Výsledky vyhledávání - "Eiji Inagaki"

THE NOVEL SELECTIVE TOLL-LIKE RECEPTOR 4 SIGNAL TRANSDUCTION INHIBITOR TAK-242 PREVENTS ENDOTOXAEMIA IN CONSCIOUS GUINEA-PIGS

Autor: Minoru Kubota, Eiji Inagaki, Kayo Nemoto, Hiroyuki Yokota, Norifumi Ninomiya, Masamune Kuno, Tatsumi Matsumoto

Publikováno v: Clinical and Experimental Pharmacology and Physiology. 36:589-593

1. TAK-242 is a novel compound that suppresses nitric oxide and cytokine production by selectively inhibiting intracellular signals from toll-like receptor (TLR)-4. In the present study, we investigated the effectiveness of TAK-242 against sepsis usi

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https://doi.org/10.1111/j.1440-1681.2008.05121.x

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Structure and implications for the thermal stability of phosphopantetheine adenylyltransferase from Thermus thermophilus

Autor: Fumio Arisaka, Masashi Miyano, Yayoi Fujimoto, Masaki Yamamoto, Seiki Kuramitsu, Hitomi Takahashi, Yuichi Nodake, Eiji Inagaki, Yuki Nakamura, Katsuhide Yutani, Tahir H. Tahirov, Chizu Kuroishi, Shigeyuki Yokoyama

Publikováno v: Acta Cryst.. :97-104

Phosphopantetheine adenylyltransferase (PPAT) is an essential enzyme in bacteria that catalyzes the rate-limiting step in coenzyme A (CoA) biosynthesis by transferring an adenylyl group from ATP to 4'-phosphopantetheine (Ppant), yielding 3'-dephospho

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http://t2r2.star.titech.ac.jp/cgi-bin/publicationinfo.cgi?q_publication_content_number=CTT100389329

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Expression, purification, crystallization and preliminary X-ray diffraction analysis of galactokinase fromPyrococcus horikoshii

Autor: Akeo Shinkai, Takaho Terada, Shigeyuki Yokoyama, Chizu Kuroishi, Eiji Inagaki, Keiko Sakamoto, Naomi Obayashi, Seiki Kuramitsu, Yoshitaka Bessho, Mikako Shirouzu

Publikováno v: Acta Crystallographica Section F Structural Biology and Crystallization Communications. 62:169-171

Galactokinase (EC 2.7.1.6) catalyzes the ATP-dependent phosphorylation of alpha-D-galactose to alpha-D-galactose-1-phosphate, in an additional metabolic branch of glycolysis. The apo-form crystal structure of the enzyme has not yet been elucidated. C

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https://doi.org/10.1107/s1744309106001813

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Novel Renin Inhibitors Containing (2S,3S,5S)-2-Amino-1-cyclohexyl-6-methyl-3,5-heptanediol Fragment as a Transition-state Mimic at the P1-P1' Cleavage Site

Autor: Ikuro Nakamura, Yoshiharu Hayashi, Kiyoteru Ikegami, Itsuo Uchida, Eiji Shirakawa, Koji Ando, Hiroki Tada, Yasuki Yamada, Saizo Shibata, Eiji Inagaki, Yukishige Ikemoto

Publikováno v: Chemical and Pharmaceutical Bulletin. 45:1631-1641

A series of renin inhibitors containing the (2S,3S,5S)-2-amino-1-cyclohexyl-6-methyl-3,5-heptanediol (2-amino-3,5-anti-diol) fragment as a novel transition-state mimic was synthesized, and their biological activities were evaluated. All of the synthe

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https://doi.org/10.1248/cpb.45.1631

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Crystallization and preliminary crystallographic analysis of 2-keto-3-deoxygluconate kinase fromThermus thermophilus

Autor: Maki Kumei, Yasuhiro Kajihara, Yoko Ukita, Tahir H. Tahirov, Eiji Inagaki

Publikováno v: Acta Crystallographica Section D Biological Crystallography. 60:761-763

2-Keto-3-deoxygluconate kinase (KDGK) catalyzes the phosphorylation of 2-keto-3-deoxygluconate (KDG) to 2-keto-3-deoxy-6-phosphogluconate. Two crystal forms of KDGK from Thermus thermophilus were obtained by vapour-diffusion and microbatch methods. C

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https://doi.org/10.1107/s0907444904002665

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X-ray Structure of a Pokeweed Antiviral Protein, Coded by a New Genomic Clone, at 0.23 nm Resolution. A Model Structure Provides a Suitable Electrostatic Field for Substrate Binding

Autor: Jiro Kataoka, Hideaki Tsuge, Eiji Inagaki, Noriyuki Habuka, Masashi Miyano, Hideo Ago, Masana Noma

Publikováno v: European Journal of Biochemistry. 225:369-374

We have determined the crystal structure of alpha-pokeweed antiviral protein, a member of ribosome-inactivating proteins, at 0.23 nm resolution, by the molecular-replacement method. The crystals belong to the space group P2(1)2(1)2 with unit-cell dim

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https://doi.org/10.1111/j.1432-1033.1994.00369.x

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The crystal and molecular structure of β-d-fructofuranosyl α-d-xylopyranoside hemihydrate

Autor: Eiji Inagaki, Tooru Taga, Kouki Fujita, Yoshihiro Fujimori, Kouzou Hara

Publikováno v: Carbohydrate Research. 241:63-69

The crystal and molecular structure of β- d -fructofuranosyl α- d -xylopyranoside (xylosucrose) hemihydrate, C 11 H 20 O 10 ·0.5H 2 O, is orthorhombic, P 2 1 2 1 2, with a = 20.919(5), b = 18.727(2), c = 7.071(1) A, V = 2770.1(2) A 3 , Z = 8, and

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https://doi.org/10.1016/0008-6215(93)80095-v

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New insights into the binding mode of coenzymes: structure of Thermus thermophilus Δ1-pyrroline-5-carboxylate dehydrogenase complexed with NADP+

Autor: Noriyasu Ohshima, Tahir H. Tahirov, Eiji Inagaki, Shigeyuki Yokoyama, Hiroaki Kato, Nigar D. Babayeva, Keiko Sakamoto

Delta(1)-Pyrroline-5-carboxylate dehydrogenase (P5CDh) is known to preferentially use NAD(+) as a coenzyme. The k(cat) value of Thermus thermophilus P5CDh (TtP5CDh) is four times lower for NADP(+) than for NAD(+). The crystal structure of NADP(+)-bou

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https://europepmc.org/articles/PMC2335078/

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Crystal structure of Thermus thermophilus Delta1-pyrroline-5-carboxylate dehydrogenase

Autor: Eiji Inagaki, Shigeyuki Yokoyama, Noriyasu Ohshima, Hitomi Takahashi, Tahir H. Tahirov, Chizu Kuroishi

Publikováno v: Journal of molecular biology. 362(3)

Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDh) plays an important role in the metabolic pathway from proline to glutamate. It irreversibly catalyzes the oxidation of glutamate-gamma-semialdehyde, the product of the non-enzymatic hydrolysis of

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::74b9867fe47d8467722690666eb92549
https://pubmed.ncbi.nlm.nih.gov/16934832

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