Search Results - "Murakawa, Takeshi"

Restriction of Flaviviruses by an Interferon-Stimulated Gene SHFL/C19orf66 by Suzuki, Youichi, Murakawa, Takeshi

“…Flaviviruses (the genus of the family) include many arthropod-borne viruses, often causing life-threatening diseases in humans, such as hemorrhaging and…”
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Molecular mechanism of a large conformational change of the quinone cofactor in the semiquinone intermediate of bacterial copper amine oxidase by Shoji, Mitsuo, Murakawa, Takeshi, Nakanishi, Shota, Boero, Mauro, Shigeta, Yasuteru, Hayashi, Hideyuki, Okajima, Toshihide

“…Copper amine oxidase from Arthrobacter globiformis (AGAO) catalyses the oxidative deamination of primary amines via a large conformational change of a…”
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Identification of the corticotropin-releasing factor receptor 1 antagonists as inhibitors of Chikungunya virus replication using a Gaussia luciferase–expressing subgenomic replicon by Watanabe, Yasuo, Suzuki, Youichi, Emi, Akino, Murakawa, Takeshi, Hishiki, Takayuki, Kato, Fumihiro, Sakaguchi, Shoichi, Wu, Hong, Yano, Takato, Lim, Chang-Kweng, Takasaki, Tomohiko, Nakano, Takashi

“…The Chikungunya virus (CHIKV), an enveloped RNA virus that has been identified in over 40 countries and is considered a growing threat to public health…”
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Serial femtosecond X‐ray crystallography of an anaerobically formed catalytic intermediate of copper amine oxidase by Murakawa, Takeshi, Suzuki, Mamoru, Fukui, Kenji, Masuda, Tetsuya, Sugahara, Michihiro, Tono, Kensuke, Tanaka, Tomoyuki, Iwata, So, Nango, Eriko, Yano, Takato, Tanizawa, Katsuyuki, Okajima, Toshihide

“…The mechanisms by which enzymes promote catalytic reactions efficiently through their structural changes remain to be fully elucidated. Recent progress in…”
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A Lynch syndrome-associated mutation at a Bergerat ATP-binding fold destabilizes the structure of the DNA mismatch repair endonuclease MutL by Izuhara, Keisuke, Fukui, Kenji, Murakawa, Takeshi, Baba, Seiki, Kumasaka, Takashi, Uchiyama, Kazuhisa, Yano, Takato

“…In humans, mutations in genes encoding homologs of the DNA mismatch repair endonuclease MutL cause a hereditary cancer that is known as Lynch syndrome. Here,…”
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Crystal structure of a nucleotide-binding domain of fatty acid kinase FakA from Thermus thermophilus HB8 by Nakatani, Maya, Nakahara, Shun-ya, Fukui, Kenji, Urano, Momoka, Fujii, Yuki, Murakawa, Takeshi, Baba, Seiki, Kumasaka, Takashi, Okanishi, Hiroki, Kanai, Yoshikatsu, Yano, Takato, Masui, Ryoji

“…[Display omitted] •Fatty acid kinase consists of a kinase FakA and a substrate-binding component FakB.•The crystal structure of the N-terminal domain of FakA…”
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Unique protonation states of aspartate and topaquinone in the active site of copper amine oxidase by Shoji, Mitsuo, Murakawa, Takeshi, Boero, Mauro, Shigeta, Yasuteru, Hayashi, Hideyuki, Okajima, Toshihide

“…The oxidative deamination of biogenic amines, crucial in the metabolism of a wealth of living organisms, is catalyzed by copper amine oxidases (CAOs). In this…”
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Reaction of threonine synthase with the substrate analogue 2-amino-5-phosphonopentanoate: implications into the proton transfer at the active site by Machida, Yasuhiro, Murakawa, Takeshi, Sakai, Akiko, Shoji, Mitsuo, Shigeta, Yasuteru, Hayashi, Hideyuki

“…Threonine synthase catalyses the conversion of O-phospho-l-homoserine and a water molecule to l-threonine and has the most complex catalytic mechanism among…”
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Neutron crystallography of copper amine oxidase reveals keto/enolate interconversion of the quinone cofactor and unusual proton sharing by Murakawa, Takeshi, Kurihara, Kazuo, Shoji, Mitsuo, Shibazaki, Chie, Sunami, Tomoko, Tamada, Taro, Yano, Naomine, Yamada, Taro, Kusaka, Katsuhiro, Suzuki, Mamoru, Shigeta, Yasuteru, Kuroki, Ryota, Hayashi, Hideyuki, Yano, Takato, Tanizawa, Katsuyuki, Adachi, Motoyasu, Okajima, Toshihide

“…Recent advances in neutron crystallographic studies have provided structural bases for quantum behaviors of protons observed in enzymatic reactions. Thus, we…”
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Re-evaluation of protein neutron crystallography with and without X-ray/neutron joint refinement by Murakawa, Takeshi, Kurihara, Kazuo, Adachi, Motoyasu, Kusaka, Katsuhiro, Tanizawa, Katsuyuki, Okajima, Toshihide

“…Protein neutron crystallography is a powerful technique to determine the positions of H atoms, providing crucial biochemical information such as the…”
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Molecular Mechanism of the Reaction Specificity in Threonine Synthase: Importance of the Substrate Conformations by Ujiie, Yuzuru, Tanaka, Wataru, Hanaoka, Kyohei, Harada, Ryuhei, Kayanuma, Megumi, Shoji, Mitsuo, Murakawa, Takeshi, Ishida, Toyokazu, Shigeta, Yasuteru, Hayashi, Hideyuki

“…Threonine synthase (ThrS) catalyzes the final chemical reaction of l-threonine biosynthesis from its precursor, O-phospho-l-homoserine. As the phosphate ion…”
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Boundary of the Nucleotide-Binding Domain of Streptococcus ComA Based on Functional and Structural Analysis by Ishii, Seiji, Yano, Takato, Okamoto, Akihiro, Murakawa, Takeshi, Hayashi, Hideyuki

“…The ATP-binding cassette (ABC) transporter ComA is a key molecule essential for the first step of the quorum-sensing system of Streptococcus. The nucleotide…”
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Microcrystal preparation for serial femtosecond X‐ray crystallography of bacterial copper amine oxidase by Murakawa, Takeshi, Suzuki, Mamoru, Arima, Toshi, Sugahara, Michihiro, Tanaka, Tomoyuki, Tanaka, Rie, Iwata, So, Nango, Eriko, Tono, Kensuke, Hayashi, Hideyuki, Fukui, Kenji, Yano, Takato, Tanizawa, Katsuyuki, Okajima, Toshihide

“…Recent advances in serial femtosecond X‐ray crystallography (SFX) using X‐ray free‐electron lasers have paved the way for determining radiation‐damage‐free…”
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Product-assisted Catalysis as the Basis of the Reaction Specificity of Threonine Synthase by Murakawa, Takeshi, Machida, Yasuhiro, Hayashi, Hideyuki

“…Threonine synthase (TS), which is a pyridoxal 5′-phosphate (PLP)-dependent enzyme, catalyzes the elimination of the γ-phosphate group from…”
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Structural insights into the substrate specificity of bacterial copper amine oxidase obtained by using irreversible inhibitors by Murakawa, Takeshi, Hayashi, Hideyuki, Taki, Masayasu, Yamamoto, Yukio, Kawano, Yoshiaki, Tanizawa, Katsuyuki, Okajima, Toshihide

“…Copper amine oxidases (CAOs) catalyse the oxidation of various aliphatic amines to the corresponding aldehydes, ammonia and hydrogen peroxide. Although CAOs…”
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Kinetic and Structural Studies on the Catalytic Role of the Aspartic Acid Residue Conserved in Copper Amine Oxidase by Chiu, Yen-Chen, Okajima, Toshihide, Murakawa, Takeshi, Uchida, Mayumi, Taki, Masayasu, Hirota, Shun, Kim, Misa, Yamaguchi, Hiroshi, Kawano, Yoshiaki, Kamiya, Nobuo, Kuroda, Shun'ichi, Hayashi, Hideyuki, Yamamoto, Yukio, Tanizawa, Katsuyuki

“…Copper amine oxidase contains a post-translationally generated quinone cofactor, topa quinone (TPQ), which mediates electron transfer from the amine substrate…”
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Reinvestigation of Metal Ion Specificity for Quinone Cofactor Biogenesis in Bacterial Copper Amine Oxidase by Okajima, Toshihide, Kishishita, Sei'ichiro, Chiu, Yen-Chen, Murakawa, Takeshi, Kim, Misa, Yamaguchi, Hiroshi, Hirota, Shun, Kuroda, Shun'ichi, Tanizawa, Katsuyuki

“…The topa quinone (TPQ) cofactor of copper amine oxidase is generated by copper-assisted self-processing of the precursor protein. Metal ion specificity for TPQ…”
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dUTP pyrophosphatases from hyperthermophilic eubacterium and archaeon: Structural and functional examinations on the suitability for PCR application by Fukui, Kenji, Kondo, Naoyuki, Murakawa, Takeshi, Baba, Seiki, Kumasaka, Takashi, Yano, Takato

“…Deoxyuridine triphosphate pyrophosphatase (DUT) suppresses incorporation of uracil into genomic DNA during replication. Thermostable DUTs from…”
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Cloning of cold-active alkaline phosphatase gene of a psychrophile, Shewanella sp., and expression of the recombinant enzyme by Murakawa, T. (Kobe Univ. (Japan). Faculty of Agriculture), Yamagata, H, Tsuruta, H, Aizono, Y

“…A psychrophilic alkaline phosphatase (EC 3.1.3.1) from Shewanella sp. is a cold-active enzyme that has high catalytic activity at low temperature [Ishida et…”
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Structural and functional insights into the mechanism by which MutS2 recognizes a DNA junction by Fukui, Kenji, Inoue, Masao, Murakawa, Takeshi, Baba, Seiki, Kumasaka, Takashi, Yano, Takato

“…MutS family proteins are classified into MutS-I and -II lineages: MutS-I recognizes mismatched DNA and initiates mismatch repair, whereas MutS-II recognizes…”
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