42 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. 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
4. 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
5. 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. 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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, Faitsch, M, Falie, D, Fanni, A, Fasoli, A, Faustin, J, Fawlk, N, Fazendeiro, L, Fedorczak, N, Felton, R, Fenton, K, Fernades, A, Fernandes, H, Ferreira, J, Fessey, J, 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, 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, Garzotti, L, Gaudio, P, Gauthier, E, Gear, D, Gee, S, Geiger, B, Gelfusa, M, Gerasimov, S, Gervasini, G, Gethins, M, Ghani, Z, Ghate, M, Gherendi, M, Giacalone, J, Giacomelli, L, Gibson, C, Giegerich, T, Gil, C, Gil, L, Gilligan, S, Gin, D, Giovannozzi, E, Girardo, J, 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, Graves, J, Grazier, N, Grazier, P, Green, N, Greuner, H, Grierson, B, Griph, F, Grisolia, C, Grist, D, Groth, M, Grove, R, Grundy, C, Grzonka, J, Guard, D, Guerard, C, Guillemaut, C, Guirlet, R, Gurl, C, Utoh, H, Hackett, L, Hacquin, S, Hagar, A, Hager, R, Hakola, A, Halitovs, M, Hall, S, Cook, S, Hamlyn-Harris, C, Hammond, K, Harrington, C, Harrison, J, Harting, D, Hasenbeck, F, Hatano, Y, Hatch, D, Haupt, T, Hawes, J, Hawkes, N, Hawkins, J, Hawkins, P, Haydon, P, Hayter, N, Hazel, S, Heesterman, P, Heinola, K, Hellesen, C, Hellsten, T, Helou, W, Hemming, O, Hender, T, Henderson, M, Henderson, S, Henriques, R, Hepple, D, Hermon, G, Hertout, P, Hidalgo, C, Highcock, E, Hill, M, Hillairet, J, Hillesheim, J, Hillis, D, Hizanidis, K, Hjalmarsson, A, Hobirk, J, Hodille, E, Hogben, C, Hogeweij, G, Hollingsworth, A, Hollis, S, Homfray, D, Horacek, J, Hornung, G, Horton, A, Horton, L, Horvath, L, Hotchin, S, Hough, M, Howarth, P, Hubbard, A, Huber, A, Huber, V, Huddleston, T, Hughes, M, Hunter, C, Huynh, P, Hynes, A, Iglesias, D, Imazawa, N, Imbeaux, F, Imrisek, M, Incelli, M, Innocente, P, Irishkin, M, Stanik, I, Jachmich, S, Jacobsen, A, 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, Hoshino, 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, Keenan, T, Keep, J, Kempenaars, M, Kennedy, C, Kenny, D, Kent, J, Kent, O, Khilkevich, E, Kim, H, Kinch, A, King, C, King, D, King, R, Kinna, D, Kiptily, V, Kirk, A, Kirov, K, Kirschner, A, Kizane, G, Klepper, C, Klix, A, Knight, P, Knipe, S, 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, 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, Laguardia, L, Lahtinen, A, Laing, A, Lam, N, Lambertz, H, Lane, C, Lang, P, Lanthaler, S, Lapins, J, Lasa, A, Last, J, Laszynska, E, Lawless, R, Lawson, A, Lawson, K, Lazaros, A, Lazzaro, E, Leddy, J, Lee, S, Lefebvre, X, Leggate, H, 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, C, Lipschultz, B, Liu, G, Liu, Y, Lo Schiavo, V, Loarer, T, Loarte, A, Lobel, R, Lomanowski, B, Lomas, P, Lonnroth, J, Lopez, J, Lopez-Razola, J, Lorenzini, R, Losada, U, Lovell, J, Loving, A, Lowry, C, Luce, T, Lucock, R, Lukin, A, Luna, C, Lungaroni, M, Lungu, C, 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, Mantica, P, Mantsinen, M, Manzanares, A, Maquet, P, Marandet, Y, Marcenko, N, Marchetto, C, Marchuk, O, Marinelli, M, Marinucci, M, Markovic, T, Marocco, D, Marot, L, Marren, C, Marshal, R, Martin, A, Martin, Y, de Aguilera, A, Martinez, F, Martin-Solis, J, Martynova, Y, Maruyama, S, Masiello, A, Maslov, M, Matejcik, S, Mattei, M, Matthews, G, Maviglia, F, Mayer, M, Mayoral, M, May-Smith, T, Mazon, D, Mazzotta, C, Mcadams, R, Mccarthy, P, Mcclements, K, Mccormack, O, Mccullen, P, Mcdonald, D, Mcintosh, S, Mckean, R, Mckehon, J, Meadows, R, Meakins, A, Medina, F, Medland, M, Medley, S, Meigh, S, Meigs, A, Meisl, G, Meitner, S, Meneses, L, Menmuir, S, Mergia, K, Merrigan, I, Mertens, P, 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, Morris, J, Moser, L, Mosher, S, Moulton, D, Murari, A, Muraro, A, Murphy, S, Asakura, N, Na, Y, Nabais, F, Naish, R, Nakano, T, Nardon, E, Naulin, V, Nave, M, Nedzelski, I, Nemtsev, G, Nespoli, F, Neto, A, Neu, R, Neverov, V, Newman, M, Nicholls, K, Nicolas, T, Nielsen, A, 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, O'Gorman, T, Okabayashi, M, Olney, R, Omolayo, O, O'Mullane, M, Ongena, J, Orsitto, F, Orszagh, J, Oswuigwe, B, Otin, R, Owen, A, Paccagnella, R, Pace, N, Pacella, D, Packer, L, Page, A, Pajuste, E, Palazzo, S, Panja, S, Papp, P, Paprok, R, Parail, V, Park, M, Diaz, F, Parsons, M, Pasqualotto, R, Patel, A, Pathak, S, Paton, D, Patten, H, Pau, A, Pawelec, E, Soldan, C, Peackoc, A, Pearson, I, Pehkonen, S, Peluso, E, Penot, C, Pereira, A, Pereira, R, Puglia, P, von Thun, C, 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, Piron, L, Pironti, A, Pisano, F, Pitts, R, Pizzo, F, Plyusnin, V, Pomaro, N, Pompilian, O, Pool, P, Popovichev, S, Porfiri, M, 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, Puiatti, M, Pulley, D, Purahoo, K, Putterich, T, Rachlew, E, Rack, M, Ragona, R, Rainford, M, Rakha, A, Ramogida, G, Ranjan, S, Rapson, C, Rasmussen, 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, Reynolds, S, Riccardo, V, Richardson, N, Riddle, K, Rigamonti, D, Rimini, F, Risner, J, Riva, M, Roach, C, Robins, R, Robinson, S, Robinson, T, Robson, D, 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, 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, Sergienko, G, Sertoli, M, Shabbir, A, Sharapov, S, 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, Simpson, J, Simpson-Hutchinson, J, Sinha, A, Sipila, S, Sips, A, Siren, P, Sirinelli, A, Sjostrand, H, Skiba, M, Skilton, R, Slabkowska, K, Slade, B, Smith, N, Smith, P, Smith, R, Smith, T, Smithies, M, Snoj, L, Soare, S, Solano, E, Somers, A, Sommariva, C, Sonato, P, Sopplesa, A, Sousa, J, Sozzi, C, Spagnolo, S, Spelzini, T, Spineanu, F, Stables, G, Stamatelatos, I, Stamp, M, Staniec, P, Stankunas, G, Stan-Sion, C, Stead, M, Stefanikova, E, Stepanov, I, Stephen, A, Stephen, M, Stevens, A, Stevens, B, Strachan, J, Strand, P, Strauss, H, Strom, P, Stubbs, G, Studholme, W, Subba, F, Summers, H, Svensson, J, Swiderski, L, Szabolics, T, Szawlowski, M, Szepesi, G, Suzuki, T, Tal, B, Tala, T, Talbot, A, Talebzadeh, S, Taliercio, C, Tamain, P, Tame, C, Tang, W, Tardocchi, M, Taroni, L, Taylor, D, Taylor, K, Tegnered, D, Telesca, G, Teplova, N, Terranova, D, Testa, D, Tholerus, E, Thomas, J, Thomas, P, Thompson, A, Thompson, C, Thompson, V, Thorne, L, Thornton, A, Thrysoe, A, Tigwell, P, 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, Turner, I, Turner, M, Turnyanskiy, M, Tvalashvili, G, Tyrrell, S, Uccello, A, Ul-Abidin, Z, Uljanovs, J, Ulyatt, D, Uytdenhouwen, I, Vadgama, A, Valcarcel, D, Valentinuzzi, M, Valisa, M, Olivares, P, Valovic, M, Van De Mortel, M, Van Eester, D, Van Renterghem, W, van Rooij, G, Varje, J, Varoutis, S, Vartanian, S, Vasava, K, Vasilopoulou, T, Vega, J, Verdoolaege, G, Verhoeven, R, Verona, C, Rinati, G, 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, Wakeling, B, Waldon, C, Walkden, N, Walker, M, Walker, R, Walsh, M, Wang, E, Wang, N, Warder, S, Warren, R, Waterhouse, J, Watkins, N, Watts, C, Wauters, T, Weckmann, A, Weiland, J, Weisen, H, Weiszflog, M, Wellstood, C, West, A, Wheatley, M, Whetham, S, 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- 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
6. Analysis of ELM stability with extended MHD models in JET, JT-60U and future JT-60SA tokamak plasmas
- Author
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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., and Seki M.
- Abstract
The stability with respect to a peelingballooning 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.
- Published
- 2018
7. Consideration on blanket structure for fusion DEMO plant at JAERI
- Author
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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.
- Published
- 2006
- Full Text
- View/download PDF
8. Design study of fusion DEMO plant at JAERI
- Author
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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.
- Published
- 2006
- Full Text
- View/download PDF
9. Adoption of a genetic algorithm (GA) for tomographic reconstruction of line-of-sight optical images
- Author
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Kihm, K. D., Okamoto, K., Tsuru, D., and Ko, H. S.
- Published
- 1996
- Full Text
- View/download PDF
10. Visualization of 3D gas density distribution using optical tomography
- Author
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Feng, J., Okamoto, K., Tsuru, D., Madarame, H., and Fumizawa, M.
- Published
- 2002
- Full Text
- View/download PDF
11. Safety activities in JAERI related to ITER
- Author
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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.
- Published
- 2001
- Full Text
- View/download PDF
12. 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
- Full Text
- View/download PDF
13. Cloning and high-level expression of the glutathione-independent formaldehyde dehydrogenase gene from Pseudomonas putida
- Author
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Ito, K, primary, Takahashi, M, additional, Yoshimoto, T, additional, and Tsuru, D, additional
- Published
- 1994
- Full Text
- View/download PDF
14. Location of the 7 alpha-hydroxysteroid dehydrogenase gene (hdhA) on the physical map of the Escherichia coli chromosome
- Author
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Yoshimoto, T, primary, Nagai, H, additional, Ito, K, additional, and Tsuru, D, additional
- Published
- 1993
- Full Text
- View/download PDF
15. Location of the protease II gene (ptrB) on the physical map of the Escherichia coli chromosome
- Author
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Kanatani, A, primary, Yoshimoto, T, additional, Nagai, H, additional, Ito, K, additional, and Tsuru, D, additional
- Published
- 1992
- Full Text
- View/download PDF
16. Cloning, sequencing, and high expression of the proline iminopeptidase gene from Bacillus coagulans
- Author
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Kitazono, A, primary, Yoshimoto, T, additional, and Tsuru, D, additional
- Published
- 1992
- Full Text
- View/download PDF
17. Acetyl-CoA carboxylase from Escherichia coli: gene organization and nucleotide sequence of the biotin carboxylase subunit.
- Author
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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
- Published
- 1991
- Full Text
- View/download PDF
18. Cloning and sequencing of the 7 alpha-hydroxysteroid dehydrogenase gene from Escherichia coli HB101 and characterization of the expressed enzyme
- Author
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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
- Full Text
- View/download PDF
19. Study on decay heat removal of compact ITER
- Author
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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
- Full Text
- View/download PDF
20. 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
- Full Text
- View/download PDF
21. 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
- Full Text
- View/download PDF
22. 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
- View/download PDF
23. 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
- Full Text
- View/download PDF
24. 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
- Full Text
- View/download PDF
25. 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
- Full Text
- View/download PDF
26. 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
- View/download PDF
27. Nucleotide sequence of the gene encoding pepstatin-insensitive acid protease B, scytalidopepsin B, of Scytalidium lignicolum.
- Author
-
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
28. 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
29. Partial purification and characterization of an esterase acting on the anticancer pro-drugs, 7-ethylcamptothecin derivatives.
- Author
-
Fujita Y, Yaegashi T, Sawada S, Oyama H, Yoshimoto T, and Tsuru D
- Subjects
- Animals, Camptothecin metabolism, Chromatography, High Pressure Liquid, Esterases antagonists & inhibitors, Esterases metabolism, Irinotecan, Liver enzymology, Male, Pancreas enzymology, Rats, Rats, Wistar, Antineoplastic Agents, Phytogenic metabolism, Camptothecin analogs & derivatives, Esterases isolation & purification, Prodrugs metabolism
- Abstract
A hydrolytic enzyme which catalyzes hydrolysis of the ester-linkage of a series of 17-O-acyl derivatives of 7-ethylcamptothecin-21-(2-dimethylamino)ethylamide [acyl derivatives of 22E] was purified from rat liver and its properties were characterized. It hydrolyzed the ester-linkage of all 22E derivatives tested as well as p-nitrophenyl acetate at pH 8-9 but had no effect on 7-ethyl-10-[4-(piperidino)-1-piperidino] carbonyloxycamptothecin (CPT-11: irinotecan), unlike CPT-11 converting carboxylesterase, which was previously purified from rat serum [Tsuji T. et al., J. Pharmacobio-Dyn., 14, 341 (1991)]. The enzyme had no effect on either acetyl choline or butyrylcholine. It was inhibited by several organophosphorous compounds such as diisopropyl fluorophosphate (DFP), bis-(p-nitrophenyl)phosphate and paraoxon, but was insensitive to inhibitors specific for choline esterases. These results indicate that this liver esterase is clearly distinct from choline esterase and serum CPT-11 converting enzyme and is able to convert pro-drugs, O-acyl derivatives of 22E, to an antitumor agent.
- Published
- 1995
- Full Text
- View/download PDF
30. Prolylcarboxypeptidase (angiotensinase C): purification and characterization of the enzyme from Xanthomanas maltophilia.
- Author
-
Suga K, Ito K, Tsuru D, and Yoshimoto T
- Subjects
- Amino Acid Sequence, Ammonium Sulfate chemistry, Carboxypeptidases antagonists & inhibitors, Carboxypeptidases chemistry, Carboxypeptidases metabolism, Chelating Agents pharmacology, Chemical Fractionation, Chloromercuribenzoates pharmacology, Chromatography, High Pressure Liquid, Electrophoresis, Polyacrylamide Gel, Hydrogen-Ion Concentration, Hydrolysis, Iodoacetamide pharmacology, Isoelectric Focusing, Isoflurophate pharmacology, Molecular Sequence Data, Molecular Weight, Phenylmethylsulfonyl Fluoride pharmacology, Proline metabolism, p-Chloromercuribenzoic Acid, Carboxypeptidases isolation & purification, Xanthomonas enzymology
- Abstract
Prolylcarboxypeptidase (Angiotensinase C, EC 3.4.16.2) was purified to homogeneity from cell free extracts of Xanthomonas maltophilia by ammonium sulfate fractionation and sequential chromatographies on DEAE-Toyopearl, Sephadex G-150, FPLC-Hiload Superdex 200 pg, and FPLC-Hitrap SP columns, with an activity recovery of 15%. The molecular weight of the enzyme was found to be 330,000 by gel filtration and 83,000 by SDS-PAGE, suggesting a tetrameric form for the native enzyme. It had an optimum pH of 8.5 and stability between pH 8.0 and 11.0. The isoelectric point of the enzyme was 6.6. The enzyme hydrolyzed Pro-X bonds when proline was in the penultimate position from the carboxyl terminal. The enzyme was strongly inhibited by diisopropylfluorophosphate (DFP), while phenylmethylsulfonyl fluoride (PMSF), p-chloromercuribenzoic acid (PCMB), iodoacetamide, and metal chelators had no effect.
- Published
- 1995
- Full Text
- View/download PDF
31. Degradation of streptomyces metalloprotease inhibitor (SMPI) by neutral protease from Bacillus subtilis var. amylosacchariticus.
- Author
-
Tsuru D, Fujita Y, Morikawa S, Ito K, and Yoshimoto T
- Subjects
- Amino Acid Sequence, Chromatography, High Pressure Liquid, Molecular Sequence Data, Substrate Specificity, Bacillus subtilis enzymology, Bacterial Proteins metabolism, Metalloendopeptidases antagonists & inhibitors, Streptomyces enzymology, Thermolysin antagonists & inhibitors
- Abstract
The zinc-containing neutral endopeptidase (neutral protease: BANP) from Bacillus subtilis var. amylosacchariticus was inhibited by the proteinaceous metalloprotease inhibitor isolated from Streptomyces nigrescens (SMPI). The degree of inhibition was, however, significantly less than that for thermolysin (TLN). During incubation of BANP with SMPI, the inhibitor was proteolytically degraded and inactivated. Analysis of the digestion products suggested that a minor diversity in their substrate specificities between TLN and BANP affects the sensitivity to the proteinaceous metalloprotease inhibitor, SMPI.
- Published
- 1992
- Full Text
- View/download PDF
32. Chemical modification of neutral protease from Bacillus subtilis var. amylosacchariticus: assignment of tyrosyl residues iodinated.
- Author
-
Morikawa S, Kanatani A, Kobayashi R, Yoshimoto T, and Tsuru D
- Subjects
- Amino Acid Sequence, Bacterial Proteins metabolism, Caseins metabolism, Iodine chemistry, Metalloendopeptidases metabolism, Molecular Sequence Data, Tyrosine chemistry, Bacillus subtilis enzymology, Bacterial Proteins chemistry, Metalloendopeptidases chemistry, Tyrosine analysis
- Abstract
The neutral protease of Bacillus subtilis var. amylosacchariticus (B. amylosacchariticus) was iodinated with a 25-fold molar excess of iodine at pH 9.4 for 3 min at 0 degree C, by which treatment the proteolytic activity toward casein was markedly reduced, while the hydrolytic activity toward an N-blocked peptide substrate was rather increased. The modified enzyme was digested with Staphylococcus aureus V8 protease at pH 8.0 and the amino acid sequences of resultant peptides were compared with those obtained from the native enzyme. One of the peptides was found to have an amino acid sequence of Thr-Ala-Asn-Leu-Ile-Tyr-Glu, which corresponds to residue Nos. 153-159 of the enzyme, where Tyr-158 was identified to be mono-iodotyrosine. The other two peptides were those containing Tyr-21 which was mono- and di-iodinated, respectively. Referring to nitration experiments on the neutral protease and the active site structure of thermolysin, it was concluded that the iodination of Tyr-158 is mainly responsible for the activity changes of B. amylosacchariticus neutral protease.
- Published
- 1991
33. Dye-sensitized photooxidation of neutral protease from Bacillus subtilis var. amylosacchariticus: assignment of histidine residue oxidized.
- Author
-
Morikawa S, Kanatani A, Yoshimoto T, and Tsuru D
- Subjects
- Amino Acid Sequence, Chromatography, High Pressure Liquid, Endopeptidases metabolism, Metalloendopeptidases metabolism, Molecular Sequence Data, Oxidation-Reduction, Peptides chemistry, Peptides isolation & purification, Photochemistry, Bacillus subtilis enzymology, Bacterial Proteins, Histidine chemistry, Metalloendopeptidases chemistry
- Abstract
The neutral protease of Bacillus subtilis var. amylosacchariticus was photooxidized in the presence of methylene blue, by which treatment the enzyme was rapidly inactivated. The inactive enzyme was digested with endoproteinase Asp-N, the resultant peptides were separated by HPLC, and their amino acid sequences were compared with those obtained from the unmodified enzyme. Of four peptides that contained histidine residues, only the recovery of one peptide was found to be decreased by the photooxidation with the appearance of a new peptide. Comparisons of amino acid compositions and sequences between these two peptides showed that the latter peptide lacked His228 of the former one, indicating that His228 was photooxidized. This result suggests that His228 is involved in the catalytic reaction of the neutral protease or interaction with substrates.
- Published
- 1991
34. CPT-11 converting enzyme from rat serum: purification and some properties.
- Author
-
Tsuji T, Kaneda N, Kado K, Yokokura T, Yoshimoto T, and Tsuru D
- Subjects
- Animals, Antineoplastic Agents, Phytogenic metabolism, Camptothecin blood, Camptothecin metabolism, Carboxylic Ester Hydrolases chemistry, Carboxylic Ester Hydrolases isolation & purification, Hydrogen-Ion Concentration, Hydrolysis, Irinotecan, Isoelectric Point, Kinetics, Male, Molecular Weight, Rats, Rats, Inbred Strains, Camptothecin analogs & derivatives, Carboxylic Ester Hydrolases blood, Prodrugs metabolism
- Abstract
A rat serum enzyme that catalyzes the conversion of a pro-drug, 7-ethyl-10-[4-(1-piperidino)-1-piperidino] carbonyloxycamptothecin (CPT-11), to an anticancer drug, 7-ethyl-10-hydroxycamptothecin (SN-38), was purified and its properties were characterized. The enzyme was purified by column chromatography on diethylaminoethyl Toyopearl 650M, QAE-Sephadex, Sephadex G-150, Con A-Sepharose and high performance liquid chromatography with an ion-exchanger column. It was most active at pH 7.5 and was stable at pH 4-9 for 1 h at 30 degrees C. The molecular weight was estimated to be 60 and 57 kDa by gel filtration and sodium dodecylsulfate-polyacrylamide gel electrophoresis methods, respectively, and the isoelectric point was 4.6, as determined by isoelectric focusing. The Km value for CPT-11 was 0.28 microM. This enzyme was inhibited by diisopropyl phosphorofluoridate (DFP) and phenylmethanesulfonyl fluoride (PMSF) but insensitive to eserine, p-chloromercuribenzoate (PCMB) and ethylenediaminetetraacetate (EDTA). The enzyme also hydrolyzed p-nitrophenylacetate (p-NPA), a commonly used substrate for esterases, but was not active toward acetylcholine, suggesting that the enzyme is a carboxylesterase[EC 3.1.1.1]. During the hydrolyses of CPT-11 and p-NPA, an initial burst phenomenon similar to that found in the alpha-chymotrypsin-catalyzed hydrolysis of p-NPA was observed. Kinetic analysis revealed that the deacylation of the enzyme is the rate-limiting step in substrate hydrolysis. This enzyme was found to also split other ester derivatives of SN-38 besides CPT-11.
- Published
- 1991
- Full Text
- View/download PDF
35. Structure activity relationship of inhibitors specific for prolyl endopeptidase.
- Author
-
Yoshimoto T, Tsuru D, Yamamoto N, Ikezawa R, and Furukawa S
- Subjects
- Models, Molecular, Molecular Conformation, Molecular Structure, Oxygen chemistry, Proline analogs & derivatives, Proline chemistry, Proline pharmacology, Prolyl Oligopeptidases, Pyrrolidines chemistry, Pyrrolidines pharmacology, Safrole analogs & derivatives, Safrole chemistry, Serine Proteinase Inhibitors chemistry, Structure-Activity Relationship, Substrate Specificity, Sulfur chemistry, Endopeptidases drug effects, Serine Endopeptidases
- Abstract
Structural requirements of N-blocked L-proline derivatives as specific inhibitors for prolyl endopeptidase were investigated using a series of substrate analogs. Replacement of L-proline by its D-isomer remarkably reduced the inhibition. Introduction of a sulfur atom in proline and/or in the penultimate pyrrolidine rings significantly increased the inhibition, but the introduction of oxygen rather diminished the activity. A peptide linkage (acid-amide bond) between the proline and the pyrrolidine ring was also required to keep the inhibitory activity. A benzyloxycarbonyl group was most effective as an N-blocked component of the inhibitors.
- Published
- 1991
36. Pyroglutamyl peptidase from chicken liver: purification and some properties.
- Author
-
Tsuru D, Sakabe K, Yoshimoto T, and Fujiwara K
- Subjects
- Amino Acid Sequence, Animals, Chickens, Hydrogen-Ion Concentration, Pyroglutamyl-Peptidase I analysis, Substrate Specificity, Aminopeptidases isolation & purification, Liver enzymology, Pyroglutamyl-Peptidase I isolation & purification
- Published
- 1982
- Full Text
- View/download PDF
37. Prolyl endopeptidase from bovine testis: purification, characterization and comparison with the enzymes from other tissues.
- Author
-
Yoshimoto T, Oyama H, Koriyama N, and Tsuru D
- Subjects
- Animals, Cattle, Endopeptidases analysis, Endopeptidases metabolism, In Vitro Techniques, Male, Prolyl Oligopeptidases, Substrate Specificity, Endopeptidases isolation & purification, Serine Endopeptidases, Testis enzymology
- Published
- 1988
- Full Text
- View/download PDF
38. An inhibitor for post-proline cleaving enzyme; distribution and partial purification from porcine pancreas.
- Author
-
Yoshimoto T, Tsukumo K, Takatsuka N, and Tsuru D
- Subjects
- Animals, Aprotinin pharmacology, Chromatography, Gel, Cytochrome c Group antagonists & inhibitors, Kinetics, Molecular Weight, Prolyl Oligopeptidases, Rats, Species Specificity, Swine, Trypsin, Endopeptidases metabolism, Pancreas metabolism, Serine Endopeptidases
- Abstract
An inhibitor(s) for post-proline cleaving enzyme was checked by using a fluorogenic substrate, Z-Gly-Pro-4-methyl coumarinamide, and was found to be distributed widely in rat and porcine organs. The highest inhibitory activity on the enzyme was observed in pancreas and the inhibitor was partially purified from porcine pancreas extract by heat treatment, chromatographies on DEAE-Sephadex and Sephadex G-50 and affinity chromatography on trypsin-Sepharose. This inhibitor was very stable against temperature, pH and trichloroacetic acid treatment. The molecular weight was estimated to be 6500 by gel filtration. This inhibitor was highly specific for prolyl endopeptidases from mammals and Flavobacterium and inhibited the enzyme competitively. It acted neither on proline specific exopeptidases such as dipeptidyl aminopeptidase IV, proline aminopeptidase, prolidase, nor usual endopeptidases such as trypsin and alpha-chymotrypsin.
- Published
- 1982
- Full Text
- View/download PDF
39. Salicylurate-hydrolyzing enzyme from intestinal bacterium in rabbit: purification and characterization.
- Author
-
Ogushi S, Watanabe H, Nakayama M, and Tsuru D
- Subjects
- Amidohydrolases isolation & purification, Animals, Feces microbiology, Hydrolysis, Intestines microbiology, Rabbits, Amidohydrolases analysis, Bacteria enzymology, Hippurates analysis
- Published
- 1988
- Full Text
- View/download PDF
40. Effects of carbon sources and base analogues of nucleic acid on the formation of bacterial amylase.
- Author
-
FUKUMOTO J, YAMAMOTO T, and TSURU D
- Subjects
- Amylases, Bacteria metabolism, Carbon, Nucleic Acids, Organic Chemicals
- Published
- 1957
- Full Text
- View/download PDF
41. BACILLUS SUBTILIS NEUTRAL PROTEINASE. I. A ZINC ENZYME OF HIGH SPECIFIC ACTIVITY.
- Author
-
MCCONN JD, TSURU D, and YASUNOBU KT
- Subjects
- Bacillus subtilis, Bacterial Proteins, Calcium, Chromatography, Cobalt, Edetic Acid, Electrophoresis, Enzyme Inhibitors, Hydrogen-Ion Concentration, Indicators and Reagents, Manganese, Metalloendopeptidases, Peptide Hydrolases, Research, Spectrophotometry, Sulfhydryl Compounds, Ultracentrifugation, Zinc
- Published
- 1964
42. BACILLUS SUBTILIS NEUTRAL PROTEINASE. II. SOME PHYSICOCHEMICAL PROPERTIES.
- Author
-
TSURU D, MCCONN JD, and YASUNOBU KT
- Subjects
- Amino Acids, Bacillus subtilis, Bacterial Proteins, Biochemical Phenomena, Biochemistry, Chemical Phenomena, Chemistry, Physical, Electrophoresis, Metalloendopeptidases, Molecular Weight, Peptide Hydrolases, Research
- Published
- 1965
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