions. In order to examine mutagenic effects, we herein describe practical and detailed protocols for enzymatic activity assays usi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::467e4f628d8797a04f51d211e8986077
https://doi.org/10.1007/978-1-4939-6472-7_30
https://doi.org/10.1007/978-1-4939-6472-7_30
Publikováno v:
Journal of biochemistry. 160(2)
The structure of the complex of maize sulfite reductase (SiR) and ferredoxin (Fd) has been determined by X-ray crystallography. Co-crystals of the two proteins prepared under different conditions were subjected to the diffraction analysis and three p
Publikováno v:
Proceedings of the International Plant Sulfur Workshop ISBN: 9783319201368
Sulfite reductase (SiR) catalyzes the reduction of sulfite to sulfide by using six electrons transported from ferredoxin (Fd) for eventual sulfur assimilation. As efficient electron flows are ensured by forming a productive Fd:SiR complex, detailed c
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::fb60627c057290e6e0d03d315342d721
https://doi.org/10.1007/978-3-319-20137-5_17
https://doi.org/10.1007/978-3-319-20137-5_17
Autor:
Ju Yaen Kim, Misaki Kinoshita, Satoshi Kume, Hanke, G. T., Toshihiko Sugiki, Ladbury, John E., Chojiro Kojima, Takahisa Ikegami, Genji Kurisu, Yuji Goto, Toshiharu Hase, Young-Ho Lee
Publikováno v:
Biochemical Journal; 11/1/2016, Vol. 473 Issue 21, p3837-3854, 18p