182 results on '"Tsuru, D."'
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2. In-vessel components for initial operation of JT-60SA
- Author
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Takechi, M., Tsuru, D., Fukumoto, M., Sasajima, T., Matsunaga, G., Nakamura, S., Yamamoto, S., Itashiki, Y., Hayashi, T., and Isayama, A.
- Published
- 2021
- Full Text
- View/download PDF
3. Completion of JT-60SA construction and contribution to ITER
- Author
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Kamada Y., Di Pietro E., Hanada M., Barabaschi P., Ide S., Davis S., Yoshida M., Giruzzi G., Sozzi C., Abdel Maksoud W., Abe H., Aiba N., Akiyama T., Ayllon-Guerola J., Arai T., Artaud J. -F., Asakura N., Ashikawa N., Balbinot L., Bando T., Baulaigue O., Belonohy E., Bin W., Bombarda F., Bolzonella T., Bonne F., Bonotto M., Botija J., Cabrera-Perez S., Cardella A., Carraro L., Cavalier J., Chernyshova M., Chiba S., Clement-Lorenzo S., Cocilovo V., Coda S., Coelho R., Coffey I., Collin B., Corato V., Cucchiaro A., Czarski T., Dairaku M., Day C., de la Luna E., De Tommasi G., Decool P., Di Pace L., Dibon M., Disset G., Ejiri A., Endo Y., Ezumi N., Falchetto G., Fassina A., Fejoz P., Ferro A., Fietz W., Figini L., Fornal T., Frello G., Fujita T., Fukuda T., Fukui K., Fukumoto M., Furukawa M., Futatani S., Gabellieri L., Gaio E., Galazka K., Garcia J., Garcia-Dominguez J., Garcia-Lopez J., Garcia-Munoz M., Garzotti L., Gasparini F., Gharafi S., Giacomelli L., Ginoulhiac G., Giudicotti L., Guillen Gonzalez R., Hajnal N., Hall S., Hamada K., Hanada K., Hasegawa K., Hatae T., Hatakeyama S., Hauer V., Hayashi N., Hayashi T., Heller R., Higashijima S., Hinata J., Hiranai S., Hiratsuka J., Hiwatari R., Hoa C., Homma H., Honda A., Honda M., Horiike H., Hoshino K., Hurzlmeier H., Iafrati M., Ibano K., Ichige H., Ichikawa M., Ichimura M., Ida K., Idei H., Iijima T., Iio S., Ikeda R., Ikeda Y., Imai T., Imazawa R., Inagaki S., Inomoto M., Inoue S., Isayama A., Ishida S., Ishii Y., Isobe M., Janky F., Joffrin E., Jokinen A., Kado S., Kajita S., Kajiwara K., Kamata I., Kaminaga A., Kamiya K., Kanapienyte D., Kashiwa Y., Kashiwagi M., Katayama K., Kawamata Y., Kawamura G., Kawano K., Kawashima H., Kin F., Kitajima S., Kiyono K., Kizu K., Kobayashi K., Kobayashi M., Kobayashi S., Kobayashi T., Kocsis G., Koide Yo., Koide Yu., Kojima A., Kokusen S., Komuro K., Konishi S., Kovacsik A., Ksiazek I., Kubkowska M., Kuhner G., Kuramochi M., Kurihara K., Kurki-Suonio T., Kurniawan A. B., Kuwata T., Lacroix B., Lamaison V., Lampasi A., Lang P., Lauber P., Lawson K., Louzguiti A., Maekawa R., Maekawa T., Maeyama S., Maffia G., Maget P., Mailloux J., Maione I., Maistrello A., Malinowski K., Marchiori G., Marechal J. -L., Massaut V., Masuzaki S., Matsunaga G., Matsunaga S., Mayri Ch., Mattei M., Medrano M., Mele A., Meyer I., Michel F., Minami T., Miyata Y., Miyazawa J., Miyo Y., Mizuuchi T., Mogaki K., Morales J., Moreau P., Mori M., Morisaki T., Morishima S., Moriyama S., Moro A., Murakami H., Murayama M., Murakami S., Nagasaki K., Naito O., Nakamura S., Nakano T., Nakashima Y., Nardino V., Narita E., Narushima Y., Natsume K., Nemoto S., Neu R., Nicollet S., Nishikawa M., Nishimura S., Nishiura M., Nishiyama T., Nocente M., Nobuta Y., Novello L., Nunio F., Ochoa S., Ogawa T., Ogawa Y., Ohdachi S., Ohmori Y., Ohno N., Ohtani Y., Ohzeki M., Oishi T., Okano F., Okano J., Okano K., Onishi Y., Osakabe M., Oshima T., Ostuni V., Oya M., Oya Y., Oyama N., Ozeki T., Pasqualotto R., Pelli S., Peretti E., Phillips G., Piccinni C., Pigatto L., Pironti A., Pizzuto A., Plockl B., Polli G., Poncet J. -M., Ponsot P., Puiatti M., Radloff D., Raimondi V., Ramos F., Rancsik P., Ricci D., Ricciarini S., Rincon E., Romano A., Rossi P., Roussel P., Rubino G., Saeki H., Sagara A., Sakakibara S., Sakamoto H., Sakamoto M., Sakamoto Y., Sakasai A., Sakata S., Sakuma T., Sakurai S., Salanon B., Salmi A., Sannazzaro G., Sano R., Sanpei A., Sasajima T., Sasaki S., Sasao H., Sato F., Sato M., Sawahata M., Scherber A., Scully S., Seki M., Seki S., Shibama Y., Shibata Y., Shikama T., Shimada K., Shimono M., Shinde J., Shinya T., Shinohara K., Shirai H., Shiraishi J., Soare S., Soleto A., Someya Y., Streciwilk-Kowalska E., Strobel H., Sueoka M., Sukegawa A., Sulistyanintyas D., Sumida S., Sunaoshi H., Suzuki H., Suzuki M., Suzuki S., Suzuki T., Suzuki Y., Svoboda J., Szabolics T., Szepesi T., Takahashi K., Takase Y., Takechi M., Takeda K., Takeiri Y., Takenaga H., Taliercio C., Tamura N., Tanaka H., Tanaka K., Tani K., Tanigawa H., Tardocchi M., Terakado A., Terakado M., Terakado T., Teuchner B., Tilia B., Tobita K., Toi K., Toida N., Tojo H., Tokitani M., Tokuzawa T., Tormarchio V., Tomine M., Torre A., Totsuka T., Tsuchiya K., Tsujii N., Tsuru D., Tsutsui H., Uchida M., Ueda Y., Uno J., Urano H., Usui K., Utoh H., Valisa M., Vallar M., Vallcorba-Carbonell R., Vallet J. -C., Varela J., Vega J., Verrecchia M., Vieillard L., Villone F., Vincenzi P., Wada K., Wada R., Wakatsuki T., Wanner M., Watanabe F., Watanabe K., Wauters T., Wiesen S., Wischmeier M., Yagi M., Yagyu J., Yajima M., Yokooka S., Yokoyama M., Yamamoto S., Yamanaka H., Yamauchi K., Yamauchi Y., Yamazaki H., Yamazaki K., Yamazaki R., Yamoto S., Yanagi S., Yanagihara K., Yoshizawa N., Zani L., Zito P., Kamada, Y., Di Pietro, E., Hanada, M., Barabaschi, P., Ide, S., Davis, S., Yoshida, M., Giruzzi, G., Sozzi, C., Abdel Maksoud, W., Abe, H., Aiba, N., Akiyama, T., Ayllon-Guerola, J., Arai, T., Artaud, J. -F., Asakura, N., Ashikawa, N., Balbinot, L., Bando, T., Baulaigue, O., Belonohy, E., Bin, W., Bombarda, F., Bolzonella, T., Bonne, F., Bonotto, M., Botija, J., Cabrera-Perez, S., Cardella, A., Carraro, L., Cavalier, J., Chernyshova, M., Chiba, S., Clement-Lorenzo, S., Cocilovo, V., Coda, S., Coelho, R., Coffey, I., Collin, B., Corato, V., Cucchiaro, A., Czarski, T., Dairaku, M., Day, C., de la Luna, E., De Tommasi, G., Decool, P., Di Pace, L., Dibon, M., Disset, G., Ejiri, A., Endo, Y., Ezumi, N., Falchetto, G., Fassina, A., Fejoz, P., Ferro, A., Fietz, W., Figini, L., Fornal, T., Frello, G., Fujita, T., Fukuda, T., Fukui, K., Fukumoto, M., Furukawa, M., Futatani, S., Gabellieri, L., Gaio, E., Galazka, K., Garcia, J., Garcia-Dominguez, J., Garcia-Lopez, J., Garcia-Munoz, M., Garzotti, L., Gasparini, F., Gharafi, S., Giacomelli, L., Ginoulhiac, G., Giudicotti, L., Guillen Gonzalez, R., Hajnal, N., Hall, S., Hamada, K., Hanada, K., Hasegawa, K., Hatae, T., Hatakeyama, S., Hauer, V., Hayashi, N., Hayashi, T., Heller, R., Higashijima, S., Hinata, J., Hiranai, S., Hiratsuka, J., Hiwatari, R., Hoa, C., Homma, H., Honda, A., Honda, M., Horiike, H., Hoshino, K., Hurzlmeier, H., Iafrati, M., Ibano, K., Ichige, H., Ichikawa, M., Ichimura, M., Ida, K., Idei, H., Iijima, T., Iio, S., Ikeda, R., Ikeda, Y., Imai, T., Imazawa, R., Inagaki, S., Inomoto, M., Inoue, S., Isayama, A., Ishida, S., Ishii, Y., Isobe, M., Janky, F., Joffrin, E., Jokinen, A., Kado, S., Kajita, S., Kajiwara, K., Kamata, I., Kaminaga, A., Kamiya, K., Kanapienyte, D., Kashiwa, Y., Kashiwagi, M., Katayama, K., Kawamata, Y., Kawamura, G., Kawano, K., Kawashima, H., Kin, F., Kitajima, S., Kiyono, K., Kizu, K., Kobayashi, K., Kobayashi, M., Kobayashi, S., Kobayashi, T., Kocsis, G., Koide, Yo., Koide, Yu., Kojima, A., Kokusen, S., Komuro, K., Konishi, S., Kovacsik, A., Ksiazek, I., Kubkowska, M., Kuhner, G., Kuramochi, M., Kurihara, K., Kurki-Suonio, T., Kurniawan, A. B., Kuwata, T., Lacroix, B., Lamaison, V., Lampasi, A., Lang, P., Lauber, P., Lawson, K., Louzguiti, A., Maekawa, R., Maekawa, T., Maeyama, S., Maffia, G., Maget, P., Mailloux, J., Maione, I., Maistrello, A., Malinowski, K., Marchiori, G., Marechal, J. -L., Massaut, V., Masuzaki, S., Matsunaga, G., Matsunaga, S., Mayri, Ch., Mattei, M., Medrano, M., Mele, A., Meyer, I., Michel, F., Minami, T., Miyata, Y., Miyazawa, J., Miyo, Y., Mizuuchi, T., Mogaki, K., Morales, J., Moreau, P., Mori, M., Morisaki, T., Morishima, S., Moriyama, S., Moro, A., Murakami, H., Murayama, M., Murakami, S., Nagasaki, K., Naito, O., Nakamura, S., Nakano, T., Nakashima, Y., Nardino, V., Narita, E., Narushima, Y., Natsume, K., Nemoto, S., Neu, R., Nicollet, S., Nishikawa, M., Nishimura, S., Nishiura, M., Nishiyama, T., Nocente, M., Nobuta, Y., Novello, L., Nunio, F., Ochoa, S., Ogawa, T., Ogawa, Y., Ohdachi, S., Ohmori, Y., Ohno, N., Ohtani, Y., Ohzeki, M., Oishi, T., Okano, F., Okano, J., Okano, K., Onishi, Y., Osakabe, M., Oshima, T., Ostuni, V., Oya, M., Oya, Y., Oyama, N., Ozeki, T., Pasqualotto, R., Pelli, S., Peretti, E., Phillips, G., Piccinni, C., Pigatto, L., Pironti, A., Pizzuto, A., Plockl, B., Polli, G., Poncet, J. -M., Ponsot, P., Puiatti, M., Radloff, D., Raimondi, V., Ramos, F., Rancsik, P., Ricci, D., Ricciarini, S., Rincon, E., Romano, A., Rossi, P., Roussel, P., Rubino, G., Saeki, H., Sagara, A., Sakakibara, S., Sakamoto, H., Sakamoto, M., Sakamoto, Y., Sakasai, A., Sakata, S., Sakuma, T., Sakurai, S., Salanon, B., Salmi, A., Sannazzaro, G., Sano, R., Sanpei, A., Sasajima, T., Sasaki, S., Sasao, H., Sato, F., Sato, M., Sawahata, M., Scherber, A., Scully, S., Seki, M., Seki, S., Shibama, Y., Shibata, Y., Shikama, T., Shimada, K., Shimono, M., Shinde, J., Shinya, T., Shinohara, K., Shirai, H., Shiraishi, J., Soare, S., Soleto, A., Someya, Y., Streciwilk-Kowalska, E., Strobel, H., Sueoka, M., Sukegawa, A., Sulistyanintyas, D., Sumida, S., Sunaoshi, H., Suzuki, H., Suzuki, M., Suzuki, S., Suzuki, T., Suzuki, Y., Svoboda, J., Szabolics, T., Szepesi, T., Takahashi, K., Takase, Y., Takechi, M., Takeda, K., Takeiri, Y., Takenaga, H., Taliercio, C., Tamura, N., Tanaka, H., Tanaka, K., Tani, K., Tanigawa, H., Tardocchi, M., Terakado, A., Terakado, M., Terakado, T., Teuchner, B., Tilia, B., Tobita, K., Toi, K., Toida, N., Tojo, H., Tokitani, M., Tokuzawa, T., Tormarchio, V., Tomine, M., Torre, A., Totsuka, T., Tsuchiya, K., Tsujii, N., Tsuru, D., Tsutsui, H., Uchida, M., Ueda, Y., Uno, J., Urano, H., Usui, K., Utoh, H., Valisa, M., Vallar, M., Vallcorba-Carbonell, R., Vallet, J. -C., Varela, J., Vega, J., Verrecchia, M., Vieillard, L., Villone, F., Vincenzi, P., Wada, K., Wada, R., Wakatsuki, T., Wanner, M., Watanabe, F., Watanabe, K., Wauters, T., Wiesen, S., Wischmeier, M., Yagi, M., Yagyu, J., Yajima, M., Yokooka, S., Yokoyama, M., Yamamoto, S., Yamanaka, H., Yamauchi, K., Yamauchi, Y., Yamazaki, H., Yamazaki, K., Yamazaki, R., Yamoto, S., Yanagi, S., Yanagihara, K., Yoshizawa, N., Zani, L., and Zito, P.
- Subjects
assembly ,Cryostat ,Nuclear and High Energy Physics ,Materials science ,Tokamak ,Nuclear engineering ,Plasma ,Condensed Matter Physics ,Field coil ,ITER risk mitigation ,Overcurrent ,law.invention ,Control theory ,law ,Electromagnetic coil ,research plan ,broader approach ,Voltage - Abstract
Construction of the JT-60SA tokamak was completed on schedule in March 2020. Manufacture and assembly of all the main tokamak components satisfied technical requirements, including dimensional accuracy and functional performances. Development of the plasma heating systems and diagnostics have also progressed, including the demonstration of the favourable electron cyclotron range of frequency (ECRF) transmission at multiple frequencies and the achievement of long sustainment of a high-energy intense negative ion beam. Development of all the tokamak operation control systems has been completed, together with an improved plasma equilibrium control scheme suitable for superconducting tokamaks including ITER. For preparation of the tokamak operation, plasma discharge scenarios have been established using this advanced equilibrium controller. Individual commissioning of the cryogenic system and the power supply system confirmed that these systems satisfy design requirements including operational schemes contributing directly to ITER, such as active control of heat load fluctuation of the cryoplant, which is essential for dynamic operation in superconducting tokamaks. The integrated commissioning (IC) is started by vacuum pumping of the vacuum vessel and cryostat, and then moved to cool-down of the tokamak and coil excitation tests. Transition to the super-conducting state was confirmed for all the TF, EF and CS coils. The TF coil current successfully reached 25.7 kA, which is the nominal operating current of the TF coil. For this nominal toroidal field of 2.25 T, ECRF was applied and an ECRF plasma was created. The IC was, however, suspended by an incident of over current of one of the superconducting equilibrium field coil and He leakage caused by insufficient voltage holding capability at a terminal joint of the coil. The unique importance of JT-60SA for H-mode and high-β steady-state plasma research has been confirmed using advanced integrated modellings. These experiences of assembly, IC and plasma operation of JT-60SA contribute to ITER risk mitigation and efficient implementation of ITER operation.
- Published
- 2022
4. Search for reality of solid breeder blanket for DEMO
- Author
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Tobita, K., Utoh, H., Liu, C., Tanigawa, H., Tsuru, D., Enoeda, M., Yoshida, T., and Asakura, N.
- Published
- 2010
- Full Text
- View/download PDF
5. Thermo-hydraulic testing and integrity of ITER Test Blanket Module (TBM) First Wall mock-up in JAEA
- Author
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Ezato, K., Seki, Y., Tanigawa, H., Hirose, T., Tsuru, D., Nishi, H., Dairaku, M., Yokoyama, K., Suzuki, S., and Enoeda, M.
- Published
- 2010
- Full Text
- View/download PDF
6. Analysis of ELM stability with extended MHD models in JET, JT-60U and future JT-60SA tokamak plasmas
- Author
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Aiba N., Pamela S., Honda M., Urano H., Giroud C., Delabie E., Frassinetti L., Lupelli I., Hayashi N., Huijsmans G. T. A., Litaudon X., Abduallev S., Abhangi M., Abreu P., Afzal M., Aggarwal K. M., Ahlgren T., Ahn J. H., Aho-Mantila L., Airila M., Albanese R., Aldred V., Alegre D., Alessi E., Aleynikov P., Alfier A., Alkseev A., Allinson M., Alper B., Alves E., Ambrosino G., Ambrosino R., Amicucci L., Amosov V., Sunden E. A., Angelone M., Anghel M., Angioni C., Appel L., Appelbee C., Arena P., Ariola M., Arnichand H., Arshad S., Ash A., Ashikawa N., Aslanyan V., Asunta O., Auriemma F., Austin Y., Avotina L., Axton M. D., Ayres C., Bacharis M., Baciero A., Baiao D., Bailey S., Baker A., Balboa I., Balden M., Balshaw N., Bament R., Banks J. W., Baranov Y. F., Barnard M. A., Barnes D., Barnes M., Barnsley R., Wiechec A. B., Orte L. B., Baruzzo M., Basiuk V., Bassan M., Bastow R., Batista A., Batistoni P., Baughan R., Bauvir B., Baylor L., Bazylev B., Beal J., Beaumont P. S., Beckers M., Beckett B., Becoulet A., Bekris N., Beldishevski M., Bell K., Belli F., Bellinger M., Belonohy E., Ayed N. B., Benterman N. A., Bergsaker H., Bernardo J., Bernert M., Berry M., Bertalot L., Besliu C., Beurskens M., Bieg B., Bielecki J., Biewer T., Bigi M., Bilkova P., Binda F., Bisoffi A., Bizarro J. P. S., Bjorkas C., Blackburn J., Blackman K., Blackman T. R., Blanchard P., Blatchford P., Bobkov V., Boboc A., Bodnar G., Bogar O., Bolshakova I., Bolzonella T., Bonanomi N., Bonelli F., Boom J., Booth J., Borba D., Borodin D., Borodkina I., Botrugno A., Bottereau C., Boulting P., Bourdelle C., Bowden M., Bower C., Bowman C., Boyce T., Boyd C., Boyer H. J., Bradshaw J. M. A., Braic V., Bravanec R., Breizman B., Bremond S., Brennan P. D., Breton S., Brett A., Brezinsek S., Bright M. D. J., Brix M., Broeckx W., Brombin M., Broslawski A., Brown D. P. D., Brown M., Bruno E., Bucalossi J., Buch J., Buchanan J., Buckley M. A., Budny R., Bufferand H., Bulman M., Bulmer N., Bunting P., Buratti P., Burckhart A., Buscarino A., Busse A., Butler N. K., Bykov I., Byrne J., Cahyna P., Calabro G., Calvo I., Camenen Y., Camp P., Campling D. C., Cane J., Cannas B., Capel A. J., Card P. J., Cardinali A., Carman P., Carr M., Carralero D., Carraro L., Carvalho B. B., Carvalho I., Carvalho P., Casson F. J., Castaldo C., Catarino N., Caumont J., Causa F., Cavazzana R., Cave-Ayland K., Cavinato M., Cecconello M., Ceccuzzi S., Cecil E., Cenedese A., Cesario R., Challis C. D., Chandler M., Chandra D., Chang C. S., Chankin A., Chapman I. T., Chapman S. C., Chernyshova M., Chitarin G., Ciraolo G., Ciric D., Citrin J., Clairet F., Clark E., Clark M., Clarkson R., Clatworthy D., Clements C., Cleverly M., Coad J. P., Coates P. A., Cobalt A., Coccorese V., Cocilovo V., Coda S., Coelho R., Coenen J. W., Coffey I., Colas L., Collins S., Conka D., Conroy S., Conway N., Coombs D., Cooper D., Cooper S. R., Corradino C., Corre Y., Corrigan G., Cortes S., Coster D., Couchman A. S., Cox M. P., Craciunescu T., Cramp S., Craven R., Crisanti F., Croci G., Croft D., Crombe K., Crowe R., Cruz N., Cseh G., Cufar A., Cullen A., Curuia M., Czarnecka A., Dabirikhah H., Dalgliesh P., Dalley S., Dankowski J., Darrow D., Davies O., Davis W., Day C., Day I. E., De Bock M., de Castro A., de la Cal E., De La Luna E., De Masi G., de Pablos J. L., De Temmerman G., De Tommasi G., De Vries P., Deakin K., Deane J., Degli Agostini F., Dejarnac R., den Harder N., Dendy R. O., Denis J., Denner P., Devaux S., Devynck P., Di Maio F., Di Siena A., Di Troia C., Dinca P., D'Inca R., Ding B., Dittmar T., Doerk H., Doerner R. P., Donne T., Dorling S. E., Dormido-Canto S., Doswon S., Douai D., Doyle P. T., Drenik A., Drewelow P., Drews P., Duckworth Ph., Dumont R., Dumortier P., Dunai D., Dunne M., Duran I., Durodie F., Dutta P., Duval B. P., Dux R., Dylst K., Dzysiuk N., Edappala P. V., Edmond J., Edwards A. M., Edwards J., Eich Th., Ekedahl A., El-Jorf R., Elsmore C. G., Enachescu M., Ericsson G., Eriksson F., Eriksson J., Eriksson L. G., Esposito B., Esquembri S., Esser H. G., Esteve D., Evans B., Evans G. E., Evison G., Ewart G. D., Fagan D., Faitsch M., Falie D., Fanni A., Fasoli A., Faustin J. M., Fawlk N., Fazendeiro L., Fedorczak N., Felton R. C., Fenton K., Fernades A., Fernandes H., Ferreira J., Fessey J. A., Fevrier O., Ficker O., Field A., Fietz S., Figueiredo A., Figueiredo J., Fil A., Finburg P., Firdaouss M., Fischer U., Fittill L., Fitzgerald M., Flammini D., Flanagan J., Fleming C., Flinders K., Fonnesu N., Fontdecaba J. M., Formisano A., Forsythe L., Fortuna L., Fortuna-Zalesna E., Fortune M., Foster S., Franke T., Franklin T., Frasca M., Freisinger M., Fresa R., Frigione D., Fuchs V., Fuller D., Futatani S., Fyvie J., Gal K., Galassi D., Galazka K., Galdon-Quiroga J., Gallagher J., Gallart D., Galvao R., Gao X., Gao Y., Garcia J., Garcia-Carrasco A., Garcia-Munoz M., Gardarein J. -L., Garzotti L., Gaudio P., Gauthier E., Gear D. F., Gee S. J., Geiger B., Gelfusa M., Gerasimov S., Gervasini G., Gethins M., Ghani Z., Ghate M., Gherendi M., Giacalone J. C., Giacomelli L., Gibson C. S., Giegerich T., Gil C., Gil L., Gilligan S., Gin D., Giovannozzi E., Girardo J. B., Giruzzi G., Gloggler S., Godwin J., Goff J., Gohil P., Goloborod'Ko V., Gomes R., Goncalves B., Goniche M., Goodliffe M., Goodyear A., Gorini G., Gosk M., Goulding R., Goussarov A., Gowland R., Graham B., Graham M. E., Graves J. P., Grazier N., Grazier P., Green N. R., Greuner H., Grierson B., Griph F. S., Grisolia C., Grist D., Groth M., Grove R., Grundy C. N., Grzonka J., Guard D., Guerard C., Guillemaut C., Guirlet R., Gurl C., Utoh H. H., Hackett L. J., Hacquin S., Hagar A., Hager R., Hakola A., Halitovs M., Hall S. J., Cook S. P. H., Hamlyn-Harris C., Hammond K., Harrington C., Harrison J., Harting D., Hasenbeck F., Hatano Y., Hatch D. R., Haupt T. D. V., Hawes J., Hawkes N. C., Hawkins J., Hawkins P., Haydon P. W., Hayter N., Hazel S., Heesterman P. J. L., Heinola K., Hellesen C., Hellsten T., Helou W., Hemming O. N., Hender T. C., Henderson M., Henderson S. S., Henriques R., Hepple D., Hermon G., Hertout P., Hidalgo C., Highcock E. G., Hill M., Hillairet J., Hillesheim J., Hillis D., Hizanidis K., Hjalmarsson A., Hobirk J., Hodille E., Hogben C. H. A., Hogeweij G. M. D., Hollingsworth A., Hollis S., Homfray D. A., Horacek J., Hornung G., Horton A. R., Horton L. D., Horvath L., Hotchin S. P., Hough M. R., Howarth P. J., Hubbard A., Huber A., Huber V., Huddleston T. M., Hughes M., Hunter C. L., Huynh P., Hynes A. M., Iglesias D., Imazawa N., Imbeaux F., Imrisek M., Incelli M., Innocente P., Irishkin M., Stanik I. I., Jachmich S., Jacobsen A. S., Jacquet P., Jansons J., Jardin A., Jarvinen A., Jaulmes F., Jednorog S., Jenkins I., Jeong C., Jepu I., Joffrin E., Johnson R., Johnson T., Johnston J., Joita L., Jones G., Jones T. T. C., Hoshino K. K., Kallenbach A., Kamiya K., Kaniewski J., Kantor A., Kappatou A., Karhunen J., Karkinsky D., Karnowska I., Kaufman M., Kaveney G., Kazakov Y., Kazantzidis V., Keeling D. L., Keenan T., Keep J., Kempenaars M., Kennedy C., Kenny D., Kent J., Kent O. N., Khilkevich E., Kim H. T., Kim H. S., Kinch A., King C., King D., King R. F., Kinna D. J., Kiptily V., Kirk A., Kirov K., Kirschner A., Kizane G., Klepper C., Klix A., Knight P., Knipe S. J., Knott S., Kobuchi T., Kochl F., Kocsis G., Kodeli I., Kogan L., Kogut D., Koivuranta S., Kominis Y., Koppen M., Kos B., Koskela T., Koslowski H. R., Koubiti M., Kovari M., Kowalska-Strzeciwilk E., Krasilnikov A., Krasilnikov V., Krawczyk N., Kresina M., Krieger K., Krivska A., Kruezi U., Ksiazek I., Kukushkin A., Kundu A., Kurki-Suonio T., Kwak S., Kwiatkowski R., Kwon O. J., Laguardia L., Lahtinen A., Laing A., Lam N., Lambertz H. T., Lane C., Lang P. T., Lanthaler S., Lapins J., Lasa A., Last J. R., Laszynska E., Lawless R., Lawson A., Lawson K. D., Lazaros A., Lazzaro E., Leddy J., Lee S., Lefebvre X., Leggate H. J., Lehmann J., Lehnen M., Leichtle D., Leichuer P., Leipold F., Lengar I., Lennholm M., Lerche E., Lescinskis A., Lesnoj S., Letellier E., Leyland M., Leysen W., Li L., Liang Y., Likonen J., Linke J., Linsmeier Ch., Lipschultz B., Liu G., Liu Y., Lo Schiavo V. P., Loarer T., Loarte A., Lobel R. C., Lomanowski B., Lomas P. J., Lonnroth J., Lopez J. M., Lopez-Razola J., Lorenzini R., Losada U., Lovell J. J., Loving A. B., Lowry C., Luce T., Lucock R. M. A., Lukin A., Luna C., Lungaroni M., Lungu C. P., Lungu M., Lunniss A., Lyssoivan A., Macdonald N., Macheta P., Maczewa K., Magesh B., Maget P., Maggi C., Maier H., Mailloux J., Makkonen T., Makwana R., Malaquias A., Malizia A., Manas P., Manning A., Manso M. E., Mantica P., Mantsinen M., Manzanares A., Maquet Ph., Marandet Y., Marcenko N., Marchetto C., Marchuk O., Marinelli M., Marinucci M., Markovic T., Marocco D., Marot L., Marren C. A., Marshal R., Martin A., Martin Y., de Aguilera A. M., Martinez F. J., Martin-Solis J. R., Martynova Y., Maruyama S., Masiello A., Maslov M., Matejcik S., Mattei M., Matthews G. F., Maviglia F., Mayer M., Mayoral M. L., May-Smith T., Mazon D., Mazzotta C., McAdams R., McCarthy P. J., McClements K. G., McCormack O., McCullen P. A., McDonald D., McIntosh S., McKean R., McKehon J., Meadows R. C., Meakins A., Medina F., Medland M., Medley S., Meigh S., Meigs A. G., Meisl G., Meitner S., Meneses L., Menmuir S., Mergia K., Merrigan I. R., Mertens Ph., Meshchaninov S., Messiaen A., Meyer H., Mianowski S., Michling R., Middleton-Gear D., Miettunen J., Militello F., Militello-Asp E., Miloshevsky G., Mink F., Minucci S., Miyoshi Y., Mlynar J., Molina D., Monakhov I., Moneti M., Mooney R., Moradi S., Mordijck S., Moreira L., Moreno R., Moro F., Morris A. W., Morris J., Moser L., Mosher S., Moulton D., Murari A., Muraro A., Murphy S., Asakura N. N., Na Y. S., Nabais F., Naish R., Nakano T., Nardon E., Naulin V., Nave M. F. F., Nedzelski I., Nemtsev G., Nespoli F., Neto A., Neu R., Neverov V. S., Newman M., Nicholls K. J., Nicolas T., Nielsen A. H., Nielsen P., Nilsson E., Nishijima D., Noble C., Nocente M., Nodwell D., Nordlund K., Nordman H., Nouailletas R., Nunes I., Oberkofler M., Odupitan T., Ogawa M. T., O'Gorman T., Okabayashi M., Olney R., Omolayo O., O'Mullane M., Ongena J., Orsitto F., Orszagh J., Oswuigwe B. I., Otin R., Owen A., Paccagnella R., Pace N., Pacella D., Packer L. W., Page A., Pajuste E., Palazzo S., Panja S., Papp P., Paprok R., Parail V., Park M., Diaz F. P., Parsons M., Pasqualotto R., Patel A., Pathak S., Paton D., Patten H., Pau A., Pawelec E., Soldan C. P., Peackoc A., Pearson I. J., Pehkonen S. P., Peluso E., Penot C., Pereira A., Pereira R., Puglia P. P. P., von Thun C. P., Peruzzo S., Peschanyi S., Peterka M., Petersson P., Petravich G., Petre A., Petrella N., Petrzilka V., Peysson Y., Pfefferle D., Philipps V., Pillon M., Pintsuk G., Piovesan P., dos Reis A. P., Piron L., Pironti A., Pisano F., Pitts R., Pizzo F., Plyusnin V., Pomaro N., Pompilian O. G., Pool P. J., Popovichev S., Porfiri M. T., Porosnicu C., Porton M., Possnert G., Potzel S., Powell T., Pozzi J., Prajapati V., Prakash R., Prestopino G., Price D., Price M., Price R., Prior P., Proudfoot R., Pucella G., Puglia P., Puiatti M. E., Pulley D., Purahoo K., Putterich Th., Rachlew E., Rack M., Ragona R., Rainford M. S. J., Rakha A., Ramogida G., Ranjan S., Rapson C. J., Rasmussen J. J., Rathod K., Ratta G., Ratynskaia S., Ravera G., Rayner C., Rebai M., Reece D., Reed A., Refy D., Regan B., Regana J., Reich M., Reid N., Reimold F., Reinhart M., Reinke M., Reiser D., Rendell D., Reux C., Cortes S. D. A. R., Reynolds S., Riccardo V., Richardson N., Riddle K., Rigamonti D., Rimini F. G., Risner J., Riva M., Roach C., Robins R. J., Robinson S. A., Robinson T., Robson D. W., Roccella R., Rodionov R., Rodrigues P., Rodriguez J., Rohde V., Romanelli F., Romanelli M., Romanelli S., Romazanov J., Rowe S., Rubel M., Rubinacci G., Rubino G., Ruchko L., Ruiz M., Ruset C., Rzadkiewicz J., Saarelma S., Sabot R., Safi E., Sagar P., Saibene G., Saint-Laurent F., Salewski M., Salmi A., Salmon R., Salzedas F., Samaddar D., Samm U., Sandiford D., Santa P., Santala M. I. K., Santos B., Santucci A., Sartori F., Sartori R., Sauter O., Scannell R., Schlummer T., Schmid K., Schmidt V., Schmuck S., Schneider M., Schopf K., Schworer D., Scott S. D., Sergienko G., Sertoli M., Shabbir A., Sharapov S. E., Shaw A., Shaw R., Sheikh H., Shepherd A., Shevelev A., Shumack A., Sias G., Sibbald M., Sieglin B., Silburn S., Silva A., Silva C., Simmons P. A., Simpson J., Simpson-Hutchinson J., Sinha A., Sipila S. K., Sips A. C. C., Siren P., Sirinelli A., Sjostrand H., Skiba M., Skilton R., Slabkowska K., Slade B., Smith N., Smith P. G., Smith R., Smith T. J., Smithies M., Snoj L., Soare S., Solano E. R., Somers A., Sommariva C., Sonato P., Sopplesa A., Sousa J., Sozzi C., Spagnolo S., Spelzini T., Spineanu F., Stables G., Stamatelatos I., Stamp M. F., Staniec P., Stankunas G., Stan-Sion C., Stead M. J., Stefanikova E., Stepanov I., Stephen A. V., Stephen M., Stevens A., Stevens B. D., Strachan J., Strand P., Strauss H. R., Strom P., Stubbs G., Studholme W., Subba F., Summers H. P., Svensson J., Swiderski L., Szabolics T., Szawlowski M., Szepesi G., Suzuki T. T., Tal B., Tala T., Talbot A. R., Talebzadeh S., Taliercio C., Tamain P., Tame C., Tang W., Tardocchi M., Taroni L., Taylor D., Taylor K. A., Tegnered D., Telesca G., Teplova N., Terranova D., Testa D., Tholerus E., Thomas J., Thomas J. D., Thomas P., Thompson A., Thompson C. -A., Thompson V. K., Thorne L., Thornton A., Thrysoe A. S., Tigwell P. A., Tipton N., Tiseanu I., Tojo H., Tokitani M., Tolias P., Tomes M., Tonner P., Towndrow M., Trimble P., Tripsky M., Tsalas M., Tsavalas P., Jun D. T., Turner I., Turner M. M., Turnyanskiy M., Tvalashvili G., Tyrrell S. G. J., Uccello A., Ul-Abidin Z., Uljanovs J., Ulyatt D., Uytdenhouwen I., Vadgama A. P., Valcarcel D., Valentinuzzi M., Valisa M., Olivares P. V., Valovic M., Van De Mortel M., Van Eester D., Van Renterghem W., van Rooij G. J., Varje J., Varoutis S., Vartanian S., Vasava K., Vasilopoulou T., Vega J., Verdoolaege G., Verhoeven R., Verona C., Rinati G. V., Veshchev E., Vianello N., Vicente J., Viezzer E., Villari S., Villone F., Vincenzi P., Vinyar I., Viola B., Vitins A., Vizvary Z., Vlad M., Voitsekhovitch I., Vondracek P., Vora N., Vu T., de Sa W. W. P., Wakeling B., Waldon C. W. F., Walkden N., Walker M., Walker R., Walsh M., Wang E., Wang N., Warder S., Warren R. J., Waterhouse J., Watkins N. W., Watts C., Wauters T., Weckmann A., Weiland J., Weisen H., Weiszflog M., Wellstood C., West A. T., Wheatley M. R., Whetham S., Whitehead A. M., Whitehead B. D., Widdowson A. M., Wiesen S., Wilkinson J., Williams J., Williams M., Wilson A. R., Wilson D. J., Wilson H. R., Wilson J., Wischmeier M., Withenshaw G., Withycombe A., Witts D. M., Wood D., Wood R., Woodley C., Wray S., Wright J., Wright J. C., Wu J., Wukitch S., Wynn A., Xu T., Yadikin D., Yanling W., Yao L., Yavorskij V., Yoo M. G., Young C., Young D., Young I. D., Young R., Zacks J., Zagorski R., Zaitsev F. S., Zanino R., Zarins A., Zastrow K. D., Zerbini M., Zhang W., Zhou Y., Zilli E., Zoita V., Zoletnik S., Zychor I., Arakawa H., Bando T., Bierwage A., Enoeda M., Fukumoto M., Hamamatsu K., Hanada M., Hatae T., Hayashi T., Higashijima S., Hirota M., Hiwatari R., Ichikawa M., Ide S., Ikeda Y., Imazawa R., Inoue S., Isayama A., Ishida S., Ishii Y., Itami K., Kamada Y., Aiba K. N., Kawano Y., Kizu K., Kawamura Y., Kobayashi T., Koide Y., Kojima A., Kubo H., Kurihara K., Kurita G., Masaki K., Matsukawa M., Matsunaga G., Matsuyama A., Miki K., Miya N., Miyata Y., Miyato N., Mori M., Moriyama S., Murakami H., Naito O., Nakamura M., Narita E., Natsume K., Oasa K., Ohtani Y., Ono M., Oyama N., Ozeki T., Sakamoto Y., Sakasai A., Sakurai S., Sano R., Sasao H., Shibama Y. K., Shibanuma K., Shimizu K., Shinohara K., Shirai H., Shiraishi J., Someya Y., Sukegawa A., Suzuki S., Takase H., Takechi M., Takenaga H., Tanigawa H., Tobita K., Toma M., Tsuchiya K., Tsuru D., Wakatsuki T., Yamoto S., Yagi M., Yoshida K., Yoshida M., Horiike H., Nobuta Y., Yamauchi Y., Idomura Y., Hatayama A., Hoshino K., Okano K., Masamune S., Sanpei A., Fukuyama A., Kado S., Kobayashi S., Konishi S., Kunugi T., Maekawa T., Minami T., Mizuuchi T., Murakami S., Nagasaki K., Shikama T., Watanabe F., Yamamoto S., Hanada K., Idei H., Katayama K., Nishikawa M., Inagaki S., Fujita T., Kajita S., Maeyama S., Ohno N., Yamazaki K., Watanabe T., Akiyama T., Isobe M., Kanno R., Kobayashi M., Masuzaki S., Miyazawa J., Morisaki T., Nakajima N., Nakamura Y., Nakata M., Narushima Y., Nishimura S., Ohdachi S., Oishi T., Osakabe M., Sagara A., Sakakibara S., Satake S., Suzuki Y., Takeiri Y., Tamura N., Tanaka K., Todo Y., Toi K., Yokoyama M., Watanabe K., Shibata Y., Fukuda T., Takizuka T., Ueda Y., Oya Y., Ejiri A., Inomoto M., Nishiura M., Ogawa Y., Takase Y., Kitajima S., Iio S., Matsuda S., Furukawa M., Ichimura M., Imai T., Nakashima Y., Sakamoto M., Sumida S., Barabaschi P., Cardella A., Clement-Lorenzo S., Coletti A., Davis S., Di Pietro E., Duglue D., Farthing J., Frello G., Hajnal N., Hurzlmeier H., Jokinen A., Kanapienyte D., Novello L., Peretti E., Phillips G., Rancsik P., Salpietro E., Scherber A., Spears B., Teuchner B., Tomarchio V., Verrecchia M., Wanner M., Zani L., Baulaigue O., Benoit F., Ciazynski D., Decool P., Dougnac H., Duchateau J. -L., Dumas N., Fejoz P., Geraud A., Gharafi S., Goncalves R., Gonde R., Gros G., Jestin F., Jiolat G., Lacroix B., Lamy S., Marechal J. -L., Nicollet S., Peluso B., Santagiustina A., Stephnie B., Torre A., Vagliani A., Vallet J. -C., Verger J. -M., Bonne F., Girard S., Hoa C., Lamaison V., Michel F., Poncet J. -M., Roussel P., Abdel Maksoud W., Ardellier F., Disset G., Donati A., Genini L., Mayri C., Molinie F., Nunio F., Ponsot P., Salanon B., Scola L., Vieillard L., Alonso J., Barrera G., Botija J., Cabrera Perez S., Fernandez P., Medrano M., Ramos F. J., Rincon E., Soleto A., Ferro A., Gaio E., Gasparini F., Maistrello A., Brolatti G., Coccoluto G., Corato V., Costa P., Cristofani C., Cucchiaro A., De Vellis A., Di Pace L., Frosi P., Ginoulhiac G., Lampasi A., Maffia G., Pizzuto A., Polli G. M., Rossi P., Starace F., Fiamozzi Zignani C., Zito P., Drotziger S., Fietz W., Heller R., Massimi A., Meyer I., Radloff D., Rita C., Urbach E., Collin B., Delrez C., Jamotton P., Massaut V., Sarkimaki K., Benkadda S., Artaud J. -F., Becoulet M., Falchetto G., Hoang T., Lotte P., Moreau P., Pegourie B., Travere J. -M., Bettini P., Canton A., Fassina A., Giudicotti L., Guo S. C., Marchiori G., Pigatto L., Vallar M., Xu X., Cismondi F., Barbato E., Mastrostefano S., de Baar M., Bruschi A., Farina D., Figini L., Granucci G., Moro A., Nowak S., Perelli-Cippo E., Platania P., Ricci D., Zuin M., Conway G., Dibon M., Fantz U., Happel T., Lauber P., Lackner K., Pautasso G., Schneider P., Kuhner G., Zocco A., Stankiewicz R., Stepniewski W., Sips G., Gleason Gonzalez C., Luo X., Scannapiego M., Bonifetto R., Decker J., Goodman T., Theiler C., Ayllon-Guerola J., Kovacsik A., Szepesi T., Kawashima H., Ogawa T., Sato M., Seki M., Universidad de Sevilla. Departamento de Física Atómica, Molecular y Nuclear, Universidad de Sevilla. RNM138: Física Nuclear Aplicada, Aiba, N, Pamela, S, Honda, M, Urano, H, Giroud, C, Delabie, E, Frassinetti, L, Lupelli, I, Hayashi, N, Huijsmans, G, Litaudon, X, Abduallev, S, Abhangi, M, Abreu, P, Afzal, M, Aggarwal, K, Ahlgren, T, Ahn, J, Aho-Mantila, L, Airila, M, Albanese, R, Aldred, V, Alegre, D, Alessi, E, Aleynikov, P, Alfier, A, Alkseev, A, Allinson, M, Alper, B, Alves, E, Ambrosino, G, Ambrosino, R, Amicucci, L, Amosov, V, Sunden, E, Angelone, M, Anghel, M, Angioni, C, Appel, L, Appelbee, C, Arena, P, Ariola, M, Arnichand, H, Arshad, S, Ash, A, Ashikawa, N, Aslanyan, V, Asunta, O, Auriemma, F, Austin, Y, Avotina, L, Axton, M, Ayres, C, Bacharis, M, Baciero, A, Baiao, D, Bailey, S, Baker, A, Balboa, I, Balden, M, Balshaw, N, Bament, R, Banks, J, Baranov, Y, Barnard, M, Barnes, D, Barnes, M, Barnsley, R, Wiechec, A, Orte, L, Baruzzo, M, Basiuk, V, Bassan, M, Bastow, R, Batista, A, Batistoni, P, Baughan, R, Bauvir, B, Baylor, L, Bazylev, B, Beal, J, Beaumont, P, Beckers, M, Beckett, B, Becoulet, A, Bekris, N, Beldishevski, M, Bell, K, Belli, F, Bellinger, M, Belonohy, E, Ayed, N, Benterman, N, Bergsaker, H, Bernardo, J, Bernert, M, Berry, M, Bertalot, L, Besliu, C, Beurskens, M, Bieg, B, Bielecki, J, Biewer, T, Bigi, M, Bilkova, P, Binda, F, Bisoffi, A, Bizarro, J, Bjorkas, C, Blackburn, J, Blackman, K, Blackman, T, Blanchard, P, Blatchford, P, Bobkov, V, Boboc, A, Bodnar, G, Bogar, O, Bolshakova, I, Bolzonella, T, Bonanomi, N, Bonelli, F, Boom, J, Booth, J, Borba, D, Borodin, D, Borodkina, I, Botrugno, A, Bottereau, C, Boulting, P, Bourdelle, C, Bowden, M, Bower, C, Bowman, C, Boyce, T, Boyd, C, Boyer, H, Bradshaw, J, Braic, V, Bravanec, R, Breizman, B, Bremond, S, Brennan, P, Breton, S, Brett, A, Brezinsek, S, Bright, M, Brix, M, Broeckx, W, Brombin, M, Broslawski, A, Brown, D, Brown, M, Bruno, E, Bucalossi, J, Buch, J, Buchanan, J, Buckley, M, Budny, R, Bufferand, H, Bulman, M, Bulmer, N, Bunting, P, Buratti, P, Burckhart, A, Buscarino, A, Busse, A, Butler, N, Bykov, I, Byrne, J, Cahyna, P, Calabro, G, Calvo, I, Camenen, Y, Camp, P, Campling, D, Cane, J, Cannas, B, Capel, A, Card, P, Cardinali, A, Carman, P, Carr, M, Carralero, D, Carraro, L, Carvalho, B, Carvalho, I, Carvalho, P, Casson, F, Castaldo, C, Catarino, N, Caumont, J, Causa, F, Cavazzana, R, Cave-Ayland, K, Cavinato, M, Cecconello, M, Ceccuzzi, S, Cecil, E, Cenedese, A, Cesario, R, Challis, C, Chandler, M, Chandra, D, Chang, C, Chankin, A, Chapman, I, Chapman, S, Chernyshova, M, Chitarin, G, Ciraolo, G, Ciric, D, Citrin, J, Clairet, F, Clark, E, Clark, M, Clarkson, R, Clatworthy, D, Clements, C, Cleverly, M, Coad, J, Coates, P, Cobalt, A, Coccorese, V, Cocilovo, V, Coda, S, Coelho, R, Coenen, J, Coffey, I, Colas, L, Collins, S, Conka, D, Conroy, S, Conway, N, Coombs, D, Cooper, D, Cooper, S, Corradino, C, Corre, Y, Corrigan, G, Cortes, S, Coster, D, Couchman, A, Cox, M, Craciunescu, T, Cramp, S, Craven, R, Crisanti, F, Croci, G, Croft, D, Crombe, K, Crowe, R, Cruz, N, Cseh, G, Cufar, A, Cullen, A, Curuia, M, Czarnecka, A, Dabirikhah, H, Dalgliesh, P, Dalley, S, Dankowski, J, Darrow, D, Davies, O, Davis, W, Day, C, Day, I, De Bock, M, de Castro, A, de la Cal, E, De La Luna, E, De Masi, G, de Pablos, J, De Temmerman, G, De Tommasi, G, De Vries, P, Deakin, K, Deane, J, Degli Agostini, F, Dejarnac, R, den Harder, N, Dendy, R, Denis, J, Denner, P, Devaux, S, Devynck, P, Di Maio, F, Di Siena, A, Di Troia, C, Dinca, P, D'Inca, R, Ding, B, Dittmar, T, Doerk, H, Doerner, R, Donne, T, Dorling, S, Dormido-Canto, S, Doswon, S, Douai, D, Doyle, P, Drenik, A, Drewelow, P, Drews, P, Duckworth, P, Dumont, R, Dumortier, P, Dunai, D, Dunne, M, Duran, I, Durodie, F, Dutta, P, Duval, B, Dux, R, Dylst, K, Dzysiuk, N, Edappala, P, Edmond, J, Edwards, A, Edwards, J, Eich, T, Ekedahl, A, El-Jorf, R, Elsmore, C, Enachescu, M, Ericsson, G, Eriksson, F, Eriksson, J, Eriksson, L, Esposito, B, Esquembri, S, Esser, H, Esteve, D, Evans, B, Evans, G, Evison, G, Ewart, G, Fagan, D, 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N., Kawano, Y., Kizu, K., Kawamura, Y., Kobayashi, T., Koide, Y., Kojima, A., Kubo, H., Kurihara, K., Kurita, G., Masaki, K., Matsukawa, M., Matsunaga, G., Matsuyama, A., Miki, K., Miya, N., Miyata, Y., Miyato, N., Mori, M., Moriyama, S., Murakami, H., Naito, O., Nakamura, M., Narita, E., Natsume, K., Oasa, K., Ohtani, Y., Ono, M., Oyama, N., Ozeki, T., Sakamoto, Y., Sakasai, A., Sakurai, S., Sano, R., Sasao, H., Shibama, Y. K., Shibanuma, K., Shimizu, K., Shinohara, K., Shirai, H., Shiraishi, J., Someya, Y., Sukegawa, A., Suzuki, S., Takase, H., Takechi, M., Takenaga, H., Tanigawa, H., Tobita, K., Toma, M., Tsuchiya, K., Tsuru, D., Wakatsuki, T., Yamoto, S., Yagi, M., Yoshida, K., Yoshida, M., Horiike, H., Nobuta, Y., Yamauchi, Y., Idomura, Y., Hatayama, A., Hoshino, K., Okano, K., Masamune, S., Sanpei, A., Fukuyama, A., Kado, S., Kobayashi, S., Konishi, S., Kunugi, T., Maekawa, T., Minami, T., Mizuuchi, T., Murakami, S., Nagasaki, K., Shikama, T., Watanabe, F., Yamamoto, S., Hanada, K., Idei, H., Katayama, K., Nishikawa, M., Inagaki, S., Fujita, T., Kajita, S., Maeyama, S., Ohno, N., Yamazaki, K., Watanabe, T., Akiyama, T., Isobe, M., Kanno, R., Kobayashi, M., Masuzaki, S., Miyazawa, J., Morisaki, T., Nakajima, N., Nakamura, Y., Nakata, M., Narushima, Y., Nishimura, S., Ohdachi, S., Oishi, T., Osakabe, M., Sagara, A., Sakakibara, S., Satake, S., Suzuki, Y., Takeiri, Y., Tamura, N., Tanaka, K., Todo, Y., Toi, K., Yokoyama, M., Watanabe, K., Shibata, Y., Fukuda, T., Takizuka, T., Ueda, Y., Oya, Y., Ejiri, A., Inomoto, M., Nishiura, M., Ogawa, Y., Takase, Y., Kitajima, S., Iio, S., Matsuda, S., Furukawa, M., Ichimura, M., Imai, T., Nakashima, Y., Sakamoto, M., Sumida, S., Barabaschi, P., Cardella, A., Clement-Lorenzo, S., Coletti, A., Davis, S., Di Pietro, E., Duglue, D., Farthing, J., Frello, G., Hajnal, N., Hurzlmeier, H., Jokinen, A., Kanapienyte, D., Novello, L., Peretti, E., Phillips, G., Rancsik, P., Salpietro, E., Scherber, A., Spears, B., Teuchner, B., Tomarchio, V., Verrecchia, M., Wanner, M., Zani, L., Baulaigue, O., Benoit, F., Ciazynski, D., Decool, P., Dougnac, H., Duchateau, J. -L., Dumas, N., Fejoz, P., Geraud, A., Gharafi, S., Goncalves, R., Gonde, R., Gros, G., Jestin, F., Jiolat, G., Lacroix, B., Lamy, S., Marechal, J. -L., Nicollet, S., Peluso, B., Santagiustina, A., Stephnie, B., Torre, A., Vagliani, A., Vallet, J. -C., Verger, J. -M., Bonne, F., Girard, S., Hoa, C., Lamaison, V., Michel, F., Poncet, J. -M., Roussel, P., Abdel Maksoud, W., Ardellier, F., Disset, G., Donati, A., Genini, L., Mayri, C., Molinie, F., Nunio, F., Ponsot, P., Salanon, B., Scola, L., Vieillard, L., Alonso, J., Barrera, G., Botija, J., Cabrera Perez, S., Fernandez, P., Medrano, M., Ramos, F. J., Rincon, E., Soleto, A., Ferro, A., Gaio, E., Gasparini, F., Maistrello, A., Brolatti, G., Coccoluto, G., Corato, V., Costa, P., Cristofani, C., Cucchiaro, A., De Vellis, A., Di Pace, L., Frosi, P., Ginoulhiac, G., Lampasi, A., Maffia, G., Pizzuto, A., Polli, G. M., Rossi, P., Starace, F., Fiamozzi Zignani, C., Zito, P., Drotziger, S., Fietz, W., Heller, R., Massimi, A., Meyer, I., Radloff, D., Rita, C., Urbach, E., Collin, B., Delrez, C., Jamotton, P., Massaut, V., Sarkimaki, K., Benkadda, S., Artaud, J. -F., Becoulet, M., Falchetto, G., Hoang, T., Lotte, P., Moreau, P., Pegourie, B., Travere, J. -M., Bettini, P., Canton, A., Fassina, A., Giudicotti, L., Guo, S. C., Marchiori, G., Pigatto, L., Vallar, M., Xu, X., Cismondi, F., Barbato, E., Mastrostefano, S., de Baar, M., Bruschi, A., Farina, D., Figini, L., Granucci, G., Moro, A., Nowak, S., Perelli-Cippo, E., Platania, P., Ricci, D., Zuin, M., Conway, G., Dibon, M., Fantz, U., Happel, T., Lauber, P., Lackner, K., Pautasso, G., Schneider, P., Kuhner, G., Zocco, A., Stankiewicz, R., Stepniewski, W., Sips, G., Gleason Gonzalez, C., Luo, X., Scannapiego, M., Bonifetto, R., Decker, J., Goodman, T., Theiler, C., Ayllon-Guerola, J., Kovacsik, A., Szepesi, T., Kawashima, H., Ogawa, T., Sato, M., and Seki, M.
- Subjects
Tokamak ,Rotation ,ELM ,extended MHD model ,H-mode ,rotation ,tokamaks ,01 natural sciences ,Stability (probability) ,010305 fluids & plasmas ,law.invention ,law ,Physics::Plasma Physics ,0103 physical sciences ,Extended MHD model ,010306 general physics ,tokamak ,Physics ,Jet (fluid) ,Plasma ,BOOTSTRAP CURRENT ,SIMULATION ,Condensed Matter Physics ,Computational physics ,Settore ING-IND/20 - Misure e Strumentazione Nucleari ,Nuclear Energy and Engineering ,Physics::Space Physics ,Magnetohydrodynamics ,Tokamaks - Abstract
The stability with respect to a peeling–ballooning mode (PBM) was investigated numerically with extended MHD simulation codes in JET, JT-60U and future JT-60SA plasmas. The MINERVA-DI code was used to analyze the linear stability, including the effects of rotation and ion diamagnetic drift ( *w i), in JET-ILW and JT-60SA plasmas, and the JOREK code was used to simulate nonlinear dynamics with rotation, viscosity and resistivity in JT-60U plasmas. It was validated quantitatively that the ELM trigger condition in JET-ILW plasmas can be reasonably explained by taking into account both the rotation and *w i effects in the numerical analysis. When deuterium poloidal rotation is evaluated based on neoclassical theory, an increase in the effective charge of plasma destabilizes the PBM because of an acceleration of rotation and a decrease in *w i. The difference in the amount of ELM energy loss in JT-60U plasmas rotating in opposite directions was reproduced qualitatively with JOREK. By comparing the ELM affected areas with linear eigenfunctions, it was confirmed that the difference in the linear stability property, due not to the rotation direction but to the plasma density profile, is thought to be responsible for changing the ELM energy loss just after the ELM crash. A predictive study to determine the pedestal profiles in JT-60SA was performed by updating the EPED1 model to include the rotation and *w i effects in the PBM stability analysis. It was shown that the plasma rotation predicted with the neoclassical toroidal viscosity degrades the pedestal performance by about 10% by destabilizing the PBM, but the pressure pedestal height will be high enough to achieve the target parameters required for the ITER-like shape inductive scenario in JT-60SA. JSPS KAKENHI 15K06656 EURATOM 633053
- Published
- 2018
7. Immunoelectron-microscopic demonstration of histamine depletion in the gastric enterochromaffin-like cells of rats treated with α-fluoromethylhistidine
- Author
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Fujiwara, K., Karasuyama, M., Murata, I., Tanabe, T., Yabuuchi, M., Inoue, Y., and Tsuru, D.
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- 2001
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8. Consideration on blanket structure for fusion DEMO plant at JAERI
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Nishio, S., Ohmori, J., Kuroda, T., Tobita, K., Enoeda, M., Tsuru, D., Hirose, T., Sato, S., Kawamura, Y., Nakamura, H., and Sato, M.
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- 2006
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9. Design study of fusion DEMO plant at JAERI
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Tobita, K., Nishio, S., Enoeda, M., Sato, M., Isono, T., Sakurai, S., Nakamura, H., Sato, S., Suzuki, S., Ando, M., Ezato, K., Hayashi, T., Hirose, T., Inoue, T., Kawamura, Y., Koizumi, N., Kudo, Y., Kurihara, R., Kuroda, T., Matsukawa, M., Mouri, K., Nakamura, Y., Nishi, M., Nomoto, Y., Ohmori, J., Oyama, N., Sakamoto, K., Suzuki, T., Takechi, M., Tanigawa, H., Tsuchiya, K., and Tsuru, D.
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- 2006
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10. Design, research and development for plasma facing components in JT-60SA
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Tsuru, D, primary, Fukumoto, M, additional, Hayashi, T, additional, Takechi, M, additional, Nakamura, S, additional, Matsunaga, G, additional, Seki, Y, additional, Ezato, K, additional, and Suzuki, S, additional
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- 2020
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11. Adoption of a genetic algorithm (GA) for tomographic reconstruction of line-of-sight optical images
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Kihm, K. D., Okamoto, K., Tsuru, D., and Ko, H. S.
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- 1996
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12. Visualization of 3D gas density distribution using optical tomography
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Feng, J., Okamoto, K., Tsuru, D., Madarame, H., and Fumizawa, M.
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- 2002
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13. Safety activities in JAERI related to ITER
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O'hira, S., Tada, E., Hada, K., Neyatani, Y., Maruo, T., Hashimoto, M., Araki, T., Nomoto, K., Tsuru, D., Ishida, K., and Tsunematsu, T.
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- 2001
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14. Evaluation of Strength on Dissimilar Metal Joints for ITER First Wall Components
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Nishi, H., primary, Enoeda, M., additional, Hirose, T., additional, Tsuru, D., additional, and Tanigawa, H., additional
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- 2010
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15. Compact DEMO, SlimCS: design progress and issues
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Tobita, K., primary, Nishio, S., additional, Enoeda, M., additional, Kawashima, H., additional, Kurita, G., additional, Tanigawa, H., additional, Nakamura, H., additional, Honda, M., additional, Saito, A., additional, Sato, S., additional, Hayashi, T., additional, Asakura, N., additional, Sakurai, S., additional, Nishitani, T., additional, Ozeki, T., additional, Ando, M., additional, Ezato, K., additional, Hamamatsu, K., additional, Hirose, T., additional, Hoshino, T., additional, Ide, S., additional, Inoue, T., additional, Isono, T., additional, Liu, C., additional, Kakudate, S., additional, Kawamura, Y., additional, Mori, S., additional, Nakamichi, M., additional, Nishi, H., additional, Nozawa, T., additional, Ochiai, K., additional, Ogiwara, H., additional, Oyama, N., additional, Sakamoto, K., additional, Sakamoto, Y., additional, Seki, Y., additional, Shibama, Y., additional, Shimizu, K., additional, Suzuki, S., additional, Takahashi, K., additional, Tsuru, D., additional, Yamanishi, T., additional, and Yoshida, T., additional
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- 2009
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16. R&D of a Li2TiO3 pebble bed for a test blanket module in JAEA
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Tanigawa, H., primary, Hoshino, T., additional, Kawamura, Y., additional, Nakamichi, M., additional, Ochiai, K., additional, Akiba, M., additional, Ando, M., additional, Enoeda, M., additional, Ezato, K., additional, Hayashi, K., additional, Hirose, T., additional, Konno, C., additional, Nakamura, H., additional, Nozawa, T., additional, Ogiwara, H., additional, Seki, Y., additional, Tanigawa, H., additional, Tsuchiya, K., additional, Tsuru, D., additional, and Yamanishi, T., additional
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- 2009
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17. Torus configuration and materials selection on a fusion DEMO reactor, SlimCS
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Tobita, K., primary, Nishio, S., additional, Tanigawa, H., additional, Enoeda, M., additional, Isono, T., additional, Nakamura, H., additional, Tsuru, D., additional, Suzuki, S., additional, Hayashi, T., additional, Tsuchiya, K., additional, and Nishitani, T., additional
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- 2009
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18. STUDIES ON BACTERIAL PROTEASES
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Tsuru, D., primary, Yoshimoto, T., additional, Yoshida, H., additional, Kira, H., additional, and Fukumoto, J., additional
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- 2009
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19. SlimCS—compact low aspect ratio DEMO reactor with reduced-size central solenoid
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Tobita, K, primary, Nishio, S, additional, Sato, M, additional, Sakurai, S, additional, Hayashi, T, additional, Shibama, Y.K, additional, Isono, T, additional, Enoeda, M, additional, Nakamura, H, additional, Sato, S, additional, Ezato, K, additional, Hirose, T, additional, Ide, S, additional, Inoue, T, additional, Kamada, Y, additional, Kawamura, Y, additional, Kawashima, H, additional, Koizumi, N, additional, Kurita, G, additional, Nakamura, Y, additional, Mouri, K, additional, Nishitani, T, additional, Ohmori, J, additional, Oyama, N, additional, Sakamoto, K, additional, Suzuki, S, additional, Suzuki, T, additional, Tanigawa, H, additional, Tsuchiya, K, additional, and Tsuru, D, additional
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- 2007
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20. Safety Design Concepts for ITER-Tritium Facility: - Toward construction in Japan -
- Author
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O’hira, S., primary, Tada, E., additional, Hada, K., additional, Neyatani, Y., additional, Maruo, T., additional, Hashimoto, M., additional, Araki, T., additional, Nomoto, K., additional, Tsuru, D., additional, Ishida, T., additional, Goto, Y., additional, and Tsunematsu, T., additional
- Published
- 2002
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- View/download PDF
21. Immunoelectron-microscopic demonstration of histamine depletion in the gastric enterochromaffin-like cells of rats treated with à-fluoromethylhistidine
- Author
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Fujiwara, K., primary, Karasuyama, M., additional, Murata, I., additional, Tanabe, T., additional, Yabuuchi, M., additional, Inoue, Y., additional, and Tsuru, D., additional
- Published
- 2001
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- View/download PDF
22. Glutaraldehyde (GA)-Hapten Adducts, but without a Carrier Protein, for Use in a Specificity Study on an Antibody against a GA-Conjugated Hapten Compound: Histamine Monoclonal Antibody (AHA-2) as a Model
- Author
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Fujiwara, K., primary, Murata, I., additional, Yagisawa, S., additional, Tanabe, T., additional, Yabuuchi, M., additional, Sakakibara, R., additional, and Tsuru, D., additional
- Published
- 1999
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23. Histamine Monoclonal Antibody for Brain Immunocytochemistry
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Fujiwara, K., primary, Masuyama, Y., additional, Yagisawa, S., additional, Tanabe, T., additional, Yabuuchi, M., additional, and Tsuru, D., additional
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- 1999
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24. The crystal structure of pyroglutamyl peptidase I from Bacillus amyloliquefaciens reveals a new structure for a cysteine protease
- Author
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Odagaki, Y, primary, Hayashi, A, additional, Okada, K, additional, Hirotsu, K, additional, Kabashima, T, additional, Ito, K, additional, Yoshimoto, T, additional, Tsuru, D, additional, Sato, M, additional, and Clardy, J, additional
- Published
- 1999
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25. Preparation of Monoclonal Antibodies against N-( -Maleimidobutyryloxy)succinimide (GMBS)-Conjugated Acetylspermine, and Development of an Enzyme-Linked Immunosorbent Assay (ELISA) for N1,N12-Diacetylspermine
- Author
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Fujiwara, K., primary, Kaminishi, Y., additional, Kitagawa, T., additional, Tsuru, D., additional, Yabuuchi, M., additional, Kanetake, H., additional, and Nomata, K., additional
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- 1998
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26. Crystallization and preliminary X-ray crystallographic studies of 7α-hydroxysteroid dehydrogenase from Escherichia coli
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Tanaka, N., primary, Nonaka, T., additional, Yoshimoto, T., additional, Tsuru, D., additional, and Mitsui, Y., additional
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- 1996
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27. RECONSTRUCTION OF THREE-DIMENSIONAL DENSITY DISTRIBUTION FROM THE LIMITED PROJECTION IMAGES WITH GENETIC ALGORITHM
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Okamoto, Koji, primary, Tsuru, D., additional, and Fumizawa, Motoo, additional
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- 1996
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28. Cloning and high-level expression of the glutathione-independent formaldehyde dehydrogenase gene from Pseudomonas putida
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Ito, K, primary, Takahashi, M, additional, Yoshimoto, T, additional, and Tsuru, D, additional
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- 1994
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29. Location of the 7 alpha-hydroxysteroid dehydrogenase gene (hdhA) on the physical map of the Escherichia coli chromosome
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Yoshimoto, T, primary, Nagai, H, additional, Ito, K, additional, and Tsuru, D, additional
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- 1993
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30. Location of the protease II gene (ptrB) on the physical map of the Escherichia coli chromosome
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Kanatani, A, primary, Yoshimoto, T, additional, Nagai, H, additional, Ito, K, additional, and Tsuru, D, additional
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- 1992
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31. Cloning, sequencing, and high expression of the proline iminopeptidase gene from Bacillus coagulans
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Kitazono, A, primary, Yoshimoto, T, additional, and Tsuru, D, additional
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- 1992
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32. Acetyl-CoA carboxylase from Escherichia coli: gene organization and nucleotide sequence of the biotin carboxylase subunit.
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Kondo, H, primary, Shiratsuchi, K, additional, Yoshimoto, T, additional, Masuda, T, additional, Kitazono, A, additional, Tsuru, D, additional, Anai, M, additional, Sekiguchi, M, additional, and Tanabe, T, additional
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- 1991
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33. Cloning and sequencing of the 7 alpha-hydroxysteroid dehydrogenase gene from Escherichia coli HB101 and characterization of the expressed enzyme
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Yoshimoto, T, primary, Higashi, H, additional, Kanatani, A, additional, Lin, X S, additional, Nagai, H, additional, Oyama, H, additional, Kurazono, K, additional, and Tsuru, D, additional
- Published
- 1991
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34. STUDIES ON BACTERIAL PROTEASES.
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Tsuru, D., Yoshida, T., Hirose, T., Yoshimoto, T., and Fukumoto, J.
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- 1970
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35. Study on decay heat removal of compact ITER
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Tsuru, D., Neyatani, Y., Araki, T., Nomoto, K., O'Hira, S., Maruo, T., Hashimoto, M., Hada, K., and Tada, E.
- Published
- 2001
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- View/download PDF
36. Proline-specific endopeptidase from Flavobacterium. Purification and properties.
- Author
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Yoshimoto, T., primary, Walter, R., additional, and Tsuru, D., additional
- Published
- 1980
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37. Mechanism of proline-specific proteinases: (I) substrate specificity of dipeptidyl peptidase IV from pig kidney and proline-specific endopeptidase from Flavobacterium meningosepticum
- Author
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Heins, J., primary, Welker, P., additional, Schönlein, Chr., additional, Born, I., additional, Hartrodt, B., additional, Neubert, K., additional, Tsuru, D., additional, and Barth, A., additional
- Published
- 1988
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38. The effects of transcranial static magnetic fields stimulation over the supplementary motor area on anticipatory postural adjustments.
- Author
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Tsuru D, Watanabe T, Chen X, Kubo N, Sunagawa T, Mima T, and Kirimoto H
- Subjects
- Adult, Female, Humans, Male, Movement physiology, Muscle Contraction physiology, Muscle, Skeletal physiology, Psychomotor Performance physiology, Young Adult, Adaptation, Physiological physiology, Anticipation, Psychological physiology, Electromyography methods, Motor Cortex physiology, Postural Balance physiology, Transcranial Magnetic Stimulation methods
- Abstract
We investigated the influence of transcranial static magnetic field stimulation (tSMS) over the supplementary motor area (SMA) on anticipatory postural adjustments (APAs), in which the activation of the postural muscles of the legs and trunk that control standing posture precedes the activation of the prime mover muscles during rapid shoulder flexion movement. Eighteen subjects performed a self-paced rapid shoulder flexion task before, during, and after tSMS. Electromyogram (EMG) activity was recorded from the deltoid anterior (AD) as the prime mover muscle and the biceps femoris (BF) as the postural muscle during the task. The EMG latency difference (ΔEMG onset) between the two muscles was calculated by subtracting the EMG burst onset of the BF from that of the AD. The ΔEMG onset was significantly shortened, but center-of-pressure parameters were not affected after tSMS stimulation. These findings suggest that tSMS applied over the SMA could inhibitively modulate APAs function., (Copyright © 2020 Elsevier B.V. All rights reserved.)
- Published
- 2020
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39. Flavoxobin, a serine protease from Trimeresurus flavoviridis (habu snake) venom, independently cleaves Arg726-Ser727 of human C3 and acts as a novel, heterologous C3 convertase.
- Author
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Yamamoto C, Tsuru D, Oda-Ueda N, Ohno M, Hattori S, and Kim ST
- Subjects
- Amino Acid Sequence, Animals, Chromatography, Gel, Chromatography, Ion Exchange, Complement Activation drug effects, Complement C3 chemistry, Complement C3a metabolism, Complement Membrane Attack Complex metabolism, Crotalid Venoms isolation & purification, Humans, Serine Endopeptidases isolation & purification, Snakes, Thrombin immunology, Trypsin immunology, Complement C3 metabolism, Complement C3-C5 Convertases immunology, Crotalid Venoms immunology, Serine Endopeptidases immunology
- Abstract
We have recently shown that crude Trimeresurus flavoviridis (habu snake) venom has a strong capability for activating the human alternative complement system. To identify the active component, the crude venom was fractionated and purified by serial chromatography using Sephadex G-100, CM-cellulose C-52, diethylaminoethyl-Toyopearl 650M, and Butyl-Toyopearl, and the active fractions were evaluated by the C3a-releasing and soluble membrane attack complex-forming activities. Two peak fractions with the highest activities were detected after gel filtration and ion exchange chromatography, and the first fraction was purified to homogeneity. The homogeneous protein was examined for its N-terminal amino acid sequence by Edman degradation. The determined sequence of 25 amino acids completely coincided with that of a previously reported serine protease with coagulant activity, flavoxobin, purified from the same snake venom. To elucidate the molecular mechanism of the complement activation, the reactive products of the mixture of the purified human C3 and flavoxobin were examined by sodium dodecyl sulphate-polyacrylamide gel electrophoresis. The digesting pattern revealed that flavoxobin cleaves the alpha chain of the C3 molecule into two fragments. The N-terminal amino acid sequences for the remnant fragments of C3 disclosed that flavoxobin severs the human C3 at the Arg726-Ser727 site to form C3b and C3a the way C3bBb, the human alternative C3 convertase, does. In conclusion, flavoxobin acts as a novel, heterologous C3 convertase that independently cleaves human C3 and kick-starts the complement cascade.
- Published
- 2002
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40. Trimeresurus flavoviridis (habu snake) venom induces human erythrocyte lysis through enzymatic lipolysis, complement activation and decreased membrane expression of CD55 and CD59.
- Author
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Yamamoto C, Tsuru D, Oda-Ueda N, Ohno M, Hattori S, and Kim ST
- Subjects
- Animals, Complement Activation physiology, Dose-Response Relationship, Drug, Erythrocyte Membrane drug effects, Erythrocyte Membrane metabolism, Erythrocyte Membrane ultrastructure, Flow Cytometry, Fluorescent Antibody Technique, Hemolysis physiology, Humans, In Vitro Techniques, Lipolysis physiology, CD55 Antigens metabolism, CD59 Antigens metabolism, Complement Activation drug effects, Crotalid Venoms pharmacology, Hemolysis drug effects, Lipolysis drug effects, Trimeresurus
- Abstract
Trimeresurus flavoviridis (habu snake) bites can be fatal to man because of its virulent venom, which is clinicopathologically classified as haemorrhagic, necrotic, and haemolytic toxins. Trimeresurus flavoviridis venom causes lysis of human erythrocytes in conditions where plasma is present as well as in plasma-free conditions in a dose-dependent manner. The haemolytic process requires Ca2+ and Mg2+ ions in the solution. Additionally, the venom initiates activation of the human complement cascade as evidenced by C3a and C5a releases, complement consumption indicated by CH50 and formation of soluble membrane attack complex. The insertion of membrane attack complex into the erythrocyte membranes is morphologically identified by electronmicroscopy. Immunofluorescence analysis reveals that incubation of erythrocytes with the venom decreased cell-surface expression of CD55 (decay accelerating factor) and CD59 (protectin), which renders erythrocyte more vulnerable to adherent C3 and C5 convertases and to polymerization of C9 into membranes, and may enhance autologous complement-mediated haemolysis triggered by the venom. Our data demonstrate that Trimeresurus flavoviridis venom induces haemolysis in the presence of plasma by three distinct mechanisms, direct lipolysis through PLA2 activity, activation of the human complement system, and cleavages of CD55 and CD59 from erythrocyte membranes.
- Published
- 2001
- Full Text
- View/download PDF
41. A monoclonal antibody against the glutaraldehyde-conjugated polyamine, putrescine: application to immunocytochemistry.
- Author
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Fujiwara K, Tanabe T, Yabuuchi M, Ueoka R, and Tsuru D
- Subjects
- Animals, Antibodies, Monoclonal biosynthesis, Antibody Formation, Antibody Specificity, Chromatography, High Pressure Liquid methods, Enzyme-Linked Immunosorbent Assay methods, HeLa Cells, Humans, Immunoenzyme Techniques, Mice, Polyamines, Tumor Cells, Cultured, Antibodies, Monoclonal immunology, Glutaral, Putrescine immunology
- Abstract
We developed a mouse monoclonal antibody (mAb; APUT-32, IgG1 subisotype mAb) against putrescine (Put) conjugated to bovine serum albumin using a glutaraldehyde (GA)-sodium borohydride procedure, for applications in immunocytochemistry (ICC). The antibody specificity was evaluated by an ELISA binding test, simulating the ICC of tissue sections. APUT-32 mAb was highly specific to Put, and distinguished alterations in the chemical structure of other polyamine (PA) analogs, showing 3.8% crossreaction with cadaverine, 3.3% with spermidine (Spd), and 2.3% with 1,3-diaminopropane. Comparable results in immunoreactivity of APUT-32 mAb were obtained with the ELISA inhibition test. By the indirect immunoperoxidase method using the APUT-32 mAb, Put-like immunoreactivities were observed in the cytoplasm of HeLa and MCF-7 cell lines fixed with GA in combination with NaBH4 reduction, but almost no immunoreaction was seen in the cytoplasm of the human melanoma BD cell line. On the other hand, the same method but using a previously prepared ASPM-29 mAb, specific for spermine (Spm) and Spd, produced intense immunostaining in the cytoplasm of all the three cell types. The Put-like immunoreaction was completely abolished by absorption of the APUT-32 mAb with 10 microg/ml Put-human serum albumin conjugate prepared using GA and NaBH4. HPLC analysis was also performed for the levels of each of the PAs in the three types of cell, showing that the levels of Put detected were much lower than those of Spm and Spd, and were strikingly different in the three cell lines among which the human melanoma BD cell line contained the lowest levels of Put. These results strongly suggest that APUT-32 mAb reacts specifically with Put in the tumor cells and therefore has the potential as a new tool for elucidating the biological roles of Put in cells and tissues.
- Published
- 2001
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42. Expression and secretion of scytalidopepsin B, an acid protease from Scytalidium lignicolum, in yeast.
- Author
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Shimuta K, Oda-Ueda N, Washio M, Oyama H, Oda K, and Tsuru D
- Subjects
- Amino Acid Sequence, Base Sequence, DNA, Fungal, Electrophoresis, Polyacrylamide Gel methods, Mitosporic Fungi genetics, Molecular Sequence Data, Saccharomyces cerevisiae metabolism, Aspartic Acid Endopeptidases genetics, Enzyme Precursors genetics, Gene Expression, Mitosporic Fungi enzymology
- Abstract
An expression and secretion system for scytalidopepsin B, an acid protease from Scytalidium lignicolum, was constructed in yeast. Saccharomyces cerevisiae AH22 was transformed with an yeast-E. coli shuttle vector, pAM82, in which an yeast invertase signal segment and the cDNA encoding the pro- and mature enzyme regions were inserted. The transformant was found to secret a pepstatin-insensitive acid protease, when cultured aerobically in a low phosphate (Pi) medium. Amino terminal amino acid sequencing analysis indicated that the recombinant acid protease was accurately processed and secreted as a mature form.
- Published
- 2000
- Full Text
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43. Immunocytochemical localization of histamine in enterochromaffin-like (ECL) cells in rat oxyntic mucosa: a transmission electron microscopy study using monoclonal antibodies and conventional glutaraldehyde-based fixation.
- Author
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Fujiwara K, Bai G, Tamura C, and Tsuru D
- Subjects
- Animals, Antibodies, Monoclonal, Enterochromaffin Cells drug effects, Fixatives pharmacology, Gastric Mucosa drug effects, Glutaral pharmacology, Histamine immunology, Male, Microscopy, Electron, Parietal Cells, Gastric drug effects, Parietal Cells, Gastric metabolism, Rats, Rats, Wistar, Enterochromaffin Cells metabolism, Gastric Mucosa metabolism, Histamine metabolism
- Abstract
Histamine (HA), contained in the enterochromaffin-like (ECL) cells of the gastric mucosa in animals, plays an important role in gastric acid secretion, although methods for its exact morphological localization are still lacking. We used a pre-embedding indirect immunoperoxidase approach to define the fine structural localization of HA in rat oxyntic mucosa that was fixed with a glutaraldehyde-based fixative and HA monoclonal antibodies (MAbs AHA-1 and 2). Transmission electron microscopy showed that the peroxidase endproduct not only was concentrated in the cores of cytoplasmic granules but also was distributed to a high degree in the cytoplasm peripheral to the granules of the ECL cells. These results suggest that in ECL cells HA is enzymatically synthesized in the cytoplasm, then is transported and stored in the cores of the granules before its release from the basal lamina. The present HA immunoelectron microscopic method with MAbs would be applicable more generally to the ultrastructural identification of HA-containing cells.
- Published
- 1999
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44. Immunoelectron microscopic study for polyamines.
- Author
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Fujiwara K, Bai G, Kitagawa T, and Tsuru D
- Subjects
- Animals, Endoplasmic Reticulum, Rough chemistry, Male, Medulla Oblongata chemistry, Medulla Oblongata ultrastructure, Neurons chemistry, Neurons ultrastructure, Rats, Rats, Wistar, Ribosomes chemistry, Microscopy, Immunoelectron, Polyamines analysis
- Abstract
The polyamines (PAs) are ubiquitous polycationic metabolites in eukaryotic and prokaryotic cells and are believed to be intimately involved in the regulation of DNA, RNA, and protein biosynthesis, the exact function of which remains unclear, mainly because of a lack of knowledge of PA subcellular localization. In this study, using immunoelectron microscopy, we have demonstrated that PAs are predominantly located on free and attached ribosomes of the rough endoplasmic reticulum in the neurons of the lateral reticular nucleus of rat medulla oblongata. The nuclei, axons, and nerve endings were devoid of PA. This suggests that PAs are one of the components of biologically active ribosomes, being closely involved in the translation processes of protein biosynthesis.
- Published
- 1998
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- View/download PDF
45. Nucleotide sequence of the gene encoding the precursor protein of pepstatin insensitive acid protease B, scytalidopepsin B, from Scytalidium lignicolum.
- Author
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Oda N, Gotoh Y, Oyama H, Murao S, Oda K, and Tsuru D
- Subjects
- Amino Acid Sequence, Aspartic Acid Endopeptidases chemistry, Base Sequence, DNA Primers chemistry, Enzyme Precursors chemistry, Mitosporic Fungi enzymology, Molecular Sequence Data, Pepstatins chemistry, Polymerase Chain Reaction, Protease Inhibitors chemistry, Protein Precursors chemistry, Sequence Analysis, DNA, Sequence Homology, Amino Acid, Aspartic Acid Endopeptidases genetics, Enzyme Precursors genetics, Mitosporic Fungi genetics, Protein Precursors genetics
- Abstract
A chromosomal DNA of Scytalidium lignicolum was digested with Sau3AI. The digest was self-ligated and amplified by inverse PCR procedure using primers designed based on the nucleotide sequences of up- and down-stream regions of an intron present in the scytalidopepsin B gene. Analysis of the nucleotide sequence of PCR product (700 bp) showed that the enzyme is synthesized as a precursor protein consisting of the prepro- and mature enzyme regions. The deduced amino acid sequence was highly similar to those of aspergillopepsin A and recently reported endothiapepsins B and C, but quite different from those of pepstatin-insensitive bacterial acid proteases and the pepstatin-sensitive aspartic protease family.
- Published
- 1998
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46. Preparation of monoclonal antibodies against N-(gamma-maleimidobutyryloxy)succinimide (GMBS)-conjugated acetylspermine, and development of an enzyme-linked immunosorbent assay (ELISA) for N1,N12-diacetylspermine.
- Author
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Fujiwara K, Kaminishi Y, Kitagawa T, Tsuru D, Yabuuchi M, Kanetake H, and Nomata K
- Subjects
- Animals, Humans, Mice, Mice, Inbred BALB C, Sensitivity and Specificity, Spermine immunology, Spermine urine, Antibodies, Monoclonal immunology, Enzyme-Linked Immunosorbent Assay methods, Spermine analogs & derivatives, Succinimides immunology
- Abstract
We have developed three mouse monoclonal antibodies (mAb) of types IgG1 and IgG2b, i.e. anti-acetylspermine (Ac-Spm)-1 and 2 (ACSPM-1 and 2), and anti-acetylspermine (Ac-Spm)-3 (ACSPM-3), respectively, against Ac-Spm conjugated to bovine serum albumin via a heterobifunctional cross-linker, N-(gamma-maleimidobutyryloxy)succinimide (GMBS). Among these mAbs, ACSPM-2 was the most useful for the development of an enzyme-linked immunosorbent assay (ELISA) for acetylpolyamines (Ac-PAs) with glutaraldehyde (GA)-conjugated N1,N12-diacetylspermine (2Ac-Spm) or acetylspermine (Ac-Spm) as the solid phase antigen. However, GMBS-conjugated Ac-Spm did not behave as a solid phase antigen in the competitive ELISA. The ELISA is based on the principle of competition between an analyte and the conjugated antigen for the mAb, followed by immunoreaction with biotinylated anti-mouse immunoglobulin and horseradish peroxidase-streptavidin. The ACSPM-2 mAb reacted with 2Ac-Spm to the highest degree, followed by Ac-Spm, N1-acetylspermidine (N1-Ac-Spd), N8,N8-diacetylspermidine (2Ac-Spd), and spermine (Spm), the EC50 values being 0.06, 0.25, 7.0, 10, and 60 microM, respectively, but exhibited almost no cross-reaction with other polyamine-related compounds or amino acids. The method was used to determine the urinary Ac-PA levels in healthy subjects, the average value of 0.36 microg of 2Ac-Spm/g creatinine (n = 16) being obtained. The ACSPM-2 ELISA for 2Ac-Spm, which was the PA most relevant to the analysis of human urine among the five PA analogs mentioned above, might have potential for elucidation of the correlation of urinary 2Ac-Spm levels in cancers.
- Published
- 1998
- Full Text
- View/download PDF
47. Glutathione-independent formaldehyde dehydrogenase from Pseudomons putida: survey of functional groups with special regard for cysteine residues.
- Author
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Tsuru D, Oda N, Matsuo Y, Ishikawa S, Ito K, and Yoshimoto T
- Subjects
- Aldehyde Oxidoreductases biosynthesis, Aldehyde Oxidoreductases genetics, Amino Acid Sequence, Animals, Cysteine analysis, Horses, Kinetics, Models, Structural, Molecular Sequence Data, Mutagenesis, Site-Directed, Pseudomonas putida genetics, Recombinant Proteins biosynthesis, Aldehyde Oxidoreductases physiology, Cysteine metabolism, Glutathione physiology, Pseudomonas putida enzymology
- Abstract
The role of cysteine residues for structure and function of formaldehyde dehydrogenase from Pseudomonas putida was analysed by amino acid sequence comparison, homology-based structure modeling, site-directed mutagenesis, and chemical modification. Five out of seven cysteine residues found in the enzyme were concluded to coordinate with an active site zinc (Cys-46) and structural zinc atoms (Cys-97, -100, -103, and -111) from the sequence comparison with other Zn-containing medium-chain alcohol dehydrogenase homologues. The three-dimensional structure model based on the known structure of the horse liver E-type alcohol dehydrogenase (ADH) indicated that Cys-257 is located very far from the active site Zn and NAD+ binding region, suggesting that Cys-257 does not participate in the enzyme reaction. The structure also suggested that Cys-166 does not coordinate to active site Zn, but Asp-169 functions as a Zn-ligand, instead.
- Published
- 1997
- Full Text
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48. Nucleotide sequence of the gene encoding pepstatin-insensitive acid protease B, scytalidopepsin B, of Scytalidium lignicolum.
- Author
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Kakimori T, Yoshimoto T, Oyama H, Oda N, Gotoh Y, Oda K, Murao S, and Tsuru D
- Subjects
- Amino Acid Sequence, Aspartic Acid Endopeptidases biosynthesis, Base Sequence, Blotting, Southern, DNA, Fungal analysis, DNA, Fungal isolation & purification, Molecular Sequence Data, Molecular Weight, Polymerase Chain Reaction, Restriction Mapping, Aspartic Acid Endopeptidases genetics, Mitosporic Fungi genetics, Mitosporic Fungi metabolism, Pepstatins pharmacology, Protease Inhibitors pharmacology
- Abstract
A chromosomal DNA fragment of Scytalidium lignicolum that encodes the mature enzyme region of acid protease B (Scytalidopepsin B), was cloned and its nucleotides sequenced. The fragment contained a 76-bp intron at the middle of the mature enzyme-coding region. The mature enzyme was composed of 206 amino acid residues with a molecular weight of 21,550. There were some discrepancies between the amino acid sequence deduced from these results and that previously established by protein sequencing.
- Published
- 1996
- Full Text
- View/download PDF
49. Crystal structures of the binary and ternary complexes of 7 alpha-hydroxysteroid dehydrogenase from Escherichia coli.
- Author
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Tanaka N, Nonaka T, Tanabe T, Yoshimoto T, Tsuru D, and Mitsui Y
- Subjects
- Amino Acid Sequence, Animals, Binding Sites, Computer Simulation, Crystallization, Crystallography, X-Ray, Drosophila, Glycochenodeoxycholic Acid analogs & derivatives, Glycochenodeoxycholic Acid metabolism, Hydroxysteroid Dehydrogenases isolation & purification, Hydroxysteroid Dehydrogenases metabolism, Macromolecular Substances, Models, Molecular, Models, Structural, Molecular Sequence Data, NAD metabolism, Rats, Sequence Homology, Amino Acid, Software, Streptomyces enzymology, Substrate Specificity, Thermodynamics, Escherichia coli enzymology, Hydroxysteroid Dehydrogenases chemistry, Protein Conformation, Protein Structure, Secondary
- Abstract
7 alpha-Hydroxysteroid dehydrogenase (7 alpha-HSDH;1 EC 1.1.1.159) is an NAD+-dependent oxidoreductase belonging to the short-chain dehydrogenase/reductase (SDR) 1 family. It catalyzes the dehydrogenation of a hydroxyl group at position 7 of the steroid skeleton of bile acids. The crystal structure of the binary (complexed with NAD+) complex of 7 alpha-HSDH has been solved at 2.3 A resolution by the multiple isomorphous replacement method. The structure of the ternary complex [the enzyme complexed with NADH, 7-oxoglycochenodeoxycholic acid (as a reaction product), and possibly partially glycochenodeoxycholic acid (as a substrate)] has been determined by a difference Fourier method at 1.8 A resolution. The enzyme 7 alpha-HSDH is an alpha/beta doubly wound protein having a Rossmann-fold domain for NAD (H) binding. Upon substrate binding, large conformation changes occur at the substrate binding loop (between the beta F strand and alpha G helix) and the C-terminal segment (residues 250-255). The variable amino acid sequences of the substrate-binding loop appear to be responsible for the wide variety of substrate specificities observed among the enzymes of the SDR family. The crystal structure of the ternary complex of 7 alpha-HSDH, which is the only structure available as the ternary complex among the enzymes of the SDR family, indicates that the highly conserved Tyr159 and Ser146 residues most probably directly interact with the hydroxyl group of the substrates although this observation cannot be definite due to an insufficiently characterized nature of the ternary complex. The strictly conserved Lys163 is hydrogen-bonded to both the 2'- and 3'-hydroxyl groups of the nicotinamide ribose of NAD(H). We propose a new catalytic mechanism possibly common to all the enzymes belonging to the SDR family in which a tyrosine residue (Tyr159) acts as a catalytic base and a serine residue (Ser146) plays a subsidiary role of stabilizing substrate binding.
- Published
- 1996
- Full Text
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50. Prolidase from Xanthomonas maltophilia: purification and characterization of the enzyme.
- Author
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Suga K, Kabashima T, Ito K, Tsuru D, Okamura H, Kataoka J, and Yoshimoto T
- Subjects
- Chromatography, Ion Exchange, Dipeptidases antagonists & inhibitors, Dipeptidases metabolism, Hydrogen-Ion Concentration, Indicators and Reagents, Metals pharmacology, Substrate Specificity, Temperature, Dipeptidases isolation & purification, Xanthomonas enzymology
- Abstract
Prolidase (iminodipeptidase, EC 3.4.13.9) was purified from an extract of Xanthomonas maltophilia, by ammonium sulfate fractionation and sequential chromatographies on DEAE-Toyopearl, Toyopearl HW65C, FPLC-Hiload Superdex 200 pg, and FPLC-Hitrap Q columns, which an activity recovery of 2.3%. The enzyme was the most active at pH 7.5 with Leu-Pro as substrate. It was stable between pH 6.0 and 8.5 for 60 min at 37 degrees C and retained half of activity after 60 min at 37 degrees C. The isoelectric point of the enzyme was 3.7. Its molecular weight was estimated to be 100,000 by gel filtration on FPLC-Hiload Superdex 200 and 51,000 by SDS-PAGE, suggesting that it is a dimer. It hydrolyzed dipeptides only if proline is located at the carboxyl terminal position. The enzyme was inhibited by PCMB and o-phenanthroline, and was activated by Mn2+.
- Published
- 1995
- Full Text
- View/download PDF
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