Zobrazeno 1 - 10
of 32
pro vyhledávání: '"Fusako Takeuchi"'
Publikováno v:
Biochemistry. 57:1611-1619
Nitric oxide synthase (NOS) is a cytochrome P450-type mono-oxygenase that catalyzes the oxidation of l-arginine (Arg) to nitric oxide (NO) through a reaction intermediate N-hydroxy-l-arginine (NHA). The mechanism underlying the reaction catalyzed by
Autor:
Fusako Takeuchi, Tetsunari Kimura, Akikazu Asada, Eri Chatani, Mohammed El Behery, Motonari Tsubaki
Publikováno v:
journal of the Kapisanang Kimika ng Pilipinas. 30(1):1-3
A candidate human tumor suppressor gene 101F6 product was expressed successfully in Pichia pastoris yeast cells. The purified 101F6 protein was successfully incorporated into phospholipid bilayer nanodiscs with different sizes by employing two recons
Publikováno v:
Biochemistry. 57(10)
Nitric oxide synthase (NOS) is a cytochrome P450-type mono-oxygenase that catalyzes the oxidation of l-arginine (Arg) to nitric oxide (NO) through a reaction intermediate N-hydroxy-l-arginine (NHA). The mechanism underlying the reaction catalyzed by
Autor:
Yumiko Seike, Kazuo Kobayashi, Akinori Saeki, Takahiro Kozawa, Motonari Tsubaki, Fusako Takeuchi
Publikováno v:
ChemPhysChem. 15:2994-2997
The dynamics of free-radical species in a model cellular system are examined by measuring the formation and decay of ascorbate radicals within a liposome with pulse radiolysis techniques. Upon pulse radiolysis of an N2O-saturated aqueous solution con
Autor:
Fusako Takeuchi, Md. Motiur Rahman, Motonari Tsubaki, Yoichi Sakamoto, Mariam C. Recuenco, Hiroshi Hori
Publikováno v:
The Journal of Biochemistry. 153:233-242
Candidate human tumour suppressor gene product, 101F6 protein, is a highly hydrophobic transmembrane protein and a member of cytochrome b(561) family. Purified 101F6 protein expressed in Pichia pastoris cells showed visible absorption spectra similar
Publikováno v:
Journal of Bioscience and Bioengineering. 113:322-331
A group of membrane proteins having a single COOH-terminal hydrophobic domain capable of post-translational insertion into lipid bilayer is known as tail-anchored (TA) proteins. To clarify the insertion mechanism of the TA-domain of human cytochrome
Publikováno v:
Journal of Bioscience and Bioengineering. 108:286-292
Well-conserved three consecutive Pro residues (Pro247-249) in the NADH-binding subdomain of NADH-cytochrome b(5) reductase were proposed to form a basal part of the NADH-binding site. To investigate the structural and mechanistic roles of these resid
Autor:
Fusako Takeuchi, Md. Motiur Rahman, Motonari Tsubaki, Nobuyuki Nakanishi, Yoichi Sakamoto, Masahiro Miura, Sam-Yong Park
Publikováno v:
Journal of Biochemistry. 146:857-866
Cytochromes b(561) constitute a novel class of proteins in eukaryotic cells with a number of highly relevant common features including six transmembrane alpha-helices and two haem groups. Of particular interest is the presence of a large number of pl
Autor:
Mariam C, Recuenco, Masamitsu, Fujito, Md Motiur, Rahman, Yoichi, Sakamoto, Fusako, Takeuchi, Motonari, Tsubaki
Publikováno v:
BioFactors. 34:219-230
A highly hydrophobic protein with six transmembrane structure that is coded by the candidate tumor suppressor gene 101F6 located in the human chromosome 3p.21.3 and a possible member of the cytochrome b 561 protein family was expressed, purified, and
Publikováno v:
Journal of Biochemistry. 142:553-560
Cytochromes b(561) are a family of transmembrane proteins found in most eukaryotic cells and contain two haem b prosthetic groups per molecule being coordinated with four His residues from four different transmembrane alpha-helices. Although cytochro