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2. High Energy Physics Opportunities Using Reactor Antineutrinos

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Awe, C., Barbeau, P. S., Haghighat, A., Huber, P., Li, S. C., Link, J. M., Mascolino, V., Subedi, T., Walkup, K., Aguilar-Arevalo, A., Bertou, X., Bonifazi, C., Cancelo, G., Cervantes-Vergara, B. A., Chavez, C., D Olivo, J. C., Egea, J. M., Dos Anjos, J. C., Estrada, J., Neto, A. R. F., Fernandez-Moroni, G., Foguel, A., Ford, R., Gasanego, J., Gollo, V., Izraelevitch, F., Kilminster, B., Lima, Jr H. P., Makler, M., Mendes, L. H., Molina, J., Mota, P., Nasteva, I., Paolini, E., Romero, C., Sarkis, Y., Haro, M. S., Soto, A., Stalder, D., Tiffenberg, J., Torres, C., Lindner, M., An, F. P., Balantekin, A. B., Band, H. R., Bishai, M., Blyth, S., Cao, G. F., Cao, J., Chang, J. F., Chang, Y., Chen, H. S., Chen, S. M., Chen, Y., Chen, Y. X., Cheng, J., Cheng, Z. K., Cherwinka, J. J., Chu, M. C., Cummings, J. P., Dalager, O., Deng, F. S., Ding, Y. Y., Diwan, M. V., Dohnal, T., Dove, J., Dvořák, M., Dwyer, D. A., Gallo, J. P., Gonchar, M., Gong, G. H., Gong, H., Gu, W. Q., Guo, J. Y., Guo, L., Guo, X. H., Guo, Y. H., Guo, Z., Hackenburg, R. W., Hans, S., He, M., Heeger, K. M., Heng, Y. K., Higuera, A., Hor, Y. K., Hsiung, Y. B., Hu, B. Z., Hu, J. R., Hu, T., Hu, Z. J., Huang, H. X., Huang, X. T., Jaffe, D. E., Jen, K. L., Ji, X. L., Ji, X. P., Johnson, R. A., Jones, D., Kang, L., Kettell, S. H., Kohn, S., Kramer, M., Langford, T. J., Lee, J., Lee, J. H. C., Lei, R. T., Leitner, R., Leung, J. K. C., Li, F., Li, H. L., Li, J. J., Li, Q. J., Li, S., Li, W. D., Li, X. N., Li, X. Q., Li, Y. F., Li, Z. B., Liang, H., Lin, C. J., Lin, G. L., Lin, S., Ling, J. J., Littenberg, L., Littlejohn, B. R., Liu, J. C., Liu, J. L., Lu, C., Lu, H. Q., Lu, J. S., Luk, K. B., Ma, X. B., Ma, X. Y., Ma, Y. Q., Mandujano, R. C., Marshall, C., Martinez Caicedo, D. A., Mcdonald, K. T., Mckeown, R. D., Meng, Y., Napolitano, J., Naumov, D., Naumova, E., Ochoa-Ricoux, J. P., Olshevskiy, A., Pan, H. -R, Park, J., Patton, S., Peng, J. C., Pun, C. S. J., Qi, F. Z., Qi, M., Qian, X., Raper, N., Ren, J., Reveco, C. Morales, Rosero, R., Roskovec, B., Ruan, X. C., Steiner, H., Sun, J. L., Tmej, T., Treskov, K., Tse, W. -H, Tull, C. E., Viren, B., Vorobel, V., Wang, C. H., Wang, J., Wang, M., Wang, N. Y., Wang, R. G., Wang, W., Wang, X., Wang, Y., Wang, Y. F., Wang, Z., Wang, Z. M., Wei, H. Y., Wei, L. H., Wen, L. J., Whisnant, K., White, C. G., Wong, H. L. H., Worcester, E., Wu, D. R., Wu, F. L., Wu, Q., Wenjie Wu, Xia, D. M., Xie, Z. Q., Xing, Z. Z., Xu, J. L., Xu, T., Xue, T., Yang, C. G., Yang, L., Yang, Y. Z., Yao, H. F., Ye, M., Yeh, M., Young, B. L., Yu, H. Z., Yu, Z. Y., Yue, B. B., Zeng, S., Zeng, Y., Zhan, L., Zhang, C., Zhang, F. Y., Zhang, H. H., Zhang, J. W., Zhang, Q. M., Zhang, X. T., Zhang, Y. M., Zhang, Y. X., Zhang, Y. Y., Zhang, Z. J., Zhang, Z. P., Zhang, Z. Y., Zhao, J., Zhou, L., Zhuang, H. L., Zou, J. H., Abusleme, A., Adam, T., Ahmad, S., Ahmed, R., Aiello, S., An, G. P., An, Q., Andronico, G., Anfimov, N., Antonelli, V., Antoshkina, T., Asavapibhop, B., André, J. P. A. M., Auguste, D., Babic, A., Baldini, W., Barresi, A., Baussan, E., Bellato, M., Bergnoli, A., Bernieri, E., Birkenfeld, T., Blin, S., Blum, D., Bolshakova, A., Bongrand, M., Bordereau, C., Breton, D., Brigatti, A., Brugnera, R., Bruno, R., Budano, A., Buesken, M., Buscemi, M., Busto, Jose, Butorov, I., Cabrera, A., Cai, H., Cai, X., Cai, Y. K., Cai, Z. Y., Cammi, A., Campeny, A., Cao, C. Y., Caruso, R., Cerna, C., Chakaberia, I., Chen, P. P., Chen, P. A., Chen, S., Chen, X., Chen, Y. W., Chen, Z., Cheng, Y., Chiesa, D., Chimenti, P., Chukanov, A., Chuvashova, A., Claverie, G., Clementi, C., Clerbaux, B., Di Lorenzo, S., Corti, D., Costa, S., Corso, F. D., La Taille, C., Deng, J., Deng, Z., Deng, Z. Y., Depnering, W., Diaz, M., Ding, X. F., Dirgantara, B., Dmitrievsky, S., Donchenko, G., Dong, J. M., Dornic, D., Doroshkevich, E., Dracos, M., Druillole, F., Du, S. X., Dusini, S., Dvorak, M., Enqvist, T., Enzmann, H., Fabbri, A., Fajt, L., Fan, D. H., Fan, L., Fang, C., Fang, J., Fang, W. X., Fargetta, M., Fatkina, A., Fedoseev, D., Fekete, V., Feng, L. C., Feng, Q. C., Formozov, A., Fournier, A., Gan, H. N., Gao, F., Garfagnini, A., Göttel, A., Genster, C., Giammarchi, M., Giaz, A., Giudice, N., Gong, G., Gorchakov, O., Gornushkin, Y., Grassi, M., Grewing, C., Gromov, V., Gu, M., Gu, X., Gu, Y., Guan, M. Y., Guardone, N., Gul, M., Guo, C., Guo, W. L., Hackspacher, P., Hagner, C., Han, R., Han, Y., Hassan, M., He, W., Heinz, T., Hellmuth, P., Herrera, R., Hong, D. J., Hou, S. J., Hsiung, Y., Hu, H., Hu, J., Hu, S. Y., Huang, C. H., Huang, G. H., Huang, Q. H., Huang, W. H., Huang, X., Huang, Y. B., Hui, J. Q., Huo, L., Huo, W., Huss, C., Hussain, S., Insolia, A., Ioannisian, A., Isocrate, R., Ji, X. Z., Jia, H. H., Jia, J. J., Jian, S. Y., Jiang, D., Jiang, X. S., Jin, R. Y., Jing, X. P., Jollet, C., Joutsenvaara, J., Jungthawan, S., Kalousis, L., Kampmann, P., Karagounis, M., Kazarian, N., Khan, A., Khan, W., Khosonthongkee, K., Kinz, P., Korablev, D., Kouzakov, K., Krasnoperov, A., Krumshteyn, Z., Kruth, A., Kutovskiy, N., Kuusiniemi, P., Lachenmaier, T., Landini, C., Leblanc, S., Lebrin, V., Lefevre, F., Lei, R., Leung, J., Li, C., Li, D., Li, H., Li, J., Li, K. J., Li, M. Z., Li, M., Li, N., Li, R. H., Li, S. F., Li, S. J., Li, T., Li, W. G., Li, X. M., Li, X. L., Li, Y., Li, Z., Li, Z. Y., Liang, J. J., Liebau, D., Limphirat, A., Limpijumnong, S., Lin, S. X., Lin, T., Lippi, I., Liu, F., Liu, H. D., Liu, H. B., Liu, H. J., Liu, H. T., Liu, H., Liu, M., Liu, Q., Liu, R. X., Liu, S. Y., Liu, S. B., Liu, S. L., Liu, X. W., Liu, X., Liu, Y., Lokhov, A., Lombardi, P., Lombardo, C., Loo, K., Lu, J. B., Lu, J. G., Lu, S. X., Lu, X. X., Lubsandorzhiev, B., Lubsandorzhiev, S., Ludhova, L., Luo, F. J., Luo, G., Luo, P. W., Luo, S., Luo, W. M., Lyashuk, V., Ma, Q. M., Ma, S., Maalmi, J., Malyshkin, Y., Mantovani, F., Manzali, F., Mao, X., Mao, Y. J., Mari, S. M., Marini, F., Marium, S., Martellini, C., Martin-Chassard, G., Martini, A., Mayilyan, D., Müller, A., Mednieks, I., Meregaglia, A., Meroni, E., Meyhöfer, D., Mezzetto, M., Miller, J., Miramonti, L., Monforte, S., Montini, P., Montuschi, M., Morozov, N., Muhammad, A., Muralidharan, P., Nastasi, M., Naumov, D. V., Nemchenok, I., Ning, F. P., Ning, Z., Nunokawa, H., Oberauer, L., Orestano, D., Ortica, F., Pan, H. R., Paoloni, A., Parkalian, N., Parmeggiano, S., Payupol, T., Pei, Y., Pelliccia, N., Peng, A., Peng, H., Perrot, F., Petitjean, P. A., Petrucci, F., Piñeres Rico, L. F., Pilarczyk, O., Popov, A., Poussot, P., Pratumwan, W., Previtali, E., Qi, F., Qian, S., Qian, X. H., Qiao, H., Qin, Z. H., Qiu, S. K., Rajput, M., Ranucci, G., Re, A., Rebber, H., Rebii, A., Ren, B., Rezinko, T., Ricci, B., Robens, M., Roche, M., Rodphai, N., Romani, A., Roth, C., Ruan, X., Rujirawat, S., Rybnikov, A., Sadovsky, A., Saggese, P., Salamanna, G., Sanfilippo, S., Sangka, A., Sanguansak, N., Sawangwit, U., Sawatzki, J., Sawy, F., Schever, M., Schuler, J., Schwab, C., Schweizer, K., Selivanov, D., Selyunin, A., Serafini, A., Settanta, G., Settimo, M., Shao, Z., Sharov, V., Shi, J., Shutov, V., Sidorenkov, A., Simkovic, F., Sirignano, C., Siripak, J., Sisti, M., Slupecki, M., Smirnov, M., Smirnov, O., Sogo-Bezerra, T., Songwadhana, J., Soonthornthum, B., Sotnikov, A., Sramek, O., Sreethawong, W., Stahl, A., Stanco, L., Stankevich, K., Stefanik, D., Steiger, H., Steinmann, J., Sterr, T., Stock, M. R., Strati, V., Studenikin, A., Sun, G. X., Sun, S. F., Sun, X. L., Sun, Y. J., Sun, Y. Z., Suwonjandee, N., Szelezniak, M., Tang, J., Tang, Q., Tang, X., Tietzsch, A., Tkachev, I., Triossi, A., Troni, G., Trzaska, W., Tuve, C., Ushakov, N., Waasen, S., Boom, J. Vanden, Vanroyen, G., Vassilopoulos, N., Vedin, V., Verde, G., Vialkov, M., Viaud, B., Volpe, C., Voronin, D., Votano, L., Walker, P., Wang, C., Wang, E., Wang, G., Wang, K. Y., Wang, L., Wang, M. F., Wang, S. G., Wang, W. S., Wang, X. Y., Wang, Y. G., Wang, Y. Q., Wang, Z. Y., Waqas, M., Watcharangkool, A., Wei, W., Wei, Y. D., Wiebusch, C., Wong, S. C. F., Wonsak, B., Wu, D., Wu, W. J., Wu, Z., Wurm, M., Wurtz, J., Wysotzki, C., Xi, Y. F., Xie, Y. G., Xu, B., Xu, C., Xu, D. L., Xu, F. R., Xu, H. K., Xu, J., Xu, M. H., Xu, Y., Yan, B. J., Yan, T., Yan, W. Q., Yan, X. B., Yan, Y. P., Yang, A. B., Yang, H., Yang, J., Yang, X. Y., Yang, Y., Yang, Y. F., Yasin, Z., Ye, J. X., Ye, Z. P., Yegin, U., Yermia, F., Yi, P. H., Yin, X. W., You, Z. Y., Yu, B. X., Yu, C. Y., Yu, C. X., Yu, M., Yu, X. H., Yuan, C. Z., Yuan, Y., Yuan, Z. X., Yuan, Z. Y., Zafar, N., Zambanini, A., Zeng, T. X., Zeng, Y. D., Zhang, G. Q., Zhang, H. Q., Zhang, J., Zhang, J. B., Zhang, P., Zhang, S., Zhang, T., Zhang, X. M., Zhang, Y., Zhang, Y. H., Zhang, Y. P., Zhao, F. Y., Zhao, R., Zhao, S. J., Zhao, T. C., Zheng, D. Q., Zheng, H., Zheng, M. S., Zheng, Y. H., Zhong, W. R., Zhou, J., Zhou, N., Zhou, S., Zhou, X., Zhu, J., Zhu, K. J., Zhuang, B., Zong, L., Rasco, B. C., Han, B. Y., Jeon, E. J., Jeong, Y., Jo, H. S., Kim, D. K., Kim, J. Y., Kim, J. G., Kim, Y. D., Ko, Y. J., Lee, H. M., Lee, M. H., Moon, C. S., Oh, Y. M., Park, H. K., Park, K. S., Seo, S. H., Siyeon, K., Sun, G. M., Yoon, Y. S., Yu, I., Borusinski, M. J., Dorrill, R., Druetzler, A., Learned, J., Li, V., Markoff, D., Maricic, J., Matsuno, S., Mumm, H. P., Nishimura, K., Irani, A., Pitt, M., Rasco, C., Thibodeau, B., Varner, G., Vogelaar, B., Wright, T., Andriamirado, M., Bass, C. D., Bergeron, D. E., Berish, D., Bowden, N. S., Brodsky, J. P., Bryan, C. D., Carr, R., Classen, T., Conant, A. J., Deichert, G., Dolinski, M. J., Erickson, A., Foust, B. T., Gaison, J. K., Galindo-Uribarri, A., Gilbert, C. E., Grant, C., Hackett, B. T., Hansell, A. B., Ji, X., Jones, D. C., Kyzylova, O., Lane, C. E., Larosa, J., Lu, X., Mendenhall, M. P., Meyer, A. M., Milincic, R., Mitchell, I., Mueller, P. E., Nave, C., Neilson, R., Nikkel, J. A., Norcini, D., Nour, S., Palomino, J. L., Pushin, D. A., Romero-Romero, E., Surukuchi, P. T., Tyra, M. A., Varner, R. L., Venegas-Vargas, D., Weatherly, P. B., White, C., Wilhelmi, J., Woolverton, A., Zhang, A., Zhang, X., Choi, J. H., Jang, H. I., Jang, J. S., Jeon, S. H., Joo, K. K., Ju, K., Jung, D. E., Kim, J. H., Kim, S. B., Kim, S. Y., Kim, W., Kwon, E., Lee, D. H., Lee, H. G., Lim, I. T., Moon, D. H., Pac, M. Y., Seo, H., Seo, J. W., Shin, C. D., Yang, B. S., Yoo, J., Yoon, S. G., Yeo, I. S., Chang, C., Bergé, L., Broniatowski, A., Dumoulin, L., Giuliani, A., Chapellier, M., Marcillac, P., Marnieros, S., Olivieri, E., Poda, D., Calvo, M., Goupy, J., Monfardini, A., Arnaud, Q., Augier, C., Billard, J., Cazes, A., Colas, J., Filippini, J., Gascon, J., Jesus, M., Lattaud, H., Juillard, A., Salagnac, T., Soldner, T., Lubashevskiy, A., Yakushev, E., Rozov, S., Lamblin, J., Mom, B., Stutz, A., Formaggio, J. A., Mayer, D. W., Johnston, J., Harrington, P., Heine, S., Sibille, V., Chen, R., Figueroa-Feliciano, E., Ziqing, H., Hertel, S., Patel, P., Pinckney, D., Serafin, A., Shilcusky, A., Decheine, N., Palladino, K., Weber, S., Hirjibehedin, C., Akindele, O. A., Carman, L., Dazeley, S., Ford, M., Jovanovic, I., Sutanto, F., Zaitseva, N., Beaumont, W., Binet, S., Bolognino, I., Borg, J., Buridon, V., Chanal, H., Coupé, B., Crochet, P., Cussans, D., Roeck, A., Durand, D., Fallot, M., Galbinski, D., Gallego, S., Giot, L., Guillon, B., Henaff, D., Hayashida, S., Hosseini, B., Kalcheva, S., Lehaut, G., Michiels, I., Monteil, S., Newbold, D., Roy, N., Ryckbosch, D., Sfar, H. Rejeb, Simard, L., Vacheret, A., Vandierendonck, G., Dyck, S., Remortel, N., Vercaemer, S., Verstraeten, M., Weber, A., Yeresko, M., Bonhomme, A., Buck, C., Del Amo Sanchez, P., El Atmani, I., Labit, L., Letourneau, A., Lhuillier, D., Licciardi, M., Materna, T., Pessard, H., Rogly, R., Savu, V., Schoppmann, S., Vialat, M., Algora, A., Beloeuvre, A., Estienne, M., Kean, R., Porta, A., Tain, J. L., Sidelnik, I., Anderson, T., Askins, M., Bagdasarian, Z., Baldoni, A., Barna, A., Benson, T., Bergevin, M., Bernstein, A., Birrittella, B., Bogetic, S., Boissevain, J., Borusinki, J., Boyd, S., Brooks, T., Budsworth, Mat, Burns, J., Calle, M., Camilo, C., Carroll, A., Coleman, J., Collins, R., Connor, C., Cowen, D., Crow, B., Curry, J., Dalnoki-Veress, F., Danielson, D., Diwan, M., Dixon, S., Drakopoulou, L., Duron, J., Dye, S., Fargher, S., Fienberg, A., Fischer, V., Foster, R., Frankiewicz, Kat, Gamble, T., Gooding, D., Gokhale, S., Gregorio, R., Gribble, J., Griskevich, J., Hadley, D., He, J., Healey, K., Hecla, J., Holt, G., Jabbari, C., Jewkes, K., Kaiser, R., Keenan, M., Keener, P., Kneale, Liz, Kudryavtsev, V., Kunkle, P., Litchfield, P., Liu, X. Ran, Lynch, G., Malek, M., Marr-Laundrie, P., Masic, B., Mauger, C., Mccauley, N., Metelko, C., Mills, R., Mitra, A., Muheim, F., Mullen, A., Murphy, A., Needham, M., Neights, E., Ogren, K., Orebi Gann, G., Oxborough, L., Paling, S., Papatyi, A., Paulos, B., Pershing, T., Pickard, L., Quillin, S., Resoro, R., Richards, B., Sabarots, L., Scarff, A., Schnellbach, Yan-Jie, Scovell, P., Seitz, B., Shea, O., Shebalin, V., Smith, G., Smy, M., Song, H., Spooner, N., Stanton, C., Stone, O., Svoboda, R., Szoldos, S., Thompson, L., Thomson, F., Toth, C., Vagins, M., Berg, Rick, Ventura, S., Walsh, B., Webster, J., Weiss, M., Westphal, D., Wetstein, M., Wilson, T., Wilson, S., Wolcott, S., Wright, M., Berryman, J. M., Collar, J. I., Erlandson, A., Gariazzo, S., Garzelli, M. V., Giunti, C., Goldblum, B. L., Hayes, A., Hedges, S., Mariani, C., Minic, D., Mougeot, X., Naim, D., Newby, J., Ni, K., O Donnell, T., Ozturk, S., Périssé, L., Pestes, R., Sonzogni, A. A., Tabrizi, Z., Vivier, M., Institut de Physique Nucléaire d'Orsay (IPNO), Université Paris-Sud - Paris 11 (UP11)-Institut National de Physique Nucléaire et de Physique des Particules du CNRS (IN2P3)-Centre National de la Recherche Scientifique (CNRS), Institut Pluridisciplinaire Hubert Curien (IPHC), Université de Strasbourg (UNISTRA)-Université de Haute-Alsace (UHA) Mulhouse - Colmar (Université de Haute-Alsace (UHA))-Institut National de Physique Nucléaire et de Physique des Particules du CNRS (IN2P3)-Centre National de la Recherche Scientifique (CNRS), Laboratoire de Physique des 2 Infinis Irène Joliot-Curie (IJCLab), Institut National de Physique Nucléaire et de Physique des Particules du CNRS (IN2P3)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS), Centre d'Etudes Nucléaires de Bordeaux Gradignan (CENBG), Université Sciences et Technologies - Bordeaux 1 (UB)-Institut National de Physique Nucléaire et de Physique des Particules du CNRS (IN2P3)-Centre National de la Recherche Scientifique (CNRS), Centre de Physique des Particules de Marseille (CPPM), Aix Marseille Université (AMU)-Institut National de Physique Nucléaire et de Physique des Particules du CNRS (IN2P3)-Centre National de la Recherche Scientifique (CNRS), Laboratoire Neutrino de Champagne Ardenne (LNCA - UMS 3263), Institut de Recherches sur les lois Fondamentales de l'Univers (IRFU), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Institut National de Physique Nucléaire et de Physique des Particules du CNRS (IN2P3)-Centre National de la Recherche Scientifique (CNRS), Laboratoire de physique subatomique et des technologies associées (SUBATECH), Institut National de Physique Nucléaire et de Physique des Particules du CNRS (IN2P3)-Centre National de la Recherche Scientifique (CNRS)-IMT Atlantique (IMT Atlantique), Institut Mines-Télécom [Paris] (IMT)-Institut Mines-Télécom [Paris] (IMT)-Nantes université - UFR des Sciences et des Techniques (Nantes univ - UFR ST), Nantes Université - pôle Sciences et technologie, Nantes Université (Nantes Univ)-Nantes Université (Nantes Univ)-Nantes Université - pôle Sciences et technologie, Nantes Université (Nantes Univ)-Nantes Université (Nantes Univ), Centre de Sciences Nucléaires et de Sciences de la Matière (CSNSM), Cryogénie (NEEL - Cryo), Institut Néel (NEEL), Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes (UGA)-Institut polytechnique de Grenoble - Grenoble Institute of Technology (Grenoble INP ), Université Grenoble Alpes (UGA)-Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes (UGA)-Institut polytechnique de Grenoble - Grenoble Institute of Technology (Grenoble INP ), Université Grenoble Alpes (UGA), Hélium : du fondamental aux applications (NEEL - HELFA), Institut de Physique des 2 Infinis de Lyon (IP2I Lyon), Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Institut National de Physique Nucléaire et de Physique des Particules du CNRS (IN2P3)-Centre National de la Recherche Scientifique (CNRS), Laboratoire de Physique Subatomique et de Cosmologie (LPSC), Institut National de Physique Nucléaire et de Physique des Particules du CNRS (IN2P3)-Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes (UGA)-Institut polytechnique de Grenoble - Grenoble Institute of Technology (Grenoble INP ), Laboratoire de Physique de Clermont (LPC), Institut National de Physique Nucléaire et de Physique des Particules du CNRS (IN2P3)-Centre National de la Recherche Scientifique (CNRS)-Université Clermont Auvergne (UCA), Laboratoire de physique corpusculaire de Caen (LPCC), Université de Caen Normandie (UNICAEN), Normandie Université (NU)-Normandie Université (NU)-École Nationale Supérieure d'Ingénieurs de Caen (ENSICAEN), Normandie Université (NU)-Institut National de Physique Nucléaire et de Physique des Particules du CNRS (IN2P3)-Centre National de la Recherche Scientifique (CNRS), Laboratoire de l'Accélérateur Linéaire (LAL), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay, Laboratoire d'Annecy de Physique des Particules (LAPP), Institut National de Physique Nucléaire et de Physique des Particules du CNRS (IN2P3)-Université Savoie Mont Blanc (USMB [Université de Savoie] [Université de Chambéry])-Centre National de la Recherche Scientifique (CNRS), Institut Laue-Langevin (ILL), Laboratoire d'Intégration des Systèmes et des Technologies (LIST (CEA)), Direction de Recherche Technologique (CEA) (DRT (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA), Département de Physique Nucléaire (ex SPhN) (DPHN), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay, CHANDLER, CONNIE, CONUS, Daya Bay, JUNO, MTAS, NEOS, NuLat, PROSPECT, RENO, Ricochet, ROADSTR Near-Field Working Group, SoLid, Stereo, Valencia-Nantes TAGS, vIOLETA, WATCHMAN, and HEP, INSPIRE

Subjects
High Energy Physics - Experiment (hep-ex), [PHYS.HEXP] Physics [physics]/High Energy Physics - Experiment [hep-ex], hep-ex, neutrino: energy spectrum, antineutrino: nuclear reactor, [PHYS.HEXP]Physics [physics]/High Energy Physics - Experiment [hep-ex], FOS: Physical sciences, neutrino: oscillation, neutrino: nuclear reactor, Particle Physics - Experiment, neutrino: flux, High Energy Physics - Experiment
Abstract

Nuclear reactors are uniquely powerful, abundant, and flavor-pure sources of antineutrinos that continue to play a vital role in the US neutrino physics program. The US reactor antineutrino physics community is a diverse interest group encompassing many detection technologies and many particle physics topics, including Standard Model and short-baseline oscillations, BSM physics searches, and reactor flux and spectrum modeling. The community's aims offer strong complimentary with numerous aspects of the wider US neutrino program and have direct relevance to most of the topical sub-groups composing the Snowmass 2021 Neutrino Frontier. Reactor neutrino experiments also have a direct societal impact and have become a strong workforce and technology development pipeline for DOE National Laboratories and universities. This white paper, prepared as a submission to the Snowmass 2021 community organizing exercise, will survey the state of the reactor antineutrino physics field and summarize the ways in which current and future reactor antineutrino experiments can play a critical role in advancing the field of particle physics in the next decade., Contribution to Snowmass 2021

Published
2022

4. Clinicopathological and prognostic value of long noncoding RNA SNHG7 in cancer patients: a meta-analysis.

Author

ZHU, Y., QIAN, X.-H., JI, G.-Z., and YANG, L.-H.

Abstract

OBJECTIVE: Recent studies have provided evidence that long noncoding RNA SNHG7 is highly expressed and associated with poor clinical outcomes in cancer patients. The meta-analysis is aimed to evaluate the prognostic value of SNHG7 across various cancers. MATERIALS AND METHODS: Eligible studies about prognosis and clinicopathological features of SNHG7 expression in all kinds of tumors were collected by searching the databases of PubMed, Web of Science, Embase, Cochrane Library from inception through August 13, 2020. Odds ratios (ORs) and hazard ratios (HRs) with 95% confidence intervals (CIs) from eligible studies were extracted and pooled to investigate the association between SNHG7 and survival or clinicopathology by STATA 16.0 software. RESULTS: A total of 13 studies enrolling 1029 cancer patients met the inclusion criteria in this meta-analysis. Based on the results, over-expressed SNHG7 was associated with deeper tumor invasion (OR: 2.76; 95% CI: 1.98-3.86; p: 0.000), earlier lymphatic metastasis (OR: 4.22; 95% CI: 3.04-5.86; p: 0.000), more advanced tumor stage (OR: 3.49; 95% CI: 2.45-4.98; p: 0.000) and poor histologic grade (OR: 2.23; 95% CI: 1.33-3.74; p: 0.002), but not with sex, age, tumor size and distant metastasis. As for prognosis, patients with high expression of SNHG7 were more likely to have shorter overall survival (OS) (HR: 1.64; 95% CI: 1.38-1.94; p: 0.000) and disease- free survival (DFS) (HR: 1.37; 95% CI: 1.09- 1.71; p: 0.006). CONCLUSIONS: SNHG7 may serve as a novel biomarker in terms of predicting prognosis and clinicopathological characters in various human cancers. [ABSTRACT FROM AUTHOR]

Published
2021

5. Modulated spin orbit torque in a Pt/Co/Pt/YIG multilayer by nonequilibrium proximity effect.

Author

Liu, Q. B., Meng, K. K., Cai, Y. Z., Qian, X. H., Wu, Y. C., Zheng, S. Q., and Jiang, Y.

Subjects
SPIN-orbit coupling constants, SPIN transfer torque, PROXIMITY effect (Superconductivity), HALL effect, MAGNETIZATION
Abstract

We have compared the spin orbit torque (SOT) induced magnetization switching in Pt/Co/Pt/ Y3Fe5O12 (YIG) and Pt/Co/Pt/SiO2 multilayers. The critical switching current in Pt/Co/Pt/YIG is almost half of that in Pt/Co/Pt/SiO2. Through harmonic measurements, we demonstrated the enhancement of the effective spin Hall angle in Pt/Co/Pt/YIG. The increased efficiency of SOT is ascribed to the nonequilibrium proximity effect at the Pt/YIG interface, which suppresses the spin current reflection and enhances the effective spin accumulation at the Co/Pt interface. Our method can effectively reduce the switching current density and provide another way to modulate SOT. [ABSTRACT FROM AUTHOR]

Published
2018
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6. HBx protein of hepatitis B virus (HBV) can form complex with mitochondrial HSP60 and HSP70.

Author

Zhang, S. M., Sun, D. C., Lou, S., Bo, X. C., Lu, Z., Qian, X. H., and Wang, S. Q.

Subjects
HEPATITIS B virus, HEPATITIS viruses, HEPATITIS B, HEAT shock proteins, MITOCHONDRIA
Abstract

HBx, a transcriptional transactivating protein of hepatitis B virus (HBV), is required for viral infection and has been implicated in virus-mediated liver oncogenesis. However, the molecular mechanism for its influence on cell remains largely unknown. It was proved that HBx need the help of host cell proteins to exert its function by binding to them. During purifying of GSTX (fusion protein of GST and HBx) expressed in E. coli, we found that it can bind specifically with GrpE (HSP60) and DnaK (HSP70) of E. coli while GST cannot. Using GST pull-down, two-dimensional gel electrophoresis and mass spectrum, we found that GSTX can also bind to human mitochondrial HSP60 and HSP70, which are homologues of GrpE and DnaK. These interactions between HBx and mitochondrial HSP60 and HSP70 are supported by the result of co-immunoprecipitation experiment. It means that HBx can form complex with E. coli and human HSP60 and HSP70. The implication of HBx, HSP60 and HSP70 complex in molecular mechanism of virus infection is discussed. [ABSTRACT FROM AUTHOR]

Published
2005
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10. Immunomodulatory effects of IL-33 and IL-25 in an ovalbumin-induced allergic rhinitis mouse model.

Author

Yang C, Chen N, Tang XL, Qian XH, and Cai CP

Subjects
Animals, Cytokines, Disease Models, Animal, Immunity, Interleukin-33, Mice, Mice, Inbred BALB C, Nasal Mucosa, Ovalbumin, Th2 Cells, Interleukin-17, Rhinitis, Allergic chemically induced, Rhinitis, Allergic drug therapy
Abstract

Both interleukin (IL)-33 and IL-25 induce Th2-type cytokine production by various cell types, suggesting that they may contribute to development of allergic disorders, however, the immunomodulatory effects of IL-33 and IL-25 in ovalbumin (OVA)-induced allergic rhinitis (AR) remain unclear. In the present study, anti-IL-33 and anti-IL-25 Abs were administrated intranasally during rechallenge in OVA-induced AR. Immunomodulatory effects were evaluated by measuring nasal rubbing, sneezing occurrence, serum OVA-specific antibodies, Th2 immune responses, neutrophil, eosinophil and mast cell recruitment into the nasal mucosa. We found that treatment with anti-IL-33 Ab markedly reduced nasal rubbing, sneezing events, Th2 immune responses, serum OVA-specific IgE and IgG1 levels, mucosal neutrophil, eosinophil and mast cell infiltration. In contrast, the effect of IL-25 antagonism was limited to attenuating the Th2 immune responses, and neutrophil and eosinophil infiltration. These observations indicate that IL-33 and IL-25 play a pathogenic role in an established AR mouse model, with a greater contribution of IL-33 than IL-25. Our findings suggest that IL-33 neutralization may be a potential approach for treatment of AR., (Copyright 2020 Biolife Sas. www.biolifesas.org.)

Published
2021
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11. MRI findings in Duane's ocular retraction syndrome.

Author

Xia S, Li RL, Li YP, Qian XH, Chong V, and Qi J

Subjects
Abducens Nerve abnormalities, Adult, Child, Child, Preschool, China epidemiology, Diagnosis, Differential, Duane Retraction Syndrome genetics, Duane Retraction Syndrome physiopathology, Female, Humans, Male, Oculomotor Muscles innervation, Oculomotor Nerve physiopathology, Abducens Nerve pathology, Duane Retraction Syndrome pathology, Magnetic Resonance Imaging, Oculomotor Muscles pathology, Oculomotor Nerve pathology
Abstract

Aim: To investigate the innervation pattern of extra-ocular muscles in patients with clinically diagnosed Duane's ocular retraction syndrome (DRS) using magnetic resonance imaging (MRI)., Materials and Methods: The study population consisted of 11 patients. Six patients had type I DRS (eight eyes), four patients had type II DRS (five eyes) and one patient had inverse DRS. Images were acquired using a Siemens 3 T MRI system. The type of DRS, corresponding innervation findings, and condition of the affected muscles were evaluated by two experienced neuroradiologists in consensus., Results: All patients with clinically diagnosed DRS type I showed absence of the abducens nerve (CN6), hypoplasia of the superior oblique muscle (SOM), and aberrant innervation of lateral rectus muscle (LRM) by an extra branch of oculomotor nerve (CN3). All patients with type II DRS show dual-innervation of the LRM (by CN6 and an aberrant CN3 branch) and hypoplasia of SOM. The single patient with inverse DRS showed hypoplasia of CN3, the medial rectus muscle (MRM), the inferior rectus muscle (IRM), and the inferior oblique muscle (IOM)., Conclusion: Each type of DRS has characteristic MRI appearances. Therefore, MRI is a useful diagnostic tool for the confirmation and classification of suspected cases of DRS., (Copyright © 2014 The Royal College of Radiologists. Published by Elsevier Ltd. All rights reserved.)

Published
2014
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12. Fetal hemoglobin induction by the histone deacetylase inhibitor, scriptaid.

Author

Johnson J, Hunter R, McElveen R, Qian XH, Baliga BS, and Pace BS

Subjects
Anemia, Sickle Cell drug therapy, Animals, Butyrates pharmacology, Enzyme Inhibitors pharmacology, Erythroid Precursor Cells chemistry, Erythroid Precursor Cells metabolism, Fetal Hemoglobin biosynthesis, Gene Silencing, Globins biosynthesis, Humans, Hydroxamic Acids pharmacology, Hydroxylamines therapeutic use, Imidazoles pharmacology, K562 Cells, Mice, Mice, Transgenic, Pyridines pharmacology, Quinolines therapeutic use, RNA, Messenger genetics, RNA, Messenger metabolism, Signal Transduction drug effects, p38 Mitogen-Activated Protein Kinases physiology, Erythroid Precursor Cells drug effects, Fetal Hemoglobin genetics, Gene Expression Regulation drug effects, Globins genetics, Histone Deacetylase Inhibitors, Hydroxylamines pharmacology, Quinolines pharmacology
Abstract

Many different classes of drugs induce fetal hemoglobin (HbF) including histone deacetylase (HDAC) inhibitors such as butyrate and trichostatin A. Although these agents induce gamma-globin expression in culture many are ineffective in vivo, therefore research efforts continue to identify clinically useful fetal globin inducers. We and others demonstrated a role for p38 mitogen activated protein kinase (MAPK) in gamma-globin promoter activation by HDAC inhibitors. In this study we determined the ability of scriptaid, a novel HDAC inhibitor, to induce gamma-globin expression via p38 MAPK signaling. Scriptaid induced gamma-globin in K562 cells and human erythroid progenitors. Furthermore the p38-selective inhibitor SB203580 completely reversed the ability of scriptaid to induce HbF. To test the potential efficacy of scriptaid in humans, in vivo studies were completed in beta-YAC transgenic mice where the gamma-gene is completely silenced. Scriptaid induced reticulocytosis and human gamma-globin mRNA synthesis. At a concentration of 1 mg/kg/day given by intraperitoneal injections twice weekly we observed a significant 1.8-fold increase in gamma-globin mRNA transcripts. The potential for scriptaid as a treatment option for sickle cell disease will be discussed.

Published
2005

13. Affinity capillary electrophoresis investigation of an epitope on human immunodeficiency virus recognized by a monoclonal antibody.

Author

Qian XH and Tomer KB

Subjects
Amino Acid Sequence, Antibodies, Monoclonal, Antigen-Antibody Reactions, HIV Antibodies, Humans, Kinetics, Peptide Fragments chemistry, Peptide Fragments immunology, Protein Binding, Electrophoresis, Capillary methods, Epitopes chemistry, HIV Core Protein p24 chemistry, HIV Core Protein p24 immunology
Abstract

Affinity capillary electrophoresis (ACE) has been used to investigate the epitope on the human immunodeficiency virus (HIV) core protein p24 recognized by the monoclonal antibody (mAb) 13-102-100. The affinity of a series of peptides with N- and C-terminal truncations of the epitope sequence determined by mass spectrometry was studied. The peak area change assay was used for the study of the interactions of the mAb with those peptides, exhibiting tight binding to the mAb, and the migration time shift assay was used to probe the relative affinities of peptides showing weak binding to the mAb. The experimental results show that the monoclonal antibody 13-102-100 recognizes the peptide VHPVHAGPIAP with highest affinity. Smaller peptides incorporating only part of the epitope, however, are recognized to some extent in the ACE experiments.

Published
1998
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14. Inhibition of breast cancer progression by an antibody to a thrombospondin-1 receptor.

Author

Wang TN, Qian XH, Granick MS, Solomon MP, Rothman VL, Berger DH, and Tuszynski GP

Subjects
Animals, Antibody Specificity, Cell Adhesion Molecules physiology, Cell Transformation, Neoplastic immunology, Disease Models, Animal, Female, Humans, Mice, Mice, Nude, Neoplasm Transplantation, Peritoneal Neoplasms secondary, Rabbits, Tumor Cells, Cultured chemistry, Tumor Cells, Cultured cytology, Tumor Cells, Cultured physiology, Breast Neoplasms pathology, CD36 Antigens immunology
Abstract

Background: Thrombospondin-1 (TSP-1) is a matrix-bound adhesive glycoprotein. Breast carcinoma cells exhibit increased expression of a novel TSP-1 receptor. We evaluated the role of this receptor in breast cancer adhesion and progression., Methods: Adhesion assays were performed to evaluate MDA-MB-231 breast cancer cell adhesion to TSP-1 in vitro in the presence of either nonimmune immunoglobulin G(IgG) or anti-TSP-1 receptor IgG. Receptor-mediated tumor cell progression was evaluated in athymic nude mice. Mice were inoculated with MDA-MB-231 breast cancer cells and randomized to treatment with intraperitoneal injections of saline solution, nonspecific IgG antibody, or an anti-TSP-1 receptor antibody every other day for 20 days. Mice were killed at 21 days. The peritoneal cavity was examined grossly for primary tumor implantation. The liver and lungs were examined histologically for micrometastases., Results: MDA-MB-231 breast cancer cells adhered to TSP-1 in vitro. This adhesion was inhibited to 10% of control by anti-TSP-1 receptor antibody (p < 0.005). Anti-TSP-1 receptor antibody inhibited in vivo breast cancer progression. Mice treated with control IgG antibody or saline solution alone exhibited extensive intraperitoneal seeding. Only one mouse treated with the anti-TSP-1 receptor antibody exhibited any intraperitoneal tumor seeding (p < 0.01)., Conclusions: These data suggest that TSP-1 and its receptor play an important role in breast cancer progression.

Published
1996
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15. The effect of thrombospondin on oral squamous carcinoma cell invasion of collagen.

Author

Wang TN, Qian XH, Granick MS, Solomon MP, Rothman VL, and Tuszynski GP

Subjects
Amino Acid Sequence, Antibodies, Monoclonal, CD36 Antigens drug effects, CD36 Antigens immunology, CD36 Antigens physiology, Carcinoma, Squamous Cell metabolism, Cell Adhesion Molecules administration & dosage, Cell Adhesion Molecules immunology, Cell Count, Collagen metabolism, Culture Media, Serum-Free, Diffusion Chambers, Culture, Disease Progression, Dose-Response Relationship, Drug, Humans, Immunoglobulin G, Integrins drug effects, Integrins immunology, Integrins physiology, Membrane Glycoproteins administration & dosage, Membrane Glycoproteins immunology, Membranes, Artificial, Microscopy, Phase-Contrast, Mouth Neoplasms metabolism, Neoplasm Invasiveness, Polycarboxylate Cement, Thrombospondins, Transforming Growth Factor beta immunology, Transforming Growth Factor beta pharmacology, Tumor Cells, Cultured, Carcinoma, Squamous Cell pathology, Cell Adhesion Molecules pharmacology, Collagen drug effects, Membrane Glycoproteins pharmacology, Mouth Neoplasms pathology
Abstract

Background: Thrombospondin (TSP), a cell matrix protein, and transforming growth factor beta (TGF-beta), a growth regulatory protein, play roles in tumor progression. The purpose of this study was to investigate the effects of TSP and TGF-beta on tumor cell invasion., Materials and Methods: Tumor cell invasion assays were performed using a modified Boyden chamber apparatus with collagen-coated membranes. The KB oral carcinoma cell line was studied in serum-free media. Invasion was measured as the summation of the number of cells in five representative low-power fields (x 100) traversing the collagen barrier after a 3-hour incubation period. The effects of antibodies against TSP, TGF-beta and the cysteine-serine-valine-threonine-cysteine-glycine (CSVTCG)-specific TSP receptor were also evaluated., Results: TSP caused a dose-dependent stimulation of tumor cell invasion. Antibodies against TSP, its CSVTCG-specific receptor, and TGF-beta inhibited TSP-promoted invasion by 50% to 71%., Conclusions: TSP and its CSVTCG-specific receptor promote KB cell invasion of collagen through the production and/or activation of TGF-beta.

Published
1995
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16. Asymmetry in active complexes of FLP recombinase.

Author

Qian XH and Cox MM

Subjects
Base Sequence, Binding Sites, DNA Nucleotidyltransferases chemistry, Fungal Proteins metabolism, Kinetics, Macromolecular Substances, Molecular Sequence Data, Mutagenesis, Site-Directed, Protein Conformation, Recombinant Proteins chemistry, Recombinant Proteins metabolism, Recombination, Genetic, Substrate Specificity, DNA Nucleotidyltransferases metabolism, Plasmids, Saccharomyces cerevisiae genetics, Saccharomyces cerevisiae metabolism
Abstract

The FLP recombinase promotes a site-specific recombination reaction in the 2mu plasmid of yeast. The protein-DNA complex that carries out the reaction is asymmetric. Three FLP monomers bound to specific FLP-recognition sequences are required to efficiently carry out one set of reciprocal DNA cleavage and strand exchange events on a Holliday junction substrate. If a fourth monomer plays an auxiliary role in the reaction, it is bound without sequence specificity. The data suggest a modified model for cleavage of DNA in trans by the FLP recombinase that might help reconcile some seemingly conflicting resulted obtained with integrase class recombinases.

Published
1995
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17. Detection of the BCR/ABL fusion gene in chronic myeloid leukemia by RNA polymerase chain reaction.

Author

Qian XH, Yang AD, Fei HB, and Wang CC

Subjects
Adolescent, Adult, Base Sequence, Child, Chromosomes, Human, Pair 22, Female, Humans, Male, Middle Aged, Molecular Sequence Data, Philadelphia Chromosome, Polymerase Chain Reaction, Translocation, Genetic, Fusion Proteins, bcr-abl genetics, Genes, abl genetics, Leukemia, Myelogenous, Chronic, BCR-ABL Positive genetics, RNA, Neoplasm genetics
Abstract

The bcr/abl fusion gene in 20 patients with chronic myeloid leukemia (CML) was detected by RNA polymerase chain reaction, which used mRNA as the starting material to generate cDNA with reverse transcriptase followed by PCR amplification (RNA/PCR). Amplification of a sequence spanning the bcr/abl junction region was achieved by using peripheral blood cells as the source of mRNA from all 20 patients with CML, including 3 cases of Ph (-) CML, and cell line K562 was derived from patients with CML. No amplification was seen when mononuclear cells from 3 normal individuals, 2 patients with lymphoma and cell line HL-60 were used. The presence or absence of bcr exon 3 in the fusion mRNA was determined by the size of the amplified fragments. Of the 20 CML patients, 15 showed only the 165-bp amplified band (indicating retention of bcr exon 3), one showed only the 90-bp amplified band, and 4 showed both 165-bp and 90-bp bands. Both bands were seen more frequently in blast crisis than in remission and chronic phase.

Published
1993
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18. Reactions between half- and full-FLP recombination target sites. A model system for analyzing early steps in FLP protein-mediated site-specific recombination.

Author

Qian XH, Inman RB, and Cox MM

Subjects
Base Sequence, DNA genetics, DNA metabolism, DNA ultrastructure, DNA Nucleotidyltransferases genetics, Microscopy, Electron, Models, Genetic, Molecular Sequence Data, Plasmids, Substrate Specificity, DNA Nucleotidyltransferases metabolism, Recombination, Genetic
Abstract

The FLP recombination target (FRT) can be cut in half so that only one FLP protein binding site is present (a "half site"). FLP protein binds the half sites and joins them into dimeric, asymmetric head-to-head complexes held together chiefly by strong noncovalent interactions. These complexes react with full (normal) FRT sites to generate a variety of products. Analysis of these DNA species reveals that the reaction follows a well-defined reaction pathway that generally parallels the normal reaction pathway. The system is useful in analyzing early steps in recombination, since the identity of the products in a given recombination event unambiguously pinpoints the order in which the cleavage and strand exchange reactions occur. Two conclusions are derived from the present study: (i) Formation of the dimeric head-to-head complex of half sites is a prerequisite to further steps in recombination. (ii) The identity of the base pairs at positions 6 and -6 within the FRT site has a subtle effect in directing the first strand exchange event in the reaction to predominantly one of two possible cleavage sites. In addition, results are presented that suggest that a DNA-DNA pairing intermediate involving only two base pairs of the core sequence is formed prior to the first cleavage and strand exchange. DNA-DNA interactions may therefore not be limited to the isomerization step that follows the first strand exchange.

Published
1992

19. Fibrinolytic enzyme from Agkistrodon halys brevicaudus (Korean mamushi) snake venom.

Author

Qian XH and Ma L

Subjects
Amino Acids analysis, Chemical Phenomena, Chemistry, Physical, Chromatography, DEAE-Cellulose, Chromatography, Gel, Chromatography, Ion Exchange, Crotalid Venoms chemistry, Crotalid Venoms pharmacology, Isoelectric Focusing, Molecular Weight, Urokinase-Type Plasminogen Activator analysis, Crotalid Venoms enzymology, Fibrinolytic Agents pharmacology
Abstract

By means of DEAE-Sepharose CL-6B ion exchange chromatography and TSK-GEL G2000 SW high-performance gel filtration, a purified protein with fibrinolytic activity was obtained from the venom of Agkistrodon halys brevicaudus (Korean mamushi). The protein was homogeneous as judged by isoelectric focusing electrophoresis and high-performance gel filtration. Its mol. wt is 39,200 and its isoelectric point 4.12. The specific fibrinolytic activity of the protein was 3.2 times higher than that of the crude venom. The fibrinolytic activity of the purified principle was 33 units/mg protein (units of standard urokinase activity).

Published
1991
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