Zobrazeno 1 - 10
of 105
pro vyhledávání: '"Masaru Goto"'
Publikováno v:
Journal of Enzyme Inhibition and Medicinal Chemistry, Vol 38, Iss 1 (2023)
Ricin toxin A chain (RTA), from Ricinus communis, is a deadly protein that inactivates ribosomes by degrading an adenine residue at position 4324 in 28S rRNA. Recently, we have demonstrated that pterin-7-carboxamides with peptide pendants were potent
Externí odkaz:
https://doaj.org/article/e032e04e7fd74899b46396c48dd1ad16
Autor:
Tatsuya Kubota, Erika Kurihara, Kazuya Watanabe, Kohei Ogata, Ryosuke Kaneko, Masaru Goto, Toshihisa Ohshima, Kazuaki Yoshimune
Publikováno v:
Communications Biology, Vol 5, Iss 1, Pp 1-7 (2022)
Heat-induced maturation of homoserine dehydrogenase from a hyperthermophilic archaeon requires conformational changes within the catalytic region.
Externí odkaz:
https://doaj.org/article/13843f348b5b4fd6bf590f12efb216a5
Autor:
Ryota Saito, Masaru Goto, Shun Katakura, Taro Ohba, Rena Kawata, Kazuki Nagatsu, Shoko Higashi, Kaede Kurisu, Kaori Matsumoto, Kouta Ohtsuka
Publikováno v:
PLoS ONE, Vol 17, Iss 12, p e0277770 (2022)
The Ricin toxin A chain (RTA), which depurinates an adenine base at a specific region of the ribosome leading to death, has two adjacent specificity pockets in its active site. Based on this structural information, many attempts have been made to dev
Externí odkaz:
https://doaj.org/article/fdb3451072e8499da9cac41061bfd8f7
Autor:
Yuki Hirato, Masaru Goto, Taichi Mizobuchi, Hisashi Muramatsu, Minoru Tanigawa, Katsushi Nishimura
Publikováno v:
Acta Crystallographica Section F Structural Biology Communications. 79:31-37
D-Threonine aldolase (DTA) is a pyridoxal-5′-phosphate-dependent enzyme which catalyzes the reversible aldol reaction of glycine with a corresponding aldehyde to yield the D-form β-hydroxy-α-amino acid. This study produced and investigated the cr
Autor:
Masaru Goto, Shoko Higashi, Taro Ohba, Rena Kawata, Kazuki Nagatsu, Saori Suzuki, Eric V. Anslyn, Ryota Saito
Publikováno v:
Biochemical and biophysical research communications. 627
Ricin toxin A-chain (RTA), a toxic protein from Ricinus communis, inactivates ribosomes to induce toxicity. The active site of RTA consists of two binding pockets. Many studies have focused on developing RTA inhibitors that can simultaneously bind to
Autor:
Ryo Matsumoto, Hidenori Yoshimura, Masaaki Otsu, Takuya Miura, Masato Okada, Masaru Goto, Takayuki Muranaka
Publikováno v:
Journal of the Japan Society for Technology of Plasticity. 61:167-174
Autor:
Shohei Noda, Kazunobu Matsushita, Masaru Goto, Yuki Hodoya, Toshiharu Yakushi, Minenosuke Matsutani, Osao Adachi, Thuy Minh Nguyen, Naoya Kataoka
Publikováno v:
J Bacteriol
Gluconobacter sp. strain CHM43 oxidizes mannitol to fructose and then oxidizes fructose to 5-keto-d-fructose (5KF) in the periplasmic space. Since NADPH-dependent 5KF reductase was found in the soluble fraction of Gluconobacter spp., 5KF might be tra
Autor:
Toshiya Komatsu, Maiko Noumi, Ryota Saito, Masaru Goto, Shoko Higashi, Kana Ishibashi, Sota Uno, Shunsuke Kuwahara
Publikováno v:
Chemical and Pharmaceutical Bulletin. 67:556-565
Aldose reductase (AR) is associated with the onset of diabetic complications. Botryllazine A and its analogues were synthesized and evaluated for human AR inhibitory activity. Analogues possessing aromatic bicyclic systems at the C5 position of the c
Autor:
Yuki Hirato, Yuya Shimekake, Hideyuki Suzuki, Shouji Takahashi, Masaru Goto, Takehiro Furuichi, Yoshio Kera, Rikako Funabashi, Sayoko Okazaki
Publikováno v:
Acta Crystallogr F Struct Biol Commun
D-Amino-acid oxidases (DAAOs) catalyze the oxidative deamination of neutral and basic D-amino acids. The DAAO from the thermophilic fungus Rasamsonia emersonii strain YA (ReDAAO) has a high thermal stability and a unique broad substrate specificity t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fcfd6b07c2f1363acc033d69a1c585f8
https://europepmc.org/articles/PMC7605106/
https://europepmc.org/articles/PMC7605106/
Autor:
Kohei Ogata, Sanenori Nakamura, Toshihisa Ohshima, Yui Yajima, Masaru Goto, Ryosuke Kaneko, Kazuaki Yoshimune
Publikováno v:
Scientific Reports, Vol 8, Iss 1, Pp 1-8 (2018)
Scientific Reports
Scientific Reports
Homoserine dehydrogenase (EC 1.1.1.3, HSD) is an important regulatory enzyme in the aspartate pathway, which mediates synthesis of methionine, threonine and isoleucine from aspartate. Here, HSD from the hyperthermophilic archaeon Sulfolobus tokodaii