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84 results on '"Kouzuma Y"'

1. First Muon-Neutrino Disappearance Study with an Off-Axis Beam

Author: T2K Collaboration, Abe, K., Abgrall, N., Ajima, Y., Aihara, H., Albert, J. B., Andreopoulos, C., Andrieu, B., Anerella, M. D., Aoki, S., Araoka, O., Argyriades, J., Ariga, A., Ariga, T., Assylbekov, S., Autiero, D., Badertscher, A., Barbi, M., Barker, G. J., Barr, G., Bass, M., Batkiewicz, M., Bay, F., Bentham, S., Berardi, V., Berger, B. E., Bertram, I., Besnier, M., Beucher, J., Beznosko, D., Bhadra, S., Blaszczyk, F. d. M., Blocki, J., Blondel, A., Bojechko, C., Bouchez, J., Boyd, S. B., Bravar, A., Bronner, C., Brook-Roberge, D. G., Buchanan, N., Budd, H., Calland, R., Calvet, D., Rodriguez, J. Caravaca, Cartwright, S. L., Carver, A., Castillo, R., Catanesi, M. G., Cazes, A., Cervera, A., Chavez, C., Choi, S., Christodoulou, G., Coleman, J., Collazuol, G., Coleman, W., Connolly, K., Curioni, A., Dabrowska, A., Danko, I., Das, R., Davies, G. S., Davis, S., Day, M., De Rosa, G., de André, J. P. A. M., de Perio, P., Dealtry, T., Delbart, A., Densham, C., Di Lodovico, F., Di Luise, S., Tran, P. Dinh, Dobson, J., Dore, U., Drapier, O., Duboyski, T., Dufour, F., Dumarchez, J., Dytman, S., Dziewiecki, M., Dziomba, M., Emery, S., Ereditato, A., Escallier, J. E., Escudero, L., Esposito, L. S., Fechner, M., Ferrero, A., Finch, A. J., Frank, E., Fujii, Y., Fukuda, Y., Galymov, V., Ganetis, G. L., Gannaway, F. C., Gaudin, A., Gendotti, A., George, M. A., Giffin, S., Giganti, C., Gilje, K., Ghosh, A. K., Golan, T., Goldhaber, M., Gomez-Cadenas, J. J., Gomi, S., Gonin, M., Grant, N., Grant, A., Gumplinger, P., Guzowski, P., Hadley, D. R., Haesler, A., Haigh, M. D., Hamano, K., Hansen, C., Hansen, D., Hara, T., Harrison, P. F., Hartfiel, B., Hartz, M., Haruyama, T., Hasegawa, T., Hastings, N. C., Hatzikoutelis, A., Hayashi, K., Hayato, Y., Hearty, C., Helmer, R. L., Henderson, R., Higashi, N., Hignight, J., Hillairet, A., Hiraki, T., Hirose, E., Holeczek, J., Horikawa, S., Huang, K., Hyndman, A., Ichikawa, A. K., Ieki, K., Ieva, M., Iida, M., Ikeda, M., Ilic, J., Imber, J., Ishida, T., Ishihara, C., Ishii, T., Ives, S. J., Iwasaki, M., Iyogi, K., Izmaylov, A., Jamieson, B., Johnson, R. A., Joo, K. K., Jover-Manas, G. V., Jung, C. K., Kaji, H., Kajita, T., Kakuno, H., Kameda, J., Kaneyuki, K., Karlen, D., Kasami, K., Kato, I., Kawamuko, H., Kearns, E., Khabibullin, M., Khanam, F., Khotjantsev, A., Kielczewska, D., Kikawa, T., Kim, J., Kim, J. Y., Kim, S. B., Kimura, N., Kirby, B., Kisiel, J., Kitching, P., Kobayashi, T., Kogan, G., Koike, S., Konaka, A., Kormos, L. L., Korzenev, A., Koseki, K., Koshio, Y., Kouzuma, Y., Kowalik, K., Kravtsov, V., Kreslo, I., Kropp, W., Kubo, H., Kubota, J., Kudenko, Y., Kulkarni, N., Kurimoto, Y., Kurjata, R., Kutter, T., Lagoda, J., Laihem, K., Laing, A., Laveder, M., Lawe, M., Lee, K. P., Le, P. T., Levy, J. M., Licciardi, C., Lim, I. T., Lindner, T., Lister, C., Litchfield, R. P., Litos, M., Longhin, A., Lopez, G. D., Loverre, P. F., Ludovici, L., Lux, T., Macaire, M., Magaletti, L., Mahn, K., Makida, Y., Malek, M., Manly, S., Marchionni, A., Marino, A. D., Marone, A. J., Marteau, J., Martin, J. F., Maruyama, T., Maryon, T., Marzec, J., Masliah, P., Mathie, E. L., Matsumura, C., Matsuoka, K., Matveev, V., Mavrokoridis, K., Mazzucato, E., McCauley, N., McFarland, K. S., McGrew, C., McLachlan, T., Messina, M., Metcalf, W., Metelko, C., Mezzetto, M., Mijakowski, P., Miller, C. A., Minamino, A., Mineev, O., Mine, S., Missert, A. D., Mituka, G., Miura, M., Mizouchi, K., Monfregola, L., Moreau, F., Morgan, B., Moriyama, S., Muir, A., Murakami, A., Muratore, J. F., Murdoch, M., Murphy, S., Myslik, J., Nagai, N., Nakadaira, T., Nakahata, M., Nakai, T., Nakajima, K., Nakamoto, T., Nakamura, K., Nakayama, S., Nakaya, T., Nakayoshi, K., Naples, D., Navin, M. L., Nicholls, T. C., Nielsen, B., Nielsen, C., Nishikawa, K., Nishino, H., Nitta, K., Nobuhara, T., Nowak, J. A., Obayashi, Y., Ogitsu, T., Ohhata, H., Okamura, T., Okumura, K., Okusawa, T., Oser, S. M., Otani, M., Owen, R. A., Oyama, Y., Ozaki, T., Pac, M. Y., Palladino, V., Paolone, V., Paul, P., Payne, D., Pearce, G. F., Perkin, J. D., Pettinacci, V., Pierre, F., Poplawska, E., Popov, B., Posiadala, M., Poutissou, J. -M., Poutissou, R., Przewlocki, P., Qian, W., Raaf, J. L., Radicioni, E., Ratoff, P. N., Raufer, T. M., Ravonel, M., Raymond, M., Retiere, F., Robert, A., Rodrigues, P. A., Rondio, E., Roney, J. M., Rossi, B., Roth, S., Rubbia, A., Ruterbories, D., Sabouri, S., Sacco, R., Sakashita, K., Sánchez, F., Sarrat, A., Sasaki, K., Scholberg, K., Schwehr, J., Scott, M., Scully, D. I., Seiya, Y., Sekiguchi, T., Sekiya, H., Shibata, M., Shimizu, Y., Shiozawa, M., Short, S., Sinclair, P. D., Siyad, M., Smith, B. M., Smith, R. J., Smy, M., Sobczyk, J. T., Sobel, H., Sorel, M., Stahl, A., Stamoulis, P., Steinmann, J., Still, B., Stone, J., Stodulski, M., Strabel, C., Sulej, R., Suzuki, A., Suzuki, K., Suzuki, S., Suzuki, S. Y., Suzuki, Y., Swierblewski, J., Szeglowski, T., Szeptycka, M., Tacik, R., Tada, M., Taguchi, M., Takahashi, S., Takeda, A., Takenaga, Y., Takeuchi, Y., Tanaka, K., Tanaka, H. A., Tanaka, M., Tanaka, M. M., Tanimoto, N., Tashiro, K., Taylor, I., Terashima, A., Terhorst, D., Terri, R., Thompson, L. F., Thorley, A., Toki, W., Tobayama, S., Tomaru, T., Totsuka, Y., Touramanis, C., Tsukamoto, T., Tzanov, M., Uchida, Y., Ueno, K., Vacheret, A., Vagins, M., Vasseur, G., Veledar, O., Wachala, T., Walding, J. J., Waldron, A. V., Walter, C. W., Wanderer, P. J., Wang, J., Ward, M. A., Ward, G. P., Wark, D., Wascko, M. O., Weber, A., Wendell, R., West, N., Whitehead, L. H., Wikström, G., Wilkes, R. J., Wilking, M. J., Williamson, Z., Wilson, J. R., Wilson, R. J., Wongjirad, T., Yamada, S., Yamada, Y., Yamamoto, A., Yamamoto, K., Yamanoi, Y., Yamaoka, H., Yamauchi, T., Yanagisawa, C., Yano, T., Yen, S., Yershov, N., Yokoyama, M., Yuan, T., Zalewska, A., Zalipska, J., Zambelli, L., Zaremba, K., Ziembicki, M., Zimmerman, E. D., Zito, M., and Zmuda, J.
Subjects: High Energy Physics - Experiment
Abstract: We report a measurement of muon-neutrino disappearance in the T2K experiment. The 295-km muon-neutrino beam from Tokai to Kamioka is the first implementation of the off-axis technique in a long-baseline neutrino oscillation experiment. With data corresponding to 1.43 10**20 protons on target, we observe 31 fully-contained single muon-like ring events in Super-Kamiokande, compared with an expectation of 104 +- 14 (syst) events without neutrino oscillations. The best-fit point for two-flavor nu_mu -> nu_tau oscillations is sin**2(2 theta_23) = 0.98 and |\Delta m**2_32| = 2.65 10**-3 eV**2. The boundary of the 90 % confidence region includes the points (sin**2(2 theta_23),|\Delta m**2_32|) = (1.0, 3.1 10**-3 eV**2), (0.84, 2.65 10**-3 eV**2) and (1.0, 2.2 10**-3 eV**2)., Comment: 7 pages, 4 figures
Published: 2012
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2. Measurements of the T2K neutrino beam properties using the INGRID on-axis near detector

Author: Abe, K., Abgrall, N., Ajima, Y., Aihara, H., Albert, J. B., Andreopoulos, C., Andrieu, B., Anerella, M. D., Aoki, S., Araoka, O., Argyriades, J., Ariga, A., Ariga, T., Assylbekov, S., Autiero, D., Badertscher, A., Barbi, M., Barker, G. J., Barr, G., Bass, M., Batkiewicz, M., Bay, F., Bentham, S., Berardi, V., Berger, B. E., Bertram, I., Besnier, M., Beucher, J., Beznosko, D., Bhadra, S., Blaszczyk, F. d. M., Blocki, J., Blondel, A., Bojechko, C., Bouchez, J., Boyd, S. B., Bravar, A., Bronner, C., Brook-Roberge, D. G., Buchanan, N., Budd, H., Calvet, D., Cartwright, S. L., Carver, A., Castillo, R., Catanesi, M. G., Cazes, A., Cervera, A., Chavez, C., Choi, S., Christodoulou, G., Coleman, J., Collazuol, G., Coleman, W., Connolly, K., Curioni, A., Dabrowska, A., Danko, I., Das, R., Davies, G. S., Davis, S., Day, M., De Rosa, G., de André, J. P. A. M., de Perio, P., Dealtry, T., Delbart, A., Densham, C., Di Lodovico, F., Di Luise, S., Tran, P. Dinh, Dobson, J., Dore, U., Drapier, O., Dufour, F., Dumarchez, J., Dytman, S., Dziewiecki, M., Dziomba, M., Emery, S., Ereditato, A., Escallier, J. E., Escudero, L., Esposito, L. S., Fechner, M., Ferrero, A., Finch, A. J., Frank, E., Fujii, Y., Fukuda, Y., Galymov, V., Ganetis, G. L., Gannaway, F. C., Gaudin, A., Gendotti, A., George, M., Giffin, S., Giganti, C., Gilje, K., Ghosh, A. K., Golan, T., Goldhaber, M., Gomez-Cadenas, J. J., Gomi, S., Gonin, M., Grant, N., Grant, A., Gumplinger, P., Guzowski, P., Haesler, A., Haigh, M. D., Hamano, K., Hansen, C., Hansen, D., Hara, T., Harrison, P. F., Hartfiel, B., Hartz, M., Haruyama, T., Hasegawa, T., Hastings, N. C., Hatzikoutelis, A., Hayashi, K., Hayato, Y., Hearty, C., Helmer, R. L., Henderson, R., Higashi, N., Hignight, J., Hillairet, A., Hirose, E., Holeczek, J., Horikawa, S., Hyndman, A., Ichikawa, A. K., Ieki, K., Ieva, M., Iida, M., Ikeda, M., Ilic, J., Imber, J., Ishida, T., Ishihara, C., Ishii, T., Ives, S. J., Iwasaki, M., Iyogi, K., Izmaylov, A., Jamieson, B., Johnson, R. A., Joo, K. K., Jover-Manas, G. V., Jung, C. K., Kaji, H., Kajita, T., Kakuno, H., Kameda, J., Kaneyuki, K., Karlen, D., Kasami, K., Kato, I., Kawamuko, H., Kearns, E., Khabibullin, M., Khanam, F., Khotjantsev, A., Kielczewska, D., Kikawa, T., Kim, J., Kim, J. Y., Kim, S. B., Kimura, N., Kirby, B., Kisiel, J., Kitching, P., Kobayashi, T., Kogan, G., Koike, S., Konaka, A., Kormos, L. L., Korzenev, A., Koseki, K., Koshio, Y., Kouzuma, Y., Kowalik, K., Kravtsov, V., Kreslo, I., Kropp, W., Kubo, H., Kubota, J., Kudenko, Y., Kulkarni, N., Kurimoto, Y., Kurjata, R., Kutter, T., Lagoda, J., Laihem, K., Laveder, M., Lee, K. P., Le, P. T., Levy, J. M., Licciardi, C., Lim, I. T., Lindner, T., Litchfield, R. P., Litos, M., Longhin, A., Lopez, G. D., Loverre, P. F., Ludovici, L., Lux, T., Macaire, M., Mahn, K., Makida, Y., Malek, M., Manly, S., Marchionni, A., Marino, A. D., Marone, A. J., Marteau, J., Martin, J. F., Maruyama, T., Maryon, T., Marzec, J., Masliah, P., Mathie, E. L., Matsumura, C., Matsuoka, K., Matveev, V., Mavrokoridis, K., Mazzucato, E., McCauley, N., McFarland, K. S., McGrew, C., McLachlan, T., Messina, M., Metcalf, W., Metelko, C., Mezzetto, M., Mijakowski, P., Miller, C. A., Minamino, A., Mineev, O., Mine, S., Missert, A. D., Mituka, G., Miura, M., Mizouchi, K., Monfregola, L., Moreau, F., Morgan, B., Moriyama, S., Muir, A., Murakami, A., Muratore, J. F., Murdoch, M., Murphy, S., Myslik, J., Nagai, N., Nakadaira, T., Nakahata, M., Nakai, T., Nakajima, K., Nakamoto, T., Nakamura, K., Nakayama, S., Nakaya, T., Naples, D., Navin, M. L., Nelson, B., Nicholls, T. C., Nielsen, C., Nishikawa, K., Nishino, H., Nitta, K., Nobuhara, T., Nowak, J. A., Obayashi, Y., Ogitsu, T., Ohhata, H., Okamura, T., Okumura, K., Okusawa, T., Oser, S. M., Otani, M., Owen, R. A., Oyama, Y., Ozaki, T., Pac, M. Y., Palladino, V., Paolone, V., Paul, P., Payne, D., Pearce, G. F., Perkin, J. D., Pettinacci, V., Pierre, F., Poplawska, E., Popov, B., Posiadala, M., Poutissou, J. -M., Poutissou, R., Przewlocki, P., Qian, W., Raaf, J. L., Radicioni, E., Ratoff, P. N., Raufer, T. M., Ravonel, M., Raymond, M., Retiere, F., Robert, A., Rodrigues, P. A., Rondio, E., Roney, J. M., Rossi, B., Roth, S., Rubbia, A., Ruterbories, D., Sabouri, S., Sacco, R., Sakashita, K., Sánchez, F., Sarrat, A., Sasaki, K., Scholberg, K., Schwehr, J., Scott, M., Scully, D. I., Seiya, Y., Sekiguchi, T., Sekiya, H., Shibata, M., Shimizu, Y., Shiozawa, M., Short, S., Siyad, M., Smith, R. J., Smy, M., Sobczyk, J. T., Sobel, H., Sorel, M., Stahl, A., Stamoulis, P., Steinmann, J., Still, B., Stone, J., Stodulski, M., Strabel, C., Sulej, R., Suzuki, A., Suzuki, K., Suzuki, S., Suzuki, S. Y., Suzuki, Y., Swierblewski, J., Szeglowski, T., Szeptycka, M., Tacik, R., Tada, M., Taguchi, M., Takahashi, S., Takeda, A., Takenaga, Y., Takeuchi, Y., Tanaka, K., Tanaka, H. A., Tanaka, M., Tanaka, M. M., Tanimoto, N., Tashiro, K., Taylor, I., Terashima, A., Terhorst, D., Terri, R., Thompson, L. F., Thorley, A., Toki, W., Tobayama, S., Tomaru, T., Totsuka, Y., Touramanis, C., Tsukamoto, T., Tzanov, M., Uchida, Y., Ueno, K., Vacheret, A., Vagins, M., Vasseur, G., Wachala, T., Walding, J. J., Waldron, A. V., Walter, C. W., Wanderer, P. J., Wang, J., Ward, M. A., Ward, G. P., Wark, D., Wascko, M. O., Weber, A., Wendell, R., West, N., Whitehead, L. H., Wikström, G., Wilkes, R. J., Wilking, M. J., Williamson, Z., Wilson, J. R., Wilson, R. J., Wongjirad, T., Yamada, S., Yamada, Y., Yamamoto, A., Yamamoto, K., Yamanoi, Y., Yamaoka, H., Yamauchi, T., Yanagisawa, C., Yano, T., Yen, S., Yershov, N., Yokoyama, M., Yuan, T., Zalewska, A., Zalipska, J., Zambelli, L., Zaremba, K., Ziembicki, M., Zimmerman, E. D., Zito, M., and Zmuda, J.
Subjects: Physics - Instrumentation and Detectors
Abstract: Precise measurement of neutrino beam direction and intensity was achieved based on a new concept with modularized neutrino detectors. INGRID (Interactive Neutrino GRID) is an on-axis near detector for the T2K long baseline neutrino oscillation experiment. INGRID consists of 16 identical modules arranged in horizontal and vertical arrays around the beam center. The module has a sandwich structure of iron target plates and scintillator trackers. INGRID directly monitors the muon neutrino beam profile center and intensity using the number of observed neutrino events in each module. The neutrino beam direction is measured with accuracy better than 0.4 mrad from the measured profile center. The normalized event rate is measured with 4% precision., Comment: 32 pages, 27 figures, submitted to Nucl. Instr. and Meth. A
Published: 2011
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3. An Indirect Search for WIMPs in the Sun using 3109.6 days of upward-going muons in Super-Kamiokande

Author: Collaboration, The Super-Kamiokande, Tanaka, T., Abe, K., Hayato, Y., Iida, T., Kameda, J., Koshio, Y., Kouzuma, Y., Miura, M., Moriyama, S., Nakahata, M., Nakayama, S., Obayashi, Y., Sekiya, H., Shiozawa, M., Suzuki, Y., Takeda, A., Takenaga, Y., Ueno, K., Ueshima, K., Yamada, S., Yokozawa, T., Ishihara, C., Hazama, S., Kaji, H., Kajita, T., Kaneyuki, K., McLachlan, T., Okumura, K., Shimizu, Y., Tanimoto, N., Dufour, F., Kearns, E., Litos3, M., Raaf, J. L., Stone, J. L., Sulak, L. R., Cravens, J. P., Bays, K., Kropp, W. R., Mine, S., Regis, C., Smy, M. B., Sobel, H. W., Ganezer, K. S., Hill, J., Keig, W. E., Jang, J. S., Kim, J. Y., Lim, I. T., Albert, J. B., Scholberg, K., Walter, C. W., Wendell, R., Wongjirad, T., Ishizuka, T., Tasaka, S., Learned, J. G., Matsuno, S., Smith, S., Martens, K., Vagins, M., Watanabe, Y., Hasegawa, T., Ishida, T., Ishii, T., Kobayashi, T., Nakadaira, T., Nakamura, K., Nishikawa, K., Nishino, H., Oyama, Y., Sakashita, K., Sekiguchi, T., Tsukamoto, T., Suzuki, A. T., Takeuchi, Y., Ikeda, M., Minamino, A., Nakaya, T., Labarga, L., Fukuda, Y., Itow, Y., Mitsuka, G., Jung, C. K., McGrew, C., Lopez, G., Yanagisawa, C., Tamura, N., Ishino, H., Kibayashi, A., Sakuda, M., Kuno, Y., Yoshida, M., Kim, S. B., Yang, B. S., Okazawa, H., Choi, Y., Nishijima, K., Yokosawa, Y., Koshiba, M., Totsuka, Y., Yokoyama, M., Chen, S., Heng, Y., Yang, Z., Zhang, H., Kielczewska, D., Mijakowski, P., Connolly, K., Dziomba, M., Thrane, E., and Wilkes, R. J.
Subjects: Astrophysics - High Energy Astrophysical Phenomena, High Energy Physics - Experiment
Abstract: We present the result of an indirect search for high energy neutrinos from WIMP annihilation in the Sun using upward-going muon (upmu) events at Super-Kamiokande. Datasets from SKI-SKIII (3109.6 days) were used for the analysis. We looked for an excess of neutrino signal from the Sun as compared with the expected atmospheric neutrino background in three upmu categories: stopping, non-showering, and showering. No significant excess was observed. The 90% C.L. upper limits of upward-going muon flux induced by WIMPs of 100 GeV/c$^2$ were 6.4$\times10^{-15}$ cm$^{-2}$ sec$^{-1}$ and 4.0$\times10^{-15}$ cm$^{-2}$ sec$^{-1}$ for the soft and hard annihilation channels, respectively. These limits correspond to upper limits of 4.5$\times10^{-39}$ cm$^{-2}$ and 2.7$\times10^{-40}$ cm$^{-2}$ for spin-dependent WIMP-nucleon scattering cross sections in the soft and hard annihilation channels, respectively., Comment: Add journal reference. Also fixed typo and cosmetic things in the old draft
Published: 2011
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4. Indication of Electron Neutrino Appearance from an Accelerator-produced Off-axis Muon Neutrino Beam

Author: T2K Collaboration, Abe, K., Abgrall, N., Ajima, Y., Aihara, H., Albert, J. B., Andreopoulos, C., Andrieu, B., Aoki, S., Araoka, O., Argyriades, J., Ariga, A., Ariga, T., Assylbekov, S., Autiero, D., Badertscher, A., Barbi, M., Barker, G. J., Barr, G., Bass, M., Bay, F., Bentham, S., Berardi, V., Berger, B. E., Bertram, I., Besnier, M., Beucher, J., Beznosko, D., Bhadra, S., Blaszczyk, F. d. M., Blondel, A., Bojechko, C., Bouchez, J., Boyd, S. B., Bravar, A., Bronner, C., Brook-Roberge, D. G., Buchanan, N., Budd, H., Calvet, D., Cartwright, S. L., Carver, A., Castillo, R., Catanesi, M. G., Cazes, A., Cervera, A., Chavez, C., Choi, S., Christodoulou, G., Coleman, J., Coleman, W., Collazuol, G., Connolly, K., Curioni, A., Dabrowska, A., Danko, I., Das, R., Davies, G. S., Davis, S., Day, M., DeRosa, G., de Andre, J. P. A. M., dePerio, P., Delbart, A., Densham, C., DiLodovico, F., DiLuise, S., Tran, P. Dinh, Dobson, J., Dore, U., Drapier, O., Dufour, F., Dumarchez, J., Dytman, S., Dziewiecki, M., Dziomba, M., Emery, S., Ereditato, A., Escudero, L., Esposito, L. S., Fechner, M., Ferrero, A., Finch, A. J., Frank, E., Fujii, Y., Fukuda, Y., Galymov, V., Gannaway, F. C., Gaudin, A., Gendotti, A., George, M., Giffin, S., Giganti, C., Gilje, K., Golan, T., Goldhaber, M., Gomez-Cadenas, J. J., Gonin, M., Grant, N., Grant, A., Gumplinger, P., Guzowski, P., Haesler, A., Haigh, M. D., Hamano, K., Hansen, C., Hansen, D., Hara, T., Harrison, P. F., Hartfiel, B., Hartz, M., Haruyama, T., Hasegawa, T., Hastings, N. C., Hastings, S., Hatzikoutelis, A., Hayashi, K., Hayato, Y., Hearty, C., Helmer, R. L., Henderson, R., Higashi, N., Hignight, J., Hirose, E., Holeczek, J., Horikawa, S., Hyndman, A., Ichikawa, A. K., Ieki, K., Ieva, M., Iida, M., Ikeda, M., Ilic, J., Imber, J., Ishida, T., Ishihara, C., Ishii, T., Ives, S. J., Iwasaki, M., Iyogi, K., Izmaylov, A., Jamieson, B., Johnson, R. A., Joo, K. K., Jover-Manas, G. V., Jung, C. K., Kaji, H., Kajita, T., Kakuno, H., Kameda, J., Kaneyuki, K., Karlen, D., Kasami, K., Kato, I., Kearns, E., Khabibullin, M., Khanam, F., Khotjantsev, A., Kielczewska, D., Kikawa, T., Kim, J., Kim, J. Y., Kim, S. B., Kimura, N., Kirby, B., Kisiel, J., Kitching, P., Kobayashi, T., Kogan, G., Koike, S., Konaka, A., Kormos, L. L., Korzenev, A., Koseki, K., Koshio, Y., Kouzuma, Y., Kowalik, K., Kravtsov, V., Kreslo, I., Kropp, W., Kubo, H., Kudenko, Y., Kulkarni, N., Kurjata, R., Kutter, T., Lagoda, J., Laihem, K., Laveder, M., Lee, K. P., Le, P. T., Levy, J. M., Licciardi, C., Lim, I. T., Lindner, T., Litchfield, R. P., Litos, M., Longhin, A., Lopez, G. D., Loverre, P. F., Ludovici, L., Lux, T., Macaire, M., Mahn, K., Makida, Y., Malek, M., Manly, S., Marchionni, A., Marino, A. D., Marteau, J., Martin, J. F., Maruyama, T., Maryon, T., Marzec, J., Masliah, P., Mathie, E. L., Matsumura, C., Matsuoka, K., Matveev, V., Mavrokoridis, K., Mazzucato, E., McCauley, N., McFarland, K. S., McGrew, C., McLachlan, T., Messina, M., Metcalf, W., Metelko, C., Mezzetto, M., Mijakowski, P., Miller, C. A., Minamino, A., Mineev, O., Mine, S., Missert, A. D., Mituka, G., Miura, M., Mizouchi, K., Monfregola, L., Moreau, F., Morgan, B., Moriyama, S., Muir, A., Murakami, A., Murdoch, M., Murphy, S., Myslik, J., Nakadaira, T., Nakahata, M., Nakai, T., Nakajima, K., Nakamoto, T., Nakamura, K., Nakayama, S., Nakaya, T., Naples, D., Navin, M. L., Nelson, B., Nicholls, T. C., Nishikawa, K., Nishino, H., Nowak, J. A., Noy, M., Obayashi, Y., Ogitsu, T., Ohhata, H., Okamura, T., Okumura, K., Okusawa, T., Oser, S. M., Otani, M., Owen, R. A., Oyama, Y., Ozaki, T., Pac, M. Y., Palladino, V., Paolone, V., Paul, P., Payne, D., Pearce, G. F., Perkin, J. D., Pettinacci, V., Pierre, F., Poplawska, E., Popov, B., Posiadala, M., Poutissou, J. -M., Poutissou, R., Przewlocki, P., Qian, W., Raaf, J. L., Radicioni, E., Ratoff, P. N., Raufer, T. M., Ravonel, M., Raymond, M., Retiere, F., Robert, A., Rodrigues, P. A., Rondio, E., Roney, J. M., Rossi, B., Roth, S., Rubbia, A., Ruterbories, D., Sabouri, S., Sacco, R., Sakashita, K., Sanchez, F., Sarrat, A., Sasaki, K., Scholberg, K., Schwehr, J., Scott, M., Scully, D. I., Seiya, Y., Sekiguchi, T., Sekiya, H., Shibata, M., Shimizu, Y., Shiozawa, M., Short, S., Syiad, M., Smith, R. J., Smy, M., Sobczyk, J. T., Sobel, H., Sorel, M., Stahl, A., Stamoulis, P., Steinmann, J., Still, B., Stone, J., Strabel, C., Sulak, L. R., Sulej, R., Sutcliffe, P., Suzuki, A., Suzuki, K., Suzuki, S., Suzuki, S. Y., Suzuki, Y., Szeglowski, T., Szeptycka, M., Tacik, R., Tada, M., Takahashi, S., Takeda, A., Takenaga, Y., Takeuchi, Y., Tanaka, K., Tanaka, H. A., Tanaka, M., Tanaka, M. M., Tanimoto, N., Tashiro, K., Taylor, I., Terashima, A., Terhorst, D., Terri, R., Thompson, L. F., Thorley, A., Toki, W., Tomaru, T., Totsuka, Y., Touramanis, C., Tsukamoto, T., Tzanov, M., Uchida, Y., Ueno, K., Vacheret, A., Vagins, M., Vasseur, G., Wachala, T., Walding, J. J., Waldron, A. V., Walter, C. W., Wanderer, P. J., Wang, J., Ward, M. A., Ward, G. P., Wark, D., Wascko, M. O., Weber, A., Wendell, R., West, N., Whitehead, L. H., Wikstrom, G., Wilkes, R. J., Wilking, M. J., Wilson, J. R., Wilson, R. J., Wongjirad, T., Yamada, S., Yamada, Y., Yamamoto, A., Yamamoto, K., Yamanoi, Y., Yamaoka, H., Yanagisawa, C., Yano, T., Yen, S., Yershov, N., Yokoyama, M., Zalewska, A., Zalipska, J., Zambelli, L., Zaremba, K., Ziembicki, M., Zimmerman, E. D., Zito, M., and Zmuda, J.
Subjects: High Energy Physics - Experiment
Abstract: The T2K experiment observes indications of $\nu_\mu\rightarrow \nu_e$ appearance in data accumulated with $1.43\times10^{20}$ protons on target. Six events pass all selection criteria at the far detector. In a three-flavor neutrino oscillation scenario with $|\Delta m_{23}^2|=2.4\times10^{-3}$ eV$^2$, $\sin^2 2\theta_{23}=1$ and $\sin^2 2\theta_{13}=0$, the expected number of such events is 1.5$\pm$0.3(syst.). Under this hypothesis, the probability to observe six or more candidate events is 7$\times10^{-3}$, equivalent to 2.5$\sigma$ significance. At 90% C.L., the data are consistent with 0.03(0.04)$<\sin^2 2\theta_{13}<$ 0.28(0.34) for $\delta_{\rm CP}=0$ and a normal (inverted) hierarchy., Comment: 20 pages, 6 figures, version published in PRL
Published: 2011
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5. The T2K Experiment

Author: T2K Collaboration, Abe, K., Abgrall, N., Aihara, H., Ajima, Y., Albert, J. B., Allan, D., Amaudruz, P. -A., Andreopoulos, C., Andrieu, B., Anerella, M. D., Angelsen, C., Aoki, S., Araoka, O., Argyriades, J., Ariga, A., Ariga, T., Assylbekov, S., de André, J. P. A. M., Autiero, D., Badertscher, A., Ballester, O., Barbi, M., Barker, G. J., Baron, P., Barr, G., Bartoszek, L., Batkiewicz, M., Bay, F., Bentham, S., Berardi, V., Berger, B. E., Berns, H., Bertram, I., Besnier, M., Beucher, J., Beznosko, D., Bhadra, S., Birney, P., Bishop, D., Blackmore, E., Blaszczyk, F. d. M., Blocki, J., Blondel, A., Bodek, A., Bojechko, C., Bouchez, J., Boussuge, T., Boyd, S. B., Boyer, M., Braam, N., Bradford, R., Bravar, A., Briggs, K., Brinson, J. D., Bronner, C., Brook-Roberge, D. G., Bryant, M., Buchanan, N., Budd, H., Cadabeschi, M., Calland, R. G., Calvet, D., Rodríguez, J. Caravaca, Carroll, J., Cartwright, S. L., Carver, A., Castillo, R., Catanesi, M. G., Cavata, C., Cazes, A., Cervera, A., Charrier, J. P., Chavez, C., Choi, S., Chollet, S., Christodoulou, G., Colas, P., Coleman, J., Coleman, W., Collazuol, G., Connolly, K., Cooke, P., Curioni, A., Dabrowska, A., Danko, I., Das, R., Davies, G. S., Davis, S., Day, M., De La Broise, X., de Perio, P., De Rosa, G., Dealtry, T., Debraine, A., Delagnes, E., Delbart, A., Densham, C., Di Lodovico, F., Di Luise, S., Tran, P. Dinh, Dobson, J., Doornbos, J., Dore, U., Drapier, O., Druillole, F., Dufour, F., Dumarchez, J., Durkin, T., Dytman, S., Dziewiecki, M., Dziomba, M., Ellison, B., Emery, S., Ereditato, A., Escallier, J. E., Escudero, L., Esposito, L. S., Faszer, W., Fechner, M., Ferrero, A., Finch, A., Fisher, C., Fitton, M., Flight, R., Forbush, D., Frank, E., Fransham, K., Fujii, Y., Fukuda, Y., Gallop, M., Galymov, V., Ganetis, G. L., Gannaway, F. C., Gaudin, A., Gaweda, J., Gendotti, A., George, M., Giffin, S., Giganti, C., Gilje, K., Giomataris, I., Giraud, J., Ghosh, A. K., Golan, T., Goldhaber, M., Gomez-Cadenas, J. J., Gomi, S., Gonin, M., Goyette, M., Grant, A., Grant, N., Grañena, F., Greenwood, S., Gumplinger, P., Guzowski, P., Haigh, M. D., Hamano, K., Hansen, C., Hara, T., Harrison, P. F., Hartfiel, B., Hartz, M., Haruyama, T., Hasanen, R., Hasegawa, T., Hastings, N. C., Hastings, S., Hatzikoutelis, A., Hayashi, K., Hayato, Y., Haycock, T. D. J., Hearty, C., Helmer, R. L., Henderson, R., Herlant, S., Higashi, N., Hignight, J., Hiraide, K., Hirose, E., Holeczek, J., Honkanen, N., Horikawa, S., Hyndman, A., Ichikawa, A. K., Ieki, K., Ieva, M., Iida, M., Ikeda, M., Ilic, J., Imber, J., Ishida, T., Ishihara, C., Ishii, T., Ives, S. J., Iwasaki, M., Iyogi, K., Izmaylov, A., Jamieson, B., Johnson, R. A., Joo, K. K., Jover-Manas, G., Jung, C. K., Kaji, H., Kajita, T., Kakuno, H., Kameda, J., Kaneyuki, K., Karlen, D., Kasami, K., Kasey, V., Kato, I., Kawamuko, H., Kearns, E., Kellet, L., Khabibullin, M., Khaleeq, M., Khan, N., Khotjantsev, A., Kielczewska, D., Kikawa, T., Kim, J. Y., Kim, S. -B., Kimura, N., Kirby, B., Kisiel, J., Kitching, P., Kobayashi, T., Kogan, G., Koike, S., Komorowski, T., Konaka, A., Kormos, L. L., Korzenev, A., Koseki, K., Koshio, Y., Kouzuma, Y., Kowalik, K., Kravtsov, V., Kreslo, I., Kropp, W., Kubo, H., Kubota, J., Kudenko, Y., Kulkarni, N., Kurchaninov, L., Kurimoto, Y., Kurjata, R., Kurosawa, Y., Kutter, T., Lagoda, J., Laihem, K., Langstaff, R., Laveder, M., Lawson, T. B., Le, P. T., Coguie, A. Le, Ross, M. Le, Lee, K. P., Lenckowski, M., Licciardi, C., Lim, I. T., Lindner, T., Litchfield, R. P., Longhin, A., Lopez, G. D., Lu, P., Ludovici, L., Lux, T., Macaire, M., Magaletti, L., Mahn, K., Makida, Y., Malafis, C. J., Malek, M., Manly, S., Marchionni, A., Mark, C., Marino, A. D., Marone, A. J., Marteau, J., Martin, J. F., Maruyama, T., Maryon, T., Marzec, J., Masliah, P., Mathie, E. L., Matsumura, C., Matsuoka, K., Matveev, V., Mavrokoridis, K., Mazzucato, E., McCauley, N., McFarland, K. S., McGrew, C., McLachlan, T., Mercer, I., Messina, M., Metcalf, W., Metelko, C., Mezzetto, M., Mijakowski, P., Miller, C. A., Minamino, A., Mineev, O., Mine, S., Minvielle, R. E., Mituka, G., Miura, M., Mizouchi, K., Mols, J. -P., Monfregola, L., Monmarthe, E., Moreau, F., Morgan, B., Moriyama, S., Morris, D., Muir, A., Murakami, A., Muratore, J. F., Murdoch, M., Murphy, S., Myslik, J., Nagashima, G., Nakadaira, T., Nakahata, M., Nakamoto, T., Nakamura, K., Nakayama, S., Nakaya, T., Naples, D., Nelson, B., Nicholls, T. C., Nishikawa, K., Nishino, H., Nitta, K., Nizery, F., Nowak, J. A., Noy, M., Obayashi, Y., Ogitsu, T., Ohhata, H., Okamura, T., Okumura, K., Okusawa, T., Ohlmann, C., Olchanski, K., Openshaw, R., Oser, S. M., Otani, M., Owen, R. A., Oyama, Y., Ozaki, T., Pac, M. Y., Palladino, V., Paolone, V., Paul, P., Payne, D., Pearce, G. F., Pearson, C., Perkin, J. D., Pfleger, M., Pierre, F., Pierrepont, D., Plonski, P., Poffenberger, P., Poplawska, E., Popov, B., Posiadala, M., Poutissou, J. -M., Poutissou, R., Preece, R., Przewlocki, P., Qian, W., Raaf, J. L., Radicioni, E., Ramos, K., Ratoff, P., Raufer, T. M., Ravonel, M., Raymond, M., Retiere, F., Richards, D., Ritou, J. -L., Robert, A., Rodrigues, P. A., Rondio, E., Roney, M., Rooney, M., Ross, D., Rossi, B., Roth, S., Rubbia, A., Ruterbories, D., Sacco, R., Sadler, S., Sakashita, K., Sanchez, F., Sarrat, A., Sasaki, K., Schaack, P., Schmidt, J., Scholberg, K., Schwehr, J., Scott, M., Scully, D. I., Seiya, Y., Sekiguchi, T., Sekiya, H., Sheffer, G., Shibata, M., Shimizu, Y., Shiozawa, M., Short, S., Siyad, M., Smith, D., Smith, R. J., Smy, M., Sobczyk, J., Sobel, H., Sooriyakumaran, S., Sorel, M., Spitz, J., Stahl, A., Stamoulis, P., Star, O., Statter, J., Stawnyczy, L., Steinmann, J., Steffens, J., Still, B., Stodulski, M., Stone, J., Strabel, C., Strauss, T., Sulej, R., Sutcliffe, P., Suzuki, A., Suzuki, K., Suzuki, S., Suzuki, S. Y., Suzuki, Y., Swierblewski, J., Szeglowski, T., Szeptycka, M., Tacik, R., Tada, M., Tadepalli, A. S., Taguchi, M., Takahashi, S., Takeda, A., Takenaga, Y., Takeuchi, Y., Tanaka, H. A., Tanaka, K., Tanaka, M., Tanaka, M. M., Tanimoto, N., Tashiro, K., Taylor, I. J., Terashima, A., Terhorst, D., Terri, R., Thompson, L. F., Thorley, A., Thorpe, M., Toki, W., Tomaru, T., Totsuka, Y., Touramanis, C., Tsukamoto, T., Tvaskis, V., Tzanov, M., Uchida, Y., Ueno, K., Usseglio, M., Vacheret, A., Vagins, M., Van Schalkwyk, J. F., Vanel, J. -C., Vasseur, G., Veledar, O., Vincent, P., Wachala, T., Waldron, A. V., Walter, C. W., Wanderer, P. J., Ward, M. A., Ward, G. P., Wark, D., Warner, D., Wascko, M. O., Weber, A., Wendell, R., Wendland, J., West, N., Whitehead, L. H., Wikström, G., Wilkes, R. J., Wilking, M. J., Williamson, Z., Wilson, J. R., Wilson, R. J., Wong, K., Wongjirad, T., Yamada, S., Yamada, Y., Yamamoto, A., Yamamoto, K., Yamanoi, Y., Yamaoka, H., Yanagisawa, C., Yano, T., Yen, S., Yershov, N., Yokoyama, M., Zalewska, A., Zalipska, J., Zaremba, K., Ziembicki, M., Zimmerman, E. D., Zito, M., and Zmuda, J.
Subjects: Physics - Instrumentation and Detectors, High Energy Physics - Experiment
Abstract: The T2K experiment is a long-baseline neutrino oscillation experiment. Its main goal is to measure the last unknown lepton sector mixing angle {\theta}_{13} by observing {\nu}_e appearance in a {\nu}_{\mu} beam. It also aims to make a precision measurement of the known oscillation parameters, {\Delta}m^{2}_{23} and sin^{2} 2{\theta}_{23}, via {\nu}_{\mu} disappearance studies. Other goals of the experiment include various neutrino cross section measurements and sterile neutrino searches. The experiment uses an intense proton beam generated by the J-PARC accelerator in Tokai, Japan, and is composed of a neutrino beamline, a near detector complex (ND280), and a far detector (Super-Kamiokande) located 295 km away from J-PARC. This paper provides a comprehensive review of the instrumentation aspect of the T2K experiment and a summary of the vital information for each subsystem., Comment: 33 pages, 32 figures, Submitted and accepted by NIM A. Editor: Prof. Chang Kee Jung, Department of Physics and Astronomy, SUNY Stony Brook, chang.jung@sunysb.edu, 631-632-8108 Submit Edited to remove line numbers
Published: 2011
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6. Investigation of Layer Structure of the Takamatsuzuka Mural Paintings by Terahertz Imaging Technique

Author: Inuzuka, M., Kouzuma, Y., Sugioka, N., Fukunaga, K., and Tateishi, T.
Published: 2017
Full Text: View/download PDF

7. The T2K experiment

Author: Abe, K., Abgrall, N., Aihara, H., Ajima, Y., Albert, J.B., Allan, D., Amaudruz, P.-A., Andreopoulos, C., Andrieu, B., Anerella, M.D., Angelsen, C., Aoki, S., Araoka, O., Argyriades, J., Ariga, A., Ariga, T., Assylbekov, S., de André, J.P.A.M., Autiero, D., Badertscher, A., Ballester, O., Barbi, M., Barker, G.J., Baron, P., Barr, G., Bartoszek, L., Batkiewicz, M., Bay, F., Bentham, S., Berardi, V., Berger, B.E., Berns, H., Bertram, I., Besnier, M., Beucher, J., Beznosko, D., Bhadra, S., Birney, P., Bishop, D., Blackmore, E., Blaszczyk, F.d.M., Blocki, J., Blondel, A., Bodek, A., Bojechko, C., Bouchez, J., Boussuge, T., Boyd, S.B., Boyer, M., Braam, N., Bradford, R., Bravar, A., Briggs, K., Brinson, J.D., Bronner, C., Brook-Roberge, D.G., Bryant, M., Buchanan, N., Budd, H., Cadabeschi, M., Calland, R.G., Calvet, D., Caravaca Rodríguez, J., Carroll, J., Cartwright, S.L., Carver, A., Castillo, R., Catanesi, M.G., Cavata, C., Cazes, A., Cervera, A., Charrier, J.P., Chavez, C., Choi, S., Chollet, S., Christodoulou, G., Colas, P., Coleman, J., Coleman, W., Collazuol, G., Connolly, K., Cooke, P., Curioni, A., Dabrowska, A., Danko, I., Das, R., Davies, G.S., Davis, S., Day, M., De La Broise, X., de Perio, P., De Rosa, G., Dealtry, T., Debraine, A., Delagnes, E., Delbart, A., Densham, C., Di Lodovico, F., Di Luise, S., Dinh Tran, P., Dobson, J., Doornbos, J., Dore, U., Drapier, O., Druillole, F., Dufour, F., Dumarchez, J., Durkin, T., Dytman, S., Dziewiecki, M., Dziomba, M., Ellison, B., Emery, S., Ereditato, A., Escallier, J.E., Escudero, L., Esposito, L.S., Faszer, W., Fechner, M., Ferrero, A., Finch, A., Fisher, C., Fitton, M., Flight, R., Forbush, D., Frank, E., Fransham, K., Fujii, Y., Fukuda, Y., Gallop, M., Galymov, V., Ganetis, G.L., Gannaway, F.C., Gaudin, A., Gaweda, J., Gendotti, A., George, M., Giffin, S., Giganti, C., Gilje, K., Giomataris, I., Giraud, J., Ghosh, A.K., Golan, T., Goldhaber, M., Gomez-Cadenas, J.J., Gomi, S., Gonin, M., Goyette, M., Grant, A., Grant, N., Grañena, F., Greenwood, S., Gumplinger, P., Guzowski, P., Haigh, M.D., Hamano, K., Hansen, C., Hara, T., Harrison, P.F., Hartfiel, B., Hartz, M., Haruyama, T., Hasanen, R., Hasegawa, T., Hastings, N.C., Hastings, S., Hatzikoutelis, A., Hayashi, K., Hayato, Y., Haycock, T.D.J., Hearty, C., Helmer, R.L., Henderson, R., Herlant, S., Higashi, N., Hignight, J., Hiraide, K., Hirose, E., Holeczek, J., Honkanen, N., Horikawa, S., Hyndman, A., Ichikawa, A.K., Ieki, K., Ieva, M., Iida, M., Ikeda, M., Ilic, J., Imber, J., Ishida, T., Ishihara, C., Ishii, T., Ives, S.J., Iwasaki, M., Iyogi, K., Izmaylov, A., Jamieson, B., Johnson, R.A., Joo, K.K., Jover-Manas, G., Jung, C.K., Kaji, H., Kajita, T., Kakuno, H., Kameda, J., Kaneyuki, K., Karlen, D., Kasami, K., Kasey, V., Kato, I., Kawamuko, H., Kearns, E., Kellet, L., Khabibullin, M., Khaleeq, M., Khan, N., Khotjantsev, A., Kielczewska, D., Kikawa, T., Kim, J.Y., Kim, S.-B., Kimura, N., Kirby, B., Kisiel, J., Kitching, P., Kobayashi, T., Kogan, G., Koike, S., Komorowski, T., Konaka, A., Kormos, L.L., Korzenev, A., Koseki, K., Koshio, Y., Kouzuma, Y., Kowalik, K., Kravtsov, V., Kreslo, I., Kropp, W., Kubo, H., Kubota, J., Kudenko, Y., Kulkarni, N., Kurchaninov, L., Kurimoto, Y., Kurjata, R., Kurosawa, Y., Kutter, T., Lagoda, J., Laihem, K., Langstaff, R., Laveder, M., Lawson, T.B., Le, P.T., Le Coguie, A., Le Ross, M., Lee, K.P., Lenckowski, M., Licciardi, C., Lim, I.T., Lindner, T., Litchfield, R.P., Longhin, A., Lopez, G.D., Lu, P., Ludovici, L., Lux, T., Macaire, M., Magaletti, L., Mahn, K., Makida, Y., Malafis, C.J., Malek, M., Manly, S., Marchionni, A., Mark, C., Marino, A.D., Marone, A.J., Marteau, J., Martin, J.F., Maruyama, T., Maryon, T., Marzec, J., Masliah, P., Mathie, E.L., Matsumura, C., Matsuoka, K., Matveev, V., Mavrokoridis, K., Mazzucato, E., McCauley, N., McFarland, K.S., McGrew, C., McLachlan, T., Mercer, I., Messina, M., Metcalf, W., Metelko, C., Mezzetto, M., Mijakowski, P., Miller, C.A., Minamino, A., Mineev, O., Mine, S., Minvielle, R.E., Mituka, G., Miura, M., Mizouchi, K., Mols, J.-P., Monfregola, L., Monmarthe, E., Moreau, F., Morgan, B., Moriyama, S., Morris, D., Muir, A., Murakami, A., Muratore, J.F., Murdoch, M., Murphy, S., Myslik, J., Nagashima, G., Nakadaira, T., Nakahata, M., Nakamoto, T., Nakamura, K., Nakayama, S., Nakaya, T., Naples, D., Nelson, B., Nicholls, T.C., Nishikawa, K., Nishino, H., Nitta, K., Nizery, F., Nowak, J.A., Noy, M., Obayashi, Y., Ogitsu, T., Ohhata, H., Okamura, T., Okumura, K., Okusawa, T., Ohlmann, C., Olchanski, K., Openshaw, R., Oser, S.M., Otani, M., Owen, R.A., Oyama, Y., Ozaki, T., Pac, M.Y., Palladino, V., Paolone, V., Paul, P., Payne, D., Pearce, G.F., Pearson, C., Perkin, J.D., Pfleger, M., Pierre, F., Pierrepont, D., Plonski, P., Poffenberger, P., Poplawska, E., Popov, B., Posiadala, M., Poutissou, J.-M., Poutissou, R., Preece, R., Przewlocki, P., Qian, W., Raaf, J.L., Radicioni, E., Ramos, K., Ratoff, P., Raufer, T.M., Ravonel, M., Raymond, M., Retiere, F., Richards, D., Ritou, J.-L., Robert, A., Rodrigues, P.A., Rondio, E., Roney, M., Rooney, M., Ross, D., Rossi, B., Roth, S., Rubbia, A., Ruterbories, D., Sacco, R., Sadler, S., Sakashita, K., Sanchez, F., Sarrat, A., Sasaki, K., Schaack, P., Schmidt, J., Scholberg, K., Schwehr, J., Scott, M., Scully, D.I., Seiya, Y., Sekiguchi, T., Sekiya, H., Sheffer, G., Shibata, M., Shimizu, Y., Shiozawa, M., Short, S., Siyad, M., Smith, D., Smith, R.J., Smy, M., Sobczyk, J., Sobel, H., Sooriyakumaran, S., Sorel, M., Spitz, J., Stahl, A., Stamoulis, P., Star, O., Statter, J., Stawnyczy, L., Steinmann, J., Steffens, J., Still, B., Stodulski, M., Stone, J., Strabel, C., Strauss, T., Sulej, R., Sutcliffe, P., Suzuki, A., Suzuki, K., Suzuki, S., Suzuki, S.Y., Suzuki, Y., Swierblewski, J., Szeglowski, T., Szeptycka, M., Tacik, R., Tada, M., Tadepalli, A.S., Taguchi, M., Takahashi, S., Takeda, A., Takenaga, Y., Takeuchi, Y., Tanaka, H.A., Tanaka, K., Tanaka, M., Tanaka, M.M., Tanimoto, N., Tashiro, K., Taylor, I.J., Terashima, A., Terhorst, D., Terri, R., Thompson, L.F., Thorley, A., Thorpe, M., Toki, W., Tomaru, T., Totsuka, Y., Touramanis, C., Tsukamoto, T., Tvaskis, V., Tzanov, M., Uchida, Y., Ueno, K., Usseglio, M., Vacheret, A., Vagins, M., Van Schalkwyk, J.F., Vanel, J.-C., Vasseur, G., Veledar, O., Vincent, P., Wachala, T., Waldron, A.V., Walter, C.W., Wanderer, P.J., Ward, M.A., Ward, G.P., Wark, D., Warner, D., Wascko, M.O., Weber, A., Wendell, R., Wendland, J., West, N., Whitehead, L.H., Wikström, G., Wilkes, R.J., Wilking, M.J., Williamson, Z., Wilson, J.R., Wilson, R.J., Wong, K., Wongjirad, T., Yamada, S., Yamada, Y., Yamamoto, A., Yamamoto, K., Yamanoi, Y., Yamaoka, H., Yanagisawa, C., Yano, T., Yen, S., Yershov, N., Yokoyama, M., Zalewska, A., Zalipska, J., Zaremba, K., Ziembicki, M., Zimmerman, E.D., Zito, M., and Zmuda, J.
Subjects: Physics::Instrumentation and Detectors, High Energy Physics::Phenomenology, High Energy Physics::Experiment
Abstract: The T2K experiment is a long baseline neutrino oscillation experiment. Its main goal is to measure the\ud last unknown lepton sector mixing angle y13 by observing ne appearance in a nm beam. It also aims to\ud make a precision measurement of the known oscillation parameters, Dm2\ud 23 and sin2\ud 2y23, via nm\ud disappearance studies. Other goals of the experiment include various neutrino cross-section measurements and sterile neutrino searches. The experiment uses an intense proton beam generated by the\ud J-PARC accelerator in Tokai, Japan, and is composed of a neutrino beamline, a near detector complex\ud (ND280), and a far detector (Super-Kamiokande) located 295 km away from J-PARC. This paper\ud provides a comprehensive review of the instrumentation aspect of the T2K experiment and a summary\ud of the vital information for each subsystem.
Published: 2011

8. An Indirect Search for WIMPs in the Sun using 3109.6 days of upward-going muons in Super-Kamiokande

Author: Kamiokande Collaboration, Tanaka, T., Abe, K., Hayato, Y., Iida, T., Kameda, J., Koshio, Y., Kouzuma, Y., Miura, M., Moriyama, S., Nakahata, M., Nakayama, S., Obayashi, Y., Sekiya, H., Shiozawa, M., Suzuki, Y., Takeda, A., Takenaga, Y., Ueno, K., Ueshima, K., Yamada, S., Yokozawa, T., Ishihara, C., Hazama, S., Kaji, H., Kajita, T., Kaneyuki, K., McLachlan, T., Okumura, K., Shimizu, Y., Tanimoto, N., Dufour, F., Kearns, E., Litos3, M., Raaf, J. L., Stone, J. L., Sulak, L. R., Cravens, J. P., Bays, K., Kropp, W. R., Mine, S., Regis, C., Smy, M. B., Sobel, H. W., Ganezer, K. S., Hill, J., Keig, W. E., Jang, J. S., Kim, J. Y., Lim, I. T., Albert, J. B., Scholberg, K., Walter, C. W., Wendell, R., Wongjirad, T., Ishizuka, T., Tasaka, S., Learned, J. G., Matsuno, S., Smith, S., Martens, K., Vagins, M., Watanabe, Y., Hasegawa, T., Ishida, T., Ishii, T., Kobayashi, T., Nakadaira, T., Nakamura, K., Nishikawa, K., Nishino, H., Oyama, Y., Sakashita, K., Sekiguchi, T., Tsukamoto, T., Suzuki, A. T., Takeuchi, Y., Ikeda, M., Minamino, A., Nakaya, T., Labarga, L., Fukuda, Y., Itow, Y., Mitsuka, G., Jung, C. K., McGrew, C., Lopez, G., Yanagisawa, C., Tamura, N., Ishino, H., Kibayashi, A., Sakuda, M., Kuno, Y., Yoshida, M., Kim, S. B., Yang, B. S., Okazawa, H., Choi, Y., Nishijima, K., Yokosawa, Y., Koshiba, M., Totsuka, Y., Yokoyama, M., Chen, S., Heng, Y., Yang, Z., Zhang, H., Kielczewska, D., Mijakowski, P., Connolly, K., Dziomba, M., Thrane, E., and Wilkes, R. J.
Subjects: High Energy Astrophysical Phenomena (astro-ph.HE), High Energy Physics - Experiment (hep-ex), Physics::Instrumentation and Detectors, Astrophysics::High Energy Astrophysical Phenomena, FOS: Physical sciences, High Energy Physics::Experiment, Astrophysics - High Energy Astrophysical Phenomena, High Energy Physics - Experiment
Abstract: We present the result of an indirect search for high energy neutrinos from WIMP annihilation in the Sun using upward-going muon (upmu) events at Super-Kamiokande. Datasets from SKI-SKIII (3109.6 days) were used for the analysis. We looked for an excess of neutrino signal from the Sun as compared with the expected atmospheric neutrino background in three upmu categories: stopping, non-showering, and showering. No significant excess was observed. The 90% C.L. upper limits of upward-going muon flux induced by WIMPs of 100 GeV/c$^2$ were 6.4$\times10^{-15}$ cm$^{-2}$ sec$^{-1}$ and 4.0$\times10^{-15}$ cm$^{-2}$ sec$^{-1}$ for the soft and hard annihilation channels, respectively. These limits correspond to upper limits of 4.5$\times10^{-39}$ cm$^{-2}$ and 2.7$\times10^{-40}$ cm$^{-2}$ for spin-dependent WIMP-nucleon scattering cross sections in the soft and hard annihilation channels, respectively., Add journal reference. Also fixed typo and cosmetic things in the old draft
Published: 2011

9. Measurements of the T2K neutrino beam properties using the INGRID on-axis near detector

Author: Abe, K., primary, Abgrall, N., additional, Ajima, Y., additional, Aihara, H., additional, Albert, J.B., additional, Andreopoulos, C., additional, Andrieu, B., additional, Anerella, M.D., additional, Aoki, S., additional, Araoka, O., additional, Argyriades, J., additional, Ariga, A., additional, Ariga, T., additional, Assylbekov, S., additional, Autiero, D., additional, Badertscher, A., additional, Barbi, M., additional, Barker, G.J., additional, Barr, G., additional, Bass, M., additional, Batkiewicz, M., additional, Bay, F., additional, Bentham, S., additional, Berardi, V., additional, Berger, B.E., additional, Bertram, I., additional, Besnier, M., additional, Beucher, J., additional, Beznosko, D., additional, Bhadra, S., additional, Blaszczyk, F.d.M., additional, Blocki, J., additional, Blondel, A., additional, Bojechko, C., additional, Bouchez, J., additional, Boyd, S.B., additional, Bravar, A., additional, Bronner, C., additional, Brook-Roberge, D.G., additional, Buchanan, N., additional, Budd, H., additional, Calvet, D., additional, Cartwright, S.L., additional, Carver, A., additional, Castillo, R., additional, Catanesi, M.G., additional, Cazes, A., additional, Cervera, A., additional, Chavez, C., additional, Choi, S., additional, Christodoulou, G., additional, Coleman, J., additional, Collazuol, G., additional, Coleman, W., additional, Connolly, K., additional, Curioni, A., additional, Dabrowska, A., additional, Danko, I., additional, Das, R., additional, Davies, G.S., additional, Davis, S., additional, Day, M., additional, De Rosa, G., additional, de André, J.P.A.M., additional, de Perio, P., additional, Dealtry, T., additional, Delbart, A., additional, Densham, C., additional, Di Lodovico, F., additional, Di Luise, S., additional, Dinh Tran, P., additional, Dobson, J., additional, Dore, U., additional, Drapier, O., additional, Dufour, F., additional, Dumarchez, J., additional, Dytman, S., additional, Dziewiecki, M., additional, Dziomba, M., additional, Emery, S., additional, Ereditato, A., additional, Escallier, J.E., additional, Escudero, L., additional, Esposito, L.S., additional, Fechner, M., additional, Ferrero, A., additional, Finch, A.J., additional, Frank, E., additional, Fujii, Y., additional, Fukuda, Y., additional, Galymov, V., additional, Ganetis, G.L., additional, Gannaway, F.C., additional, Gaudin, A., additional, Gendotti, A., additional, George, M., additional, Giffin, S., additional, Giganti, C., additional, Gilje, K., additional, Ghosh, A.K., additional, Golan, T., additional, Goldhaber, M., additional, Gomez-Cadenas, J.J., additional, Gomi, S., additional, Gonin, M., additional, Grant, N., additional, Grant, A., additional, Gumplinger, P., additional, Guzowski, P., additional, Haesler, A., additional, Haigh, M.D., additional, Hamano, K., additional, Hansen, C., additional, Hansen, D., additional, Hara, T., additional, Harrison, P.F., additional, Hartfiel, B., additional, Hartz, M., additional, Haruyama, T., additional, Hasegawa, T., additional, Hastings, N.C., additional, Hatzikoutelis, A., additional, Hayashi, K., additional, Hayato, Y., additional, Hearty, C., additional, Helmer, R.L., additional, Henderson, R., additional, Higashi, N., additional, Hignight, J., additional, Hillairet, A., additional, Hirose, E., additional, Holeczek, J., additional, Horikawa, S., additional, Hyndman, A., additional, Ichikawa, A.K., additional, Ieki, K., additional, Ieva, M., additional, Iida, M., additional, Ikeda, M., additional, Ilic, J., additional, Imber, J., additional, Ishida, T., additional, Ishihara, C., additional, Ishii, T., additional, Ives, S.J., additional, Iwasaki, M., additional, Iyogi, K., additional, Izmaylov, A., additional, Jamieson, B., additional, Johnson, R.A., additional, Joo, K.K., additional, Jover-Manas, G.V., additional, Jung, C.K., additional, Kaji, H., additional, Kajita, T., additional, Kakuno, H., additional, Kameda, J., additional, Kaneyuki, K., additional, Karlen, D., additional, Kasami, K., additional, Kato, I., additional, Kawamuko, H., additional, Kearns, E., additional, Khabibullin, M., additional, Khanam, F., additional, Khotjantsev, A., additional, Kielczewska, D., additional, Kikawa, T., additional, Kim, J., additional, Kim, J.Y., additional, Kim, S.B., additional, Kimura, N., additional, Kirby, B., additional, Kisiel, J., additional, Kitching, P., additional, Kobayashi, T., additional, Kogan, G., additional, Koike, S., additional, Konaka, A., additional, Kormos, L.L., additional, Korzenev, A., additional, Koseki, K., additional, Koshio, Y., additional, Kouzuma, Y., additional, Kowalik, K., additional, Kravtsov, V., additional, Kreslo, I., additional, Kropp, W., additional, Kubo, H., additional, Kubota, J., additional, Kudenko, Y., additional, Kulkarni, N., additional, Kurimoto, Y., additional, Kurjata, R., additional, Kutter, T., additional, Lagoda, J., additional, Laihem, K., additional, Laveder, M., additional, Lee, K.P., additional, Le, P.T., additional, Levy, J.M., additional, Licciardi, C., additional, Lim, I.T., additional, Lindner, T., additional, Litchfield, R.P., additional, Litos, M., additional, Longhin, A., additional, Lopez, G.D., additional, Loverre, P.F., additional, Ludovici, L., additional, Lux, T., additional, Macaire, M., additional, Mahn, K., additional, Makida, Y., additional, Malek, M., additional, Manly, S., additional, Marchionni, A., additional, Marino, A.D., additional, Marone, A.J., additional, Marteau, J., additional, Martin, J.F., additional, Maruyama, T., additional, Maryon, T., additional, Marzec, J., additional, Masliah, P., additional, Mathie, E.L., additional, Matsumura, C., additional, Matsuoka, K., additional, Matveev, V., additional, Mavrokoridis, K., additional, Mazzucato, E., additional, McCauley, N., additional, McFarland, K.S., additional, McGrew, C., additional, McLachlan, T., additional, Messina, M., additional, Metcalf, W., additional, Metelko, C., additional, Mezzetto, M., additional, Mijakowski, P., additional, Miller, C.A., additional, Minamino, A., additional, Mineev, O., additional, Mine, S., additional, Missert, A.D., additional, Mituka, G., additional, Miura, M., additional, Mizouchi, K., additional, Monfregola, L., additional, Moreau, F., additional, Morgan, B., additional, Moriyama, S., additional, Muir, A., additional, Murakami, A., additional, Muratore, J.F., additional, Murdoch, M., additional, Murphy, S., additional, Myslik, J., additional, Nagai, N., additional, Nakadaira, T., additional, Nakahata, M., additional, Nakai, T., additional, Nakajima, K., additional, Nakamoto, T., additional, Nakamura, K., additional, Nakayama, S., additional, Nakaya, T., additional, Naples, D., additional, Navin, M.L., additional, Nelson, B., additional, Nicholls, T.C., additional, Nielsen, C., additional, Nishikawa, K., additional, Nishino, H., additional, Nitta, K., additional, Nobuhara, T., additional, Nowak, J.A., additional, Obayashi, Y., additional, Ogitsu, T., additional, Ohhata, H., additional, Okamura, T., additional, Okumura, K., additional, Okusawa, T., additional, Oser, S.M., additional, Otani, M., additional, Owen, R.A., additional, Oyama, Y., additional, Ozaki, T., additional, Pac, M.Y., additional, Palladino, V., additional, Paolone, V., additional, Paul, P., additional, Payne, D., additional, Pearce, G.F., additional, Perkin, J.D., additional, Pettinacci, V., additional, Pierre, F., additional, Poplawska, E., additional, Popov, B., additional, Posiadala, M., additional, Poutissou, J.-M., additional, Poutissou, R., additional, Przewlocki, P., additional, Qian, W., additional, Raaf, J.L., additional, Radicioni, E., additional, Ratoff, P.N., additional, Raufer, T.M., additional, Ravonel, M., additional, Raymond, M., additional, Retiere, F., additional, Robert, A., additional, Rodrigues, P.A., additional, Rondio, E., additional, Roney, J.M., additional, Rossi, B., additional, Roth, S., additional, Rubbia, A., additional, Ruterbories, D., additional, Sabouri, S., additional, Sacco, R., additional, Sakashita, K., additional, Sánchez, F., additional, Sarrat, A., additional, Sasaki, K., additional, Scholberg, K., additional, Schwehr, J., additional, Scott, M., additional, Scully, D.I., additional, Seiya, Y., additional, Sekiguchi, T., additional, Sekiya, H., additional, Shibata, M., additional, Shimizu, Y., additional, Shiozawa, M., additional, Short, S., additional, Siyad, M., additional, Smith, R.J., additional, Smy, M., additional, Sobczyk, J.T., additional, Sobel, H., additional, Sorel, M., additional, Stahl, A., additional, Stamoulis, P., additional, Steinmann, J., additional, Still, B., additional, Stone, J., additional, Stodulski, M., additional, Strabel, C., additional, Sulej, R., additional, Suzuki, A., additional, Suzuki, K., additional, Suzuki, S., additional, Suzuki, S.Y., additional, Suzuki, Y., additional, Swierblewski, J., additional, Szeglowski, T., additional, Szeptycka, M., additional, Tacik, R., additional, Tada, M., additional, Taguchi, M., additional, Takahashi, S., additional, Takeda, A., additional, Takenaga, Y., additional, Takeuchi, Y., additional, Tanaka, K., additional, Tanaka, H.A., additional, Tanaka, M., additional, Tanaka, M.M., additional, Tanimoto, N., additional, Tashiro, K., additional, Taylor, I., additional, Terashima, A., additional, Terhorst, D., additional, Terri, R., additional, Thompson, L.F., additional, Thorley, A., additional, Toki, W., additional, Tobayama, S., additional, Tomaru, T., additional, Totsuka, Y., additional, Touramanis, C., additional, Tsukamoto, T., additional, Tzanov, M., additional, Uchida, Y., additional, Ueno, K., additional, Vacheret, A., additional, Vagins, M., additional, Vasseur, G., additional, Wachala, T., additional, Walding, J.J., additional, Waldron, A.V., additional, Walter, C.W., additional, Wanderer, P.J., additional, Wang, J., additional, Ward, M.A., additional, Ward, G.P., additional, Wark, D., additional, Wascko, M.O., additional, Weber, A., additional, Wendell, R., additional, West, N., additional, Whitehead, L.H., additional, Wikström, G., additional, Wilkes, R.J., additional, Wilking, M.J., additional, Williamson, Z., additional, Wilson, J.R., additional, Wilson, R.J., additional, Wongjirad, T., additional, Yamada, S., additional, Yamada, Y., additional, Yamamoto, A., additional, Yamamoto, K., additional, Yamanoi, Y., additional, Yamaoka, H., additional, Yamauchi, T., additional, Yanagisawa, C., additional, Yano, T., additional, Yen, S., additional, Yershov, N., additional, Yokoyama, M., additional, Yuan, T., additional, Zalewska, A., additional, Zalipska, J., additional, Zambelli, L., additional, Zaremba, K., additional, Ziembicki, M., additional, Zimmerman, E.D., additional, Zito, M., additional, and Zmuda, J., additional
Published: 2012
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10. Commissioning of the New Electronics and Online System for the Super-Kamiokande Experiment

Author: Yamada, S., primary, Awai, K., additional, Hayato, Y., additional, Kaneyuki, K., additional, Kouzuma, Y., additional, Nakayama, S., additional, Nishino, H., additional, Okumura, K., additional, Obayashi, Y., additional, Shimizu, Y., additional, Shiozawa, M., additional, Takeda, A., additional, Heng, Y., additional, Yang, B., additional, Chen, S., additional, Tanaka, T., additional, Yokozawa, T., additional, Koshio, Y., additional, Moriyama, S., additional, Arai, Y., additional, Ishikawa, K., additional, Minegishi, A., additional, and Uchida, T., additional
Published: 2010
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11. Commissioning of the new electronics and online system for the Super-Kamiokande experiment

Author: Yamada, S., primary, Awai, K., additional, Hayato, Y., additional, Kaneyuki, K., additional, Kouzuma, Y., additional, Nakayama, S., additional, Nishino, H., additional, Okumura, K., additional, Obayashi, Y., additional, Shimizu, Y., additional, Shiozawa, M., additional, Takeda, A., additional, Yokozawa, T., additional, Koshio, Y., additional, Moriyama, S., additional, Heng, Y., additional, Chen, S., additional, Yang, B., additional, Tanaka, T., additional, Arai, Y., additional, Ishikawa, K., additional, Minegishi, A., additional, and Uchida, T., additional
Published: 2009
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12. Crystal Structure of Hemolytic Lectin CEL-III Complexed with GalNac

Author: Hatakeyama, T., primary, Unno, H., additional, Eto, S., additional, Hidemura, H., additional, Uchida, T., additional, and Kouzuma, Y., additional
Published: 2007
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13. Crystal Structure of Hemolytic Lectin CEL-III Complexed with methyl-alpha-D-galactopylanoside

Author: Hatakeyama, T., primary, Unno, H., additional, Eto, S., additional, Hidemura, H., additional, Uchida, T., additional, and Kouzuma, Y., additional
Published: 2007
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14. Transgenic Anopheline mosquitoes expressing lectin CEL-III form a marine organism impair in transmission of a malaria parasite(Symposium,Proceedings of the 58th Annual Meeting of Eastern Region)

Author: Shimada, Y., primary, Kondoh, D., additional, Kouzuma, Y., additional, and Yoshida, S., additional
Published: 2007
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15. A28 Genetically engineering mosquito expressing the CEL-III gene impaired in transmission of a malaria parasite(General presentation,Abstract,The 58th Annual Meeting of the Japan Society of Medical Entomology and Zoology)

Author: Shimada, Y, primary, Kondoh, D, additional, Kouzuma, Y, additional, and Yoshida, S, additional
Published: 2006
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16. 3P342 N-terminal segmental dynamics of Cystatin as a regulatory factor for its crystallization

Author: Takahashi, D., primary, Kouzuma, Y., additional, Nishimoto, E., additional, and Yamashita, S., additional
Published: 2005
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17. Time dependence of nucleation density and crystallinity of diamond in low-pressure, ion-enhanced deposition

Author: Kouzuma, Y., primary, Teii, K., additional, Mizobe, S., additional, Uchino, K., additional, and Muraoka, K., additional
Published: 2004
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18. Characterization of Functional Domains of the Hemolytic Lectin CEL-III from the Marine Invertebrate Cucumaria echinata

Author: Kouzuma, Y., primary
Published: 2003
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19. Molecular Cloning and Functional Expression of cDNA Encoding the Cysteine Proteinase Inhibitor with Three Cystatin Domains from Sunflower Seeds

Author: Kouzuma, Y., primary, Inanaga, H., additional, Doi-Kawano, K., additional, Yamasaki, N., additional, and Kimura, M., additional
Published: 2000
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20. Conformation of the Primary Binding Loop Folded through an Intramolecular Interaction Contributes to the Strong Chymotrypsin Inhibitory Activity of the Chymotrypsin Inhibitor from Erythrina variegata Seeds

Author: wanaga, S. I, primary, Nagata, R., additional, Miyamoto, A., additional, Kouzuma, Y., additional, Yamasaki, N., additional, and Kimura, M., additional
Published: 1999
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21. Molecular Cloning, Functional Expression, and Mutagenesis of cDNA Encoding a Cysteine Proteinase Inhibitor from Sunflower Seeds

Author: Doi-Kawano, K., primary, Kouzuma, Y., additional, Yamasaki, N., additional, and Kimura, M., additional
Published: 1998
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22. The Tissue-Type Plasminogen Activator Inhibitor ETIa from Erythrina variegata: Structural Basis for the Inhibitory Activity by Cloning, Expression, and Mutagenesis of the cDNA Encoding ETIa

Author: Kouzuma, Y., primary, Yamasaki, N., additional, and Kimura, M., additional
Published: 1997
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23. Purification, Characterization, and Sequencing of Two Cysteine Proteinase Inhibitors, Sea and Scb, from Sunflower (Helianthus annuus) Seeds

Author: Kouzuma, Y., primary, Kawano, K., additional, Kimura, M., additional, Yamasaki, N., additional, Kadowaki, T., additional, and Yamamoto, K., additional
Published: 1996
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24. First muon-neutrino disappearance study with an off-axis beam

Author: Abe, K, Abgrall, N, Ajima, Y, Aihara, H, Albert, JB, Andreopoulos, C, Andrieu, B, Anerella, MD, Aoki, S, Araoka, O, Argyriades, J, Ariga, A, Ariga, T, Assylbekov, S, Autiero, D, Badertscher, A, Barbi, M, Barker, GJ, Barr, G, Bass, M, Batkiewicz, M, Bay, F, Bentham, S, Berardi, V, Berger, BE, Bertram, I, Besnier, M, Beucher, J, Beznosko, D, Bhadra, S, Blaszczyk, FDMM, Blondel, A, Bojechko, C, Bouchez, J, Boyd, SB, Bravar, A, Bronner, C, Brook-Roberge, DG, Buchanan, N, Budd, H, Calland, RG, Calvet, D, Caravaca Rodríguez, J, Cartwright, SL, Carver, A, Castillo, R, Catanesi, MG, Cazes, A, Cervera, A, Chavez, C, Choi, S, Christodoulou, G, Coleman, J, Collazuol, G, Coleman, W, Connolly, K, Curioni, A, Dabrowska, A, Danko, I, Das, R, Davies, GS, Davis, S, Day, M, De Rosa, G, De André, JPAM, De Perio, P, Dealtry, T, Delbart, A, Densham, C, Di Lodovico, F, Di Luise, S, Dinh Tran, P, Dobson, J, Dore, U, Drapier, O, Duboyski, T, Dufour, F, Dumarchez, J, Dytman, S, Dziewiecki, M, Dziomba, M, Emery, S, Ereditato, A, Escallier, JE, Escudero, L, Esposito, LS, Fechner, M, Ferrero, A, Finch, AJ, Frank, E, Fujii, Y, Fukuda, Y, Galymov, V, Ganetis, GL, Gannaway, FC, Gaudin, A, Gendotti, A, George, MA, Giffin, S, Giganti, C, Gilje, K, Ghosh, AK, Golan, T, Goldhaber, M, Gomez-Cadenas, JJ, Gomi, S, Gonin, M, Grant, N, Grant, A, Gumplinger, P, Guzowski, P, Hadley, DR, Haesler, A, Haigh, MD, Hamano, K, Hansen, C, Hansen, D, Hara, T, Harrison, PF, Hartfiel, B, Hartz, M, Haruyama, T, Hasegawa, T, Hastings, NC, Hatzikoutelis, A, Hayashi, K, Hayato, Y, Hearty, C, Helmer, RL, Henderson, R, Higashi, N, Hignight, J, Hillairet, A, Hiraki, T, Hirose, E, Holeczek, J, Horikawa, S, Huang, K, Hyndman, A, Ichikawa, AK, Ieki, K, Ieva, M, Iida, M, Ikeda, M, Ilic, J, Imber, J, Ishida, T, Ishihara, C, Ishii, T, Ives, SJ, Iwasaki, M, Iyogi, K, Izmaylov, A, Jamieson, B, Johnson, RA, Joo, KK, Jover-Manas, GV, Jung, CK, Kaji, H, Kajita, T, Kakuno, H, Kameda, J, Kaneyuki, K, Karlen, D, Kasami, K, Kato, I, Kawamuko, H, Kearns, E, Khabibullin, M, Khanam, F, Khotjantsev, A, Kielczewska, D, Kikawa, T, Kim, J, Kim, JY, Kim, SB, Kimura, N, Kirby, B, Kisiel, J, Kitching, P, Kobayashi, T, Kogan, G, Koike, S, Konaka, A, Kormos, LL, Korzenev, A, Koseki, K, Koshio, Y, Kouzuma, Y, Kowalik, K, Kravtsov, V, Kreslo, I, Kropp, W, Kubo, H, Kubota, J, Kudenko, Y, Kulkarni, N, Kurimoto, Y, Kurjata, R, Kutter, T, Lagoda, J, Laihem, K, Laveder, M, Lawe, M, Lee, KP, Le, PT, Levy, JM, Licciardi, C, Lim, IT, Lindner, T, Lister, C, Litchfield, RP, Litos, M, Longhin, A, Lopez, GD, Loverre, PF, Ludovici, L, Lux, T, MacAire, M, Magaletti, L, Mahn, K, Makida, Y, Malek, M, Manly, S, Marchionni, A, Marino, AD, Marone, AJ, Marteau, J, Martin, JF, Maruyama, T, Maryon, T, Marzec, J, Masliah, P, Mathie, EL, Matsumura, C, Matsuoka, K, Matveev, V, Mavrokoridis, K, Mazzucato, E, McCauley, N, McFarland, KS, McGrew, C, McLachlan, T, Messina, M, Metcalf, W, Metelko, C, Mezzetto, M, Mijakowski, P, Miller, CA, Minamino, A, Mineev, O, Mine, S, Missert, AD, Mituka, G, Miura, M, Mizouchi, K, Monfregola, L, Moreau, F, Morgan, B, Moriyama, S, Muir, A, Murakami, A, Muratore, JF, Murdoch, M, Murphy, S, Myslik, J, Nagai, N, Nakadaira, T, Nakahata, M, Nakai, T, Nakajima, K, Nakamoto, T, Nakamura, K, Nakayama, S, Nakaya, T, Naples, D, Navin, ML, Nicholls, TC, Nielsen, B, Nielsen, C, Nishikawa, K, Nishino, H, Nitta, K, Nobuhara, T, Nowak, JA, Obayashi, Y, Ogitsu, T, Ohhata, H, Okamura, T, Okumura, K, Okusawa, T, Oser, SM, Otani, M, Owen, RA, Oyama, Y, Ozaki, T, Pac, MY, Palladino, V, Paolone, V, Paul, P, Payne, D, Pearce, GF, Perkin, JD, Pettinacci, V, Pierre, F, Poplawska, E, Popov, B, Posiadala, M, Poutissou, J-M, Poutissou, R, Przewlocki, P, Qian, W, Raaf, JL, Radicioni, E, Ratoff, PN, Raufer, TM, Ravonel, M, Raymond, M, Reeves, M, Retiere, F, Robert, A, Rodrigues, PA, Rondio, E, Roney, JM, Rossi, B, Roth, S, Rubbia, A, Ruterbories, D, Sabouri, S, Sacco, R, Sakashita, K, Sánchez, F, Sarrat, A, Sasaki, K, Scholberg, K, Schwehr, J, Scott, M, Scully, DI, Seiya, Y, Sekiguchi, T, Sekiya, H, Shibata, M, Shimizu, Y, Shiozawa, M, Short, S, Sinclair, PD, Siyad, M, Smith, BM, Smith, RJ, Smy, M, Sobczyk, JT, Sobel, H, Sorel, M, Stahl, A, Stamoulis, P, Steinmann, J, Still, B, Stone, J, Strabel, C, Sulej, R, Suzuki, A, Suzuki, K, Suzuki, S, Suzuki, SY, Suzuki, Y, Szeglowski, T, Szeptycka, M, Tacik, R, Tada, M, Taguchi, M, Takahashi, S, Takeda, A, Takenaga, Y, Takeuchi, Y, Tanaka, K, Tanaka, HA, Tanaka, M, Tanaka, MM, Tanimoto, N, Tashiro, K, Taylor, I, Terashima, A, Terhorst, D, Terri, R, Thompson, LF, Thorley, A, Toki, W, Tobayama, S, Tomaru, T, Totsuka, Y, Touramanis, C, Tsukamoto, T, Tzanov, M, Uchida, Y, Ueno, K, Vacheret, A, Vagins, M, Vasseur, G, Veledar, O, Wachala, T, Walding, JJ, Waldron, AV, Walter, CW, Wanderer, PJ, Wang, J, Ward, MA, Ward, GP, Wark, D, Wascko, MO, Weber, A, Wendell, R, West, N, Whitehead, LH, Wikström, G, Wilkes, RJ, Wilking, MJ, Williamson, Z, Wilson, Wilson, RJ, Wongjirad, T, Yamada, S, Yamada, Y, Yamamoto, A, Yamamoto, K, Yamanoi, Y, Yamaoka, H, Yamauchi, T, Yanagisawa, C, Yano, T, Yen, S, Yershov, N, Yokoyama, M, Yuan, T, Zalewska, A, Zalipska, J, Zambelli, L, Zaremba, K, Ziembicki, M, Zimmerman, ED, Zito, M, and Zmuda, J
Subjects: Physics::Instrumentation and Detectors, hep-ex, Astrophysics::High Energy Astrophysical Phenomena, High Energy Physics::Phenomenology, Physics::Accelerator Physics, High Energy Physics::Experiment, 7. Clean energy
Abstract: We report a measurement of muon-neutrino disappearance in the T2K experiment. The 295-km muon-neutrino beam from Tokai to Kamioka is the first implementation of the off-axis technique in a long-baseline neutrino oscillation experiment.

25. Measurements of the T2K neutrino beam properties using the INGRID on-axis near detector

Author: Abe, K., Abgrall, N., Ajima, Y., Aihara, H., Albert, J. B., Andreopoulos, C., Andrieu, B., Anerella, M. D., Aoki, S., Araoka, O., Argyriades, J., Ariga, A., Ariga, T., Assylbekov, S., Autiero, D., Badertscher, A., Barbi, M., Barker, G. J., Barr, G., Bass, M., Batkiewicz, M., Bay, F., Bentham, S., Berardi, V., Berger, B. E., Bertram, I., Besnier, M., Beucher, J., Beznosko, D., Bhadra, S., Blaszczyk, F. d. M., Blocki, J., Blondel, A., Bojechko, C., Bouchez, J., Boyd, S. B., Bravar, A., Bronner, C., Brook-Roberge, D. G., Buchanan, N., Budd, H., Calvet, D., Cartwright, S. L., Carver, A., Castillo, R., Catanesi, M. G., Cazes, A., Cervera, A., Chavez, C., Choi, S., Christodoulou, G., Coleman, J., Collazuol, G., Coleman, W., Connolly, K., Curioni, A., Dabrowska, A., Danko, I., Das, R., Davies, G. S., Davis, S., Day, M., De Rosa, G., de André, J. P. A. M., de Perio, P., Dealtry, T., Delbart, A., Densham, C., Di Lodovico, F., Di Luise, S., Tran, P. Dinh, Dobson, J., Dore, U., Drapier, O., Dufour, F., Dumarchez, J., Dytman, S., Dziewiecki, M., Dziomba, M., Emery, S., Ereditato, A., Escallier, J. E., Escudero, L., Esposito, L. S., Fechner, M., Ferrero, A., Finch, A. J., Frank, E., Fujii, Y., Fukuda, Y., Galymov, V., Ganetis, G. L., Gannaway, F. C., Gaudin, A., Gendotti, A., George, M., Giffin, S., Giganti, C., Gilje, K., Ghosh, A. K., Golan, T., Goldhaber, M., Gomez-Cadenas, J. J., Gomi, S., Gonin, M., Grant, N., Grant, A., Gumplinger, P., Guzowski, P., Haesler, A., Haigh, M. D., Hamano, K., Hansen, C., Hansen, D., Hara, T., Harrison, P. F., Hartfiel, B., Hartz, M., Haruyama, T., Hasegawa, T., Hastings, N. C., Hatzikoutelis, A., Hayashi, K., Hayato, Y., Hearty, C., Helmer, R. L., Henderson, R., Higashi, N., Hignight, J., Hillairet, A., Hirose, E., Holeczek, J., Horikawa, S., Hyndman, A., Ichikawa, A. K., Ieki, K., Ieva, M., Iida, M., Ikeda, M., Ilic, J., Imber, J., Ishida, T., Ishihara, C., Ishii, T., Ives, S. J., Iwasaki, M., Iyogi, K., Izmaylov, A., Jamieson, B., Johnson, R. A., Joo, K. K., Jover-Manas, G. V., Jung, C. K., Kaji, H., Kajita, T., Kakuno, H., Kameda, J., Kaneyuki, K., Karlen, D., Kasami, K., Kato, I., Kawamuko, H., Kearns, E., Khabibullin, M., Khanam, F., Khotjantsev, A., Kielczewska, D., Kikawa, T., Kim, J., Kim, J. Y., Kim, S. B., Kimura, N., Kirby, B., Kisiel, J., Kitching, P., Kobayashi, T., Kogan, G., Koike, S., Konaka, A., Kormos, L. L., Korzenev, A., Koseki, K., Koshio, Y., Kouzuma, Y., Kowalik, K., Kravtsov, V., Kreslo, I., Kropp, W., Kubo, H., Kubota, J., Kudenko, Y., Kulkarni, N., Kurimoto, Y., Kurjata, R., Kutter, T., Lagoda, J., Laihem, K., Laveder, M., Lee, K. P., Le, P. T., levy, J. M., Licciardi, C., Lim, I. T., Lindner, T., Litchfield, R. P., Litos, M., Longhin, A., Lopez, G. D., Loverre, P. F., Ludovici, L., Lux, T., Macaire, M., Mahn, K., Makida, Y., Malek, M., Manly, S., Marchionni, A., Marino, A. D., Marone, A. J., Marteau, J., Martin, J. F., Maruyama, T., Maryon, T., Marzec, J., Masliah, P., Mathie, E. L., Matsumura, C., Matsuoka, K., Matveev, V., Mavrokoridis, K., Mazzucato, E., Mccauley, N., McFarland, K. S., Mcgrew, C., McLachlan, T., Messina, M., Metcalf, W., Metelko, C., Mezzetto, M., Mijakowski, P., Miller, C. A., Minamino, A., Mineev, O., Mine, S., Missert, A. D., Mituka, G., Miura, M., Mizouchi, K., Monfregola, L., Moreau, F., Morgan, B., Moriyama, S., Muir, A., Murakami, A., Muratore, J. F., Murdoch, M., Murphy, S., Myslik, J., Nagai, N., Nakadaira, T., Nakahata, M., Nakai, T., Nakajima, K., Nakamoto, T., Nakamura, K., Nakayama, S., Nakaya, T., Naples, D., Navin, M. L., Nelson, B., Nicholls, T. C., Nielsen, C., Nishikawa, K., Nishino, H., Nitta, K., Nobuhara, T., Nowak, J. A., Obayashi, Y., Ogitsu, T., Ohhata, H., Okamura, T., Okumura, K., Okusawa, T., Oser, S. M., Otani, M., Owen, R. A., Oyama, Y., Ozaki, T., Pac, M. Y., Palladino, V., Paolone, V., Paul, P., Payne, D., Pearce, G. F., Perkin, J. D., Pettinacci, V., Pierre, F., Poplawska, E., Popov, B., Posiadala, M., Poutissou, J. -M., Poutissou, R., Przewlocki, P., Qian, W., Raaf, J. L., Radicioni, E., Ratoff, P. N., Raufer, T. M., Ravonel, M., Raymond, M., Retiere, F., Robert, A., Rodrigues, P. A., Rondio, E., Roney, J. M., Rossi, B., Roth, S., Rubbia, A., Ruterbories, D., Sabouri, S., Sacco, R., Sakashita, K., Sánchez, F., Sarrat, A., Sasaki, K., Scholberg, K., Schwehr, J., Scott, M., Scully, D. I., Seiya, Y., Sekiguchi, T., Sekiya, H., Shibata, M., Shimizu, Y., Shiozawa, M., Short, S., Siyad, M., Smith, R. J., Smy, M., Sobczyk, J. T., Sobel, H., Sorel, M., Stahl, A., Stamoulis, P., Steinmann, J., Still, B., Stone, J., Stodulski, M., Strabel, C., Sulej, R., Suzuki, A., Suzuki, K., Suzuki, S., Suzuki, S. Y., Suzuki, Y., Swierblewski, J., Szeglowski, T., Szeptycka, M., Tacik, R., Tada, M., Taguchi, M., Takahashi, S., Takeda, A., Takenaga, Y., Takeuchi, Y., Tanaka, K., Tanaka, H. A., Tanaka, M., Tanaka, M. M., Tanimoto, N., Tashiro, K., Taylor, I., Terashima, A., Terhorst, D., Terri, R., Thompson, L. F., Thorley, A., Toki, W., Tobayama, S., Tomaru, T., Totsuka, Y., Touramanis, C., Tsukamoto, T., Tzanov, M., Uchida, Y., Ueno, K., Vacheret, A., Vagins, M., Vasseur, G., Wachala, T., Walding, J. J., Waldron, A. V., Walter, C. W., Wanderer, P. J., Wang, J., Ward, M. A., Ward, G. P., Wark, D., Wascko, M. O., Weber, A., Wendell, R., West, N., Whitehead, L. H., Wikström, G., Wilkes, R. J., Wilking, M. J., Williamson, Z., Wilson, J. R., Wilson, R. J., Wongjirad, T., Yamada, S., Yamada, Y., Yamamoto, A., Yamamoto, K., Yamanoi, Y., Yamaoka, H., Yamauchi, T., Yanagisawa, C., Yano, T., Yen, S., Yershov, N., Yokoyama, M., Yuan, T., Zalewska, A., Zalipska, J., Zambelli, L., Zaremba, K., Ziembicki, M., Zimmerman, E. D., Zito, M., Zmuda, J., Abe, K., Abgrall, N., Ajima, Y., Aihara, H., Albert, J. B., Andreopoulos, C., Andrieu, B., Anerella, M. D., Aoki, S., Araoka, O., Argyriades, J., Ariga, A., Ariga, T., Assylbekov, S., Autiero, D., Badertscher, A., Barbi, M., Barker, G. J., Barr, G., Bass, M., Batkiewicz, M., Bay, F., Bentham, S., Berardi, V., Berger, B. E., Bertram, I., Besnier, M., Beucher, J., Beznosko, D., Bhadra, S., Blaszczyk, F. d. M., Blocki, J., Blondel, A., Bojechko, C., Bouchez, J., Boyd, S. B., Bravar, A., Bronner, C., Brook-Roberge, D. G., Buchanan, N., Budd, H., Calvet, D., Cartwright, S. L., Carver, A., Castillo, R., Catanesi, M. G., Cazes, A., Cervera, A., Chavez, C., Choi, S., Christodoulou, G., Coleman, J., Collazuol, G., Coleman, W., Connolly, K., Curioni, A., Dabrowska, A., Danko, I., Das, R., Davies, G. S., Davis, S., Day, M., De Rosa, G., de André, J. P. A. M., de Perio, P., Dealtry, T., Delbart, A., Densham, C., Di Lodovico, F., Di Luise, S., Tran, P. Dinh, Dobson, J., Dore, U., Drapier, O., Dufour, F., Dumarchez, J., Dytman, S., Dziewiecki, M., Dziomba, M., Emery, S., Ereditato, A., Escallier, J. E., Escudero, L., Esposito, L. S., Fechner, M., Ferrero, A., Finch, A. J., Frank, E., Fujii, Y., Fukuda, Y., Galymov, V., Ganetis, G. L., Gannaway, F. C., Gaudin, A., Gendotti, A., George, M., Giffin, S., Giganti, C., Gilje, K., Ghosh, A. K., Golan, T., Goldhaber, M., Gomez-Cadenas, J. J., Gomi, S., Gonin, M., Grant, N., Grant, A., Gumplinger, P., Guzowski, P., Haesler, A., Haigh, M. D., Hamano, K., Hansen, C., Hansen, D., Hara, T., Harrison, P. F., Hartfiel, B., Hartz, M., Haruyama, T., Hasegawa, T., Hastings, N. C., Hatzikoutelis, A., Hayashi, K., Hayato, Y., Hearty, C., Helmer, R. L., Henderson, R., Higashi, N., Hignight, J., Hillairet, A., Hirose, E., Holeczek, J., Horikawa, S., Hyndman, A., Ichikawa, A. K., Ieki, K., Ieva, M., Iida, M., Ikeda, M., Ilic, J., Imber, J., Ishida, T., Ishihara, C., Ishii, T., Ives, S. J., Iwasaki, M., Iyogi, K., Izmaylov, A., Jamieson, B., Johnson, R. A., Joo, K. K., Jover-Manas, G. V., Jung, C. K., Kaji, H., Kajita, T., Kakuno, H., Kameda, J., Kaneyuki, K., Karlen, D., Kasami, K., Kato, I., Kawamuko, H., Kearns, E., Khabibullin, M., Khanam, F., Khotjantsev, A., Kielczewska, D., Kikawa, T., Kim, J., Kim, J. Y., Kim, S. B., Kimura, N., Kirby, B., Kisiel, J., Kitching, P., Kobayashi, T., Kogan, G., Koike, S., Konaka, A., Kormos, L. L., Korzenev, A., Koseki, K., Koshio, Y., Kouzuma, Y., Kowalik, K., Kravtsov, V., Kreslo, I., Kropp, W., Kubo, H., Kubota, J., Kudenko, Y., Kulkarni, N., Kurimoto, Y., Kurjata, R., Kutter, T., Lagoda, J., Laihem, K., Laveder, M., Lee, K. P., Le, P. T., levy, J. M., Licciardi, C., Lim, I. T., Lindner, T., Litchfield, R. P., Litos, M., Longhin, A., Lopez, G. D., Loverre, P. F., Ludovici, L., Lux, T., Macaire, M., Mahn, K., Makida, Y., Malek, M., Manly, S., Marchionni, A., Marino, A. D., Marone, A. J., Marteau, J., Martin, J. F., Maruyama, T., Maryon, T., Marzec, J., Masliah, P., Mathie, E. L., Matsumura, C., Matsuoka, K., Matveev, V., Mavrokoridis, K., Mazzucato, E., Mccauley, N., McFarland, K. S., Mcgrew, C., McLachlan, T., Messina, M., Metcalf, W., Metelko, C., Mezzetto, M., Mijakowski, P., Miller, C. A., Minamino, A., Mineev, O., Mine, S., Missert, A. D., Mituka, G., Miura, M., Mizouchi, K., Monfregola, L., Moreau, F., Morgan, B., Moriyama, S., Muir, A., Murakami, A., Muratore, J. F., Murdoch, M., Murphy, S., Myslik, J., Nagai, N., Nakadaira, T., Nakahata, M., Nakai, T., Nakajima, K., Nakamoto, T., Nakamura, K., Nakayama, S., Nakaya, T., Naples, D., Navin, M. L., Nelson, B., Nicholls, T. C., Nielsen, C., Nishikawa, K., Nishino, H., Nitta, K., Nobuhara, T., Nowak, J. A., Obayashi, Y., Ogitsu, T., Ohhata, H., Okamura, T., Okumura, K., Okusawa, T., Oser, S. M., Otani, M., Owen, R. A., Oyama, Y., Ozaki, T., Pac, M. Y., Palladino, V., Paolone, V., Paul, P., Payne, D., Pearce, G. F., Perkin, J. D., Pettinacci, V., Pierre, F., Poplawska, E., Popov, B., Posiadala, M., Poutissou, J. -M., Poutissou, R., Przewlocki, P., Qian, W., Raaf, J. L., Radicioni, E., Ratoff, P. N., Raufer, T. M., Ravonel, M., Raymond, M., Retiere, F., Robert, A., Rodrigues, P. A., Rondio, E., Roney, J. M., Rossi, B., Roth, S., Rubbia, A., Ruterbories, D., Sabouri, S., Sacco, R., Sakashita, K., Sánchez, F., Sarrat, A., Sasaki, K., Scholberg, K., Schwehr, J., Scott, M., Scully, D. I., Seiya, Y., Sekiguchi, T., Sekiya, H., Shibata, M., Shimizu, Y., Shiozawa, M., Short, S., Siyad, M., Smith, R. J., Smy, M., Sobczyk, J. T., Sobel, H., Sorel, M., Stahl, A., Stamoulis, P., Steinmann, J., Still, B., Stone, J., Stodulski, M., Strabel, C., Sulej, R., Suzuki, A., Suzuki, K., Suzuki, S., Suzuki, S. Y., Suzuki, Y., Swierblewski, J., Szeglowski, T., Szeptycka, M., Tacik, R., Tada, M., Taguchi, M., Takahashi, S., Takeda, A., Takenaga, Y., Takeuchi, Y., Tanaka, K., Tanaka, H. A., Tanaka, M., Tanaka, M. M., Tanimoto, N., Tashiro, K., Taylor, I., Terashima, A., Terhorst, D., Terri, R., Thompson, L. F., Thorley, A., Toki, W., Tobayama, S., Tomaru, T., Totsuka, Y., Touramanis, C., Tsukamoto, T., Tzanov, M., Uchida, Y., Ueno, K., Vacheret, A., Vagins, M., Vasseur, G., Wachala, T., Walding, J. J., Waldron, A. V., Walter, C. W., Wanderer, P. J., Wang, J., Ward, M. A., Ward, G. P., Wark, D., Wascko, M. O., Weber, A., Wendell, R., West, N., Whitehead, L. H., Wikström, G., Wilkes, R. J., Wilking, M. J., Williamson, Z., Wilson, J. R., Wilson, R. J., Wongjirad, T., Yamada, S., Yamada, Y., Yamamoto, A., Yamamoto, K., Yamanoi, Y., Yamaoka, H., Yamauchi, T., Yanagisawa, C., Yano, T., Yen, S., Yershov, N., Yokoyama, M., Yuan, T., Zalewska, A., Zalipska, J., Zambelli, L., Zaremba, K., Ziembicki, M., Zimmerman, E. D., Zito, M., and Zmuda, J.
Abstract: Precise measurement of neutrino beam direction and intensity was achieved based on a new concept with modularized neutrino detectors. INGRID (Interactive Neutrino GRID) is an on-axis near detector for the T2K long baseline neutrino oscillation experiment. INGRID consists of 16 identical modules arranged in horizontal and vertical arrays around the beam center. The module has a sandwich structure of iron target plates and scintillator trackers. INGRID directly monitors the muon neutrino beam profile center and intensity using the number of observed neutrino events in each module. The neutrino beam direction is measured with accuracy better than 0.4 mrad from the measured profile center. The normalized event rate is measured with 4% precision.
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26. The T2K Experiment

Author: Abe, K., Abgrall, N., Aihara, H., Ajima, Y., Albert, J. B., Allan, D., Amaudruz, P. -A., Andreopoulos, C., Andrieu, B., Anerella, M. D., Angelsen, C., Aoki, S., Araoka, O., Argyriades, J., Ariga, A., Ariga, T., Assylbekov, S., de André, J. P. A. M., Autiero, D., Badertscher, A., Ballester, O., Barbi, M., Barker, G. J., Baron, P., Barr, G., Bartoszek, L., Batkiewicz, M., Bay, F., Bentham, S., Berardi, V., Berger, B. E., Berns, H., Bertram, I., Besnier, M., Beucher, J., Beznosko, D., Bhadra, S., Birney, P., Bishop, D., Blackmore, E., Blaszczyk, F. d. M., Blocki, J., Blondel, A., Bodek, A., Bojechko, C., Bouchez, J., Boussuge, T., Boyd, S. B., Boyer, M., Braam, N., Bradford, R., Bravar, A., Briggs, K., Brinson, J. D., Bronner, C., Brook-Roberge, D. G., Bryant, M., Buchanan, N., Budd, H., Cadabeschi, M., Calland, R. G., Calvet, D., Rodríguez, J. Caravaca, Carroll, J., Cartwright, S. L., Carver, A., Castillo, R., Catanesi, M. G., Cavata, C., Cazes, A., Cervera, A., Charrier, J. P., Chavez, C., Choi, S., Chollet, S., Christodoulou, G., Colas, P., Coleman, J., Coleman, W., Collazuol, G., Connolly, K., Cooke, P., Curioni, A., Dabrowska, A., Danko, I., Das, R., Davies, G. S., Davis, S., Day, M., De La Broise, X., de Perio, P., De Rosa, G., Dealtry, T., Debraine, A., Delagnes, E., Delbart, A., Densham, C., Di Lodovico, F., Di Luise, S., Tran, P. Dinh, Dobson, J., Doornbos, J., Dore, U., Drapier, O., Druillole, F., Dufour, F., Dumarchez, J., Durkin, T., Dytman, S., Dziewiecki, M., Dziomba, M., Ellison, B., Emery, S., Ereditato, A., Escallier, J. E., Escudero, L., Esposito, L. S., Faszer, W., Fechner, M., Ferrero, A., Finch, A., Fisher, C., Fitton, M., Flight, R., Forbush, D., Frank, E., Fransham, K., Fujii, Y., Fukuda, Y., Gallop, M., Galymov, V., Ganetis, G. L., Gannaway, F. C., Gaudin, A., Gaweda, J., Gendotti, A., George, M., Giffin, S., Giganti, C., Gilje, K., Giomataris, I., Giraud, J., Ghosh, A. K., Golan, T., Goldhaber, M., Gomez-Cadenas, J. J., Gomi, S., Gonin, M., Goyette, M., Grant, A., Grant, N., Grañena, F., Greenwood, S., Gumplinger, P., Guzowski, P., Haigh, M. D., Hamano, K., Hansen, C., Hara, T., Harrison, P. F., Hartfiel, B., Hartz, M., Haruyama, T., Hasanen, R., Hasegawa, T., Hastings, N. C., Hastings, S., Hatzikoutelis, A., Hayashi, K., Hayato, Y., Haycock, T. D. J., Hearty, C., Helmer, R. L., Henderson, R., Herlant, S., Higashi, N., Hignight, J., Hiraide, K., Hirose, E., Holeczek, J., Honkanen, N., Horikawa, S., Hyndman, A., Ichikawa, A. K., Ieki, K., Ieva, M., Iida, M., Ikeda, M., Ilic, J., Imber, J., Ishida, T., Ishihara, C., Ishii, T., Ives, S. J., Iwasaki, M., Iyogi, K., Izmaylov, A., Jamieson, B., Johnson, R. A., Joo, K. K., Jover-Manas, G., Jung, C. K., Kaji, H., Kajita, T., Kakuno, H., Kameda, J., Kaneyuki, K., Karlen, D., Kasami, K., Kasey, V., Kato, I., Kawamuko, H., Kearns, E., Kellet, L., Khabibullin, M., Khaleeq, M., Khan, N., Khotjantsev, A., Kielczewska, D., Kikawa, T., Kim, J. Y., Kim, S. -B., Kimura, N., Kirby, B., Kisiel, J., Kitching, P., Kobayashi, T., Kogan, G., Koike, S., Komorowski, T., Konaka, A., Kormos, L. L., Korzenev, A., Koseki, K., Koshio, Y., Kouzuma, Y., Kowalik, K., Kravtsov, V., Kreslo, I., Kropp, W., Kubo, H., Kubota, J., Kudenko, Y., Kulkarni, N., Kurchaninov, L., Kurimoto, Y., Kurjata, R., Kurosawa, Y., Kutter, T., Lagoda, J., Laihem, K., Langstaff, R., Laveder, M., Lawson, T. B., Le, P. T., Coguie, A. Le, Ross, M. Le, Lee, K. P., Lenckowski, M., Licciardi, C., Lim, I. T., Lindner, T., Litchfield, R. P., Longhin, A., Lopez, G. D., Lu, P., Ludovici, L., Lux, T., Macaire, M., Magaletti, L., Mahn, K., Makida, Y., Malafis, C. J., Malek, M., Manly, S., Marchionni, A., Mark, C., Marino, A. D., Marone, A. J., Marteau, J., Martin, J. F., Maruyama, T., Maryon, T., Marzec, J., Masliah, P., Mathie, E. L., Matsumura, C., Matsuoka, K., Matveev, V., Mavrokoridis, K., Mazzucato, E., McCauley, N., McFarland, K. S., McGrew, C., McLachlan, T., Mercer, I., Messina, M., Metcalf, W., Metelko, C., Mezzetto, M., Mijakowski, P., Miller, C. A., Minamino, A., Mineev, O., Mine, S., Minvielle, R. E., Mituka, G., Miura, M., Mizouchi, K., Mols, J. -P., Monfregola, L., Monmarthe, E., Moreau, F., Morgan, B., Moriyama, S., Morris, D., Muir, A., Murakami, A., Muratore, J. F., Murdoch, M., Murphy, S., Myslik, J., Nagashima, G., Nakadaira, T., Nakahata, M., Nakamoto, T., Nakamura, K., Nakayama, S., Nakaya, T., Naples, D., Nelson, B., Nicholls, T. C., Nishikawa, K., Nishino, H., Nitta, K., Nizery, F., Nowak, J. A., Noy, M., Obayashi, Y., Ogitsu, T., Ohhata, H., Okamura, T., Okumura, K., Okusawa, T., Ohlmann, C., Olchanski, K., Openshaw, R., Oser, S. M., Otani, M., Owen, R. A., Oyama, Y., Ozaki, T., Pac, M. Y., Palladino, V., Paolone, V., Paul, P., Payne, D., Pearce, G. F., Pearson, C., Perkin, J. D., Pfleger, M., Pierre, F., Pierrepont, D., Plonski, P., Poffenberger, P., Poplawska, E., Popov, B., Posiadala, M., Poutissou, J. -M., Poutissou, R., Preece, R., Przewlocki, P., Qian, W., Raaf, J. L., Radicioni, E., Ramos, K., Ratoff, P., Raufer, T. M., Ravonel, M., Raymond, M., Retiere, F., Richards, D., Ritou, J. -L., Robert, A., Rodrigues, P. A., Rondio, E., Roney, M., Rooney, M., Ross, D., Rossi, B., Roth, S., Rubbia, A., Ruterbories, D., Sacco, R., Sadler, S., Sakashita, K., Sanchez, F., Sarrat, A., Sasaki, K., Schaack, P., Schmidt, J., Scholberg, K., Schwehr, J., Scott, M., Scully, D. I., Seiya, Y., Sekiguchi, T., Sekiya, H., Sheffer, G., Shibata, M., Shimizu, Y., Shiozawa, M., Short, S., Siyad, M., Smith, D., Smith, R. J., Smy, M., Sobczyk, J., Sobel, H., Sooriyakumaran, S., Sorel, M., Spitz, J., Stahl, A., Stamoulis, P., Star, O., Statter, J., Stawnyczy, L., Steinmann, J., Steffens, J., Still, B., Stodulski, M., Stone, J., Strabel, C., Strauss, T., Sulej, R., Sutcliffe, P., Suzuki, A., Suzuki, K., Suzuki, S., Suzuki, S. Y., Suzuki, Y., Swierblewski, J., Szeglowski, T., Szeptycka, M., Tacik, R., Tada, M., Tadepalli, A. S., Taguchi, M., Takahashi, S., Takeda, A., Takenaga, Y., Takeuchi, Y., Tanaka, H. A., Tanaka, K., Tanaka, M., Tanaka, M. M., Tanimoto, N., Tashiro, K., Taylor, I. J., Terashima, A., Terhorst, D., Terri, R., Thompson, L. F., Thorley, A., Thorpe, M., Toki, W., Tomaru, T., Totsuka, Y., Touramanis, C., Tsukamoto, T., Tvaskis, V., Tzanov, M., Uchida, Y., Ueno, K., Usseglio, M., Vacheret, A., Vagins, M., Van Schalkwyk, J. F., Vanel, J. -C., Vasseur, G., Veledar, O., Vincent, P., Wachala, T., Waldron, A. V., Walter, C. W., Wanderer, P. J., Ward, M. A., Ward, G. P., Wark, D., Warner, D., Wascko, M. O., Weber, A., Wendell, R., Wendland, J., West, N., Whitehead, L. H., Wikström, G., Wilkes, R. J., Wilking, M. J., Williamson, Z., Wilson, J. R., Wilson, R. J., Wong, K., Wongjirad, T., Yamada, S., Yamada, Y., Yamamoto, A., Yamamoto, K., Yamanoi, Y., Yamaoka, H., Yanagisawa, C., Yano, T., Yen, S., Yershov, N., Yokoyama, M., Zalewska, A., Zalipska, J., Zaremba, K., Ziembicki, M., Zimmerman, E. D., Zito, M., Zmuda, J., Abe, K., Abgrall, N., Aihara, H., Ajima, Y., Albert, J. B., Allan, D., Amaudruz, P. -A., Andreopoulos, C., Andrieu, B., Anerella, M. D., Angelsen, C., Aoki, S., Araoka, O., Argyriades, J., Ariga, A., Ariga, T., Assylbekov, S., de André, J. P. A. M., Autiero, D., Badertscher, A., Ballester, O., Barbi, M., Barker, G. J., Baron, P., Barr, G., Bartoszek, L., Batkiewicz, M., Bay, F., Bentham, S., Berardi, V., Berger, B. E., Berns, H., Bertram, I., Besnier, M., Beucher, J., Beznosko, D., Bhadra, S., Birney, P., Bishop, D., Blackmore, E., Blaszczyk, F. d. M., Blocki, J., Blondel, A., Bodek, A., Bojechko, C., Bouchez, J., Boussuge, T., Boyd, S. B., Boyer, M., Braam, N., Bradford, R., Bravar, A., Briggs, K., Brinson, J. D., Bronner, C., Brook-Roberge, D. G., Bryant, M., Buchanan, N., Budd, H., Cadabeschi, M., Calland, R. G., Calvet, D., Rodríguez, J. Caravaca, Carroll, J., Cartwright, S. L., Carver, A., Castillo, R., Catanesi, M. G., Cavata, C., Cazes, A., Cervera, A., Charrier, J. P., Chavez, C., Choi, S., Chollet, S., Christodoulou, G., Colas, P., Coleman, J., Coleman, W., Collazuol, G., Connolly, K., Cooke, P., Curioni, A., Dabrowska, A., Danko, I., Das, R., Davies, G. S., Davis, S., Day, M., De La Broise, X., de Perio, P., De Rosa, G., Dealtry, T., Debraine, A., Delagnes, E., Delbart, A., Densham, C., Di Lodovico, F., Di Luise, S., Tran, P. Dinh, Dobson, J., Doornbos, J., Dore, U., Drapier, O., Druillole, F., Dufour, F., Dumarchez, J., Durkin, T., Dytman, S., Dziewiecki, M., Dziomba, M., Ellison, B., Emery, S., Ereditato, A., Escallier, J. E., Escudero, L., Esposito, L. S., Faszer, W., Fechner, M., Ferrero, A., Finch, A., Fisher, C., Fitton, M., Flight, R., Forbush, D., Frank, E., Fransham, K., Fujii, Y., Fukuda, Y., Gallop, M., Galymov, V., Ganetis, G. L., Gannaway, F. C., Gaudin, A., Gaweda, J., Gendotti, A., George, M., Giffin, S., Giganti, C., Gilje, K., Giomataris, I., Giraud, J., Ghosh, A. K., Golan, T., Goldhaber, M., Gomez-Cadenas, J. J., Gomi, S., Gonin, M., Goyette, M., Grant, A., Grant, N., Grañena, F., Greenwood, S., Gumplinger, P., Guzowski, P., Haigh, M. D., Hamano, K., Hansen, C., Hara, T., Harrison, P. F., Hartfiel, B., Hartz, M., Haruyama, T., Hasanen, R., Hasegawa, T., Hastings, N. C., Hastings, S., Hatzikoutelis, A., Hayashi, K., Hayato, Y., Haycock, T. D. J., Hearty, C., Helmer, R. L., Henderson, R., Herlant, S., Higashi, N., Hignight, J., Hiraide, K., Hirose, E., Holeczek, J., Honkanen, N., Horikawa, S., Hyndman, A., Ichikawa, A. K., Ieki, K., Ieva, M., Iida, M., Ikeda, M., Ilic, J., Imber, J., Ishida, T., Ishihara, C., Ishii, T., Ives, S. J., Iwasaki, M., Iyogi, K., Izmaylov, A., Jamieson, B., Johnson, R. A., Joo, K. K., Jover-Manas, G., Jung, C. K., Kaji, H., Kajita, T., Kakuno, H., Kameda, J., Kaneyuki, K., Karlen, D., Kasami, K., Kasey, V., Kato, I., Kawamuko, H., Kearns, E., Kellet, L., Khabibullin, M., Khaleeq, M., Khan, N., Khotjantsev, A., Kielczewska, D., Kikawa, T., Kim, J. Y., Kim, S. -B., Kimura, N., Kirby, B., Kisiel, J., Kitching, P., Kobayashi, T., Kogan, G., Koike, S., Komorowski, T., Konaka, A., Kormos, L. L., Korzenev, A., Koseki, K., Koshio, Y., Kouzuma, Y., Kowalik, K., Kravtsov, V., Kreslo, I., Kropp, W., Kubo, H., Kubota, J., Kudenko, Y., Kulkarni, N., Kurchaninov, L., Kurimoto, Y., Kurjata, R., Kurosawa, Y., Kutter, T., Lagoda, J., Laihem, K., Langstaff, R., Laveder, M., Lawson, T. B., Le, P. T., Coguie, A. Le, Ross, M. Le, Lee, K. P., Lenckowski, M., Licciardi, C., Lim, I. T., Lindner, T., Litchfield, R. P., Longhin, A., Lopez, G. D., Lu, P., Ludovici, L., Lux, T., Macaire, M., Magaletti, L., Mahn, K., Makida, Y., Malafis, C. J., Malek, M., Manly, S., Marchionni, A., Mark, C., Marino, A. D., Marone, A. J., Marteau, J., Martin, J. F., Maruyama, T., Maryon, T., Marzec, J., Masliah, P., Mathie, E. L., Matsumura, C., Matsuoka, K., Matveev, V., Mavrokoridis, K., Mazzucato, E., McCauley, N., McFarland, K. S., McGrew, C., McLachlan, T., Mercer, I., Messina, M., Metcalf, W., Metelko, C., Mezzetto, M., Mijakowski, P., Miller, C. A., Minamino, A., Mineev, O., Mine, S., Minvielle, R. E., Mituka, G., Miura, M., Mizouchi, K., Mols, J. -P., Monfregola, L., Monmarthe, E., Moreau, F., Morgan, B., Moriyama, S., Morris, D., Muir, A., Murakami, A., Muratore, J. F., Murdoch, M., Murphy, S., Myslik, J., Nagashima, G., Nakadaira, T., Nakahata, M., Nakamoto, T., Nakamura, K., Nakayama, S., Nakaya, T., Naples, D., Nelson, B., Nicholls, T. C., Nishikawa, K., Nishino, H., Nitta, K., Nizery, F., Nowak, J. A., Noy, M., Obayashi, Y., Ogitsu, T., Ohhata, H., Okamura, T., Okumura, K., Okusawa, T., Ohlmann, C., Olchanski, K., Openshaw, R., Oser, S. M., Otani, M., Owen, R. A., Oyama, Y., Ozaki, T., Pac, M. Y., Palladino, V., Paolone, V., Paul, P., Payne, D., Pearce, G. F., Pearson, C., Perkin, J. D., Pfleger, M., Pierre, F., Pierrepont, D., Plonski, P., Poffenberger, P., Poplawska, E., Popov, B., Posiadala, M., Poutissou, J. -M., Poutissou, R., Preece, R., Przewlocki, P., Qian, W., Raaf, J. L., Radicioni, E., Ramos, K., Ratoff, P., Raufer, T. M., Ravonel, M., Raymond, M., Retiere, F., Richards, D., Ritou, J. -L., Robert, A., Rodrigues, P. A., Rondio, E., Roney, M., Rooney, M., Ross, D., Rossi, B., Roth, S., Rubbia, A., Ruterbories, D., Sacco, R., Sadler, S., Sakashita, K., Sanchez, F., Sarrat, A., Sasaki, K., Schaack, P., Schmidt, J., Scholberg, K., Schwehr, J., Scott, M., Scully, D. I., Seiya, Y., Sekiguchi, T., Sekiya, H., Sheffer, G., Shibata, M., Shimizu, Y., Shiozawa, M., Short, S., Siyad, M., Smith, D., Smith, R. J., Smy, M., Sobczyk, J., Sobel, H., Sooriyakumaran, S., Sorel, M., Spitz, J., Stahl, A., Stamoulis, P., Star, O., Statter, J., Stawnyczy, L., Steinmann, J., Steffens, J., Still, B., Stodulski, M., Stone, J., Strabel, C., Strauss, T., Sulej, R., Sutcliffe, P., Suzuki, A., Suzuki, K., Suzuki, S., Suzuki, S. Y., Suzuki, Y., Swierblewski, J., Szeglowski, T., Szeptycka, M., Tacik, R., Tada, M., Tadepalli, A. S., Taguchi, M., Takahashi, S., Takeda, A., Takenaga, Y., Takeuchi, Y., Tanaka, H. A., Tanaka, K., Tanaka, M., Tanaka, M. M., Tanimoto, N., Tashiro, K., Taylor, I. J., Terashima, A., Terhorst, D., Terri, R., Thompson, L. F., Thorley, A., Thorpe, M., Toki, W., Tomaru, T., Totsuka, Y., Touramanis, C., Tsukamoto, T., Tvaskis, V., Tzanov, M., Uchida, Y., Ueno, K., Usseglio, M., Vacheret, A., Vagins, M., Van Schalkwyk, J. F., Vanel, J. -C., Vasseur, G., Veledar, O., Vincent, P., Wachala, T., Waldron, A. V., Walter, C. W., Wanderer, P. J., Ward, M. A., Ward, G. P., Wark, D., Warner, D., Wascko, M. O., Weber, A., Wendell, R., Wendland, J., West, N., Whitehead, L. H., Wikström, G., Wilkes, R. J., Wilking, M. J., Williamson, Z., Wilson, J. R., Wilson, R. J., Wong, K., Wongjirad, T., Yamada, S., Yamada, Y., Yamamoto, A., Yamamoto, K., Yamanoi, Y., Yamaoka, H., Yanagisawa, C., Yano, T., Yen, S., Yershov, N., Yokoyama, M., Zalewska, A., Zalipska, J., Zaremba, K., Ziembicki, M., Zimmerman, E. D., Zito, M., and Zmuda, J.
Abstract: The T2K experiment is a long-baseline neutrino oscillation experiment. Its main goal is to measure the last unknown lepton sector mixing angle {\theta}_{13} by observing {\nu}_e appearance in a {\nu}_{\mu} beam. It also aims to make a precision measurement of the known oscillation parameters, {\Delta}m^{2}_{23} and sin^{2} 2{\theta}_{23}, via {\nu}_{\mu} disappearance studies. Other goals of the experiment include various neutrino cross section measurements and sterile neutrino searches. The experiment uses an intense proton beam generated by the J-PARC accelerator in Tokai, Japan, and is composed of a neutrino beamline, a near detector complex (ND280), and a far detector (Super-Kamiokande) located 295 km away from J-PARC. This paper provides a comprehensive review of the instrumentation aspect of the T2K experiment and a summary of the vital information for each subsystem.

27. Functional expression and mutant analysis of thioredoxin-fused CEL-III, a hemolytic lectin from the marine invertebrate Cucumaria echinata.

Author: Shimizu Y, Yonekura M, and Kouzuma Y
Subjects: Animals, Carbohydrates, Hemolysis, Invertebrates metabolism, Thioredoxins, Cucumaria metabolism, Lectins metabolism
Abstract: CEL-III is a hemolytic lectin purified from the marine invertebrate Cucumaria echinata. New expression system of CEL-III was constructed, and the recombinant thioredoxin-fused CEL-III (Trx-CEL-III) showed strong hemolytic and carbohydrate-binding activity as same as authentic CEL-III. Mutation analysis of Trx-CEL-III suggested that carbohydrate binding to subdomain 1α and 2β of CEL-III might be important for the hemolytic activity., (© The Author(s) 2022. Published by Oxford University Press on behalf of Japan Society for Bioscience, Biotechnology, and Agrochemistry.)
Published: 2022
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28. Purification, cDNA cloning and characterization of Kunitz-type protease inhibitors from Apios americana tubers.

Author: Liu J, Yonekura M, and Kouzuma Y
Subjects: Amino Acid Sequence, Base Sequence, Chromatography, Liquid methods, Escherichia coli genetics, Peptides chemistry, Peptides isolation & purification, Plant Proteins chemistry, Plant Proteins isolation & purification, Recombinant Proteins genetics, Recombinant Proteins isolation & purification, Recombinant Proteins metabolism, Sequence Homology, Amino Acid, Cloning, Molecular, DNA, Complementary genetics, Fabaceae metabolism, Peptides genetics, Plant Proteins genetics, Plant Tubers metabolism
Abstract: Two kinds of Kunitz-type protease inhibitors, AKPI1 and AKPI2, were purified from Apios americana tubers by four steps of column chromatographies and their cDNA cloning was performed. AKPI1 cDNA consist of 809 nucleotides, and the matured protein had 190 amino acids with 20,594 Da. AKPI2 cDNA consist of 794 nucleotides, and the matured protein had 177 amino acids with 19,336 Da. P1 site of AKPI2 was Leu88, suggested the target enzyme was chymotrypsin. On the other hand, Gly85-Ile86-Ser87 was positioned around P1 site of AKTI1. Sequence analysis suggested that two forms (single-chain and two-chain form) of AKPI2 protein were present in the tubers. Recombinant AKPI2 expressed by E.coli system showed inhibitory activity toward serine proteases and heat stability. The Ki values toward chymotrypsin and trypsin were 4 × 10 -7 M and 6 × 10 -6 M, respectively. Abbreviations: AAL: Apios americana lectin; AATI: Apios americana Bowman-Birk type trypsin inhibitor; ACE: angiotensin-converting enzyme; IPTG: isopropyl-β-D-thio-galactopyranoside; Ki : inhibition constant; KPIs: Kunitz-type protease inhibitors; L-BAPA: Benzoyl-L-arginine p -nitroanilide monohydrochloride; L-BTPA: Benzoyl-L-tyrosine p -nitroanilide; PFLNA: Pyr-Phe-Leu- p -nitroanilide; RP-HPLC: reverse-phase high-performance liquid chromatography; RT-PCR: reverse transcription-polymerase chain reaction; SDS-PAGE: sodium dodecyl sulfate-polyacrylamide gel electrophoresis; SLIC: sequence and ligation independent cloning; STANA: N-Succinyl-Ala-Ala-Ala- p -nitroanilide; SHR: spontaneously hypertensive rats; TFA: trifluoroacetic acid; UTR: untranslated region.
Published: 2020
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29. Identification of an aldehyde oxidase involved in indole-3-acetic acid synthesis in Bombyx mori silk gland.

Author: Takei M, Kogure S, Yokoyama C, Kouzuma Y, and Suzuki Y
Subjects: Aldehyde Oxidase chemistry, Aldehyde Oxidase isolation & purification, Amino Acid Sequence, Animals, Bombyx anatomy & histology, Bombyx enzymology, Catalysis, Chromatography methods, Electrophoresis, Polyacrylamide Gel, Sequence Homology, Amino Acid, Spectrophotometry, Ultraviolet methods, Substrate Specificity, Tandem Mass Spectrometry methods, Aldehyde Oxidase metabolism, Bombyx physiology, Indoleacetic Acids metabolism, Plant Growth Regulators metabolism
Abstract: Auxin is thought to be an important factor in the induction of galls by galling insects. We have previously shown that both galling and nongalling insects synthesize indole-3-acetic acid (IAA) from tryptophan (Trp) via two intermediates, indole-3-acetaldoxime (IAOx) and indole-3-acetaldehyde (IAAld). In this study, we isolated an enzyme that catalyzes the last step "IAAld → IAA" from a silk-gland extract of Bombyx mori. The enzyme, designated "BmIAO1", contains two 2Fe-2S iron-sulfur-cluster-binding domains, an FAD-binding domain, and a molybdopterin-binding domain, which are conserved in aldehyde oxidases. BmIAO1 causes the nonenzymatic conversion of Trp to IAAld and the enzymatic conversion of IAOx to IAA, suggesting that BmIAO1 alone is responsible for IAA production in B. mori. However, a detailed comparison of pure BmIAO1 and the crude silk-gland extract suggested the presence of other enzymes involved in IAA production from Trp. Abbreviations: BA: benzoic acid; CE: collision energy; CXP: collision cell exit potential; DP: declustering potential; IAA: indole-3-acetic acid; IBI1: IAA biosynthetic inhibitor-1; IAAld: indole-3-acetaldehyde; ICA: indole-3-carboxylic acid; IAOx: indole-3-acetaldoxime; IEtOH: indole-3-ethanol; LC-MS/MS: liquid chromatography-tandem mass spectrometry; Trp: tryptophan.
Published: 2019
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30. Which Primary Organ Is Most Suitable for Performing Pulmonary Metastasectomy?

Author: Hirai F, Kinoshita I, Matsubara T, Haratake N, Kouzuma Y, Takamori S, Akamine T, Toyokawa G, Tagawa T, Takenoyama M, and Maehara Y
Subjects: Adolescent, Adult, Aged, Aged, 80 and over, Female, Follow-Up Studies, Humans, Lung Neoplasms secondary, Male, Middle Aged, Neoplasms pathology, Prognosis, Retrospective Studies, Survival Rate, Young Adult, Lung Neoplasms surgery, Metastasectomy mortality, Neoplasms classification, Neoplasms surgery, Pneumonectomy mortality
Abstract: Background/aim: The aim of this study was to assess the appropriateness of pulmonary metastasectomy (MT), with a focus on the primary organ., Patients and Methods: The pathological status of the primary organ, outcome of the MT, disease-free interval, and overall survival were assessed., Results: The primary organ was the most significant prognostic factor analyzed, with a relative risk of 4.6 (95% confidence interval: 1.69-12.56, p=0.003). Patients with colorectal carcinoma had a better survival than those with another primary organ (p=0.003). The hazard ratios by primary organ in comparison to colorectal carcinoma were 3.2 for head and neck carcinoma, 3.5 for soft tissue sarcoma, 8.3 for hepatocellular carcinoma, and 8.9 for urinary carcinoma., Conclusion: Colorectal carcinoma is associated with a greater survival benefit than cancer of other primary organs. Colorectal carcinoma cases should be more aggressively considered for MT than other primary organ cases., (Copyright© 2018, International Institute of Anticancer Research (Dr. George J. Delinasios), All rights reserved.)
Published: 2018
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31. Novel tryptophan metabolic pathways in auxin biosynthesis in silkworm.

Author: Yokoyama C, Takei M, Kouzuma Y, Nagata S, and Suzuki Y
Subjects: Animals, Biosynthetic Pathways, Bombyx metabolism, Indoleacetic Acids metabolism, Plant Growth Regulators metabolism, Tryptophan metabolism
Abstract: In the course of our study of the biosynthetic pathway of auxin, a class of phytohormones, in insects, we proposed the biosynthetic pathway tryptophan (Trp)→indole-3-acetaldoxime (IAOx)→indole-3-acetadehyde (IAAld)→indole-3-acetic acid (IAA). In this study, we identified two branches in the metabolic pathways in the silkworm, possibly affecting the efficiency of IAA production: Trp→indole-3-pyruvic acid→indole-3-lactic acid and IAAld→indole-3-ethanol. We also determined the apparent conversion activities (2.05×10 -7 UmL -1 for Trp→IAA, 1.30×10 -5 UmL -1 for IAOx→IAA, and 3.91×10 -1 UmL -1 for IAAld→IAA), which explain why IAOx and IAAld are barely detectable as either endogenous compounds or metabolites of their precursors. The failure to detect IAAld, even in the presence of an inhibitor of the conversion IAAld→IAA, is explained by a switch in the conversion from IAAld→IAA to IAAld→IEtOH., (Copyright © 2017 Elsevier Ltd. All rights reserved.)
Published: 2017
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32. Immature Seed Endosperm and Embryo Proteomics of the Lotus ( Nelumbo Nucifera Gaertn.) by One-Dimensional Gel-Based Tandem Mass Spectrometry and a Comparison with the Mature Endosperm Proteome.

Author: Moro CF, Fukao Y, Shibato J, Rakwal R, Agrawal GK, Shioda S, Kouzuma Y, and Yonekura M
Abstract: Lotus ( Nelumbo nucifera Gaertn.) seed proteome has been the focus of our studies, and we have recently established the first proteome dataset for its mature seed endosperm. The current study unravels the immature endosperm, as well as the embryo proteome, to provide a comprehensive dataset of the lotus seed proteins and a comparison between the mature and immature endosperm tissues across the seed's development. One-dimensional gel electrophoresis (SDS-PAGE) linked with tandem mass spectrometry provided a protein inventory of the immature endosperm (122 non-redundant proteins) and embryo (141 non-redundant proteins) tissues. Comparing with the previous mature endosperm dataset (66 non-redundant proteins), a total of 206 non-redundant proteins were identified across all three tissues of the lotus seed. Results revealed some significant differences in proteome composition between the three lotus seed tissues, most notably between the mature endosperm and its immature developmental stage shifting the proteins from nutrient production to nutrient storage.
Published: 2015
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33. Unraveling the seed endosperm proteome of the lotus (Nelumbo nucifera Gaertn.) utilizing 1DE and 2DE separation in conjunction with tandem mass spectrometry.

Author: Moro CF, Fukao Y, Shibato J, Rakwal R, Timperio AM, Zolla L, Agrawal GK, Shioda S, Kouzuma Y, and Yonekura M
Subjects: Databases, Protein, Metabolic Networks and Pathways, Plant Proteins isolation & purification, Proteomics, Electrophoresis, Gel, Two-Dimensional methods, Endosperm metabolism, Nelumbo metabolism, Proteome metabolism, Tandem Mass Spectrometry methods
Abstract: Nelumbo nucifera (Gaertn.) or lotus, is an aquatic plant native to India, and presently consumed as food mainly in China and Japan. Lotus is also widely used in Indian and Chinese traditional medicine. Extracts from different parts of the lotus plant have been reported to show diverse biological activities-antioxidant, free radical scavenging, anti-inflammatory, and immunomodulatory. Despite this, little work has been done in isolating and identifying proteins responsible for these activities, or yet importantly to establish a lotus proteome. The aim of our group is to develop a proteome catalog of the lotus plant, starting with its seed, the nutrient rich food source. In this present study, the seed endosperm-most abundant in proteins, and main nutrient storage tissue-was targeted for protein extraction by testing five different extraction protocols, followed by their proteomic analyses using complementary 1DE and 2DE approaches in conjunction with MS/MS. The inventory of 66 nonredundant proteins obtained by 1DE-MS and the 30 obtained by 2DE-MS provides the first catalog of the lotus seed endosperm, where the most abundant protein functions were in categories of metabolic activities related to carbohydrate metabolism and nutrient storage., (© 2014 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.)
Published: 2015
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34. Purification and cDNA cloning of a lectin and a lectin-like protein from Apios americana Medikus tubers.

Author: Kouzuma Y, Irie S, Yamazaki R, and Yonekura M
Subjects: Amino Acid Sequence, Animals, Base Sequence, Cloning, Molecular, DNA, Complementary genetics, Erythrocytes cytology, Erythrocytes metabolism, Glycoproteins pharmacology, Hemagglutination drug effects, Lectins chemistry, Lectins pharmacology, Molecular Sequence Data, Plant Proteins chemistry, Plant Proteins pharmacology, Sequence Analysis, alpha-Amylases antagonists & inhibitors, Fabaceae genetics, Lectins genetics, Lectins isolation & purification, Plant Proteins genetics, Plant Proteins isolation & purification, Plant Structures genetics
Abstract: An Apios americana lectin (AAL) and a lectin-like protein (AALP) were purified from tubers by chromatography on Butyl-Cellulofine, ovomucoid-Cellulofine, and DEAE-Cellulofine columns. AAL showed strong hemagglutinating activity toward chicken and goose erythrocytes, but AALP showed no such activity toward any of the erythrocytes tested. The hemagglutinating activity of AAL was not inhibited by mono- or disaccharides, but was inhibited by glycoproteins, such as asialofetuin and ovomucoid, suggesting that AAL is an oligosaccharide-specific lectin. The cDNAs of AAL and AALP consist of 1,093 and 1,104 nucleotides and encode proteins of 302 and 274 amino acid residues, respectively. Both amino acid sequences showed high similarity to known legume lectins, and those of their amino acids involved in carbohydrate and metal binding were conserved.
Published: 2014
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35. Molecular cloning, functional expression, and characterization of isolectin genes of hemolytic lectin CEL-III from the marine invertebrate Cucumaria echinata.

Author: Shimizu Y, Yamazaki H, Yoshida S, Yonekura M, and Kouzuma Y
Subjects: Animals, Cucumaria genetics, DNA, Complementary genetics, Erythrocyte Membrane, Hemolysis, Hemolytic Agents, Humans, Invertebrates, Lectins physiology, Marine Biology, Recombinant Proteins biosynthesis, Cloning, Molecular, Cucumaria chemistry, Lectins genetics
Abstract: CEL-III is a hemolytic lectin purified from the marine invertebrate Cucumaria echinata. Previous research has indictated that CEL-III is composed of several isoforms. Here we identified five CEL-III isolectin genes, designated CEL-III-L1, CEL-III-L2, CEL-III-S1, CEL-III-S2, and CEL-III-LS1, by cDNA cloning. The deduced amino acid sequences suggested they shared 94.0-99.8% identical residues. Among the amino acid residues involved in carbohydrate binding, the His residue, which contributes to stacking with sugar, in subdomain 1α was replaced by Tyr in CEL-III-L2. The recombinant proteins were expressed in Escherichia coli or insect cells. rCEL-III-L2 showed higher hemolytic activity than those of the other isolectins. Furthermore, an apparent oligomer band of rCEL-III-L2 was detected on erythrocyte membranes, although the other isolectins showed smear bands. These results suggest that Tyr36 of CEL-III-L2 is important for the expression of hemolytic activity and oligomerization.
Published: 2012
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36. Indication of electron neutrino appearance from an accelerator-produced off-axis muon neutrino beam.

Author: Abe K, Abgrall N, Ajima Y, Aihara H, Albert JB, Andreopoulos C, Andrieu B, Aoki S, Araoka O, Argyriades J, Ariga A, Ariga T, Assylbekov S, Autiero D, Badertscher A, Barbi M, Barker GJ, Barr G, Bass M, Bay F, Bentham S, Berardi V, Berger BE, Bertram I, Besnier M, Beucher J, Beznosko D, Bhadra S, Blaszczyk Fd, Blondel A, Bojechko C, Bouchez J, Boyd SB, Bravar A, Bronner C, Brook-Roberge DG, Buchanan N, Budd H, Calvet D, Cartwright SL, Carver A, Castillo R, Catanesi MG, Cazes A, Cervera A, Chavez C, Choi S, Christodoulou G, Coleman J, Coleman W, Collazuol G, Connolly K, Curioni A, Dabrowska A, Danko I, Das R, Davies GS, Davis S, Day M, De Rosa G, de André JP, de Perio P, Delbart A, Densham C, Di Lodovico F, Di Luise S, Dinh Tran P, Dobson J, Dore U, Drapier O, Dufour F, Dumarchez J, Dytman S, Dziewiecki M, Dziomba M, Emery S, Ereditato A, Escudero L, Esposito LS, Fechner M, Ferrero A, Finch AJ, Frank E, Fujii Y, Fukuda Y, Galymov V, Gannaway FC, Gaudin A, Gendotti A, George MA, Giffin S, Giganti C, Gilje K, Golan T, Goldhaber M, Gomez-Cadenas JJ, Gonin M, Grant N, Grant A, Gumplinger P, Guzowski P, Haesler A, Haigh MD, Hamano K, Hansen C, Hansen D, Hara T, Harrison PF, Hartfiel B, Hartz M, Haruyama T, Hasegawa T, Hastings NC, Hastings S, Hatzikoutelis A, Hayashi K, Hayato Y, Hearty C, Helmer RL, Henderson R, Higashi N, Hignight J, Hirose E, Holeczek J, Horikawa S, Hyndman A, Ichikawa AK, Ieki K, Ieva M, Iida M, Ikeda M, Ilic J, Imber J, Ishida T, Ishihara C, Ishii T, Ives SJ, Iwasaki M, Iyogi K, Izmaylov A, Jamieson B, Johnson RA, Joo KK, Jover-Manas GV, Jung CK, Kaji H, Kajita T, Kakuno H, Kameda J, Kaneyuki K, Karlen D, Kasami K, Kato I, Kearns E, Khabibullin M, Khanam F, Khotjantsev A, Kielczewska D, Kikawa T, Kim J, Kim JY, Kim SB, Kimura N, Kirby B, Kisiel J, Kitching P, Kobayashi T, Kogan G, Koike S, Konaka A, Kormos LL, Korzenev A, Koseki K, Koshio Y, Kouzuma Y, Kowalik K, Kravtsov V, Kreslo I, Kropp W, Kubo H, Kudenko Y, Kulkarni N, Kurjata R, Kutter T, Lagoda J, Laihem K, Laveder M, Lee KP, Le PT, Levy JM, Licciardi C, Lim IT, Lindner T, Litchfield RP, Litos M, Longhin A, Lopez GD, Loverre PF, Ludovici L, Lux T, Macaire M, Mahn K, Makida Y, Malek M, Manly S, Marchionni A, Marino AD, Marteau J, Martin JF, Maruyama T, Maryon T, Marzec J, Masliah P, Mathie EL, Matsumura C, Matsuoka K, Matveev V, Mavrokoridis K, Mazzucato E, McCauley N, McFarland KS, McGrew C, McLachlan T, Messina M, Metcalf W, Metelko C, Mezzetto M, Mijakowski P, Miller CA, Minamino A, Mineev O, Mine S, Missert AD, Mituka G, Miura M, Mizouchi K, Monfregola L, Moreau F, Morgan B, Moriyama S, Muir A, Murakami A, Murdoch M, Murphy S, Myslik J, Nakadaira T, Nakahata M, Nakai T, Nakajima K, Nakamoto T, Nakamura K, Nakayama S, Nakaya T, Naples D, Navin ML, Nelson B, Nicholls TC, Nishikawa K, Nishino H, Nowak JA, Noy M, Obayashi Y, Ogitsu T, Ohhata H, Okamura T, Okumura K, Okusawa T, Oser SM, Otani M, Owen RA, Oyama Y, Ozaki T, Pac MY, Palladino V, Paolone V, Paul P, Payne D, Pearce GF, Perkin JD, Pettinacci V, Pierre F, Poplawska E, Popov B, Posiadala M, Poutissou JM, Poutissou R, Przewlocki P, Qian W, Raaf JL, Radicioni E, Ratoff PN, Raufer TM, Ravonel M, Raymond M, Retiere F, Robert A, Rodrigues PA, Rondio E, Roney JM, Rossi B, Roth S, Rubbia A, Ruterbories D, Sabouri S, Sacco R, Sakashita K, Sánchez F, Sarrat A, Sasaki K, Scholberg K, Schwehr J, Scott M, Scully DI, Seiya Y, Sekiguchi T, Sekiya H, Shibata M, Shimizu Y, Shiozawa M, Short S, Siyad M, Smith RJ, Smy M, Sobczyk JT, Sobel H, Sorel M, Stahl A, Stamoulis P, Steinmann J, Still B, Stone J, Strabel C, Sulak LR, Sulej R, Sutcliffe P, Suzuki A, Suzuki K, Suzuki S, Suzuki SY, Suzuki Y, Suzuki Y, Szeglowski T, Szeptycka M, Tacik R, Tada M, Takahashi S, Takeda A, Takenaga Y, Takeuchi Y, Tanaka K, Tanaka HA, Tanaka M, Tanaka MM, Tanimoto N, Tashiro K, Taylor I, Terashima A, Terhorst D, Terri R, Thompson LF, Thorley A, Toki W, Tomaru T, Totsuka Y, Touramanis C, Tsukamoto T, Tzanov M, Uchida Y, Ueno K, Vacheret A, Vagins M, Vasseur G, Wachala T, Walding JJ, Waldron AV, Walter CW, Wanderer PJ, Wang J, Ward MA, Ward GP, Wark D, Wascko MO, Weber A, Wendell R, West N, Whitehead LH, Wikström G, Wilkes RJ, Wilking MJ, Wilson JR, Wilson RJ, Wongjirad T, Yamada S, Yamada Y, Yamamoto A, Yamamoto K, Yamanoi Y, Yamaoka H, Yanagisawa C, Yano T, Yen S, Yershov N, Yokoyama M, Zalewska A, Zalipska J, Zambelli L, Zaremba K, Ziembicki M, Zimmerman ED, Zito M, and Żmuda J
Abstract: The T2K experiment observes indications of ν(μ) → ν(e) appearance in data accumulated with 1.43×10(20) protons on target. Six events pass all selection criteria at the far detector. In a three-flavor neutrino oscillation scenario with |Δm(23)(2)| = 2.4×10(-3) eV(2), sin(2)2θ(23) = 1 and sin(2)2θ(13) = 0, the expected number of such events is 1.5±0.3(syst). Under this hypothesis, the probability to observe six or more candidate events is 7×10(-3), equivalent to 2.5σ significance. At 90% C.L., the data are consistent with 0.03(0.04) < sin(2)2θ(13) < 0.28(0.34) for δ(CP) = 0 and a normal (inverted) hierarchy.
Published: 2011
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37. Molecular cloning of a multidomain cysteine protease and protease inhibitor precursor gene from the tobacco hornworm (Manduca sexta) and functional expression of the cathepsin F-like cysteine protease domain.

Author: Miyaji T, Murayama S, Kouzuma Y, Kimura N, Kanost MR, Kramer KJ, and Yonekura M
Subjects: Amino Acid Sequence, Animals, Base Sequence, Cathepsin F chemistry, Cathepsin F genetics, Cystatins chemistry, Cystatins metabolism, Cysteine Proteases chemistry, Cysteine Proteases metabolism, Cysteine Proteinase Inhibitors chemistry, Cysteine Proteinase Inhibitors metabolism, DNA, Complementary genetics, Genes, Insect, Hemolymph chemistry, Insect Proteins chemistry, Insect Proteins metabolism, Larva enzymology, Larva genetics, Manduca enzymology, Manduca metabolism, Molecular Sequence Data, Protein Precursors genetics, Cloning, Molecular, Cystatins genetics, Cysteine Proteases genetics, Cysteine Proteinase Inhibitors genetics, Insect Proteins genetics, Manduca genetics
Abstract: A Manduca sexta (tobacco hornworm) cysteine protease inhibitor, MsCPI, purified from larval hemolymph has an apparent molecular mass of 11.5 kDa, whereas the size of the mRNA is very large (∼9 kilobases). MsCPI cDNA consists of a 9,273 nucleotides that encode a polypeptide of 2,676 amino acids, which includes nine tandemly repeated MsCPI domains, four cystatin-like domains and one procathepsin F-like domain. The procathepsin F-like domain protein was expressed in Escherichia coli and processed to its active mature form by incubation with pepsin. The mature enzyme hydrolyzed Z-Leu-Arg-MCA, Z-Phe-Arg-MCA and Boc-Val-Leu-Lys-MCA rapidly, whereas hydrolysis of Suc-Leu-Tyr-MCA and Z-Arg-Arg-MCA was very slow. The protease was strongly inhibited by MsCPI, egg-white cystatin and sunflower cystatin with K(i) values in the nanomolar range. When the MsCPI tandem protein linked to two MsCPI domains was treated with proteases, it was degraded by the cathepsin F-like protease. However, tryptic digestion converted the MsCPI tandem protein to an active inhibitory form. These data support the hypothesis that the mature MsCPI protein is produced from the MsCPI precursor protein by trypsin-like proteases. The resulting mature MsCPI protein probably plays a role in the regulation of the activity of endogenous cysteine proteases., (Copyright © 2010 Elsevier Ltd. All rights reserved.)
Published: 2010
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38. Steady-state and time-resolved fluorescence spectroscopic studies on interaction of the N-terminal region with the hairpin loop of the phytocystatin Scb.

Author: Doi-Kawano K, Nishimoto E, Kouzuma Y, Takahashi D, Yamashita S, and Kimura M
Subjects: Cystatins isolation & purification, Helianthus chemistry, Peptides chemistry, Protein Conformation, Protein Structure, Tertiary, Seeds chemistry, Spectrometry, Fluorescence, Time Factors, Cystatins chemistry
Abstract: The steady-state and time-resolved fluorescence spectroscopy is one of the most powerful method to detect and analyze subtle conformation change and interaction between peptide elements in protein. Phytocystatin Scb isolated from sunflower seeds includes a single Trp residue at position 85. In an attempt to investigate the interaction of the N-terminal region of Scb with the first and second hairpin loops by fluorescence spectroscopy of Trp residue, two Scb mutants in which single Trp locates at position 52 and 58, respectively, and their N-terminal removed mutants were generated. The N-terminal truncation changed the fluorescence decay kinetics of Trp52 from the triple exponential to double. Furthermore, the time-resolved fluorescence anisotropy residue indicated that the segmental motion of Trp52 was significantly enhanced by its N-terminal truncation. In contrast, Trp58 and Trp85 had little influence. The N-terminal successive truncations of Scb and its mutants resulted in the weaken inhibitors to papain. These results suggested that the N-terminal region of Scb interacts with the peptide segment preceding the first hairpin loop, thereby stabilizing the conformation of the hairpin loop structure.
Published: 2009
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39. Comprehensive royal jelly (RJ) proteomics using one- and two-dimensional proteomics platforms reveals novel RJ proteins and potential phospho/glycoproteins.

Author: Furusawa T, Rakwal R, Nam HW, Shibato J, Agrawal GK, Kim YS, Ogawa Y, Yoshida Y, Kouzuma Y, Masuo Y, and Yonekura M
Subjects: Amino Acid Sequence, Animals, Bee Venoms analysis, Chromatography, Liquid, Electrophoresis, Gel, Two-Dimensional, Mass Spectrometry, Molecular Sequence Data, Bees, Fatty Acids analysis, Insect Proteins analysis, Proteome analysis
Abstract: Royal jelly (RJ) is an exclusive food for queen honey bee (Apis mellifera L.) that is synthesized and secreted by young worker bees. RJ is also widely used in medical products, cosmetics, and as health foods. However, little is known about RJ functionality and the total protein components, although recent research is attempting to unravel the RJ proteome. We have embarked on a detailed investigation of the RJ proteome, using a modified protein extraction protocol and two complementary proteomics approaches, one- and two-dimensional gel electrophoresis (1-DGE and 2-DGE) in conjunction with tandem mass spectrometry. Simultaneously, we examined total soluble protein from RJ collected at 24, 48, and 72 h after honey bee larvae deposition twice (in two flower blooming seasons), to check differences, if any, in RJ proteome therein. Both 1- and 2-D gels stained with silver nitrate revealed similar protein profiles among these three time points. However, we observed a clear difference in two bands (ca. MW of 55 and 75 kDa) on 1-D gel between the first and the second collection of RJ. A similar difference was also observed in the 2-D gel. Except for this difference, the protein profiles were similar at the 3 time points. As the RJ from 48 (or sometimes 72) is commercially used, we selected the RJ sample at 48 h for detailed analysis with the first collection. 1-DGE identified 90 and 15 proteins from the first and second selection, respectively; in total, 47 nonredundant proteins were identified. 2-DGE identified 105 proteins comprising 14 nonredundant proteins. In total, 52 nonredundant proteins were identified in this study, and other than the major royal jelly protein family and some other previously identified proteins, 42 novel proteins were identified. Furthermore, we also report potentially post-translationally modified (phosphorylation and glycosylation) RJ proteins based on the Pro-Q diamond/emerald phosphoprotein/glycoprotein gel stains; MRJP 2p and 7p were suggested as potential phosphoproteins. The 2-DGE data were integrated to develop a 2-D gel reference map, and all data are accessible through RJ proteomics portal (http://foodfunc.agr.ibaraki.ac.jp/RJP.html).
Published: 2008
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40. Proteomics of two cultivated mushrooms Sparassis crispa and Hericium erinaceum provides insight into their numerous functional protein components and diversity.

Author: Horie K, Rakwal R, Hirano M, Shibato J, Nam HW, Kim YS, Kouzuma Y, Agrawal GK, Masuo Y, and Yonekura M
Subjects: Agaricales genetics, Amino Acid Sequence, Electrophoresis, Polyacrylamide Gel methods, Fungal Proteins classification, Fungal Proteins genetics, Humans, Molecular Sequence Data, Proteome analysis, Proteome genetics, Agaricales chemistry, Fungal Proteins analysis, Proteomics methods
Abstract: Mushroom can be defined as a macrofungus with a distinctive fruiting body. Mushrooms of class Basidiomycete are primarily wood degradation fungi, but serve as food and a part of traditional medicine used by humans. Although their life cycle is fairly well-established, the information on the molecular components, especially proteins are very limited. Here, we report proteomics analysis of two edible mushrooms (fruiting bodies) Sparassis crispa and Hericium erinaceum using one- and two-dimensional gel electrophoresis (1-DGE and 2-DGE) based complementary proteomics approaches. 1-DGE coupled with liquid chromatography and mass spectrometry identified 77 (60 nonredundant proteins) and 121 (88 nonredundant proteins) proteins from S. crispa and H. erinaceum, respectively. 2-DGE analysis revealed 480 and 570 protein spots stained with colloidal coomassie brilliant blue in S. crispa and H. erinaceum, respectively. Of the 71 and 115 selected protein spots from S. crispa and H. erinaceum 2D gel blots on polyvinyldifluoride (PVDF) membranes, respectively, 29 and 35 nonredundant proteins were identified by N-terminal amino acid sequencing. Identified nonredundant proteins from 1- or 2-DGE belonged to 19 functional categories. Twenty-one proteins were found common in both S. crispa and H. erinaceum proteomes, including 14-3-3 protein and septin. Together this study provides evidence for the presence of a large number of functionally diverse proteins, expressed in the fruiting body of two economically important mushrooms, S. crispa and H. erinaceum. Data obtained from 1-DGE and 2-DGE analyses is accessible through the mushroom proteomics portal http://foodfunc.agr.ibaraki.ac.jp/mushprot.html.
Published: 2008
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41. Systematic investigation of the hemolymph proteome of Manduca sexta at the fifth instar larvae stage using one- and two-dimensional proteomics platforms.

Author: Furusawa T, Rakwal R, Nam HW, Hirano M, Shibato J, Kim YS, Ogawa Y, Yoshida Y, Kramer KJ, Kouzuma Y, Agrawal GK, and Yonekura M
Subjects: Amino Acid Sequence, Animals, Manduca growth & development, Molecular Sequence Data, Tandem Mass Spectrometry, Electrophoresis, Gel, Two-Dimensional methods, Electrophoresis, Polyacrylamide Gel methods, Hemolymph metabolism, Larva metabolism, Manduca metabolism, Proteome, Proteomics
Abstract: Manduca sexta is an excellent insect model for studying insect physiology, including hemolymph proteins. Larvae stages of this insect are highly damaging to tobacco leaves causing a drastic decrease in crop yield. Investigation on the larval biology should help in controlling its destructive potential, thus increasing crop yields. The hemolymph is the source of its immunity to disease and environmental factors, which invariably involves protein components. To better understand the physiology of M. sexta and the protein components expressed during its life cycle, two complementary proteomics approaches, one- and two-dimensional gel electrophoresis (1-DGE and 2-DGE) in conjunction with N-terminal amino acid sequencing and liquid chromatography-mass spectrometry, were employed to analyze the fifth instar larvae hemolymph proteins. These proteomics approaches together identified 123 proteins, which constituted a total of 58 nonredundant proteins and belonged to 10 functional categories. Defense (49%), transport and metabolism (15%), storage (9%), and metamorphosis (7%) categories were highly represented accounting for 80% of the identified proteins. Besides identification of previously reported proteins, 18 novel proteins were identified, which include the lipoprotein-releasing system transmembrane protein lolC, 50S ribosomal protein L24, inducible serine protease inhibitor 1, imaginal disk growth factor, protein disulfide-isomerase-like protein ERp57, etc. The 2-DGE data were integrated to develop a 2-D gel reference map. Data obtained from 1-DGE and 2-DGE analyses are accessible through the M. sexta proteomics portal ( http://foodfunc.agr.ibaraki.ac.jp/mansehemoprot.html). Together, this study provides evidence for the presence of a large number of functionally diverse protein families in the hemolymph of M. sexta. These proteins correlate well with the fifth instar stage, the transition from larvae to pupae.
Published: 2008
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42. Purification, characterization, and cDNA cloning of a Bowman-Birk type trypsin inhibitor from Apios americana Medikus tubers.

Author: Zhang Y, Kouzuma Y, Miyaji T, and Yonekura M
Subjects: Amino Acid Sequence, Base Sequence, Chromatography, Chromatography, Gel, Cloning, Molecular, DNA Primers, Drug Stability, Fabaceae chemistry, Molecular Sequence Data, Molecular Weight, Protease Inhibitors chemistry, Protease Inhibitors isolation & purification, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization, Thermodynamics, Trypsin Inhibitor, Bowman-Birk Soybean isolation & purification, Fabaceae genetics, Trypsin Inhibitor, Bowman-Birk Soybean chemistry, Trypsin Inhibitor, Bowman-Birk Soybean genetics
Abstract: An Apios americana trypsin inhibitor, AATI, was purified from Apios tubers by chromatography on DEAE Cellulofine A-500 and Sephadex G-50. The molecular mass of AATI was determined to be 6,437 Da by matrix-assisted laser desorption and ionization time-of-flight mass spectrometer (MALDI-TOF-MS). It showed strong inhibitory activity toward serine proteases, and the inhibition constants toward trypsin and chymotrypsin were 3.0 x 10(-9) M and 1.0 x 10(-6) M respectively. The inhibitory activity was not affected by heating at 80 degrees C for 2 h or by incubation at a wide range of pH values, suggesting that AATI has remarkable heat-stability and pH-stability. AATI cDNA consists of 552 nucleotides, and includes an open reading frame encoding a protein of 116 amino acids. The results of N-terminal amino acid sequencing of AATI and MALDI-TOF-MS analysis suggested that the deduced amino acid sequence had 50 and seven extra amino acids at the N- and C-termini respectively. Thus the mature AATI protein consists of 59 amino acid residues. Comparison of the amino acid sequence with those of the trypsin inhibitors from plants suggests that AATI belongs to the Bowman-Birk family and that it contains two possible reactive sites toward trypsin at Lys62 and Arg88.
Published: 2008
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43. C-type lectin-like carbohydrate recognition of the hemolytic lectin CEL-III containing ricin-type -trefoil folds.

Author: Hatakeyama T, Unno H, Kouzuma Y, Uchida T, Eto S, Hidemura H, Kato N, Yonekura M, and Kusunoki M
Subjects: Amino Acid Sequence, Animals, Binding Sites, Cell Membrane metabolism, Crystallography, X-Ray methods, Ions, Molecular Conformation, Molecular Sequence Data, Protein Binding, Protein Folding, Sequence Homology, Amino Acid, Carbohydrates chemistry, Cucumaria metabolism, Lectins chemistry, Ricin chemistry
Abstract: CEL-III is a Ca(2+)-dependent hemolytic lectin, isolated from the marine invertebrate Cucumaria echinata. The three-dimensional structure of CEL-III/GalNAc and CEL-III/methyl alpha-galactoside complexes was solved by x-ray crystallographic analysis. In these complexes, five carbohydrate molecules were found to be bound to two carbohydrate-binding domains (domains 1 and 2) located in the N-terminal 2/3 portion of the polypeptide and that contained beta-trefoil folds similar to ricin B-chain. The 3-OH and 4-OH of bound carbohydrate molecules were coordinated with Ca(2+) located at the subdomains 1alpha, 1gamma, 2alpha, 2beta, and 2gamma, simultaneously forming hydrogen bond networks with nearby amino acid side chains, which is similar to carbohydrate binding in C-type lectins. The binding of carbohydrates was further stabilized by aromatic amino acid residues, such as tyrosine and tryptophan, through a stacking interaction with the hydrophobic face of carbohydrates. The importance of amino acid residues in the carbohydrate-binding sites was confirmed by the mutational analyses. The orientation of bound GalNAc and methyl alpha-galactoside was similar to the galactose moiety of lactose bound to the carbohydrate-binding site of the ricin B-chain, although the ricin B-chain does not require Ca(2+) ions for carbohydrate binding. The binding of the carbohydrates induced local structural changes in carbohydrate-binding sites in subdomains 2alpha and 2beta. Binding of GalNAc also induced a slight change in the main chain structure of domain 3, which could be related to the conformational change upon binding of specific carbohydrates to induce oligomerization of the protein.
Published: 2007
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44. Hemolytic C-type lectin CEL-III from sea cucumber expressed in transgenic mosquitoes impairs malaria parasite development.

Author: Yoshida S, Shimada Y, Kondoh D, Kouzuma Y, Ghosh AK, Jacobs-Lorena M, and Sinden RE
Subjects: Animals, Cloning, Molecular, Cucumaria chemistry, Digestive System, Dose-Response Relationship, Drug, Erythrocytes metabolism, Erythrocytes parasitology, Female, Gene Expression, Hemolysis, Host-Parasite Interactions, Humans, In Vitro Techniques, Lectins genetics, Lectins metabolism, Malaria, Male, Mice, Mice, Inbred BALB C, Organisms, Genetically Modified, Plasmodium berghei metabolism, Plasmodium berghei pathogenicity, Plasmodium falciparum pathogenicity, Rats, Rats, Inbred BN, Anopheles genetics, Anopheles metabolism, Anopheles parasitology, Cucumaria metabolism, Hemolytic Agents metabolism, Insect Vectors genetics, Insect Vectors metabolism, Insect Vectors parasitology, Lectins pharmacology, Plasmodium berghei drug effects
Abstract: The midgut environment of anopheline mosquitoes plays an important role in the development of the malaria parasite. Using genetic manipulation of anopheline mosquitoes to change the environment in the mosquito midgut may inhibit development of the malaria parasite, thus blocking malaria transmission. Here we generate transgenic Anopheles stephensi mosquitoes that express the C-type lectin CEL-III from the sea cucumber, Cucumaria echinata, in a midgut-specific manner. CEL-III has strong and rapid hemolytic activity toward human and rat erythrocytes in the presence of serum. Importantly, CEL-III binds to ookinetes, leading to strong inhibition of ookinete formation in vitro with an IC(50) of 15 nM. Thus, CEL-III exhibits not only hemolytic activity but also cytotoxicity toward ookinetes. In these transgenic mosquitoes, sporogonic development of Plasmodium berghei is severely impaired. Moderate, but significant inhibition was found against Plasmodium falciparum. To our knowledge, this is the first demonstration of stably engineered anophelines that affect the Plasmodium transmission dynamics of human malaria. Although our laboratory-based research does not have immediate applications to block natural malaria transmission, these findings have significant implications for the generation of refractory mosquitoes to all species of human Plasmodium and elucidation of mosquito-parasite interactions.
Published: 2007
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45. Purification of a cysteine protease inhibitor from larval hemolymph of the tobacco hornworm (Manduca sexta) and functional expression of the recombinant protein.

Author: Miyaji T, Kouzuma Y, Yaguchi J, Matsumoto R, Kanost MR, Kramer KJ, and Yonekura M
Subjects: Amino Acid Sequence, Animals, Cathepsins drug effects, Cathepsins isolation & purification, Cathepsins metabolism, Cloning, Molecular, Conserved Sequence, Cysteine Proteinase Inhibitors genetics, Cysteine Proteinase Inhibitors pharmacology, DNA Primers, Escherichia coli genetics, Humans, Larva, Molecular Sequence Data, Papain antagonists & inhibitors, Polymerase Chain Reaction, Recombinant Proteins isolation & purification, Recombinant Proteins pharmacology, Sequence Alignment, Sequence Homology, Amino Acid, Cysteine Proteinase Inhibitors isolation & purification, Hemolymph chemistry, Manduca growth & development
Abstract: A cysteine protease inhibitor (CPI) with an apparent molecular mass of 11.5kDa was purified from larval hemolymph of the tobacco hornworm (Manduca sexta) by gel filtration on Sephadex G-50 followed by hydrophobic and ion-exchange column chromatographies. The purified cysteine proteinase inhibitor, denoted as MsCPI, strongly inhibited the plant cysteine protease, papain, with a K(i) value of 5.5 x 10(-9)M. Nucleotide sequence analysis of a partial cDNA encoding MsCPI indicated that MsCPI consists of 105 amino acid residues in a sequence that is similar to sarcocystatin A from Sarcophaga peregrina. However, northern blotting and PCR analyses using the specific primers of MsCPI suggested that the mRNA encoding MsCPI had a size of more than 12 kilobases, which included at least six tandemly repeated MsCPI segments. MsCPI was expressed in Escherichia coli and the recombinant protein effectively inhibited cysteine proteases from plants as well as from animals such as cathepsins B (K(i), 6.8 nM), H (3.0 nM), and L (0.87 nM). There was no inhibition exhibited toward trypsin, chymotrypsin, subtilisin, pepsin or themolysin.
Published: 2007
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46. Contribution of conserved Asn residues to the inhibitory activities of Kunitz-type protease inhibitors from plants.

Author: Iwanaga S, Yamasaki N, Kimura M, and Kouzuma Y
Subjects: Amino Acid Sequence, Asparagine, Erythrina chemistry, Escherichia coli, Molecular Sequence Data, Mutagenesis, Site-Directed, Organisms, Genetically Modified, Protein Conformation, Conserved Sequence genetics, Erythrina genetics, Peptides chemistry, Plant Proteins chemistry, Protease Inhibitors chemistry
Abstract: Plant Kunitz-type protease inhibitors contain a conserved Asn residue in the N-terminal region. To investigate the role of Asn residue in protease inhibitory activities, Erythrina variegata trypsin inhibitor a (ETIa), E. variegata chymotrypsin inhibitor (ECI), and their mutants, ETIa-N12A and ECI-N13A, were used. Both mutants exhibit weaker inhibitory activities toward their cognate proteases than the wild-type proteins and were readily cleaved at reactive sites. Furthermore, kinetic analysis of the interactions of the mutated proteins with their cognate proteases by surface plasmon resonance (SPR) measurement indicated that replacements of the Asn residue mainly affected dissociation rate constants. The conserved Asn residues of Kunitz-type inhibitors play an important role in exhibiting effective inhibitory activity by stabilizing the structures of the primary binding loop and protease-inhibitor complex.
Published: 2005
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47. Genomic cloning of ribonucleases in Nicotiana glutinosa leaves, as induced in response to wounding or to TMV-infection, and characterization of their promoters.

Author: Hayashi T, Kobayashi D, Kariu T, Tahara M, Hada K, Kouzuma Y, and Kimura M
Subjects: Base Sequence, Cloning, Molecular, Databases, Genetic, Electrophoretic Mobility Shift Assay, Genes, Reporter, Molecular Sequence Data, Plant Leaves genetics, Plant Leaves virology, Promoter Regions, Genetic genetics, Ribonucleases genetics, Nicotiana genetics, Nicotiana virology, Tobacco Mosaic Virus metabolism, Wounds and Injuries, Gene Expression Regulation, Plant physiology, Genes, Plant, Plant Leaves metabolism, Ribonucleases metabolism, Nicotiana metabolism
Abstract: We previously cloned two distinct cDNA clones, NGR1 and NGR3, encoding S-like ribonucleases (RNases) induced by wounding and tobacco mosaic virus (TMV) infection, respectively, in Nicotiana glutinosa leaves. To gain insight into the regulatory mechanism of the RNase genes, we analyzed nucleotide sequences of the genes ngr1 (4.1 kbp) and ngr3 (5.3 kbp), containing their structural genes as well as 5'-flanking regions. The ngr1 gene is organized in three exons with two intervening introns, and ngr3 has four exons interrupted by three introns. Primer extension analyses localized single transcription initiation sites at -32 and -99 upstream of the translation initiation codons ATG in the genes ngr1 and ngr3, respectively. The beta-glucuronidase (GUS) reporter gene analysis with serial 5'-deletion mutants as well as a gel shift assay defined the wound-responsive region at residues -509 to -288 in gene ngr1 and a TMV-responsive region at the residues -401 to -174 in ngr3, respectively. Sequence search using PLACE and PlantCARE data bases showed that a wound-responsive element: the WUN-motif, occurs within the wound-responsive region in ngr1, while ngr3 contains several potential cis-regulating elements, such as the elicitor responsiveness element: the W-box, a TMV responsive element: GT1, and the WUN-motif at positions between -401 and -174. These findings suggested that some of these cis-elements may be involved in inducible expressions of ngr1 and ngr3. Furthermore, the gel shift assay suggested that the dissociation of protein factor(s) upon TMV-infection from the regulatory region may cause an inducible expression of ngr3.
Published: 2003
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48. Reconstitution of archaeal ribonuclease P from RNA and four protein components.

Author: Kouzuma Y, Mizoguchi M, Takagi H, Fukuhara H, Tsukamoto M, Numata T, and Kimura M
Subjects: Animals, Archaeal Proteins chemistry, Archaeal Proteins genetics, Base Sequence, Endoribonucleases chemistry, Endoribonucleases genetics, Endoribonucleases isolation & purification, Humans, Molecular Sequence Data, Nucleic Acid Conformation, Protein Binding, Protein Subunits genetics, Protein Subunits metabolism, RNA, Archaeal chemistry, RNA, Archaeal metabolism, RNA, Catalytic chemistry, RNA, Catalytic genetics, RNA, Catalytic isolation & purification, RNA, Transfer, Tyr chemistry, RNA, Transfer, Tyr metabolism, Recombinant Proteins chemistry, Recombinant Proteins genetics, Recombinant Proteins metabolism, Ribonuclease P, Ribonucleoproteins genetics, Ribonucleoproteins isolation & purification, Ribonucleoproteins metabolism, Archaeal Proteins metabolism, Endoribonucleases metabolism, Escherichia coli Proteins, Pyrococcus enzymology, Pyrococcus genetics, RNA, Catalytic metabolism
Abstract: Ribonuclease P (RNase P) is an endonuclease responsible for generating the 5(') end of matured tRNA molecules. A homology search of the hyperthermophilic archaeon Pyrococcus horikoshii OT3 genome database revealed that the four genes, PH1481, PH1601, PH1771, and PH1877, have a significant homology to those encoding RNase P protein subunits, hpop5, Rpp21, Rpp29, and Rpp30, of human, respectively. These genes were expressed in Escherichia coli cells, and the resulting proteins Ph1481p, Ph1601p, Ph1771p, and Ph1877p were purified to apparent homogeneity in a set of column chromatographies. The four proteins were characterized in terms of their capability to bind the cognate RNase P RNA from P. horikoshii. All four proteins exhibited the binding activity to the RNase P RNA. In vitro reconstitution of four putative RNase P proteins with the in vitro transcripted P. horikoshii RNase P RNA revealed that three proteins Ph1481p, Ph1601p, and Ph1771p, and RNase P RNA are minimal components for the RNase P activity. However, addition of the fourth protein Ph1877p strongly stimulated enzymatic activity, indicating that all four proteins and RNase P RNA are essential for optimal RNase P activity. The present data will pave the way for the elucidation of the reaction mechanism for archaeal as well as eukaryotic RNase P.
Published: 2003
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49. Requirement for C-terminal extension to the RNA binding domain for efficient RNA binding by ribosomal protein L2.

Author: Hayashi T, Tahara M, Iwasaki K, Kouzuma Y, and Kimura M
Subjects: Geobacillus stearothermophilus metabolism, Kinetics, Mutation genetics, RNA, Ribosomal genetics, Ribosomal Proteins genetics, Surface Plasmon Resonance, RNA, Ribosomal metabolism, Ribosomal Proteins metabolism
Abstract: Ribosomal protein L2 is a primary 23S rRNA binding protein in the large ribosomal subunit. We examined the contribution of the N- and C-terminal regions of Bacillus stearothermophilus L2 (BstL2) to the 23S rRNA binding activity. The mutant desN, in which the N-terminal 59 residues of BstL2 were deleted, bound to the 23S rRNA fragment to the same extent as wild type BstL2, but the mutation desC, in which the C-terminal 74 amino acid residues were deleted, abolished the binding activity. These observations indicated that the C-terminal region is involved in 23S rRNA binding. Subsequent deletion analysis of the C-terminal region found that the C-terminal 70 amino acids are required for efficient 23S rRNA binding by BstL2. Furthermore, the surface plasmon resonance analysis indicated that successive truncations of the C-terminal residues increased the dissociation rate constants, while they had little influence on association rate constants. The result indicated that reduced affinities of the C-terminal deletion mutants were due only to higher dissociation rate constants, suggesting that the C-terminal region primarily functions by stabilizing the protein L2-23S rRNA complex.
Published: 2002
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50. On the interaction of ribosomal protein L5 with 5S rRNA.

Author: Iwasaki K, Kikukawa S, Kawamura S, Kouzuma Y, Tanaka I, and Kimura M
Subjects: Amino Acid Sequence, Binding Sites, Geobacillus stearothermophilus genetics, Molecular Sequence Data, Mutagenesis, Site-Directed, Protein Structure, Tertiary, Ribosomal Proteins chemistry, Ribosomal Proteins genetics, Sequence Homology, Amino Acid, Surface Plasmon Resonance, Geobacillus stearothermophilus metabolism, RNA, Ribosomal, 5S metabolism, Ribosomal Proteins metabolism
Abstract: Ribosomal protein L5, a 5S rRNA binding protein in the large subunit, is composed of a five-stranded antiparallel beta-sheet and four alpha-helices, and folds in a way that is topologically similar to the ribonucleprotein (RNP) domain [Nakashima et al., RNA 7, 692-701, 20011. The crystal structure of ribosomal protein L5 (BstL5) from Bacillus stearothermophilus suggests that a concave surface formed by an anti-parallel beta-sheet and long loop structures are strongly involved in 5S rRNA binding. To identify amino acid residues responsible for 5S rRNA binding, we made use of Ala-scanning mutagenesis of evolutionarily conserved amino acids occurred at beta-strands and loop structures in BstL5. The mutation of Lys33 at the beta 1-strand caused a significant reduction in 5S rRNA binding. In addition, the Arg92, Phe122, and Glu134 mutations on the beta2-strand, the alpha3-beta4 loop, and the beta4-beta5 loop, respectively, resulted in a moderate decrease in the 5S rRNA binding affinity. In contrast, mutation of the conserved residue Pro65 at the beta2-strand had little effect on the 5S rRNA binding activity. These results, taken together with previous results, identified Lys33, Asn37, Gln63, and Thr90 on the beta-sheet structure, and Phe77 at the beta2-beta3 loop as critical residues for the 5S rRNA binding. The contribution of these amino acids to 5S rRNA binding was further quantitatively evaluated by surface plasmon resonance (SPR) analysis by the use of BIAcore. The results showed that the amino acids on the beta-sheet structure are required to decrease the dissociation rate constant for the BstL5-5S rRNA complex, while those on the loops are to increase the association rate constant for the BstL5-5S rRNA interaction.
Published: 2002
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