Initialising ...
Initialising ...
Initialising ...
Initialising ...
Initialising ...
Initialising ...
Initialising ...
Tamii, Atsushi*; Pellegri, L.*; S
derstrm, P.-A.*; Allard, D.*; Goriely, S.*; Inakura, Tsunenori*; Khan, E.*; Kido, Eiji*; Kimura, Masaaki*; Litvinova, E.*; et al.
European Physical Journal A, 59(9), p.208_1 - 208_21, 2023/09
Times Cited Count：1 Percentile：0.02(Physics, Nuclear)no abstracts in English
Sakurai, Yosuke*; Sato, Hirotaka*; Adachi, Nozomu*; Morooka, Satoshi; Todaka, Yoshikazu*; Kamiyama, Takashi*
Applied Sciences (Internet), 11(11), p.5219_1 - 5219_17, 2021/06
Times Cited Count：3 Percentile：30.84(Chemistry, Multidisciplinary)Suzuki, Shintaro*; Takubo, Ko*; Kuga, Kentaro*; Higemoto, Wataru; Ito, Takashi; Tomita, Takahiro*; Shimura, Yasumichi*; Matsumoto, Yosuke*; Bareille, C.*; Wadachi, Hiroki*; et al.
Physical Review Research (Internet), 3(2), p.023140_1 - 023140_12, 2021/05
We report our experimental discovery of the transition temperature reaching 20 K in a Yb-based compound at ambient pressure. The Mn substitution at the Al site in an intermediate valence state of 
-YbAlB
not only induces antiferromagnetic transition at a record high temperature of 20 K but also transforms the heavy-fermion liquid state in -YbAlB into a highly resistive metallic state proximate to a Kondo insulator.
Sato, Hirotaka*; Shiota, Yoshinori*; Morooka, Satoshi; Todaka, Yoshikazu*; Adachi, Nozomu*; Sadamatsu, Sunao*; Oikawa, Kenichi; Harada, Masahide; Zhang, S.*; Su, Y. H.; et al.
Journal of Applied Crystallography, 50(6), p.1601 - 1610, 2017/12
Times Cited Count：17 Percentile：79.13(Chemistry, Multidisciplinary)Uchida, Kenichi*; Adachi, Hiroto; Kikkawa, Takashi*; Kirihara, Akihiro*; Ishida, Masahiko*; Yorozu, Shinichi*; Maekawa, Sadamichi; Saito, Eiji*
Proceedings of the IEEE, 104(10), p.1946 - 1973, 2016/10
Times Cited Count：213 Percentile：99.2(Engineering, Electrical & Electronic)Ramos, R.*; Kikkawa, Takashi*; Aguirre, M.*; Lucas, I.*; Anad
n, A.*; Oyake, Takafumi*; Uchida, Kenichi*; Adachi, Hiroto; Shiomi, Junichiro*; Algarabel, P. A.*; et al.
Physical Review B, 92(22), p.220407_1 - 220407_5, 2015/12
Times Cited Count：69 Percentile：90.84(Materials Science, Multidisciplinary)Adachi, Taihei*; Ikedo, Yutaka*; Nishiyama, Kusuo*; Yabuuchi, Atsushi*; Nagatomo, Takashi*; Strasser, P.*; Ito, Takashi; Higemoto, Wataru; Kojima, Kenji*; Makimura, Shunsuke*; et al.
JPS Conference Proceedings (Internet), 8, p.036017_1 - 036017_4, 2015/09
Kikkawa, Takashi*; Uchida, Kenichi*; Daimon, Shunsuke*; Shiomi, Yuki*; Adachi, Hiroto; Qiu, Z.*; Hou, D.*; Jin, X.-F.*; Maekawa, Sadamichi; Saito, Eiji
Physical Review B, 88(21), p.214403_1 - 214403_11, 2013/12
Times Cited Count：122 Percentile：96.1(Materials Science, Multidisciplinary)Kuno, Yusuke; Tazaki, Makiko; Akiba, Mitsunori*; Adachi, Takeo*; Takashima, Ryuta*; Izumi, Yoshinori*; Tanaka, Satoru*
Proceedings of International Nuclear Fuel Cycle Conference; Nuclear Energy at a Crossroads (GLOBAL 2013) (CD-ROM), p.965 - 974, 2013/09
Multilateral Nuclear Approach (MNA) provides services on the frontend and the backend to the states possessing nuclear power plants with nuclear non-proliferation measures and without interfering with the inalienable right in NPT may be one of the most effective and efficient manners for peaceful use of nuclear energy. Recent MNA discussions tend to focus on reliable fuel supply, namely front-end of NFC, where proliferation of uranium enrichment can be deterred. At the same time, the MNA capability to provide assurance/service that the Spent Fuel be managed properly is actually more important. In this work a regional MNA framework was studied to fulfil the above mentioned points.
Kuno, Yusuke; Tazaki, Makiko; Akiba, Mitsunori*; Adachi, Takeo*; Takashima, Ryuta*; Tanaka, Satoru*
Proceedings of INMM 54th Annual Meeting (CD-ROM), 10 Pages, 2013/07
This paper presents a specific proposal of Asian regional MNA framework as the final result of our study. The target facilities include frontend and backend, especially, enrichment, reprocessing, MOX fabrication / storage and Spent Fuel storage facilities.
Kuno, Yusuke; Tazaki, Makiko; Akiba, Mitsunori*; Adachi, Takeo*; Takashima, Ryuta*; Tanaka, Satoru*
Proceedings of INMM 54th Annual Meeting (CD-ROM), 10 Pages, 2013/07
This paper discusses the evaluation result for proposed Asian regional MNA framework.
Nagai, Yasuki; Hashimoto, Kazuyuki; Hatsukawa, Yuichi; Saeki, Hideya; Motoishi, Shoji; Sonoda, Nozomi; Kawabata, Masako; Harada, Hideo; Kin, Tadahiro*; Tsukada, Kazuaki; et al.
Journal of the Physical Society of Japan, 82(6), p.064201_1 - 064201_7, 2013/06
Times Cited Count：43 Percentile：85.02(Physics, Multidisciplinary)
O
thin filmsRamos, R.*; Kikkawa, Takashi*; Uchida, Kenichi*; Adachi, Hiroto; Lucas, I.*; Aguirre, M.*; Algarabel, P.*; Morelln, L.*; Maekawa, Sadamichi; Saito, Eiji; et al.
Applied Physics Letters, 102(7), p.072413_1 - 072413_5, 2013/02
Times Cited Count：157 Percentile：97.29(Physics, Applied)Kuno, Yusuke; Tazaki, Makiko; Akiba, Mitsunori*; Adachi, Takeo*; Takashima, Ryuta*; Omoto, Akira*; Oda, Takuji*; Choi, J.-S.*; Tanaka, Satoru*
Proceedings of INMM 53rd Annual Meeting (CD-ROM), 10 Pages, 2012/07
This paper will present brief historical review of multilateral nuclear approach (MNA), and based on which, a basic concept of a reliable framework of nuclear fuel cycle, where the fuel-cycle services could be provided without discrimination and meet the international 3S requirements, is discussed.
Kosaka, Nami*; Sugai, Tatsuhisa*; Nagasawa, Kazumichi*; Tanizaki, Yuta*; Meguro, Mizue; Aizawa, Yoichi*; Maekawa, Shun*; Adachi, Motoyasu; Kuroki, Ryota; Kato, Takashi
Journal of Experimental Biology, 214(6), p.921 - 927, 2011/03
Times Cited Count：29 Percentile：70.4(Biology)Oxygen is essential for the survival of animals. Red blood cells are responsible for transporting oxygen to tissues. We established a semi-solid colony forming assay, and showed that recombinant xlEPO induces erythroid colony formation in vitro and detected an increased level of erythropoietin activity in blood serum during acute anemic stress. In addition, the study demonstrated the possible presence of multiple, non-xlEPO, factors in anemic serum supportive of erythroid colony formation. These results indicate that erythropoiesis mediated by erythropoietin is present in amphibian species and, furthermore, that the regulatory mechanisms controlling peripheral erythrocyte number may vary among vertebrates.
Kuroki, Ryota; Okazaki, Nobuo; Adachi, Motoyasu; Ohara, Takashi; Kurihara, Kazuo; Tamada, Taro
Acta Crystallographica Section D, 66(11), p.1126 - 1130, 2010/11
Times Cited Count：2 Percentile：30.11(Biochemical Research Methods)It is generally known that enzymes represent important drug-target proteins. Elucidation of the catalytic function and the molecular-recognition mechanisms of enzymes provides important information for structure-based drug design. Neutron crystallography provides accurate information on the locations of H atoms that are essential in enzymatic function and molecular recognition. Recent examples are described of the structure determination of the drug-target proteins human immunodeficiency virus protease and porcine pancreatic elastase in complex with transition-state analogue inhibitors using the neutron diffractometers for biological crystallography (BIX-3 and BIX-4) installed at the JRR-3 research reactor.
Sakanaka, Shogo*; Akemoto, Mitsuo*; Aoto, Tomohiro*; Arakawa, Dai*; Asaoka, Seiji*; Enomoto, Atsushi*; Fukuda, Shigeki*; Furukawa, Kazuro*; Furuya, Takaaki*; Haga, Kaiichi*; et al.
Proceedings of 1st International Particle Accelerator Conference (IPAC '10) (Internet), p.2338 - 2340, 2010/05
Future synchrotron light source using a 5-GeV energy recovery linac (ERL) is under proposal by our Japanese collaboration team, and we are conducting R&D efforts for that. We are developing high-brightness DC photocathode guns, two types of cryomodules for both injector and main superconducting (SC) linacs, and 1.3 GHz high CW-power RF sources. We are also constructing the Compact ERL (cERL) for demonstrating the recirculation of low-emittance, high-current beams using above-mentioned critical technologies.
Kuroki, Ryota; Tamada, Taro; Kurihara, Kazuo; Ohara, Takashi; Adachi, Motoyasu
Yakugaku Zasshi, 130(5), p.657 - 664, 2010/05
Times Cited Count：0 Percentile：0.02(Pharmacology & Pharmacy)Crystallography enables us to obtain accurate atomic positions within proteins. High resolution X-ray crystallography provides information for most of the atoms comprising a protein, with the exception of hydrogens. Neutron diffraction data can provide information of the location of hydrogen atoms to the structural information determined by X-ray crystallography. Here, we show the recent result of the structural determination of drug-target proteins, porcine pancreatic elastase and human immuno-deficiency virus type-1 protease by both X-ray and neutron diffraction. The structure of porcine pancreatic elastase with its potent inhibitor was determined at room temperature to 1.2 
resolution by X-ray diffraction and 1.65 resolution by neutron diffraction. The structure of HIV-PR with its potent inhibitor was also determined to 1.4 resolution by X-ray diffraction and 1.9 resolution by neutron diffraction. Ultra-high resolution structures of both proteins (0.94 and 0.93 , respectively) were also determined by X-ray diffraction at 100 K. The ionization state and the location of hydrogen atoms of the catalytic residue in these enzymes were determined by neutron diffraction. Furthermore, collaborative use of both X-ray and neutron to identify the location of ambiguous hydrogen atoms will be shown.
Tamada, Taro; Kinoshita, Takayoshi*; Kurihara, Kazuo; Adachi, Motoyasu; Ohara, Takashi; Imai, Keisuke*; Kuroki, Ryota; Tada, Toshiji*
Journal of the American Chemical Society, 131(31), p.11033 - 11040, 2009/07
Times Cited Count：58 Percentile：79.01(Chemistry, Multidisciplinary)To help resolve long-standing questions regarding the catalytic activity of the serine proteases the structure of porcine pancreatic elastase has been analyzed by high-resolution neutron and X-ray crystallography. In order to mimic the tetrahedral transition intermediate a peptidic inhibitor was used. A single large crystal was used to collect room-temperature neutron data to 1.65 resolution and X-ray data to 1.20 resolution. Another crystal provided a low-temperature X-ray data set to 0.94 resolution. The neutron data are to higher resolution than previously reported for a serine protease and the X-ray data are comparable with other studies. The neutron and X-ray data show that the hydrogen bond between His57 and Asp102 (chymotrypsin numbering) is 2.60 in length and that the hydrogen-bonding hydrogen is 0.80-0.96 from the histidine nitrogen. This is not consistent with a low-barrier hydrogen which is predicted to have the hydrogen midway between the donor and acceptor atom. The observed interaction between His57 and Asp102 is essentially a short but conventional hydrogen bond, sometimes described as a short ionic hydrogen bond. The neutron analysis also shows that the oxygen of the oxopropyl group of the inhibitor is present as an oxygen anion rather than a hydroxyl group, supporting the role of the "oxyanion hole" in stabilizing the tetrahedral intermediate in catalysis.
Adachi, Motoyasu; Ohara, Takashi; Kurihara, Kazuo; Tamada, Taro; Honjo, Eijiro; Okazaki, Nobuo; Arai, Shigeki; Shoyama, Yoshinari; Kimura, Kaname*; Matsumura, Hiroyoshi*; et al.
Proceedings of the National Academy of Sciences of the United States of America, 106(12), p.4641 - 4646, 2009/03
Times Cited Count：111 Percentile：90.72(Multidisciplinary Sciences)To further understand the catalytic mechanism and inhibitor recognition of HIV-1 protease, we need to determine the locations of key hydrogen atoms in the catalytic aspartates Asp25 and Asp125. The structure of HIV-1 protease in complex with transition-state analog KNI-272 was determined by combined neutron crystallography at 1.9 resolution and X-ray crystallography at 1.4 resolution. The resulting structural data shows that the catalytic residue Asp25 is protonated and that Asp125 is deprotonated. The proton on Asp25 makes a hydrogen bond with the carbonyl group of the allophenylnorstatine group in KNI-272. The deprotonated Asp125 bonds to the hydroxyl proton of Apns. The results provide direct experimental evidence for proposed aspects of the catalytic mechanism of HIV-1 protease; and can therefore contribute substantially to the development of specific inhibitors for therapeutic application.
