Zobrazeno 1 - 10
of 11
pro vyhledávání: '"Nobuko Uodome"'
Autor:
Yoshihiro Urade, Nobuko Uodome, Kosuke Aritake, Kohji Yamamoto, Mamoru Suzuki, Atsushi Nakagawa, Akifumi Higashiura, Md. Tofazzal Hossain
Publikováno v:
Biochemical and Biophysical Research Communications. 440:762-767
Prostaglandin E synthase (PGES) catalyzes the isomerization of PGH2 to PGE2. We previously reported the identification and structural characterization of Bombyx mori PGES (bmPGES), which belongs to Sigma-class glutathione transferase. Here, we extend
Autor:
Kohji Yamamoto, Kosuke Aritake, Akifumi Higashiura, Yoshihiro Urade, Atsushi Nakagawa, Nobuko Uodome, Mamoru Suzuki
Publikováno v:
Biochimica et Biophysica Acta (BBA) - General Subjects. 1830:3711-3718
Background Glutathione transferases (GSTs) are members of a major family of detoxification enzymes. Here, we report the crystal structure of a sigma-class GST of Bombyx mori , bmGSTS1, to gain insight into the mechanism catalysis. Methods The structu
Autor:
Nobuo Okazaki, Yuji Kado, Hiroyoshi Matsumura, Kosuke Aritake, Yousuke Okano, Yoshihiro Urade, Tsuyoshi Inoue, Nobuko Uodome
Publikováno v:
Journal of Biochemistry. 151:447-455
In mast and Th2 cells, hematopoietic prostaglandin (PG) D synthase (H-PGDS) catalyses the isomerization of PGH(2) in the presence of glutathione (GSH) to produce the allergic and inflammatory mediator PGD(2). We determined the X-ray structures of hum
Autor:
Nobuko Uodome, Yasushi Kai, Masaki Yamamoto, Tsuyoshi Inoue, Masashi Miyano, Daisuke Irikura, Nobuo Okazaki, Yoshihiro Urade, Hiroyoshi Matsumura, Takashi Kumasaka, Shigehiro Kinugasa
Publikováno v:
Nat. Struct. Biol.. 10:291-296
Here we report the crystal structures of human hematopoietic prostaglandin (PG) D synthase bound to glutathione (GSH) and Ca2+ or Mg2+. Using GSH as a cofactor, prostaglandin D synthase catalyzes the isomerization of PGH2 to PGD2, a mediator for alle
Autor:
Kazue Okazaki-Hatake, Yoshihiro Urade, Nobuko Uodome, Yasushi Fujitani, Yoshihide Kanaoka, Kosuke Aritake
Publikováno v:
The Journal of Immunology. 168:443-449
PGD2 is a major lipid mediator released from mast cells, but little is known about its role in the development of allergic reactions. We used transgenic (TG) mice overexpressing human lipocalin-type PGD synthase to examine the effect of overproductio
Publikováno v:
Gene. 375
Lipocalin-type prostaglandin (PG) D synthase (L-PGDS) is a bifunctional protein possessing both the ability to synthesize PGD(2) and to serve as a carrier protein for lipophilic molecules. L-PGDS has been extensively studied in mammalian species, whe
Autor:
Shigehiro Kinugasa, Yasushi Kai, Kousuke Aritake, Yousuke Okano, Hiroyoshi Matsumura, Yuji Kado, Hideyuki Shishitani, Nobuo Okazaki, Yoshihiro Urade, Daisuke Irikura, Tsuyoshi Inoue, Nobuko Uodome
Publikováno v:
Journal of biochemistry. 135(3)
Hematopoietic prostaglandin (PG) D synthase (H-PGDS) is responsible for the production of PGD(2) as an allergy or inflammation mediator in mast and Th2 cells. We determined the X-ray structure of human H-PGDS complexed with an inhibitor, 2-(2'-benzot
Autor:
Daisaku Ohta, Genji Iwasaki, Kenji Kanaori, Atsuko Ogawa, Atsuko Y. Nosaka, Atsuko Nagai, Nobuko Uodome
Publikováno v:
Scopus-Elsevier
Histidinol dehydrogenase (HDH), a dimeric protein, catalyzes two sequential oxidation reactions to yield L-histidine from L-histidinol via L-histidinal. HDH contains 1 mol of Zn(II) per mol of subunit, and removal of this metal abolishes the enzymati
Autor:
Tsuyoshi Inoue, Daisuke Irikura, Nobuo Okazaki, Shigehiro Kinugasa, Hiroyoshi Matsumura, Nobuko Uodome, Masaki Yamamoto, Takashi Kumasaka, Masashi Miyano, Yasushi Kai, Yoshihiro Urade
Publikováno v:
Nature Structural & Molecular Biology. 10:409-409
Publikováno v:
Prostaglandins & Other Lipid Mediators. 59:229