Zobrazeno 1 - 10
of 150
pro vyhledávání: '"Tetsutaro, Iizuka"'
Autor:
Yasuyuki Kato-Yamada, R Makino, Yuki Hamajima, Tetsutaro Iizuka, Motonari Tsubaki, Yoshitsugu Shiro, Keisuke Mashima, Yuji Obata
Publikováno v:
Biochemistry. 57:1620-1631
Soluble guanylate cyclase (sGC) is a heme-containing enzyme that catalyzes cGMP production upon sensing NO. While the CO adduct, sGC-CO, is much less active, the allosteric regulator BAY 41-2272 stimulates the cGMP productivity to the same extent as
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2c0b40ac33af765b4996fce486edfb74
https://doi.org/10.1021/acs.biochem.7b01240
https://doi.org/10.1021/acs.biochem.7b01240
Autor:
Tetsutaro Iizuka, Keisuke Mashima, Yuzuru Ishimura, R Makino, Hiroshi Hori, Eiji Obayashi, Yoshitsugu Shiro
Publikováno v:
Biochemistry. 54:3604-3616
L-Tryptophan 2,3-dioxygenase (TDO) is a protoheme-containing enzyme that catalyzes the production of N-formylkynurenine by inserting O₂ into the pyrrole ring of L-tryptophan. Although a ferrous-oxy form (Fe²⁺-O₂) has been established to be an
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::7e1477e17a65a20130019819a0387907
https://doi.org/10.1021/acs.biochem.5b00048
https://doi.org/10.1021/acs.biochem.5b00048
Publikováno v:
Journal of Biological Chemistry. 286:15678-15687
Soluble guanylate cyclase is an NO-sensing hemoprotein that serves as a NO receptor in NO-mediated signaling pathways. It has been believed that this enzyme displays no measurable affinity for O2, thereby enabling the selective NO sensing in aerobic
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::420d1d61bd514bd268e1eabd4b22cdd0
https://doi.org/10.1074/jbc.m110.177576
https://doi.org/10.1074/jbc.m110.177576
Autor:
Ryu, Makino, Eiji, Obayashi, Hiroshi, Hori, Tetsutaro, Iizuka, Keisuke, Mashima, Yoshitsugu, Shiro, Yuzuru, Ishimura
Publikováno v:
Biochemistry. 54(23)
L-Tryptophan 2,3-dioxygenase (TDO) is a protoheme-containing enzyme that catalyzes the production of N-formylkynurenine by inserting O₂ into the pyrrole ring of L-tryptophan. Although a ferrous-oxy form (Fe²⁺-O₂) has been established to be an
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::e048e0da252811ce3b04376824d2d2ee
https://pubmed.ncbi.nlm.nih.gov/25996254
https://pubmed.ncbi.nlm.nih.gov/25996254
Autor:
Yasuhiro Isogai, Manabu Ishida, Naoshi Dohmae, Tetsutaro Iizuka, Yoshitsugu Shiro, Tadatake Oku
Publikováno v:
Biochemistry. 43:9823-9833
Natural c-type cytochromes are characterized by the consensus Cys-X-X-Cys-His heme-binding motif (where X is any amino acid) by which the heme is covalently attached to protein by the addition of the sulfhydryl groups of two cysteine residues to the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d8b2b7e89674ac4a2450433b0b917b0b
https://doi.org/10.1021/bi049546e
https://doi.org/10.1021/bi049546e
Publikováno v:
Proceedings of the National Academy of Sciences. 101:2742-2746
The rhizobial FixL/FixJ system, a paradigm of heme-based oxygen sensors, belongs to the ubiquitous two-component signal transduction system. Oxygen-free (deoxy) FixL is autophosphorylated at an invariant histidine residue by using ATP and catalyzes t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::139ba3a87c6897bf26f0479b9284370f
https://doi.org/10.1073/pnas.0305795101
https://doi.org/10.1073/pnas.0305795101
Autor:
Yoshitsugu Shiro, Eiichi Ito, Tetsutaro Iizuka, Kiyohiro Imai, Hiro Nakamura, Kayako Nakamura, Kaito Hosono, Ken Saito
Publikováno v:
Molecular Microbiology. 48:373-383
The rhizobial FixL/FixJ system, a member of the superfamily of bacterial two-component signal transducing systems, regulates the expression of nitrogen fixation-related genes by sensing environmental oxygen tension. Oxygen-free (deoxy) FixL is autoph
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::5f6ec40d103ed6890d4cb4e0b0337c8d
https://doi.org/10.1046/j.1365-2958.2003.03446.x
https://doi.org/10.1046/j.1365-2958.2003.03446.x
Autor:
Toshihiro Nagamine, Prabhakara V. Choudary, Yu Kawasaki, Keiju Okano, Shogo Matsumoto, Tetsutaro Iizuka
Publikováno v:
Scopus-Elsevier
Signal sequences are evolutionarily conserved and are often functionally interchangeable between prokaryotes and eukaryotes. However, we have found that the bacterial signal peptide, OmpA, functions incompletely in insect cells. Upon baculovirus-medi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b1d3ce9a2258ac8367693b57568e8179
https://doi.org/10.1247/csf.28.131
https://doi.org/10.1247/csf.28.131
Autor:
Tatzuo Ueki, Hideaki Shimizu, Y. Inoue, Yoshitsugu Shiro, Shin-ichi Adachi, T. Oguchi, Sam-Yong Park, Hajime Tanida, Tetsutaro Iizuka, Hideyuki Miyatake, Nobuo Kamiya
Publikováno v:
Nuclear Instruments and Methods in Physics Research Section A: Accelerators, Spectrometers, Detectors and Associated Equipment. :711-714
A SPring-8 bending magnet beamline, the RIKEN structural biology beamline II (BL44B2), is dedicated to monochromatic/Laue macromolecular crystallography and X-ray absorption fine structure studies. The design and the performance of the beamline are p
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::31882495325e9a389d2611295c39037e
https://doi.org/10.1016/s0168-9002(01)00472-7
https://doi.org/10.1016/s0168-9002(01)00472-7
Autor:
Hiro Nakamura, Terumasa Tsuchiya, Sam-Yong Park, Koji Tamura, Yoshitsugu Shiro, Masahiro Mukai, Shin-ichi Adachi, Kayako Nakamura, Hideyuki Miyatake, Tetsutaro Iizuka
Publikováno v:
Journal of Molecular Biology. 301:415-431
FixL of Rhizobium meliloti (RmFixL) is a sensor histidine kinase of the two-component system, which regulates the expression of the genes related to nitrogen fixation in the root nodule in response to the O(2) levels. The crystal structure of the sen
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7ac5dc421bf240e56f678028896a9190
https://doi.org/10.1006/jmbi.2000.3954
https://doi.org/10.1006/jmbi.2000.3954