26 results on '"Thevenin, J"'
Search Results
2. Study of the Li/Li3N Electrode in an Organic Electrolyte
- Author
-
Thevenin, J G and Muller, R H
- Published
- 1986
3. The Changing Landscape for Stroke Prevention in AF: Findings From the GLORIA-AF Registry Phase 2
- Author
-
Huisman, M. V., Rothman, K. J., Paquette, M., Teutsch, C., Diener, H. -C., Dubner, S. J., Halperin, J. L., C. S., Ma, Zint, K., Elsaesser, A., Bartels, D. B., Lip, G. Y. H., Abban, D., Abdul, N., Abelson, M., Ackermann, A., Adams, F., Adams, L., Adragao, P., Ageno, W., Aggarwal, R., Agosti, S., Marin, J. A., Aguilar, F., Aguilar Linares, J. A., Aguinaga, L., Ahmad, Z., Ainsworth, P., Al Ghalayini, K., Al Ismail, S., Alasfar, A., Alawwa, A., Al-Dallow, R., Alderson, L., Alexopoulos, D., Ali, A., Ali, M., Aliyar, P., Al-Joundi, T., Al Mahameed, S., Almassi, H., Almuti, K., Al-Obaidi, M., Alshehri, M., Altmann, U., Alves, A. R., Al-Zoebi, A., Amara, W., Amelot, M., Amjadi, N., Ammirati, F., Andrawis, N., Angoulvant, D., Annoni, G., Ansalone, G., Antonescu, S. A., Ariani, M., Arias, J. C., Armero, S., Arora, R., Arora, C., Ashcraft, W., Aslam, M. S., Astesiano, A., Audouin, P., Augenbraun, C., Aydin, S., Azar, R., Azim, A., Aziz, S., Backes, L. M., Baig, M., Bains, S., Bakbak, A., Baker, S., Bakhtiar, K., Bala, R., Banayan, J., Bandh, S., Bando, S., Banerjee, S., Bank, A., Barbarash, O., Baron, G., Barr, C., Barrera, C., Barton, J., Kes, V. B., Baula, G., Bayeh, H., Bazargani, N., Behrens, S., Bell, A., Benezet-Mazuecos, J., Benhalima, B., Berdague, P., Berg van den, B. J., Bergen van, P. F. M. M., Berngard, E., Bernstein, R., Berrospi, P., Berti, S., Bertomeu, V., Berz, A., Bettencourt, P., Betzu, R., Beyer-Westendorf, J., Bhagwat, R., Black, T., Blanco Ibaceta, J. H., Bloom, S., Blumberg, E., Bo, M., Bockisch, V., Bohmer, E., Bongiorni, M. G., Boriani, G., Bosch, R., Boswijk, D. J., Bott, J., Bottacchi, E., Kalan, M. B., Brandes, A., Bratland, B., Brautigam, D., Breton, N., Brouwers, P. J. A. M., Browne, K., Bruguera, J., Brunehaut, M., Brunschwig, C., Buathier, H., Buhl, A., Bullinga, J., Butcher, K., Cabrera Honorio, J. W., Caccavo, A., Cadinot, D., Cai, S., Calvi, V., Camm, J., Candeias, R., Capo, J., Capucci, A., Cardoso, J. N., Duarte Vera, Y. C., Carlson, B., Carvalho, P., Cary, S., Casanova, R., Casu, G., Cattan, S., Cavallini, C., Cayla, G., Cha, T. J., Cha, K. S., Chaaban, S., Chae, J. K., Challappa, K., Chand, S., Chandrashekar, H., Chang, M., Charbel, P., Chartier, L., Chatterjee, K., Cheema, A., Chen, S. -A., Chevallereau, P., Chiang, F. -T., Chiarella, F., Chih-Chan, L., Cho, Y. K., Choi, D. J., Chouinard, G., Danny, Chow, H. F., Chrysos, D., Chumakova, G., Jose Roberto Chuquiure Valenzuela, E. J., Cieza-Lara, T., Nica, V. C., Ciobotaru, V., Cislowski, D., Citerne, O., Claus, M., Clay, A., Clifford, P., Cohen, S., Cohen, A., Colivicchi, F., Collins, R., Compton, S., Connors, S., Conti, A., Buenostro, G. C., Coodley, G., Cooper, M., Corbett, L., Corey, O., Coronel, J., Corrigan, J., Cotrina Pereyra, R. Y., Cottin, Y., Coutu, B., Cracan, A., Crean, P., Crenshaw, J., Crijns, H. J. G. M., Crump, C., Cucher, F., Cudmore, D., Cui, L., Culp, J., Darius, H., Dary, P., Dascotte, O., Dauber, I., Davee, T., Davies, R., Davis, G., Davy, J. -M., Dayer, M., De La Briolle, A., de Mora, M., De Teresa, E., De Wolf, L., Decoulx, E., Deepak, S., Defaye, P., Del-Carpio Munoz, F., Brkljacic, D. D., Deluche, L., Destrac, S., Deumite, N. J., Di Legge, S., Dibon, O., Diemberger, I., Dillinger, J., Dionisio, P., Naydenov, S., Dotani, I., Dotcheva, E., D'Souza, A., Dubrey, S., Ducrocq, X., Dupljakov, D., Duthinh, V., Dutra, O. P., Dutta, D., Duvilla, N., Dy, J., Dziewas, R., Eaton, C., Eaves, W., Ebinger, M., Eck van, J. W. M., Edwards, T., Egocheaga, I., Ehrlich, C., Eisenberg, S., El Hallak, A., El Jabali, A., El Mahmoud, R., El Shahawy, M., Eldadah, Z., Elghelbazouri, F., Elhag, O., El-Hamdani, M., Elias, D., Ellery, A., El-Sayed, H., Elvan, A., Erickson, B., Espaliat, E., Essandoh, L., Everington, T., Evonich, R., Ezhov, A., Facila, L., Farsad, R., Fayard, M., Fedele, F., Gomes Ferreira, L. G., Ferreira, D., Santos, J. F., Ferrier, A., Finsen, A., First, B., Fisher, R., Floyd, J., Folk, T., Fonseca, C., Fonseca, L., Forman, S., Forsgren, M., Foster, M., Foster, N., Frais, M., Frandsen, B., Frappe, T., Freixa, R., French, W., Freydlin, M., Frickel, S., Fruntelata, A. G., Fujii, S., Fujino, Y., Fukunaga, H., Furukawa, Y., Gabelmann, M., Gabris, M., Gadsboll, N., Galin, P., Galinier, M., Ganim, R., Garcia, R., Quintana, A. G., Gartenlaub, O., Genz, C., Georger, F., Georges, J. -L., Georgeson, S., Ghanbasha, A., Giedrimas, E., Gierba, M., Gillespie, E., Giniger, A., Gkotsis, A., Gmehling, J., Gniot, J., Goethals, P., Goldberg, R., Goldmann, B., Goldscher, D., Golitsyn, S., Gomez Lopez, E. A., Gomez Mesa, J. E., Gonzalez, E., Cocina, E. G., Juanatey, C. G., Gorbunov, V., Gordon, B., Gorka, H., Gornick, C., Gorog, D., Goss, F., Gotte, A., Goube, P., Goudevenos, I., Goulden, D., Graham, B., Grande, A., Greco, C., Green, M., Greer, G., Gremmler, U., Grena, P., Grinshstein, Y., Grond, M., Gronda, E., Grondin, F., Gronefeld, G., Groot de, J. R., Guardigli, G., Guarnieri, T., Caiedo, C. G., Guignier, A., Gulizia, M., Gumbley, M., Gupta, D., Hack, T., Haerer, W., Hakas, J., Hall, C., Hampsey, J., Hananis, G., Hanbali, B., Handel, F., Hargrove, J., Hargroves, D., Harris, K., Hartley, D., Haruna, T., Hata, Y., Hayek, E., Healey, J., Hearne, S., Heggelund, G., Hemels, M. E. W., Hemery, Y., Henein, S., Henz, B., Her, S. -H., Hermany, P., Hernandes, M. E., Higashino, Y., Hill, M., Hisadome, T., Hishida, E., Hitchcock, J., Hoffer, E., Hoghton, M., Holmes, C., Hong, S. K., Houppe Nousse, M. -P., Howard, V., Hsu, L. F., Huang, C. -H., Huckins, D., Huehnergarth, K., Huizenga, A., Huntley, R., Hussein, G., Hwang, G. -S., Igbokidi, O., Iglesias, I., Ikpoh, M., Imberti, D., Ince, H., Indolfi, C., Ionova, T., Ip, J., Irles, D., Iseki, H., Ismail, Y., Israel, N., Isserman, S., Iteld, B., Ivanchura, G., Iyer, R., Iyer, V., Iza Villanueva, R. O., Jackson-Voyzey, E., Jaffrani, N., Jager, F., Jain, M., James, M., Jamon, Y., Jang, S. W., Pereira Jardim, C. A., Jarmukli, N., Jeanfreau, R., Jenkins, R., Jiang, X., Jiang, H., Jiang, T., Jiang, N., Jimenez, J., Jobe, R., Joffe, I., Johansson, B., Jones, N., Moura Jorge, J. C., Jouve, B., Jundi, M., Jung, W., Jung, B. C., Jung, K. T., Kabbani, S., Kabour, A., Kafkala, C., Kajiwara, K., Kalinina, L., Kampus, P., Kanda, J., Kapadia, S., Karim, A., Karolyi, L., Kashou, H., Kastrup, A., Katsivas, A., Kaufman, E., Kawai, K., Kawajiri, K., Kazmierski, J., Keeling, P., Kerfes, G. A., Kerr Saraiva, J. F., Ketova, G., Khaira, A., Khalid, M., Khludeeva, E., Khripun, A., Kim, D. I., Kim, D. K., Kim, N. H., Kim, K. S., Kim, Y. -H., Kim, J. B., Kim, J. S., Kinova, E., Klein, A., Kleinschnitz, C., Kmetzo, J., Kneller, G. L., Knezevic, A., Koch, S., Koenig, K., Angela Koh, S. M., Kohrmann, M., Koons, J., Korabathina, R., Korennova, O., Koschutnik, M., Kosinski, E., Kovacic, D., Kowalczyk, J., Koziolova, N., Kragten, J. A., Krause, L. U., Kreidieh, I., Krenning, B. J., Krishnaswamy, K., Krysiak, W., Kuck, K. -H., Kumar, S., Kumler, T., Kuniss, M., Kuo, J. -Y., Kuppers, A., Kurrelmeyer, K., Kwan, T., Kyo, E., Labovitz, A., Lacroix, A., Lam, A., Lanas Zanetti, F. T., Landau, C., Landini, G., Lang, W., Larsen, T. B., Laske, V., Lavandier, K., Law, N., Lee, M. H., Lee, D., Leitao, A., Lejay, D., Lelonek, M., Lenarczyk, R., Leprince, P., Lequeux, B., Leschke, M., Ley, N., Li, Z., Li, Y., Li, X., Li, W., Liang, J., Lieber, I., Lillestol, M., Limon Rodriguez, R. H., Lin, H., Lip, G., Litchfield, J., Liu, Z., Liu, X., Liu, Y., Liu, F., Liu, W., Llamas Esperon, G. A., Llisterri, J. L., Lo, T., Lo, E., Lobos, J. M., Lodde, B. -P., Loiselet, P., Lopez-Sendon, J., Lorga Filho, A. M., Lori, I., Luo, M., Lupovitch, S., Lyrer, P., Zuhairy, H. M., Ma, C., Ma, G., Ma, H., Madariaga, I., Maeno, K., Magnin, D., Mahmood, S., Mahood, K., Maid, G., Mainigi, S., Makaritsis, K., Maldonado Villalon, J. A., Malhotra, R., Malik, A., Mallecourt, C., Mallik, R., Manning, R., Manolis, A., Mantas, I., Manzur Jattin, F. G., Marcionni, N., Marin, F., Santana, A. M., Martinez, J., Martinez, L., Maskova, P., Hernandez, N. M., Matskeplishvili, S., Matsuda, K., Mavri, A., May, E., Mayer, N., Mazon, P., Mcclure, J., Mccormack, T., Mcgarity, W., Mcguire, M., Mcintyre, H., Mclaughlin, P., Mclaurin, B., Medina Palomino, F. A., Mehta, P., Mehzad, R., Meinel, A., Melandri, F., Mena, A., Meno, H., Menzies, D., Metcalf, K., Meyer, B., Miarka, J., Mibach, F., Michalski, D., Michel, P., Chreih, R. M., Mikdadi, G., Mikhail, M., Mikus, M., Milicic, D., Militaru, C., Miller, G., Milonas, C., Minescu, B., Mintale, I., Miralles, A., Mirault, T., Mistry, D., Mitchell, G., Miu, N. V., Miyamoto, N., Moccetti, T., Mohammed, A., Nor, A. M., Molina de Salazar, D. I., Molon, G., Molony, D., Mondillo, S., Mont, L., Moodley, R., Moore, R., Ribeiro Moreira, D. A., Mori, K., Moriarty, A., Morka, J., Moschos, N., Mota Gomes, M. A., Mousallem, N., Moya, A., Mugge, A., Mulhearn, T., Muller, J. -J., Muresan, C. M., Muse, D., Musial, W., Musumeci, F., Nadar, V., Nageh, T., Nair, P., Nakagawa, H., Nakamura, Y., Nakayama, T., Nam, K. -B., Napalkov, D., Natarajan, I., Nayak, H., Nechvatal, L., Neiman, J., Nerheim, P., Neuenschwander, F. C., Nishida, K., Nizov, A., Novikova, T., Novo, S., Nowalany-Kozielska, E., Nsah, E., Nunez Fragoso, J. C., Nyvad, O., de Los Rios Ibarra, M. O., O'Donnell, M., O'Donnell, P., D. J., Oh, Y. S., Oh, Daniel Oh, C. T., O'Hara, G., Oikonomou, K., Olalla, J. J., Olivari, Z., Oliver, R., Olympios, C., Osborne, J., Osca, J., Osman, R., Osunkoya, A., Padanilam, B., Panchenko, E., Pandey, A. S., Vicenzo de Paola, A. A., Paraschos, A., Pardell, H., Park, H. W., Park, J. S., Parkash, R., Parker, I., Parrens, E., Parris, R., Passamonti, E., Patel, J., Patel, R., Pentz, W. H., Persic, V., Perticone, F., Peters, P., Petkar, S., Pezo, L. F., Pham, D., Cao Phai, G. P., Phlaum, S., Pineau, J., Pineda-Velez, A., Pini, R., Pinter, A., Pinto, F., Pirelli, S., Pivac, N., Pizzini, A. M., Pocanic, D., Calin Podoleanu, C. G., Polanczyk, C. A., Polasek, P., Poljakovic, Z., Pollock, S., Polo, J., Poock, J., Poppert, H., Porro, Y., Pose, A., Poulain, F., Poulard, J. -E., Pouzar, J., Povolny, P., Pozzer, D., Pras, A., Prasad, N., Prevot, S., Protasov, K., Prunier, L., Puleo, J., Pye, M., Qaddoura, F., Quedillac, J. -M., Raev, D., Rahimi, S., Raisaro, A., Rama, B., Ranadive, N., Randall, K., Ranjith, N., Raposo, N., Rashid, H., Raters, C., Rauch-Kroehnert, U., Rebane, T., Regner, S., Renzi, M., Reyes Rocha, M. A., Reza, S., Ria, L., Richter, D., Rickli, H., Rickner, K., Rieker, W., Rigo, F., Ripoll, T., Fonteles Ritt, L. E., Roberts, D., Pascual, C. R., Briones, I. R., Reyes, H. R., Roelke, M., Roman, M., Romeo, F., Ronner, E., Ronziere, T., Rooyer, F. A., Rosenbaum, D., Roth, S., Rozkova, N., Rubacek, M., Rubalcava, F., Rubanenko, O., Rubin, A., Borret, M. R., Rybak, K., Sabbour, H., Morales, O. S., Sakai, T., Salacata, A., Salecker, I., Salem, A., Salfity, M., Salguero, R., Salvioni, A., Samson, M., Sanchez, G., Sandesara, C., Saporito, W. F., Sasaoka, T., Sattar, P., Savard, D., Scala, P. -J., Scemama, J., Schaupp, T., Schellinger, P., Scherr, C., Schmitz, K. -H., Schmitz, B., Schmitz, L., Schnitzler, R., Schnupp, S., Schoeniger, P., Schon, N., Schuster, S., Schwimmbeck, P., Seamark, C., Seebass, R., Seidl, K. -H., Seidman, B., Sek, J., Sekaran, L., Seko, Y., Sepulveda Varela, P. A., Sevilla, B., Shah, V., Shah, A., Shah, N., Shanes, J., Sharareh, A., Sharma, V. K., Shaw, L., Shimizu, Y., Shimomura, H., Shin, D. G., Shin, E. -S., Shite, J., Shoukfeh, M., Shoultz, C., Silver, F., Sime, I., Simmers, T. A., Singal, D., Singh, N., Siostrzonek, P., Sirajuddin, M., Skeppholm, M., Smadja, D., Smith, R., Smith, D., Soda, H., Sofley, C. W., Sokal, A., Sotolongo, R., de Souza, O. F., Sparby, J. A., Spinar, J., Sprigings, D., Spyropoulos, A., Stakos, D., Steinberg, A., Steinwender, C., Stergiou, G., Stites, H. W., Stoikov, A., Strasser, R., Streb, W., Styliadis, I., Su, G., Su, X., Suarez, R. M., Sudnik, W., Sueyoshi, A., Sukles, K., Sun, L., Suneja, R., Svensson, P., Ziekenhuis, A., Szavits-Nossan, J., Taggeselle, J., Takagi, Y., Takhar, A., Tallet, J., Tamm, A., Tanaka, S., Tanaka, K., Tang, A., Tang, S., Tassinari, T., Tayama, S., Tayebjee, M., Tebbe, U., Teixeira, J., Tesloianu, D. N., Tessier, P., The, S. H. K., Thevenin, J., Thomas, H., Timsit, S., Topkis, R., Torosoff, M., Touze, E., Traissac, T., Trendafilova, E., Troyan, B., Tsai, W. K., Tse, H. F., Tsutsui, H., Tsutsui, T., Tuininga, Y. S., Turakhia, M., Turk, S., Turner, W., Tveit, A., Twiddy, S., Tytus, R., Ukrainski, G., Valdovinos Chavez, S. B., Van De Graaff, E., Vanacker, P., Vardas, P., Vargas, M., Vassilikos, V., Vazquez, J., Venkataraman, A., Verdecchia, P., Vester, E. G., Vial, H., Vinereanu, D., Vlastaris, A., Vogel, C., vom Dahl, J., von Mering, M., Vora, K., Wakefield, P., Walia, J., Walter, T., Wang, M., Wang, N., Wang, F., Wang, X., Wang, Z., Wang, K. -Y., Watanabe, K., Wei, J., Weimar, C., Weinrich, R., Wen, M. -S., Wheelan, K., Wicke, J., Wiemer, M., Wild, B., Wilke, A., Willems, S., Williams, M., Williams, D., Winkler, A., Wirtz, J. H., Witzenbichler, B., Wong, D. H. K., Lawrence Wong, K. S., Wong, B., Wozakowska-Kaplon, B., Wu, Z., Wu, S., Wyatt, N., Xu, Y., Xu, X., Yamada, A., Yamamoto, K., Yamanoue, H., Yamashita, T., Bryan Yan, P. Y., Yang, Y., Yang, T., Yao, J., Yarlagadda, C., Yeh, K. -H., Yotov, Y., Yvorra, S., Zahn, R., Zamorano, J., Zanini, R., Zarich, S., Zebrack, J., Zenin, S., Zeuthen, E. L., Zhang, X., Zhang, Q., Zhang, D., Zhang, H., Zhao, S., Zhao, X., Zheng, Y., Zheng, Q., Zhou, J., Zimmermann, S. L., Zimmermann, R., Zukerman, L. S., Zwaan van der, C., Huisman, M, Rothman, K, Paquette, M, Teutsch, C, Diener, H, Dubner, S, Halperin, J, Ma, C, Zint, K, Elsaesser, A, Bartels, D, Lip, G, Abban, D, Abdul, N, Abelson, M, Ackermann, A, Adams, F, Adams, L, Adragão, P, Ageno, W, Aggarwal, R, Agosti, S, Marin, J, Aguilar, F, Aguilar Linares, J, Aguinaga, L, Ahmad, Z, Ainsworth, P, Al Ghalayini, K, Al Ismail, S, Alasfar, A, Alawwa, A, Al Dallow, R, Alderson, L, Alexopoulos, D, Ali, A, Ali, M, Aliyar, P, Al Joundi, T, Al Mahameed, S, Almassi, H, Almuti, K, Al Obaidi, M, Alshehri, M, Altmann, U, Alves, A, Al Zoebi, A, Amara, W, Amelot, M, Amjadi, N, Ammirati, F, Andrawis, N, Angoulvant, D, Annoni, G, Ansalone, G, Antonescu, S, Ariani, M, Arias, J, Armero, S, Arora, R, Arora, C, Ashcraft, W, Aslam, M, Astesiano, A, Audouin, P, Augenbraun, C, Aydin, S, Azar, R, Azim, A, Aziz, S, Backes, L, Baig, M, Bains, S, Bakbak, A, Baker, S, Bakhtiar, K, Bala, R, Banayan, J, Bandh, S, Bando, S, Banerjee, S, Bank, A, Barbarash, O, Barón, G, Barr, C, Barrera, C, Barton, J, Kes, V, Baula, G, Bayeh, H, Bazargani, N, Behrens, S, Bell, A, Benezet Mazuecos, J, Benhalima, B, Berdagué, P, Berg van den, B, Bergen van, P, Berngard, E, Bernstein, R, Berrospi, P, Berti, S, Bertomeu, V, Berz, A, Bettencourt, P, Betzu, R, Beyer Westendorf, J, Bhagwat, R, Black, T, Blanco Ibaceta, J, Bloom, S, Blumberg, E, Bo, M, Bockisch, V, Bøhmer, E, Bongiorni, M, Boriani, G, Bosch, R, Boswijk, D, Bott, J, Bottacchi, E, Kalan, M, Brandes, A, Bratland, B, Brautigam, D, Breton, N, Brouwers, P, Browne, K, Bruguera, J, Brunehaut, M, Brunschwig, C, Buathier, H, Buhl, A, Bullinga, J, Butcher, K, Cabrera Honorio, J, Caccavo, A, Cadinot, D, Cai, S, Calvi, V, Camm, J, Candeias, R, Capo, J, Capucci, A, Cardoso, J, Duarte Vera, Y, Carlson, B, Carvalho, P, Cary, S, Casanova, R, Casu, G, Cattan, S, Cavallini, C, Cayla, G, Cha, T, Cha, K, Chaaban, S, Chae, J, Challappa, K, Chand, S, Chandrashekar, H, Chang, M, Charbel, P, Chartier, L, Chatterjee, K, Cheema, A, Chen, S, Chevallereau, P, Chiang, F, Chiarella, F, Chih Chan, L, Cho, Y, Choi, D, Chouinard, G, Danny, N, Chow, H, Chrysos, D, Chumakova, G, José Roberto Chuquiure Valenzuela, E, Cieza Lara, T, Nica, V, Ciobotaru, V, Cislowski, D, Citerne, O, Claus, M, Clay, A, Clifford, P, Cohen, S, Cohen, A, Colivicchi, F, Collins, R, Compton, S, Connors, S, Conti, A, Buenostro, G, Coodley, G, Cooper, M, Corbett, L, Corey, O, Coronel, J, Corrigan, J, Cotrina Pereyra, R, Cottin, Y, Coutu, B, Cracan, A, Crean, P, Crenshaw, J, Crijns, H, Crump, C, Cucher, F, Cudmore, D, Cui, L, Culp, J, Darius, H, Dary, P, Dascotte, O, Dauber, I, Davee, T, Davies, R, Davis, G, Davy, J, Dayer, M, De La Briolle, A, de Mora, M, De Teresa, E, De Wolf, L, Decoulx, E, Deepak, S, Defaye, P, Del Carpio Munoz, F, Brkljacic, D, Deluche, L, Destrac, S, Deumite, N, Di Legge, S, Dibon, O, Diemberger, I, Dillinger, J, Dionísio, P, Naydenov, S, Dotani, I, Dotcheva, E, D'Souza, A, Dubrey, S, Ducrocq, X, Dupljakov, D, Duthinh, V, Dutra, O, Dutta, D, Duvilla, N, Dy, J, Dziewas, R, Eaton, C, Eaves, W, Ebinger, M, Eck van, J, Edwards, T, Egocheaga, I, Ehrlich, C, Eisenberg, S, El Hallak, A, El Jabali, A, El Mahmoud, R, El Shahawy, M, Eldadah, Z, Elghelbazouri, F, Elhag, O, El Hamdani, M, Elias, D, Ellery, A, El Sayed, H, Elvan, A, Erickson, B, Espaliat, E, Essandoh, L, Everington, T, Evonich, R, Ezhov, A, Fácila, L, Farsad, R, Fayard, M, Fedele, F, Gomes Ferreira, L, Ferreira, D, Santos, J, Ferrier, A, Finsen, A, First, B, Fisher, R, Floyd, J, Folk, T, Fonseca, C, Fonseca, L, Forman, S, Forsgren, M, Foster, M, Foster, N, Frais, M, Frandsen, B, Frappé, T, Freixa, R, French, W, Freydlin, M, Frickel, S, Fruntelata, A, Fujii, S, Fujino, Y, Fukunaga, H, Furukawa, Y, Gabelmann, M, Gabris, M, Gadsbøll, N, Galin, P, Galinier, M, Ganim, R, Garcia, R, Quintana, A, Gartenlaub, O, Genz, C, Georger, F, Georges, J, Georgeson, S, Ghanbasha, A, Giedrimas, E, Gierba, M, Gillespie, E, Giniger, A, Gkotsis, A, Gmehling, J, Gniot, J, 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J, Zimmermann, S, Zimmermann, R, Zukerman, L, and Zwaan van der, C
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Male ,oral anticoagulation ,Internationality ,Middle Aged ,registry ,Antithrombins ,Dabigatran ,Stroke ,Cross-Sectional Studies ,Fibrinolytic Agents ,Humans ,Female ,atrial fibrillation ,Prospective Studies ,Registries ,Cardiology and Cardiovascular Medicine ,Aged ,Atrial Fibrillation - Abstract
Background GLORIA-AF (Global Registry on Long-Term Oral Antithrombotic Treatment in Patients with Atrial Fibrillation) is a prospective, global registry program describing antithrombotic treatment patterns in patients with newly diagnosed nonvalvular atrial fibrillation at risk of stroke. Phase 2 began when dabigatran, the first non–vitamin K antagonist oral anticoagulant (NOAC), became available. Objectives This study sought to describe phase 2 baseline data and compare these with the pre-NOAC era collected during phase 1. Methods During phase 2, 15,641 consenting patients were enrolled (November 2011 to December 2014); 15,092 were eligible. This pre-specified cross-sectional analysis describes eligible patients’ baseline characteristics. Atrial fibrillation disease characteristics, medical outcomes, and concomitant diseases and medications were collected. Data were analyzed using descriptive statistics. Results Of the total patients, 45.5% were female; median age was 71 (interquartile range: 64, 78) years. Patients were from Europe (47.1%), North America (22.5%), Asia (20.3%), Latin America (6.0%), and the Middle East/Africa (4.0%). Most had high stroke risk (CHA2DS2-VASc [Congestive heart failure, Hypertension, Age ≥75 years, Diabetes mellitus, previous Stroke, Vascular disease, Age 65 to 74 years, Sex category] score ≥2; 86.1%); 13.9% had moderate risk (CHA2DS2-VASc = 1). Overall, 79.9% received oral anticoagulants, of whom 47.6% received NOAC and 32.3% vitamin K antagonists (VKA); 12.1% received antiplatelet agents; 7.8% received no antithrombotic treatment. For comparison, the proportion of phase 1 patients (of N = 1,063 all eligible) prescribed VKA was 32.8%, acetylsalicylic acid 41.7%, and no therapy 20.2%. In Europe in phase 2, treatment with NOAC was more common than VKA (52.3% and 37.8%, respectively); 6.0% of patients received antiplatelet treatment; and 3.8% received no antithrombotic treatment. In North America, 52.1%, 26.2%, and 14.0% of patients received NOAC, VKA, and antiplatelet drugs, respectively; 7.5% received no antithrombotic treatment. NOAC use was less common in Asia (27.7%), where 27.5% of patients received VKA, 25.0% antiplatelet drugs, and 19.8% no antithrombotic treatment. Conclusions The baseline data from GLORIA-AF phase 2 demonstrate that in newly diagnosed nonvalvular atrial fibrillation patients, NOAC have been highly adopted into practice, becoming more frequently prescribed than VKA in Europe and North America. Worldwide, however, a large proportion of patients remain undertreated, particularly in Asia and North America. (Global Registry on Long-Term Oral Antithrombotic Treatment in Patients With Atrial Fibrillation [GLORIA-AF]; NCT01468701)
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- 2017
4. The Changing Landscape for Stroke Prevention in AF: Findings From the GLORIA-AF Registry Phase 2
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Huisman, M, Rothman, K, Paquette, M, Teutsch, C, Diener, H, Dubner, S, Halperin, J, Ma, C, Zint, K, Elsaesser, A, Bartels, D, Lip, G, Abban, D, Abdul, N, Abelson, M, Ackermann, A, Adams, F, Adams, L, Adragão, P, Ageno, W, Aggarwal, R, Agosti, S, Marin, J, Aguilar, F, Aguilar Linares, J, Aguinaga, L, Ahmad, Z, Ainsworth, P, Al Ghalayini, K, Al Ismail, S, Alasfar, A, Alawwa, A, Al Dallow, R, Alderson, L, Alexopoulos, D, Ali, A, Ali, M, Aliyar, P, Al Joundi, T, Al Mahameed, S, Almassi, H, Almuti, K, Al Obaidi, M, Alshehri, M, Altmann, U, Alves, A, Al Zoebi, A, Amara, W, Amelot, M, Amjadi, N, Ammirati, F, Andrawis, N, Angoulvant, D, Annoni, G, Ansalone, G, Antonescu, S, Ariani, M, Arias, J, Armero, S, Arora, R, Arora, C, Ashcraft, W, Aslam, M, Astesiano, A, Audouin, P, Augenbraun, C, Aydin, S, Azar, R, Azim, A, Aziz, S, Backes, L, Baig, M, Bains, S, Bakbak, A, Baker, S, Bakhtiar, K, Bala, R, Banayan, J, Bandh, S, Bando, S, Banerjee, S, Bank, A, Barbarash, O, Barón, G, Barr, C, Barrera, C, 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Köhrmann, M, Koons, J, Korabathina, R, Korennova, O, Koschutnik, M, Kosinski, E, Kovacic, D, Kowalczyk, J, Koziolova, N, Kragten, J, Krause, L, Kreidieh, I, Krenning, B, Krishnaswamy, K, Krysiak, W, Kuck, K, Kumar, S, Kümler, T, Kuniss, M, Kuo, J, Küppers, A, Kurrelmeyer, K, Kwan, T, Kyo, E, Labovitz, A, Lacroix, A, Lam, A, Lanas Zanetti, F, Landau, C, Landini, G, Lang, W, Larsen, T, Laske, V, Lavandier, K, Law, N, Lee, M, Lee, D, Leitão, A, Lejay, D, Lelonek, M, Lenarczyk, R, Leprince, P, Lequeux, B, Leschke, M, Ley, N, Li, Z, Li, Y, Li, X, Li, W, Liang, J, Lieber, I, Lillestol, M, Limon Rodriguez, R, Lin, H, Litchfield, J, Liu, Z, Liu, X, Liu, Y, Liu, F, Liu, W, Llamas Esperon, G, Llisterri, J, Lo, T, Lo, E, Lobos, J, Lodde, B, Loiselet, P, López Sendón, J, Lorga Filho, A, Lori, I, Luo, M, Lupovitch, S, Lyrer, P, Zuhairy, H, Ma, G, Ma, H, Madariaga, I, Maeno, K, Magnin, D, Mahmood, S, Mahood, K, Maid, G, Mainigi, S, Makaritsis, K, Maldonado Villalon, J, Malhotra, R, Malik, A, Mallecourt, C, Mallik, R, Manning, R, Manolis, A, Mantas, I, Manzur Jattin, F, Marcionni, N, Marín, F, Santana, A, Martinez, J, Martinez, L, Maskova, P, Hernández, N, Matskeplishvili, S, Matsuda, K, Mavri, A, May, E, Mayer, N, Mazon, P, Mcclure, J, Mccormack, T, Mcgarity, W, Mcguire, M, Mcintyre, H, Mclaughlin, P, Mclaurin, B, Medina Palomino, F, Mehta, P, Mehzad, R, Meinel, A, Melandri, F, Mena, A, Meno, H, Menzies, D, Metcalf, K, Meyer, B, Miarka, J, Mibach, F, Michalski, D, Michel, P, Chreih, R, Mikdadi, G, Mikhail, M, Mikus, M, Milicic, D, Militaru, C, Miller, G, Milonas, C, Minescu, B, Mintale, I, Miralles, A, Mirault, T, Mistry, D, Mitchell, G, Miu, N, Miyamoto, N, Moccetti, T, Mohammed, A, Nor, A, Molina de Salazar, D, Molon, G, Molony, D, Mondillo, S, Mont, L, Moodley, R, Moore, R, Ribeiro Moreira, D, Mori, K, Moriarty, A, Morka, J, Moschos, N, Mota Gomes, M, Mousallem, N, Moya, A, Mügge, A, Mulhearn, T, Muller, J, Muresan, C, Muse, D, Musial, W, Musumeci, F, Nadar, V, Nageh, T, Nair, P, Nakagawa, H, Nakamura, Y, Nakayama, T, Nam, K, Napalkov, D, Natarajan, I, Nayak, H, Nechvatal, L, Neiman, J, Nerheim, P, Neuenschwander, F, Nishida, K, Nizov, A, Novikova, T, Novo, S, Nowalany Kozielska, E, Nsah, E, Nunez Fragoso, J, Nyvad, O, de Los Rios Ibarra, M, O'Donnell, M, O'Donnell, P, Oh, D, Oh, Y, Daniel Oh, C, O'Hara, G, Oikonomou, K, Olalla, J, Olivari, Z, Oliver, R, Olympios, C, Osborne, J, Osca, J, Osman, R, Osunkoya, A, Padanilam, B, Panchenko, E, Pandey, A, Vicenzo de Paola, A, Paraschos, A, Pardell, H, Park, H, Park, J, Parkash, R, Parker, I, Parrens, E, Parris, R, Passamonti, E, Patel, J, Patel, R, Pentz, W, Persic, V, Perticone, F, Peters, P, Petkar, S, Pezo, L, Pham, D, Cao Phai, G, Phlaum, S, Pineau, J, Pineda Velez, A, Pini, R, Pinter, A, Pinto, F, Pirelli, S, Pivac, N, Pizzini, A, Pocanic, D, Calin Podoleanu, C, Polanczyk, C, Polasek, P, Poljakovic, Z, Pollock, S, Polo, J, Poock, J, Poppert, H, Porro, Y, Pose, A, Poulain, F, Poulard, J, Pouzar, J, Povolny, P, Pozzer, D, Pras, A, Prasad, N, Prevot, S, Protasov, K, Prunier, L, Puleo, J, Pye, M, Qaddoura, F, Quedillac, J, Raev, D, Rahimi, S, Raisaro, A, Rama, B, Ranadive, N, Randall, K, Ranjith, N, Raposo, N, Rashid, H, Raters, C, Rauch Kroehnert, U, Rebane, T, Regner, S, Renzi, M, Reyes Rocha, M, Reza, S, Ria, L, Richter, D, Rickli, H, Rickner, K, Rieker, W, Rigo, F, Ripoll, T, Fonteles Ritt, L, Roberts, D, Pascual, C, Briones, I, Reyes, H, Roelke, M, Roman, M, Romeo, F, Ronner, E, Ronziere, T, Rooyer, F, Rosenbaum, D, Roth, S, Rozkova, N, Rubacek, M, Rubalcava, F, Rubanenko, O, Rubin, A, Borret, M, Rybak, K, Sabbour, H, Morales, O, Sakai, T, Salacata, A, Salecker, I, Salem, A, Salfity, M, Salguero, R, Salvioni, A, Samson, M, Sanchez, G, Sandesara, C, Saporito, W, Sasaoka, T, Sattar, P, Savard, D, Scala, P, Scemama, J, Schaupp, T, Schellinger, P, Scherr, C, Schmitz, K, Schmitz, B, Schmitz, L, Schnitzler, R, Schnupp, S, Schoeniger, P, Schön, N, Schuster, S, Schwimmbeck, P, Seamark, C, Seebass, R, Seidl, K, Seidman, B, Sek, J, Sekaran, L, Seko, Y, Sepulveda Varela, P, Sevilla, B, Shah, V, Shah, A, Shah, N, Shanes, J, Sharareh, A, Sharma, V, Shaw, L, Shimizu, Y, Shimomura, H, Shin, D, Shin, E, Shite, J, Shoukfeh, M, Shoultz, C, Silver, F, Sime, I, Simmers, T, Singal, D, Singh, N, Siostrzonek, P, Sirajuddin, M, Skeppholm, M, Smadja, D, Smith, R, Smith, D, Soda, H, Sofley, C, Sokal, A, Sotolongo, R, de Souza, O, Sparby, J, Spinar, J, Sprigings, D, Spyropoulos, A, Stakos, D, Steinberg, A, Steinwender, C, Stergiou, G, Stites, H, Stoikov, A, Strasser, R, Streb, W, Styliadis, I, Su, G, Su, X, Suarez, R, Sudnik, W, Sueyoshi, A, Sukles, K, Sun, L, Suneja, R, Svensson, P, Ziekenhuis, A, Szavits Nossan, J, Taggeselle, J, Takagi, Y, Takhar, A, Tallet, J, Tamm, A, Tanaka, S, Tanaka, K, Tang, A, Tang, S, Tassinari, T, Tayama, S, Tayebjee, M, Tebbe, U, Teixeira, J, Tesloianu, D, Tessier, P, The, S, Thevenin, J, Thomas, H, Timsit, S, Topkis, R, Torosoff, M, Touze, E, Traissac, T, Trendafilova, E, Troyan, B, Tsai, W, Tse, H, Tsutsui, H, Tsutsui, T, Tuininga, Y, Turakhia, M, Turk, S, Turner, W, Tveit, A, Twiddy, S, Tytus, R, Ukrainski, G, Valdovinos Chavez, S, Van De Graaff, E, Vanacker, P, Vardas, P, Vargas, M, Vassilikos, V, Vazquez, J, Venkataraman, A, Verdecchia, P, Vester, E, Vial, H, Vinereanu, D, Vlastaris, A, Vogel, C, vom Dahl, J, von Mering, M, Vora, K, Wakefield, P, Walia, J, Walter, T, Wang, M, Wang, N, Wang, F, Wang, X, Wang, Z, Wang, K, Watanabe, K, Wei, J, Weimar, C, Weinrich, R, Wen, M, Wheelan, K, Wicke, J, Wiemer, M, Wild, B, Wilke, A, Willems, S, Williams, M, Williams, D, Winkler, A, Wirtz, J, Witzenbichler, B, Wong, D, Lawrence Wong, K, Wong, B, Wozakowska Kaplon, B, Wu, Z, Wu, S, Wyatt, N, Xu, Y, Xu, X, Yamada, A, Yamamoto, K, Yamanoue, H, Yamashita, T, Bryan Yan, P, Yang, Y, Yang, T, Yao, J, Yarlagadda, C, Yeh, K, Yotov, Y, Yvorra, S, Zahn, R, Zamorano, J, Zanini, R, Zarich, S, Zebrack, J, Zenin, S, Zeuthen, E, Zhang, X, Zhang, Q, Zhang, D, Zhang, H, Zhao, S, Zhao, X, Zheng, Y, Zheng, Q, Zhou, J, Zimmermann, S, Zimmermann, R, Zukerman, L, Zwaan van der, C, Zwaan van der, C., and ANNONI, GIORGIO
- Abstract
Background GLORIA-AF (Global Registry on Long-Term Oral Antithrombotic Treatment in Patients with Atrial Fibrillation) is a prospective, global registry program describing antithrombotic treatment patterns in patients with newly diagnosed nonvalvular atrial fibrillation at risk of stroke. Phase 2 began when dabigatran, the first non–vitamin K antagonist oral anticoagulant (NOAC), became available. Objectives This study sought to describe phase 2 baseline data and compare these with the pre-NOAC era collected during phase 1. Methods During phase 2, 15,641 consenting patients were enrolled (November 2011 to December 2014); 15,092 were eligible. This pre-specified cross-sectional analysis describes eligible patients’ baseline characteristics. Atrial fibrillation disease characteristics, medical outcomes, and concomitant diseases and medications were collected. Data were analyzed using descriptive statistics. Results Of the total patients, 45.5% were female; median age was 71 (interquartile range: 64, 78) years. Patients were from Europe (47.1%), North America (22.5%), Asia (20.3%), Latin America (6.0%), and the Middle East/Africa (4.0%). Most had high stroke risk (CHA2DS2-VASc [Congestive heart failure, Hypertension, Age ≥75 years, Diabetes mellitus, previous Stroke, Vascular disease, Age 65 to 74 years, Sex category] score ≥2; 86.1%); 13.9% had moderate risk (CHA2DS2-VASc = 1). Overall, 79.9% received oral anticoagulants, of whom 47.6% received NOAC and 32.3% vitamin K antagonists (VKA); 12.1% received antiplatelet agents; 7.8% received no antithrombotic treatment. For comparison, the proportion of phase 1 patients (of N = 1,063 all eligible) prescribed VKA was 32.8%, acetylsalicylic acid 41.7%, and no therapy 20.2%. In Europe in phase 2, treatment with NOAC was more common than VKA (52.3% and 37.8%, respectively); 6.0% of patients received antiplatelet treatment; and 3.8% received no antithrombotic treatment. In North America, 52.1%, 26.2%, and 14.0% of patients rece
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- 2017
5. Properties of surface layers formed on lithium in Li-SOCl2 cells: synergetic effect of SO2 and LiAl(SO3Cl)4
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Chenebault, P., Vallin, D., Thevenin, J., and Wiart, R.
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- 1988
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6. Impedance analysis of the lithium discharge in Li-SOCl2 cells: Synergetic effect of SO2 and LiAl(SO3Cl)4
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Chenebault, P., Vallin, D., Thevenin, J., and Wiart, R.
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- 1989
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7. Control of pancreatic bile-salt-dependent-lipase secretion by the glucose-regulated protein of 94 kDa (Grp94)
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Nganga, A, Bruneau, N, Sbarra, V, Lombardo, D, and Le Petit-Thevenin, J
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Base Sequence ,Lactams, Macrocyclic ,Quinones ,Down-Regulation ,Membrane Proteins ,Sterol Esterase ,Transfection ,Rats ,Substrate Specificity ,Butyrates ,Kinetics ,Protein Transport ,Enzyme Stability ,Benzoquinones ,Tumor Cells, Cultured ,Animals ,Nucleic Acid Conformation ,HSP70 Heat-Shock Proteins ,RNA, Catalytic ,RNA, Messenger ,Pancreas ,Ubiquitins ,Research Article ,Protein Binding - Abstract
Bile-salt-dependent lipase (BSDL; EC 3.1.1.13) is an enzyme expressed by the pancreatic acinar cell and secreted as a component of the pancreatic juice. During its route towards secretion, BSDL is associated with intracellular membranes by means of a multiprotein folding complex, which includes the glucose-regulated protein of 94 kDa (Grp94). We have postulated that the association of BSDL with membranes is required for the complete O-glycosylation of the protein, which diverts BSDL from a degradation route and consequently allows its secretion. To further characterize the role of Grp94 in BSDL secretion, we have studied the effect of a ribozyme specifically targeted to Grp94 mRNA. This ribozyme has been transfected into AR4-2J cells, and we have shown that a decrease in Grp94 expression leads to a concomitant decrease in BSDL secretion and expression. Geldanamycin (GA), which alters Grp94 functions, also affects the release of BSDL into the culture medium of AR4-2J cells. BSDL expressed in GA-treated AR4-2J cells is unstable. Furthermore, under conditions that decrease the level of BSDL secretion, no intracellular accumulation of the enzyme was observed, suggesting that BSDL that cannot associate with (or be structured by) Grp94 could be rapidly degraded. We have further shown that this degradation probably occurs via the ubiquitin-dependent pathway. Altogether, these results indicate that Grp94 has a pivotal role in BSDL folding and in the sorting of this pancreatic enzyme.
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- 2000
8. Discovery and mapping of a new expressed sequence tag-single nucleotide polymorphism and simple sequence repeat panel for large-scale genetic studies and breeding of Theobroma cacao L.
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Allegre, M., primary, Argout, X., additional, Boccara, M., additional, Fouet, O., additional, Roguet, Y., additional, Berard, A., additional, Thevenin, J. M., additional, Chauveau, A., additional, Rivallan, R., additional, Clement, D., additional, Courtois, B., additional, Gramacho, K., additional, Boland-Auge, A., additional, Tahi, M., additional, Umaharan, P., additional, Brunel, D., additional, and Lanaud, C., additional
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- 2011
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9. Purification, Cloning and Functional Characterization of an Endogenous beta-Glucuronidase in Arabidopsis thaliana
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Eudes, A., primary, Mouille, G., additional, Thevenin, J., additional, Goyallon, A., additional, Minic, Z., additional, and Jouanin, L., additional
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- 2008
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10. Relationships Between Black Pod and Witches'-Broom Diseases in Theobroma cacao
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Thevenin, J.-M., primary, Umaharan, R., additional, Surujdeo-Maharaj, S., additional, Latchman, B., additional, Cilas, C., additional, and Butler, D. R., additional
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- 2005
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11. État de l'art des techniques de dosimétrie individuelle et analyse des besoins
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Rannou, A., primary, Barthe, J., additional, Aubert, B., additional, Brégeon, B., additional, Champlong, J., additional, Colson, P., additional, Espagnan, M., additional, Herbaut, Y., additional, Thevenin, J. C., additional, and Valero, M., additional
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- 1998
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12. Transient forced convection heat transfer from a circular cylinder embedded in a porous medium
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Thevenin, J., primary
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- 1995
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13. About enhancement of heat transfer over a circular cylinder embedded in a porous medium
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Thevenin, J., primary and Sadaoui, D., additional
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- 1995
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14. Impedance analysis of the lithium discharge in Li-SOCl2 cells: Synergetic effect of SO2 and LiAl(SO3Cl)4
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Chenebault, P., Vallin, D., Thevenin, J., and Wiart, R.
- Abstract
A study of the anodic discharge of the Li electrode in LiAlCl
4 /SOCl2 electrolyte shows the occurrence of a diffusion process mainly when the surface layer was formed in the presence of the inorganic additives SO2 and LiAl(SO3 Cl)4 . A model of the electrode kinetics is proposed on the assumption that the ionic diffusion is hindered by the precipitation of the solute LiAlCl4 at the bottom of holes formed in the compact polycrystalline LiCl surface layer by a dissolution-dilation mechanism.- Published
- 1989
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15. Properties of surface layers formed on lithium in Li-SOCl2 cells: synergetic effect of SO2 and LiAl(SO3Cl)4
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Chenebault, P., Vallin, D., Thevenin, J., and Wiart, R.
- Abstract
Kinetic and morphological properties of surface layers formed on the Li anode during storage in SOCl
2 /LiAlCl4 solution have been investigated. The synergetic effect of SO2 and LiAl(SO3 Cl)4 , used for voltage delay alleviation, changes the shape and size of the microcrystals of LiCl constituting the surface layer. It also leads to separate and modify the conduction and charge transfer processes involved in the kinetic properties of the surface layer at the equilibrium potential. These properties appear to be similar to those of a polycrystalline solid electrolyte where the grain boundaries induce an intergranular conduction process.- Published
- 1988
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16. Rapport IV.8. Évolution de la qualité de l’eau de Seine à l’amont de Paris
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Thevenin, J. and Plisson, A.
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More than the half of superficial water resources used for the parisian area supply comes from the river Seine upstream of Paris. Now, a tendency of the water pollution worseniny was noted, that led to several studies (Technical Department of the City of Paris, Setude, Safege). The present report states more particularly the content of the study ordered by the Seine-Normandy Basin Agency and carried out by Safege. This study put forward the following points : — necessary reagent doses for treatment are constantly increasing ; — treatment processes become more and more complicated ; — such an evolution is made necessary owing to worsening of the river Seine water quality, particularly characterized with a decrease of the water resistivity and an increase of its ammonia content. In conclusion, the report points out the required measures for protecting the drinkable water quality, supplied from the river Seine upstream of Paris., Plus de la moitié des ressources en eau superficielle utilisées pour l’alimentation de la région parisienne proviennent de la Seine à l’amont de Paris. Or on constate une tendance à l’aggravation de la pollution de l’eau, qui a motivé plusieurs études (Services Techniques de la Ville de Paris, SETUDE, SAFEGE). Le rapport expose plus particulièrement le contenu de l’étude effectuée par la SAFEGE à la demande de l’Agence de Bassin Seine Normandie. Cette étude a mis en évidence les points suivants : — les taux de réactifs nécessaires au traitement sont en augmentation constante ; — les chaînes de traitement deviennent de plus en plus complexes ; — cette évolution est rendue nécessaire par la dégradation de la qualité d’eau de Seine, marquée en particulier par une baisse de la résistivité et un accroissement de la teneur en ammoniac. Le rapport conclut en indiquant les mesures nécessaires pour que puisse être préservée la qualité de l’eau potable produite à partir de la Seine à l’amont de Paris., Thevenin J., Plisson A. Rapport IV.8. Évolution de la qualité de l’eau de Seine à l’amont de Paris. In: Influence des activités de l'homme sur le cycle hydrométéorologique. Compte-rendu des treizièmes journées de l'hydraulique. Paris, 16-18 septembre 1974. Tome 2, 1975.
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- 1975
17. On the processes responsible for the degradation of the aluminium-lithium electrode used as anode material in lithium aprotic electrolyte batteries
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Garreau, M., primary, Thevenin, J., additional, and Fekir, M., additional
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- 1983
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18. A study of the properties of the surface layers formed on lithium electrodes in sulfolane-based electrolytes (extended abstract)
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Fouache, S., primary, Garreau, M., additional, and Thevenin, J., additional
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- 1989
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19. Passivating films on lithium electrodes. An approach by means of electrode impedance spectroscopy
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Thevenin, J., primary
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- 1985
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20. Study by electrode impedance spectroscopy of the properties of lithium surface layers in aprotic organic electrolytes (extended abstract)
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Dubois, C., primary, De Guibert, A., additional, and Thevenin, J., additional
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- 1989
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21. Postoperative ileus after digestive surgery: Network meta-analysis of pharmacological intervention.
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Buscail E, Planchamp T, Le Cosquer G, Bouchet M, Thevenin J, Carrere N, Muscari F, Abbo O, Maulat C, Weyl A, Duffas JP, Philis A, Ghouti L, Canivet C, Motta JP, Vergnolle N, Deraison C, and Shourick J
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- Humans, Network Meta-Analysis, Postoperative Complications drug therapy, Postoperative Complications etiology, Postoperative Complications prevention & control, Narcotic Antagonists, Ileus drug therapy, Ileus etiology, Ileus prevention & control
- Abstract
Aims: Several medicinal treatments for avoiding postoperative ileus (POI) after abdominal surgery have been evaluated in randomized controlled trials (RCTs). This network meta-analysis aimed to explore the relative effectiveness of these different treatments on ileus outcome measures., Methods: A systematic literature review was performed to identify RCTs comparing treatments for POI following abdominal surgery. A Bayesian network meta-analysis was performed. Direct and indirect comparisons of all regimens were simultaneously compared using random-effects network meta-analysis., Results: A total of 38 RCTs were included in this network meta-analysis reporting on 6371 patients. Our network meta-analysis shows that prokinetics significantly reduce the duration of first gas (mean difference [MD] = 16 h; credible interval -30, -3.1; surface under the cumulative ranking curve [SUCRA] 0.418), duration of first bowel movements (MD = 25 h; credible interval -39, -11; SUCRA 0.25) and duration of postoperative hospitalization (MD -1.9 h; credible interval -3.8, -0.040; SUCRA 0.34). Opioid antagonists are the only treatment that significantly improve the duration of food recovery (MD -19 h; credible interval -26, -14; SUCRA 0.163)., Conclusion: Based on our meta-analysis, the 2 most consistent pharmacological treatments able to effectively reduce POI after abdominal surgery are prokinetics and opioid antagonists. The absence of clear superiority of 1 treatment over another highlights the limits of the pharmacological principles available., (© 2023 The Authors. British Journal of Clinical Pharmacology published by John Wiley & Sons Ltd on behalf of British Pharmacological Society.)
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- 2024
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22. The hepatokine FGL1 regulates hepcidin and iron metabolism during the recovery from hemorrhage-induced anemia in mice.
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Sardo U, Perrier P, Cormier K, Sotin M, Desquesnes A, Cannizzo L, Ruiz-Martinez M, Thevenin J, Billoré B, Jung G, Abboud E, Peyssonnaux C, Nemeth E, Ginzburg YZ, Ganz T, and Kautz L
- Abstract
As a functional component of erythrocyte hemoglobin, iron is essential for oxygen delivery to all tissues in the body. The liver-derived peptide hepcidin is the master regulator of iron homeostasis. During anemia, the erythroid hormone erythroferrone regulates hepcidin synthesis to ensure adequate supply of iron to the bone marrow for red blood cells production. However, mounting evidence suggested that another factor may exert a similar function. We identified the hepatokine FGL1 as a previously undescribed suppressor of hepcidin that is induced in the liver in response to hypoxia during the recovery from anemia and in thalassemic mice. We demonstrated that FGL1 is a potent suppressor of hepcidin in vitro and in vivo . Deletion of Fgl1 in mice results in a blunted repression of hepcidin after bleeding. FGL1 exerts its activity by direct binding to BMP6, thereby inhibiting the canonical BMP-SMAD signaling cascade that controls hepcidin transcription., Key Points: 1/ FGL1 regulates iron metabolism during the recovery from anemia. 2/ FGL1 is an antagonist of the BMP/SMAD signaling pathway.
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- 2023
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23. In vitro angiogenic effects of pancreatic bile salt-dependent lipase.
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Rebaï O, Le Petit-Thevenin J, Bruneau N, Lombardo D, and Vérine A
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- Animals, Cell Division drug effects, Cells, Cultured drug effects, Chemotaxis drug effects, Collagen, DNA Replication drug effects, Drug Combinations, Endothelium, Vascular cytology, Extracellular Matrix drug effects, Extracellular Matrix metabolism, Fibroblast Growth Factor 2 metabolism, Humans, Laminin, MAP Kinase Signaling System drug effects, Macaca fascicularis, Neovascularization, Physiologic physiology, Pancreas enzymology, Phosphorylation drug effects, Protein Processing, Post-Translational drug effects, Proteoglycans, Umbilical Veins, Vascular Endothelial Growth Factor A metabolism, Wound Healing, Endothelial Cells drug effects, Neovascularization, Physiologic drug effects, Sterol Esterase pharmacology
- Abstract
Objective: Bile salt-dependent lipase (BSDL), a lipolytic enzyme secreted in the duodenum by pancreatic acinar cells, has been detected in the serum of all patients and in atheromatous plaque, suggesting its potential implication in vascular pathophysiology., Methods and Results: In vitro pancreatic BSDL evokes human umbilical vein endothelial cell (HUVEC) proliferation and chemotactic migration. BSDL at mitogen concentration is capable to heal wounded HUVEC monolayer and to promote capillary network formation. HUVEC proliferation depends on the displacement of basic fibroblast growth factor and vascular endothelial growth factor from the extracellular matrix and the activation of extracellular signal-regulated kinases (ERK1/2), p38 mitogen-activated protein kinase, and focal adhesion kinase signaling pathways., Conclusions: For the first time to our knowledge, it is suggested that circulating BSDL could be involved in pathophysiological angiogenesis. We delineate the in vitro effects of pancreatic BSDL on endothelial cells, and we show that BSDL promotes proliferation, migration, capillary network formation, and wound-healing of HUVECs via the displacement of bFGF and VEGF from the ECM, suggesting that BSDL could be involved in angiogenesis.
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- 2005
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24. Phosphorylation of the oncofetal variant of the human bile salt-dependent lipase. identification of phosphorylation site and relation with secretion process.
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Verine A, Le Petit-Thevenin J, Panicot-Dubois L, Valette A, and Lombardo D
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- Animals, Base Sequence, CHO Cells, Carrier Proteins chemistry, Carrier Proteins genetics, Cricetinae, DNA Primers, DNA, Complementary, Glycoproteins chemistry, Glycoproteins genetics, Humans, Mutagenesis, Site-Directed, Phosphorylation, Sterol Esterase chemistry, Threonine metabolism, Transfection, Carrier Proteins metabolism, Glycoproteins metabolism, Lipase, Sterol Esterase metabolism
- Abstract
In this paper, we report, for the first time, the localization of the phosphorylation site of the fetoacinar pancreatic protein (FAPP), which is an oncofetal variant of the pancreatic bile salt-dependent lipase. Using Chinese hamster ovary (CHO) cells transfected with the cDNA encoding FAPP, we radiolabeled the enzyme with (32)P, and then the protein was purified by affinity chromatography on cholate-immobilized Sepharose column and submitted to a CNBr hydrolysis. Analysis of peptides by high pressure liquid chromatography, associated with the radioactivity profile, revealed that the phosphorylation site is located at threonine 340. Site-specific mutagenesis experiments, in which the threonine was replaced by an alanine residue, were used to invalidate the phosphorylation of FAPP and to study the influence of the modification on the activity and secretion of the enzyme. These studies showed that CHO cells, transfected with the mutated cDNA of FAPP, kept all of their ability to synthesize the protein, but the loss of the phosphorylation motif prevented the release of the protein in the extracellular compartment. However, the mutated enzyme, which was sequestrated in the transfected CHO cells, remains active on bile salt-dependent lipase substrates.
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- 2001
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25. Control of pancreatic bile-salt-dependent-lipase secretion by the glucose-regulated protein of 94 kDa (Grp94).
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Nganga A, Bruneau N, Sbarra V, Lombardo D, and Le Petit-Thevenin J
- Subjects
- Animals, Base Sequence, Benzoquinones, Butyrates pharmacology, Down-Regulation, Enzyme Stability drug effects, HSP70 Heat-Shock Proteins genetics, Kinetics, Lactams, Macrocyclic, Membrane Proteins genetics, Nucleic Acid Conformation, Pancreas cytology, Pancreas drug effects, Pancreas metabolism, Protein Binding drug effects, Protein Transport drug effects, Quinones pharmacology, RNA, Catalytic chemistry, RNA, Catalytic genetics, RNA, Catalytic metabolism, RNA, Messenger genetics, RNA, Messenger metabolism, Rats, Substrate Specificity, Transfection, Tumor Cells, Cultured, Ubiquitins metabolism, HSP70 Heat-Shock Proteins metabolism, Membrane Proteins metabolism, Sterol Esterase metabolism
- Abstract
Bile-salt-dependent lipase (BSDL; EC 3.1.1.13) is an enzyme expressed by the pancreatic acinar cell and secreted as a component of the pancreatic juice. During its route towards secretion, BSDL is associated with intracellular membranes by means of a multiprotein folding complex, which includes the glucose-regulated protein of 94 kDa (Grp94). We have postulated that the association of BSDL with membranes is required for the complete O-glycosylation of the protein, which diverts BSDL from a degradation route and consequently allows its secretion. To further characterize the role of Grp94 in BSDL secretion, we have studied the effect of a ribozyme specifically targeted to Grp94 mRNA. This ribozyme has been transfected into AR4-2J cells, and we have shown that a decrease in Grp94 expression leads to a concomitant decrease in BSDL secretion and expression. Geldanamycin (GA), which alters Grp94 functions, also affects the release of BSDL into the culture medium of AR4-2J cells. BSDL expressed in GA-treated AR4-2J cells is unstable. Furthermore, under conditions that decrease the level of BSDL secretion, no intracellular accumulation of the enzyme was observed, suggesting that BSDL that cannot associate with (or be structured by) Grp94 could be rapidly degraded. We have further shown that this degradation probably occurs via the ubiquitin-dependent pathway. Altogether, these results indicate that Grp94 has a pivotal role in BSDL folding and in the sorting of this pancreatic enzyme.
- Published
- 2000
26. Immunodetection and molecular cloning of a bile-salt-dependent lipase isoform in HepG2 cells.
- Author
-
Vérine A, Bruneau N, Valette A, Le Petit-Thevenin J, Pasqualini E, and Lombardo D
- Subjects
- Amino Acid Sequence, Base Sequence, Bile Acids and Salts pharmacology, Blotting, Western, Cloning, Molecular, Cross Reactions, Cytosol drug effects, Cytosol enzymology, Humans, Isoenzymes chemistry, Isoenzymes genetics, Isoenzymes immunology, Isoenzymes metabolism, Liver Neoplasms enzymology, Microsomes, Liver drug effects, Molecular Sequence Data, Molecular Weight, Pancreas enzymology, Protein Biosynthesis, RNA, Messenger analysis, RNA, Messenger genetics, Sterol Esterase chemistry, Sterol Esterase immunology, Tumor Cells, Cultured, Microsomes, Liver enzymology, Sterol Esterase genetics, Sterol Esterase metabolism
- Abstract
In this article, we report the nucleotide sequence of the cDNA encoding an isoform of bile-salt-dependent lipase (BSDL) expressed by human hepatoma cells. The BSDL is a 100-kDa glycoprotein normally expressed by the human pancreas. Using a polyclonal antibody raised against an internal peptide located between Ile(327) and Glu(350) of the human pancreatic BSDL, we have immunodetected an isoform of human pancreatic BSDL, with an apparent molecular mass of about 62 kDa. This isoform of BSDL was mainly associated with the cytosol of a human hepatoma cell line (HepG2), the remaining protein being found in the microsome fraction. In addition, esterolytic activity on p-nitrophenyl hexanoate measured in microsomes and cytosol appeared very low and was weakly stimulated by bile salts, such as taurocholate. In contrast to human pancreatic BSDL, which is secreted as a component of pancreatic juice, this isoform appeared to be retained in the HepG2 cells. Reverse transcription, followed by PCR and amplification, performed on RNA extracted from HepG2 cells using specific primers hybridizing to the sequence coding for the entire normal human pancreatic BSDL, allowed us to amplify a 1. 7-kb transcript that appeared to be 0.5 kb shorter than the transcript of the pancreatic enzyme (2.2 kb). From the sequence of the transcript thus obtained, a protein with a molecular mass of 62 kDa might be predicted, which is in good agreement with the size of the isoform of BSDL immunodetected in HepG2 cells. The N-terminal amino-acid sequence, deduced from the 1.7-kb transcript sequence, matched that of the pancreatic BSDL. However, the C-terminal domain appeared truncated, bearing only a single mucin-like sequence compared with sixteen for the human pancreatic BSDL. The actual intracellular function of this human BSDL hepatoma isoform remains to be elucidated.
- Published
- 1999
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