Zobrazeno 1 - 10
of 154
pro vyhledávání: '"Ryoji Masui"'
Publikováno v:
PLoS ONE, Vol 15, Iss 5, p e0233689 (2020)
Nucleoside monophosphate kinases play crucial roles in biosynthesis and regeneration of nucleotides. These are bi-substrate enzymes that catalyze reversible transfers of a phosphoryl group between ATP and nucleoside monophosphate. These enzymes are c
Externí odkaz:
https://doaj.org/article/42541a1dc07a4dc885da31c5c9876a0a
Publikováno v:
Biochemistry and Biophysics Reports, Vol 11, Iss C, Pp 93-98 (2017)
Uridine-cytidine kinase (UCK), including human UCK2, are a family of enzymes that generally phosphorylate both uridine and cytidine. However, UCK of Thermus thermophilus HB8 (ttCK) phosphorylates only cytidine. This cytidine-restricted activity is th
Externí odkaz:
https://doaj.org/article/97a4f10538ea4a398534fce516e2fd6c
Publikováno v:
PLoS ONE, Vol 6, Iss 4, p e19053 (2011)
Oxidative stress generates harmful reactive oxygen species (ROS) that attack biomolecules including DNA. In living cells, there are several mechanisms for detoxifying ROS and repairing oxidatively-damaged DNA. In this study, transcriptomic analyses c
Externí odkaz:
https://doaj.org/article/59657e6664444af384c15db9dd08e7e1
Autor:
Rihito Morita, Shuhei Nakane, Atsuhiro Shimada, Masao Inoue, Hitoshi Iino, Taisuke Wakamatsu, Kenji Fukui, Noriko Nakagawa, Ryoji Masui, Seiki Kuramitsu
Publikováno v:
Journal of Nucleic Acids, Vol 2010 (2010)
DNA is subjected to many endogenous and exogenous damages. All organisms have developed a complex network of DNA repair mechanisms. A variety of different DNA repair pathways have been reported: direct reversal, base excision repair, nucleotide excis
Externí odkaz:
https://doaj.org/article/90b4101dbbbb49a3883e71b9b2888b93
Autor:
Yusuke Fujino, Hiroki Okanishi, Masao Inoue, Yoshikatsu Kanai, Takero Miyagawa, Ryoji Masui, Masayuki Torii, Yuki Fujii
Publikováno v:
FEBS Letters. 595:264-274
Thermophilic proteins maintain their structure at high temperatures through a combination of various factors. Here, we report the ligand-induced stabilization of a thermophilic Ser/Thr protein kinase. Thermus thermophilus TpkD unfolds completely at 5
Autor:
Akihide Yoshihara, Yota Takamatsu, Susumu Mochizuki, Hiromi Yoshida, Ryoji Masui, Ken Izumori, Shigehiro Kamitori
Publikováno v:
Applied microbiology and biotechnology. 107(1)
Transketolase is a key enzyme in the pentose phosphate pathway in all organisms, recognizing sugar phosphates as substrates. Transketolase with a cofactor of thiamine pyrophosphate catalyzes the transfer of a 2-carbon unit from D-xylulose-5-phosphate
Autor:
Maya Nakatani, Shun-ya Nakahara, Kenji Fukui, Momoka Urano, Yuki Fujii, Takeshi Murakawa, Seiki Baba, Takashi Kumasaka, Hiroki Okanishi, Yoshikatsu Kanai, Takato Yano, Ryoji Masui
Publikováno v:
Journal of Structural Biology. 214:107904
Fatty acid kinase is necessary for the incorporation of exogenous fatty acids into membrane phospholipids. Fatty acid kinase consists of two components: a kinase component, FakA, that phosphorylates a fatty acid bound to a fatty acid-binding componen
Publikováno v:
PLoS ONE
PLoS ONE, Vol 15, Iss 5, p e0233689 (2020)
PLoS ONE, Vol 15, Iss 5, p e0233689 (2020)
Nucleoside monophosphate kinases play crucial roles in biosynthesis and regeneration of nucleotides. These are bi-substrate enzymes that catalyze reversible transfers of a phosphoryl group between ATP and nucleoside monophosphate. These enzymes are c
Publikováno v:
Biochemistry and Biophysics Reports
Biochemistry and Biophysics Reports, Vol 11, Iss C, Pp 93-98 (2017)
Biochemistry and Biophysics Reports, Vol 11, Iss C, Pp 93-98 (2017)
Uridine-cytidine kinase (UCK), including human UCK2, are a family of enzymes that generally phosphorylate both uridine and cytidine. However, UCK of Thermus thermophilus HB8 (ttCK) phosphorylates only cytidine. This cytidine-restricted activity is th
Autor:
Jin Inoue, Yuya Nishida, Yutaka Ito, Teppei Ikeya, Yasunori Shintani, Seiji Takashima, Tsutomu Mikawa, Ryoji Masui, Seiki Kuramitsu
Publikováno v:
Biochemistry and Biophysics Reports
In prokaryotic cells, genomic DNA forms an aggregated structure with various nucleoid-associated proteins (NAPs). The functions of genomic DNA are cooperatively modulated by NAPs, of which HU is considered to be one of the most important. HU binds do