191 results on '"Meco, M."'
Search Results
2. P108 FIVE YEARS RESULTS OF BIORESORBABLE VASCULAR SCAFFOLDS VERSUS CONVENTIONAL DRUG–ELUTING STENTS. A META–ANALYSIS OF RANDOMIZED CONTROLLED TRIALS
- Author
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Meco, M, primary, Guido, B, additional, Fouladvand, F, additional, and Agosteo, E, additional
- Published
- 2023
- Full Text
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3. P100 RENAL DENERVATION FOR ATRIAL FIBRILLATION IN DRUG–RESISTANT HYPERTENSIVE PATIENTS. AN UPDATED META–ANALYSIS OF RANDOMIZED CONTROLLED TRIALS
- Author
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Meco, M, primary, Belli, G, additional, Fouladvand, F, additional, and Agosteo, E, additional
- Published
- 2023
- Full Text
- View/download PDF
4. P386 ATRIAL FIBRILLATION ABLATION IN PATIENTS WITH SEVERELY DEPRESSED EJECTION FRACTION. META–ANALYSIS OF RANDOMIZED CONTROLLED TRIALS
- Author
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Meco, M, primary, Belli, G, additional, Fouladvand, F, additional, and Agosteo, E, additional
- Published
- 2023
- Full Text
- View/download PDF
5. A new and simple method for the correct localization of the intra-aortic balloon: the celiac artery Doppler ultrasound
- Author
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Meco, M., Caratti, A., and Cirri, S.
- Published
- 2011
- Full Text
- View/download PDF
6. Erratum to: Guidelines for the use and interpretation of assays for monitoring autophagy (3rd edition) (Autophagy, 12, 1, 1-222, 10.1080/15548627.2015.1100356
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Klionsky, D. J., Abdelmohsen, K., Abe, A., Abedin, M. J., Abeliovich, H., Arozena, A. A., Adachi, H., Adams, C. M., Adams, P. D., Adeli, K., Adhihetty, P. J., Adler, S. G., Agam, G., Agarwal, R., Aghi, M. K., Agnello, M., Agostinis, P., Aguilar, P. V., Aguirre-Ghiso, J., Airoldi, E. M., Ait-Si-Ali, S., Akematsu, T., Akporiaye, E. T., Al-Rubeai, M., Albaiceta, G. M., Albanese, C., Albani, D., Albert, M. L., Aldudo, J., Algül, H., Alirezaei, M., Alloza, I., Almasan, A., Almonte-Beceril, M., Alnemri, E. S., Alonso, C., Altan-Bonnet, N., Altieri, D. C., Alvarez, S., Alvarez-Erviti, L., Alves, S., Amadoro, G., Amano, A., Amantini, C., Ambrosio, S., Amelio, I., Amer, A. O., Amessou, M., Amon, A., An, Z., Anania, F. A., Andersen, S. U., Andley, U. P., Andreadi, C. K., Andrieu-Abadie, N., Anel, A., Ann, D. K., Anoopkumar-Dukie, S., Antonioli, M., Aoki, H., Apostolova, N., Aquila, S., Aquilano, K., Araki, K., Arama, E., Aranda, A., Araya, J., Arcaro, A., Arias, E., Arimoto, H., Ariosa, A. R., Armstrong, J. L., Arnould, T., Arsov, I., Asanuma, K., Askanas, V., Asselin, E., Atarashi, R., Atherton, S. S., Atkin, J. D., Attardi, L. D., Auberger, P., Auburger, G., Aurelian, L., Autelli, R., Avagliano, L., Avantaggiati, M. L., Avrahami, L., Azad, N., Awale, S., Bachetti, T., Backer, J. M., Bae, D. -H., Bae, J. -S., Bae, O. -N., Bae, S. H., Baehrecke, E. H., Baek, S. -H., Baghdiguian, S., Bagniewska-Zadworna, A., Bai, H., Bai, J., Bai, X. -Y., Bailly, Y., Balaji, K. N., Balduini, W., Ballabio, A., Balzan, R., Banerjee, R., Bánhegyi, G., Bao, H., Barbeau, B., Barrachina, M. D., Barreiro, E., Bartel, B., Bartolomé, A., Bassham, D. C., Bassi, M. T., Bast, R. C., J, R., Basu, A., Batista, M. T., Batoko, H., Battino, M., Bauckman, K., Baumgarner, B. L., Bayer, K. U., Beale, R., Beaulieu, J. -F., Beck, G. R., Becker, C., Beckham, J. D., Bédard, P. -A., Bednarski, P. J., Begley, T. J., Behl, C., Behrends, C., Behrens, G. M. N., Behrns, K. 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T., Chuang, T. -H., Chun, T., Chung, H., Chung, T., Chung, Y. -L., Chwae, Y. -J., Cianfanelli, V., Ciarcia, R., Ciechomska, I. A., Ciriolo, M. R., Cirone, M., Claerhout, S., Clague, M. J., Cl� ria, J., Clarke, P. G. H., Clarke, R., Clementi, E., Cleyrat, C., Cnop, M., Coccia, E. M., Cocco, T., Codogno, P., Coers, J., Cohen, E. E. W., Colecchia, D., Coletto, L., Coll, N. S., Colucci-Guyon, E., Comincini, S., Condello, M., Cook, K. L., Coombs, G. H., Cooper, C. D., Cooper, J. M., Coppens, I., Corasaniti, M. T., Corazzari, M., Corbalan, R., Corcelle-Termeau, E., Cordero, M. D., Corral-Ramos, C., Corti, O., Cossarizza, A., Costelli, P., Costes, S., Cotman, S. L., Coto-Montes, A., Cottet, S., Couve, E., Covey, L. R., Cowart, L. A., Cox, J. S., Coxon, F. P., Coyne, C. B., Cragg, M. S., Craven, R. J., Crepaldi, T., Crespo, J. L., Criollo, A., Crippa, V., Cruz, M. T., Cuervo, A. M., Cuezva, J. M., Cui, T., Cutillas, P. R., Czaja, M. J., Czyzyk-Krzeska, M. F., Dagda, R. K., Dahmen, U., Dai, C., Dai, W., Dai, Y., Dalby, K. N., Valle, L. D., Dalmasso, G., D'Amelio, M., Damme, M., Darfeuille-Michaud, A., Dargemont, C., Darley-Usmar, V. M., Dasarathy, S., Dasgupta, B., Dash, S., Dass, C. R., Davey, H. M., Davids, L. M., Dávila, D., Davis, R. J., Dawson, T. M., Dawson, V. L., Daza, P., de Belleroche, J., de Figueiredo, P., de Figueiredo, R. C. B. Q., de la Fuente, J., De Martino, L., De Matteis, A., De Meyer, G. R. Y., De Milito, A., De Santi, M., de Souza, W., De Tata, V., De Zio, D., Debnath, J., Dechant, R., Decuypere, J. -P., Deegan, S., Dehay, B., Del Bello, B., Del Re, D. P., Delage-Mourroux, R., Delbridge, L. M. D., Deldicque, L., Delorme-Axford, E., Deng, Y., Dengjel, J., Denizot, M., Dent, P., Der, C. J., Deretic, V., Derrien, B., Deutsch, E., Devarenne, T. P., Devenish, R. J., Di Bartolomeo, S., Di Daniele, N., Di Domenico, F., Di Nardo, A., Di Paola, S., Di Pietro, A., Di Renzo, L., Di Antonio, A., Díaz-Araya, G., Díaz-Laviada, I., Diaz-Meco, M. T., Diaz-Nido, J., Dickey, C. A., Dickson, R. C., Diederich, M., Digard, P., Dikic, I., Dinesh-Kumar, S. P., Ding, C., Ding, W. -X., Ding, Z., Dini, L., Distler, J. H. W., Diwan, A., Djavaheri-Mergny, M., Dmytruk, K., Dobson, R. C. J., Doetsch, V., Dokladny, K., Dokudovskaya, S., Donadelli, M., Dong, X. C., Dong, X., Dong, Z., Donohue, T. M., Donohue-Jr, T. M., Doran, K. S., D'Orazi, G., Dorn, G. W., Dosenko, V., Dridi, S., Drucker, L., Du, J., L. -L., Du, Du, L., du Toit, A., Dua, P., Duan, L., Duann, P., Dubey, V. K., Duchen, M. R., Duchosal, M. A., Duez, H., Dugail, I., Dumit, V. I., Duncan, M. C., Dunlop, E. A., Dunn, W. A., Dupont, N., Dupuis, L., Durán, R. V., Durcan, T. M., Duvezin-Caubet, S., Duvvuri, U., Eapen, V., Ebrahimi-Fakhari, D., Echard, A., Eckhart, L., Edelstein, C. L., Edinger, A. L., Eichinger, L., Eisenberg, T., Eisenberg-Lerner, A., Eissa, N. T., El-Deiry, W. S., El-Khoury, V., Elazar, Z., Eldar-Finkelman, H., Elliott, C. J. H., Emanuele, E., Emmenegger, U., Engedal, N., Engelbrecht, A. -M., Engelender, S., Enserink, J. M., Erdmann, R., Erenpreisa, J., Eri, R., Eriksen, J. L., Erman, A., Escalante, R., Eskelinen, E. -L., Espert, L., Esteban-Martínez, L., Evans, T. J., Fabri, M., Fabrias, G., Fabrizi, C., Facchiano, A., Færgeman, N. J., Faggioni, A., Fairlie, W. D., Fan, C., Fan, D., Fan, J., Fang, S., Fanto, M., Fanzani, A., Farkas, T., Faure, M., Favier, F. B., Fearnhead, H., Federici, M., Fei, E., Felizardo, T. C., Feng, H., Feng, Y., Ferguson, T. A., Fernández, Á. F., Fernandez-Barrena, M. G., Fernandez-Checa, J. C., Fernández-López, A., Fernandez-Zapico, M. E., Feron, O., Ferraro, E., Ferreira-Halder, C. V., Fesus, L., Feuer, R., Fiesel, F. C., Filippi-Chiela, E. C., Filomeni, G., Fimia, G. M., Fingert, J. 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A., Geng, J., Genschik, P., Gerner, L., Gestwicki, J. E., Gewirtz, D. A., Ghavami, S., Ghigo, E., Ghosh, D., Giammarioli, A. M., Giampieri, F., Giampietri, C., Giatromanolaki, A., Gibbings, D. J., Gibellini, L., Gibson, S. B., Ginet, V., Giordano, A., Giorgini, F., Giovannetti, E., Girardin, S. E., Gispert, S., Giuliano, S., Gladson, C. L., Glavic, A., Gleave, M., Godefroy, N., Gogal, R. M., Gokulan, K., Goldman, G. H., Goletti, D., Goligorsky, M. S., Gomes, A. V., Gomes, L. C., Gomez, H., Gomez-Manzano, C., Gómez-Sánchez, R., Gonçalves, D. A. P., Goncu, E., Gong, Q., Gongora, C., Gonzalez, C. B., Gonzalez-Alegre, P., Gonzalez-Cabo, P., González-Polo, R. A., Goping, I. S., Gorbea, C., Gorbunov, N. V., Goring, D. R., Gorman, A. M., Gorski, S. M., Goruppi, S., Goto-Yamada, S., Gotor, C., Gottlieb, R. A., Gozes, I., Gozuacik, D., Graba, Y., Graef, M., Granato, G. E., Grant, G. D., Grant, S., Gravina, G. L., Green, D. R., Greenhough, A., Greenwood, M. 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R., Higaki, K., Hilfiker, S., Hill, B. G., Hill, J. A., Hill, W. D., Hino, K., Hofius, D., Hofman, P., Höglinger, G. U., Höhfeld, J., Holz, M. K., Hong, Y., Hood, D. A., Hoozemans, J. J. M., Hoppe, T., Hsu, C., Hsu, C. -Y., Hsu, L. -C., Hu, D., Hu, G., H. -M., Hu, Hu, H., M. C., Hu, Y. -C., Hu, Z. -W., Hu, Hua, F., Hua, Y., Huang, C., Huang, H. -L., Huang, K. -H., Huang, K. -Y., Huang, S., Huang, W. -P., Huang, Y. -R., Huang, Y., Huber, T. B., Huebbe, P., Huh, W. -K., Hulmi, J. J., Hur, G. M., Hurley, J. H., Husak, Z., Hussain, S. N. A., Hussain, S., Hwang, J. J., Hwang, S., Hwang, T. I. S., Ichihara, A., Imai, Y., Imbriano, C., Inomata, M., Into, T., Iovane, V., Iovanna, J. L., Iozzo, R. V., N. Y., Ip, Irazoqui, J. E., Iribarren, P., Isaka, Y., Isakovic, A. J., Ischiropoulos, H., Isenberg, J. S., Ishaq, M., Ishida, H., Ishii, I., Ishmael, J. E., Isidoro, C., Isobe, K. -I., Isono, E., Issazadeh-Navikas, S., Itahana, K., Itakura, E., Ivanov, A. I., Iyer, A. K. V., Izquierdo, J. M., Izumi, Y., Izzo, V., Jäättelä, M., Jaber, N., Jackson, D. J., Jackson, W. T., Jacob, T. G., Jacques, T. S., Jagannath, C., Jain, A., Jana, N. R., Jang, B. K., Jani, A., Janji, B., Jannig, P. R., Jansson, P. J., Jean, S., Jendrach, M., Jeon, J. -H., Jessen, N., Jeung, E. -B., Jia, K., Jia, L., Jiang, H., Jiang, L., Jiang, T., Jiang, X., Jiang, Y., Jiménez, A., Jin, C., Jin, H., Jin, L., Jin, M., Jin, S., Jinwal, U. K., E. -K., Jo, Johansen, T., Johnson, D. E., Johnson, G. V. W., Johnson, J. D., Jonasch, E., Jones, C., Joosten, L. A. B., Jordan, J., Joseph, A. -M., Joseph, B., Joubert, A. M., Ju, D., Ju, J., Juan, H. -F., Juenemann, K., Juhász, G., Jung, H. S., Jung, J. U., Jung, Y. -K., Jungbluth, H., Justice, M. J., Jutten, B., Kaakoush, N. O., Kaarniranta, K., Kaasik, A., Kabuta, T., Kaeffer, B., Kågedal, K., Kahana, A., Kajimura, S., Kakhlon, O., Kalia, M., Kalvakolanu, D. V., Kamada, Y., Kambas, K., Kaminskyy, V. O., Kampinga, H. H., Kandouz, M., Kang, C., Kang, R., Kang, T. -C., Kanki, T., Kanneganti, T. -D., Kanno, H., Kanthasamy, A. G., Kantorow, M., Kaparakis-Liaskos, M., Kapuy, O., Karantza, V., Karim, M. R., Karmakar, P., Kaser, A., Kaushik, S., Kawula, T., Kaynar, A. M., P. -Y., Ke, Z. -J., Ke, Kehrl, J. H., Keller, K. E., Kemper, J. K., Kenworthy, A. K., Kepp, O., Kern, A., Kesari, S., Kessel, D., Ketteler, R., Kettelhut, I. C., Khambu, B., Khan, M. M., Khandelwal, V. K. M., Khare, S., Kiang, J. G., Kiger, A. A., Kihara, A., Kim, A. L., Kim, C. H., Kim, D. R., Kim, D. -H., Kim, E. K., Kim, H. Y., Kim, H. -R., Kim, J. -S., Kim, J. H., Kim, J. C., Kim, K. W., Kim, M. D., Kim, M. -M., Kim, P. K., Kim, S. W., Kim, S. -Y., Kim, Y. -S., Kim, Y., Kimchi, A., Kimmelman, A. C., Kimura, T., King, J. S., Kirkegaard, K., Kirkin, V., Kirshenbaum, L. A., Kishi, S., Kitajima, Y., Kitamoto, K., Kitaoka, Y., Kitazato, K., Kley, R. A., Klimecki, W. 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D., Lanzi, C., Lapaquette, P., Lapierre, L. R., Laporte, J., Laukkarinen, J., Laurie, G. W., Lavandero, S., Lavie, L., Lavoie, M. J., Law, B. Y. K., Law, H. K. -W., Law, K. B., Layfield, R., Lazo, P. A., Le Cam, L., Le Roch, K. G., Le Stunff, H., Leardkamolkarn, V., Lecuit, M., Lee, B. -H., Lee, C. -H., Lee, E. F., Lee, G. M., Lee, H. -J., Lee, H., Lee, J. K., Lee, J., Lee, J. -H., Lee, J. H., Lee, M., Lee, M. -S., Lee, P. J., Lee, S. W., Lee, S. -J., Lee, S. Y., Lee, S. H., Lee, S. S., Lee, S., Lee, Y. -R., Lee, Y. J., Lee, Y. H., Leeuwenburgh, C., Lefort, S., Legouis, R., Lei, J., Lei, Q. -Y., Leib, D. A., Leibowitz, G., Lekli, I., Lemaire, S. D., Lemasters, J. J., Lemberg, M. K., Lemoine, A., Leng, S., Lenz, G., Lenzi, P., Lerman, L. O., Barbato, D. L., Leu, J. I. J., Leung, H. Y., Levine, B., Lewis, P. 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Robin, Higaki, Katsumi, Hilfiker, Sabine, Hill, Bradford G., Hill, Joseph A., Hill, William D., Hino, Keisuke, Hofius, Daniel, Hofman, Paul, Höglinger, Günter U., Höhfeld, Jörg, Holz, Marina K., Hong, Yonggeun, Hood, David A., Hoozemans, Jeroen J.M., Hoppe, Thorsten, Hsu, Chin, Hsu, Chin-Yuan, Hsu, Li-Chung, Hu, Dong, Hu, Guochang, Hu, Hong-Ming, Hu, Hongbo, Hu, Ming Chang, Hu, Yu-Chen, Hu, Zhuo-Wei, Hua, Fang, Hua, Ya, Huang, Canhua, Huang, Huey-Lan, Huang, Kuo-How, Huang, Kuo-Yang, Huang, Shile, Huang, Shiqian, Huang, Wei-Pang, Huang, Yi-Ran, Huang, Yong, Huang, Yunfei, Huber, Tobias B., Huebbe, Patricia, Huh, Won-Ki, Hulmi, Juha J., Hur, Gang Min, Hurley, James H., Husak, Zvenyslava, Hussain, Sabah N.A., Hussain, Salik, Hwang, Jung Jin, Hwang, Seungmin, Hwang, Thomas I.S., Ichihara, Atsuhiro, Imai, Yuzuru, Imbriano, Carol, Inomata, Megumi, Into, Takeshi, Iovane, Valentina, Iovanna, Juan L., Iozzo, Renato V., Ip, Nancy Y., Irazoqui, Javier E., Iribarren, Pablo, Isaka, Yoshitaka, Isakovic, Aleksandra J., Ischiropoulos, Harry, Isenberg, Jeffrey S., Ishaq, Mohammad, Ishida, Hiroyuki, Ishii, Isao, Ishmael, Jane E., Isidoro, Ciro, Isobe, Ken-Ichi, Isono, Erika, Issazadeh-Navikas, Shohreh, Itahana, Koji, Itakura, Eisuke, Ivanov, Andrei I., Iyer, Anand Krishnan V., Izquierdo, José M., Izumi, Yotaro, Izzo, Valentina, Jäättelä, Marja, Jaber, Nadia, Jackson, Daniel John, Jackson, William T., Jacob, Tony George, Jacques, Thomas S., Jagannath, Chinnaswamy, Jain, Ashish, Jana, Nihar Ranjan, Jang, Byoung Kuk, Jani, Alkesh, Janji, Bassam, Jannig, Paulo Roberto, Jansson, Patric J., Jean, Steve, Jendrach, Marina, Jeon, Ju-Hong, Jessen, Niel, Jeung, Eui-Bae, Jia, Kailiang, Jia, Lijun, Jiang, Hong, Jiang, Hongchi, Jiang, Liwen, Jiang, Teng, Jiang, Xiaoyan, Jiang, Xuejun, Jiang, Ying, Jiang, Yongjun, Jiménez, Alberto, Jin, Cheng, Jin, Hongchuan, Jin, Lei, Jin, Meiyan, Jin, Shengkan, Jinwal, Umesh Kumar, Jo, Eun-Kyeong, Johansen, Terje, Johnson, Daniel E., Johnson, Gail V.W., Johnson, James D., Jonasch, Eric, Jones, Chri, Joosten, Leo A.B., Jordan, Joaquin, Joseph, Anna-Maria, Joseph, Bertrand, Joubert, Annie M., Ju, Dianwen, Ju, Jingfang, Juan, Hsueh-Fen, Juenemann, Katrin, Juhász, Gábor, Jung, Hye Seung, Jung, Jae U., Jung, Yong-Keun, Jungbluth, Heinz, Justice, Matthew J., Jutten, Barry, Kaakoush, Nadeem O., Kaarniranta, Kai, Kaasik, Allen, Kabuta, Tomohiro, Kaeffer, Bertrand, Kågedal, Katarina, Kahana, Alon, Kajimura, Shingo, Kakhlon, Or, Kalia, Manjula, Kalvakolanu, Dhan V., Kamada, Yoshiaki, Kambas, Konstantino, Kaminskyy, Vitaliy O., Kampinga, Harm H., Kandouz, Mustapha, Kang, Chanhee, Kang, Rui, Kang, Tae-Cheon, Kanki, Tomotake, Kanneganti, Thirumala-Devi, Kanno, Haruo, Kanthasamy, Anumantha G., Kantorow, Marc, Kaparakis-Liaskos, Maria, Kapuy, Orsolya, Karantza, Vassiliki, Karim, Md Razaul, Karmakar, Parimal, Kaser, Arthur, Kaushik, Susmita, Kawula, Thoma, Kaynar, A. Murat, Ke, Po-Yuan, Ke, Zun-Ji, Kehrl, John H., Keller, Kate E., Kemper, Jongsook Kim, Kenworthy, Anne K., Kepp, Oliver, Kern, Andrea, Kesari, Santosh, Kessel, David, Ketteler, Robin, Kettelhut, Isis do Carmo, Khambu, Bilon, Khan, Muzamil Majid, Khandelwal, Vinoth K.M., Khare, Sangeeta, Kiang, Juliann G., Kiger, Amy A., Kihara, Akio, Kim, Arianna L., Kim, Cheol Hyeon, Kim, Deok Ryong, Kim, Do-Hyung, Kim, Eung Kweon, Kim, Hye Young, Kim, Hyung-Ryong, Kim, Jae-Sung, Kim, Jeong Hun, Kim, Jin Cheon, Kim, Jin Hyoung, Kim, Kwang Woon, Kim, Michael D., Kim, Moon-Moo, Kim, Peter K., Kim, Seong Who, Kim, Soo-Youl, Kim, Yong-Sun, Kim, Yonghyun, Kimchi, Adi, Kimmelman, Alec C., Kimura, Tomonori, King, Jason S., Kirkegaard, Karla, Kirkin, Vladimir, Kirshenbaum, Lorrie A., Kishi, Shuji, Kitajima, Yasuo, Kitamoto, Katsuhiko, Kitaoka, Yasushi, Kitazato, Kaio, Kley, Rudolf A., Klimecki, Walter T., Klinkenberg, Michael, Klucken, Jochen, Knævelsrud, Helene, Knecht, Erwin, Knuppertz, Laura, Ko, Jiunn-Liang, Kobayashi, Satoru, Koch, Jan C., Koechlin-Ramonatxo, Christelle, Koenig, Ulrich, Koh, Young Ho, Köhler, Katja, Kohlwein, Sepp D., Koike, Masato, Komatsu, Masaaki, Kominami, Eiki, Kong, Dexin, Kong, Hee Jeong, Konstantakou, Eumorphia G., Kopp, Benjamin T., Korcsmaros, Tama, Korhonen, Laura, Korolchuk, Viktor I., Koshkina, Nadya V., Kou, Yanjun, Koukourakis, Michael I., Koumenis, Constantino, Kovács, Attila L., Kovács, Tibor, Kovacs, Werner J., Koya, Daisuke, Kraft, Claudine, Krainc, Dimitri, Kramer, Helmut, Kravic-Stevovic, Tamara, Krek, Wilhelm, Kretz-Remy, Carole, Krick, Roswitha, Krishnamurthy, Malathi, Kriston-Vizi, Jano, Kroemer, Guido, Kruer, Michael C., Kruger, Rejko, Ktistakis, Nicholas T., Kuchitsu, Kazuyuki, Kuhn, Christian, Kumar, Addanki Pratap, Kumar, Anuj, Kumar, Ashok, Kumar, Deepak, Kumar, Dhiraj, Kumar, Rakesh, Kumar, Sharad, Kundu, Mondira, Kung, Hsing-Jien, Kuno, Atsushi, Kuo, Sheng-Han, Kuret, Jeff, Kurz, Tino, Kwok, Terry, Kwon, Taeg Kyu, Kwon, Yong Tae, Kyrmizi, Irene, La Spada, Albert R., Lafont, Frank, Lahm, Tim, Lakkaraju, Aparna, Lam, Truong, Lamark, Trond, Lancel, Steve, Landowski, Terry H., Lane, Darius J.R., Lane, Jon D., Lanzi, Cinzia, Lapaquette, Pierre, Lapierre, Louis R., Laporte, Jocelyn, Laukkarinen, Johanna, Laurie, Gordon W., Lavandero, Sergio, Lavie, Lena, Lavoie, Matthew J., Law, Betty Yuen Kwan, Law, Helen Ka-Wai, Law, Kelsey B., Layfield, Robert, Lazo, Pedro A., Le Cam, Laurent, Le Roch, Karine G., Le Stunff, Hervé, Leardkamolkarn, Vijittra, Lecuit, Marc, Lee, Byung-Hoon, Lee, Che-Hsin, Lee, Erinna F., Lee, Gyun Min, Lee, He-Jin, Lee, Hsinyu, Lee, Jae Keun, Lee, Jongdae, Lee, Ju-Hyun, Lee, Jun Hee, Lee, Michael, Lee, Myung-Shik, Lee, Patty J., Lee, Sam W., Lee, Seung-Jae, Lee, Shiow-Ju, Lee, Stella Y., Lee, Sug Hyung, Lee, Sung Sik, Lee, Sung-Joon, Lee, Sunhee, Lee, Ying-Ray, Lee, Yong J., Lee, Young H., Leeuwenburgh, Christiaan, Lefort, Sylvain, Legouis, Renaud, Lei, Jinzhi, Lei, Qun-Ying, Leib, David A., Leibowitz, Gil, Lekli, Istvan, Lemaire, Stéphane D., Lemasters, John J., Lemberg, Marius K., Lemoine, Antoinette, Leng, Shuilong, Lenz, Guido, Lenzi, Paola, Lerman, Lilach O., Barbato, Daniele Lettieri, Leu, Julia I. 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Sue, Menna-Barreto, Rubem F.S., Menon, Manoj B., Meraz-Ríos, Marco A., Merla, Giuseppe, Merlini, Luciano, Merlot, Angelica M., Meryk, Andrea, Meschini, Stefania, Meyer, Joel N., Mi, Man-Tian, Miao, Chao-Yu, Micale, Lucia, Michaeli, Simon, Michiels, Carine, Migliaccio, Anna Rita, Mihailidou, Anastasia Susie, Mijaljica, Dalibor, Mikoshiba, Katsuhiko, Milan, Enrico, Miller-Fleming, Leonor, Mills, Gordon B., Mills, Ian G., Minakaki, Georgia, Minassian, Berge A., Ming, Xiu-Fen, Minibayeva, Farida, Minina, Elena A., Mintern, Justine D., Minucci, Saverio, Miranda-Vizuete, Antonio, Mitchell, Claire H., Miyamoto, Shigeki, Miyazawa, Keisuke, Mizushima, Noboru, Mnich, Katarzyna, Mograbi, Baharia, Mohseni, Simin, Moita, Luis Ferreira, Molinari, Marco, Molinari, Maurizio, Møller, Andreas Buch, Mollereau, Bertrand, Mollinedo, Faustino, Mongillo, Marco, Monick, Martha M., Montagnaro, Serena, Montell, Craig, Moore, Darren J., Moore, Michael N., Mora-Rodriguez, Rodrigo, Moreira, Paula I., Morel, Etienne, Morelli, Maria Beatrice, Moreno, Sandra, Morgan, Michael J., Moris, Arnaud, Moriyasu, Yuji, Morrison, Janna L., Morrison, Lynda A., Morselli, Eugenia, Moscat, Jorge, Moseley, Pope L., Mostowy, Serge, Motori, Elisa, Mottet, Deni, Mottram, Jeremy C., Moussa, Charbel E.-H., Mpakou, Vassiliki E., Mukhtar, Hasan, Levy, Jean M. Mulcahy, Muller, Sylviane, Muñoz-Moreno, Raquel, Muñoz-Pinedo, Cristina, Münz, Christian, Murphy, Maureen E., Murray, James T., Murthy, Aditya, Mysorekar, Indira U., Nabi, Ivan R., Nabissi, Massimo, Nader, Gustavo A., Nagahara, Yukitoshi, Nagai, Yoshitaka, Nagata, Kazuhiro, Nagelkerke, Anika, Nagy, Péter, Naidu, Samisubbu R., Nair, Sreejayan, Nakano, Hiroyasu, Nakatogawa, Hitoshi, Nanjundan, Meera, Napolitano, Gennaro, Naqvi, Naweed I., Nardacci, Roberta, Narendra, Derek P., Narita, Masashi, Nascimbeni, Anna Chiara, Natarajan, Ramesh, Navegantes, Luiz C., Nawrocki, Steffan T., Nazarko, Taras Y., Nazarko, Volodymyr Y., Neill, Thoma, Neri, Luca M., Netea, Mihai G., Netea-Maier, Romana T., Neves, Bruno M., Ney, Paul A., Nezis, Ioannis P., Nguyen, Hang T.T., Nguyen, Huu Phuc, Nicot, Anne-Sophie, Nilsen, Hilde, Nilsson, Per, Nishimura, Mikio, Nishino, Ichizo, Niso-Santano, Mireia, Niu, Hua, Nixon, Ralph A., Njar, Vincent C.O., Noda, Takeshi, Noegel, Angelika A., Nolte, Elsie Magdalena, Norberg, Erik, Norga, Koenraad K., Noureini, Sakineh Kazemi, Notomi, Shoji, Notterpek, Lucia, Nowikovsky, Karin, Nukina, Nobuyuki, Nürnberger, Thorsten, O'donnell, Valerie B., O'donovan, Tracey, O'dwyer, Peter J., Oehme, Ina, Oeste, Clara L., Ogawa, Michinaga, Ogretmen, Besim, Ogura, Yuji, Oh, Young J., Ohmuraya, Masaki, Ohshima, Takayuki, Ojha, Rani, Okamoto, Koji, Okazaki, Toshiro, Oliver, F. Javier, Ollinger, Karin, Olsson, Stefan, Orban, Daniel P., Ordonez, Paulina, Orhon, Idil, Orosz, Laszlo, O'rourke, Eyleen J., Orozco, Helena, Ortega, Angel L., Ortona, Elena, Osellame, Laura D., Oshima, Junko, Oshima, Shigeru, Osiewacz, Heinz D., Otomo, Takanobu, Otsu, Kinya, Ou, Jing-Hsiung Jame, Outeiro, Tiago F., Ouyang, Dong-Yun, Ouyang, Hongjiao, Overholtzer, Michael, Ozbun, Michelle A., Ozdinler, P. Hande, Ozpolat, Bulent, Pacelli, Consiglia, Paganetti, Paolo, Page, Guyléne, Pages, Gille, Pagnini, Ugo, Pajak, Beata, Pak, Stephen C., Pakos-Zebrucka, Karolina, Pakpour, Nazzy, Palková, Zdena, Palladino, Francesca, Pallauf, Kathrin, Pallet, Nicola, Palmieri, Marta, Paludan, Søren R., Palumbo, Camilla, Palumbo, Silvia, Pampliega, Olatz, Pan, Hongming, Pan, Wei, Panaretakis, Theochari, Pandey, Aseem, Pantazopoulou, Areti, Papackova, Zuzana, Papademetrio, Daniela L., Papassideri, Issidora, Papini, Alessio, Parajuli, Nirmala, Pardo, Julian, Parekh, Vrajesh V., Parenti, Giancarlo, Park, Jong-In, Park, Junsoo, Park, Ohkmae K., Parker, Roy, Parlato, Rosanna, Parys, Jan B., Parzych, Katherine R., Pasquet, Jean-Max, Pasquier, Benoit, Pasumarthi, Kishore B.S., Patschan, Daniel, Pattingre, Sophie, Pattison, Scott, Pause, Arnim, Pavenstädt, Hermann, Pavone, Flaminia, Pedrozo, Zully, Peña, Fernando J., Peñalva, Miguel A., Pende, Mario, Peng, Jianxin, Penna, Fabio, Penninger, Josef M., Pensalfini, Anna, Pepe, Salvatore, Pereira, Gustavo J.S., Pereira, Paulo C., de la Cruz, Verónica Pérez, Pérez-Pérez, María Esther, Pérez-Rodríguez, Diego, Pérez-Sala, Dolore, Perier, Celine, Perl, Andra, Perlmutter, David H., Perrotta, Ida, Pervaiz, Shazib, Pesonen, Maija, Pessin, Jeffrey E., Peters, Godefridus J., Petersen, Morten, Petrache, Irina, Petrof, Basil J., Petrovski, Goran, Phang, James M., Piacentini, Mauro, Pierdominici, Marina, Pierre, Philippe, Pierrefite-Carle, Valérie, Pietrocola, Federico, Pimentel-Muiños, Felipe X., Pinar, Mario, Pineda, Benjamin, Pinkas-Kramarski, Ronit, Pinti, Marcello, Pinton, Paolo, Piperdi, Bilal, Piret, James M., Platanias, Leonidas C., Platta, Harald W., Plowey, Edward D., Pöggeler, Stefanie, Poirot, Marc, Polčic, Peter, Poletti, Angelo, Poon, Audrey H., Popelka, Hana, Popova, Blagovesta, Poprawa, Izabela, Poulose, Shibu M., Poulton, Joanna, Powers, Scott K., Powers, Ted, Pozuelo-Rubio, Mercede, Prak, Krisna, Prange, Reinhild, Prescott, Mark, Priault, Muriel, Prince, Sharon, Proia, Richard L., Proikas-Cezanne, Tassula, Prokisch, Holger, Promponas, Vasilis J., Przyklenk, Karin, Puertollano, Rosa, Pugazhenthi, Subbiah, Puglielli, Luigi, Pujol, Aurora, Puyal, Julien, Pyeon, Dohun, Qi, Xin, Qian, Wen-Bin, Qin, Zheng-Hong, Qiu, Yu, Qu, Ziwei, Quadrilatero, Joe, Quinn, Frederick, Raben, Nina, Rabinowich, Hannah, Radogna, Flavia, Ragusa, Michael J., Rahmani, Mohamed, Raina, Komal, Ramanadham, Sasanka, Ramesh, Rajagopal, Rami, Abdelhaq, Randall-Demllo, Sarron, Randow, Felix, Rao, Hai, Rao, V. Ashutosh, Rasmussen, Blake B., Rasse, Tobias M., Ratovitski, Edward A., Rautou, Pierre-Emmanuel, Ray, Swapan K., Razani, Babak, Reed, Bruce H., Reggiori, Fulvio, Rehm, Marku, Reichert, Andreas S., Rein, Theo, Reiner, David J., Reits, Eric, Ren, Jun, Ren, Xingcong, Renna, Maurizio, Reusch, Jane E.B., Revuelta, Jose L., Reyes, Leticia, Rezaie, Alireza R., Richards, Robert I., Richardson, Des R., Richetta, Clémence, Riehle, Michael A., Rihn, Bertrand H., Rikihisa, Yasuko, Riley, Brigit E., Rimbach, Gerald, Rippo, Maria Rita, Ritis, Konstantino, Rizzi, Federica, Rizzo, Elizete, Roach, Peter J., Robbins, Jeffrey, Roberge, Michel, Roca, Gabriela, Roccheri, Maria Carmela, Rocha, Sonia, Rodrigues, Cecilia M.P., Rodríguez, Clara I., de Cordoba, Santiago Rodriguez, Rodriguez-Muela, Natalia, Roelofs, Jeroen, Rogov, Vladimir V., Rohn, Troy T., Rohrer, Bärbel, Romanelli, Davide, Romani, Luigina, Romano, Patricia Silvia, Roncero, M. Isabel G., Rosa, Jose Lui, Rosello, Alicia, Rosen, Kirill V., Rosenstiel, Philip, Rost-Roszkowska, Magdalena, Roth, Kevin A., Roué, Gael, Rouis, Mustapha, Rouschop, Kasper M., Ruan, Daniel T., Ruano, Diego, Rubinsztein, David C., Rucker, Edmund B., Rudich, Assaf, Rudolf, Emil, Rudolf, Ruediger, Ruegg, Markus A., Ruiz-Roldan, Carmen, Ruparelia, Avnika Ashok, Rusmini, Paola, Russ, David W., Russo, Gian Luigi, Russo, Giuseppe, Russo, Rossella, Rusten, Tor Erik, Ryabovol, Victoria, Ryan, Kevin M., Ryter, Stefan W., Sabatini, David M., Sacher, Michael, Sachse, Carsten, Sack, Michael N., Sadoshima, Junichi, Saftig, Paul, Sagi-Eisenberg, Ronit, Sahni, Sumit, Saikumar, Pothana, Saito, Tsunenori, Saitoh, Tatsuya, Sakakura, Koichi, Sakoh-Nakatogawa, Machiko, Sakuraba, Yasuhito, Salazar-Roa, María, Salomoni, Paolo, Saluja, Ashok K., Salvaterra, Paul M., Salvioli, Rosa, Samali, Afshin, Sanchez, Anthony M.J., Sánchez-Alcázar, José A., Sanchez-Prieto, Ricardo, Sandri, Marco, Sanjuan, Miguel A., Santaguida, Stefano, Santambrogio, Laura, Santoni, Giorgio, Dos Santos, Claudia Nune, Saran, Shweta, Sardiello, Marco, Sargent, Graeme, Sarkar, Pallabi, Sarkar, Sovan, Sarrias, Maria Rosa, Sarwal, Minnie M., Sasakawa, Chihiro, Sasaki, Motoko, Sass, Miklo, Sato, Ken, Sato, Miyuki, Satriano, Joseph, Savaraj, Niramol, Saveljeva, Svetlana, Schaefer, Liliana, Schaible, Ulrich E., Scharl, Michael, Schatzl, Hermann M., Schekman, Randy, Scheper, Wiep, Schiavi, Alfonso, Schipper, Hyman M., Schmeisser, Hana, Schmidt, Jen, Schmitz, Ingo, Schneider, Bianca E., Schneider, E. Marion, Schneider, Jaime L., Schon, Eric A., Schönenberger, Miriam J., Schönthal, Axel H., Schorderet, Daniel F., Schröder, Bernd, Schuck, Sebastian, Schulze, Ryan J., Schwarten, Melanie, Schwarz, Thomas L., Sciarretta, Sebastiano, Scotto, Kathleen, Scovassi, A. Ivana, Screaton, Robert A., Screen, Mark, Seca, Hugo, Sedej, Simon, Segatori, Laura, Segev, Nava, Seglen, Per O., Seguí-Simarro, Jose M., Segura-Aguilar, Juan, Seiliez, Iban, Seki, Ekihiro, Sell, Christian, Semenkovich, Clay F., Semenza, Gregg L., Sen, Utpal, Serra, Andreas L., Serrano-Puebla, Ana, Sesaki, Hiromi, Setoguchi, Takao, Settembre, Carmine, Shacka, John J., Shajahan-Haq, Ayesha N., Shapiro, Irving M., Sharma, Shweta, She, Hua, Shen, C.-K. Jame, Shen, Chiung-Chyi, Shen, Han-Ming, Shen, Sanbing, Shen, Weili, Sheng, Rui, Sheng, Xianyong, Sheng, Zu-Hang, Shepherd, Trevor G., Shi, Junyan, Shi, Qiang, Shi, Qinghua, Shi, Yuguang, Shibutani, Shusaku, Shibuya, Kenichi, Shidoji, Yoshihiro, Shieh, Jeng-Jer, Shih, Chwen-Ming, Shimada, Yohta, Shimizu, Shigeomi, Shin, Dong Wook, Shinohara, Mari L., Shintani, Michiko, Shintani, Takahiro, Shioi, Tetsuo, Shirabe, Ken, Shiri-Sverdlov, Ronit, Shirihai, Orian, Shore, Gordon C., Shu, Chih-Wen, Shukla, Deepak, Sibirny, Andriy A., Sica, Valentina, Sigurdson, Christina J., Sigurdsson, Einar M., Sijwali, Puran Singh, Sikorska, Beata, Silveira, Wilian A., Silvente-Poirot, Sandrine, Silverman, Gary A., Simak, Jan, Simmet, Thoma, Simon, Anna Katharina, Simon, Hans-Uwe, Simone, Cristiano, Simons, Matia, Simonsen, Anne, Singh, Rajat, Singh, Shivendra V., Singh, Shrawan K., Sinha, Debasish, Sinha, Sangita, Sinicrope, Frank A., Sirko, Agnieszka, Sirohi, Kapil, Sishi, Balindiwe J.N., Sittler, Annie, Siu, Parco M., Sivridis, Efthimio, Skwarska, Anna, Slack, Ruth, Slaninová, Iva, Slavov, Nikolai, Smaili, Soraya S., Smalley, Keiran S.M., Smith, Duncan R., Soenen, Stefaan J., Soleimanpour, Scott A., Solhaug, Anita, Somasundaram, Kumaravel, Son, Jin H., Sonawane, Avinash, Song, Chunjuan, Song, Fuyong, Song, Hyun Kyu, Song, Ju-Xian, Song, Wei, Soo, Kai Y., Sood, Anil K., Soong, Tuck Wah, Soontornniyomkij, Virawudh, Sorice, Maurizio, Sotgia, Federica, Soto-Pantoja, David R., Sotthibundhu, Areechun, Sousa, Maria João, Spaink, Herman P., Span, Paul N., Spang, Anne, Sparks, Janet D., Speck, Peter G., Spector, Stephen A., Spies, Claudia D., Springer, Wolfdieter, Clair, Daret St, Stacchiotti, Alessandra, Staels, Bart, Stang, Michael T., Starczynowski, Daniel T., Starokadomskyy, Petro, Steegborn, Clemen, Steele, John W., Stefanis, Leonida, Steffan, Joan, Stellrecht, Christine M., Stenmark, Harald, Stepkowski, Tomasz M., Stern, Stęphan T., Stevens, Craig, Stockwell, Brent R., Stoka, Veronika, Storchova, Zuzana, Stork, Björn, Stratoulias, Vassili, Stravopodis, Dimitrios J., Strnad, Pavel, Strohecker, Anne Marie, Ström, Anna-Lena, Stromhaug, Per, Stulik, Jiri, Su, Yu-Xiong, Su, Zhaoliang, Subauste, Carlos S., Subramaniam, Srinivasa, Sue, Carolyn M., Suh, Sang Won, Sui, Xinbing, Sukseree, Supawadee, Sulzer, David, Sun, Fang-Lin, Sun, Jiaren, Sun, Jun, Sun, Shi-Yong, Sun, Yang, Sun, Yi, Sun, Yingjie, Sundaramoorthy, Vinod, Sung, Joseph, Suzuki, Hidekazu, Suzuki, Kuninori, Suzuki, Naoki, Suzuki, Tadashi, Suzuki, Yuichiro J., Swanson, Michele S., Swanton, Charle, Swärd, Karl, Swarup, Ghanshyam, Sweeney, Sean T., Sylvester, Paul W., Szatmari, Zsuzsanna, Szegezdi, Eva, Szlosarek, Peter W., Taegtmeyer, Heinrich, Tafani, Marco, Taillebourg, Emmanuel, Tait, Stephen W.G., Takacs-Vellai, Krisztina, Takahashi, Yoshinori, Takáts, Szabolc, Takemura, Genzou, Takigawa, Nagio, Talbot, Nicholas J., Tamagno, Elena, Tamburini, Jerome, Tan, Cai-Ping, Tan, Lan, Tan, Mei Lan, Tan, Ming, Tan, Yee-Joo, Tanaka, Keiji, Tanaka, Masaki, Tang, Daolin, Tang, Dingzhong, Tang, Guomei, Tanida, Isei, Tanji, Kunikazu, Tannous, Bakhos A., Tapia, Jose A., Tasset-Cuevas, Inmaculada, Tatar, Marc, Tavassoly, Iman, Tavernarakis, Nektario, Taylor, Allen, Taylor, Graham S., Taylor, Gregory A., Taylor, J. Paul, Taylor, Mark J., Tchetina, Elena V., Tee, Andrew R., Teixeira-Clerc, Fatima, Telang, Sucheta, Tencomnao, Tewin, Teng, Ba-Bie, Teng, Ru-Jeng, Terro, Faraj, Tettamanti, Gianluca, Theiss, Arianne L., Theron, Anne E., Thomas, Kelly Jean, Thomé, Marcos P., Thomes, Paul G., Thorburn, Andrew, Thorner, Jeremy, Thum, Thoma, Thumm, Michael, Thurston, Teresa L.M., Tian, Ling, Till, Andrea, Ting, Jenny Pan-Yun, Ting, Jenny Pan Yun, Titorenko, Vladimir I., Toker, Lilach, Toldo, Stefano, Tooze, Sharon A., Topisirovic, Ivan, Torgersen, Maria Lyngaa, Torosantucci, Liliana, Torriglia, Alicia, Torrisi, Maria Rosaria, Tournier, Cathy, Towns, Roberto, Trajkovic, Vladimir, Travassos, Leonardo H., Triola, Gemma, Tripathi, Durga Nand, Trisciuoglio, Daniela, Troncoso, Rodrigo, Trougakos, Ioannis P., Truttmann, Anita C., Tsai, Kuen-Jer, Tschan, Mario P., Tseng, Yi-Hsin, Tsukuba, Takayuki, Tsung, Allan, Tsvetkov, Andrey S., Tu, Shuiping, Tuan, Hsing-Yu, Tucci, Marco, Tumbarello, David A., Turk, Bori, Turk, Vito, Turner, Robin F.B., Tveita, Anders A., Tyagi, Suresh C., Ubukata, Makoto, Uchiyama, Yasuo, Udelnow, Andrej, Ueno, Takashi, Umekawa, Midori, Umemiya-Shirafuji, Rika, Underwood, Benjamin R., Ungermann, Christian, Ureshino, Rodrigo P., Ushioda, Ryo, Uversky, Vladimir N., Uzcátegui, Néstor L., Vaccari, Thoma, Vaccaro, Maria I., Váchová, Libuše, Vakifahmetoglu-Norberg, Helin, Valdor, Rut, Valente, Enza Maria, Vallette, Francoi, Valverde, Angela M., Van den Berghe, Greet, Van Den Bosch, Ludo, van den Brink, Gijs R., van der Goot, F. Gisou, van der Klei, Ida J., van der Laan, Luc J.W., van Doorn, Wouter G., van Egmond, Marjolein, van Golen, Kenneth L., Van Kaer, Luc, Campagne, Menno van Lookeren, Vandenabeele, Peter, Vandenberghe, Wim, Vanhorebeek, Ilse, Varela-Nieto, Isabel, Vasconcelos, M. Helena, Vasko, Radovan, Vavvas, Demetrios G., Vega-Naredo, Ignacio, Velasco, Guillermo, Velentzas, Athanassios D., Velentzas, Panagiotis D., Vellai, Tibor, Vellenga, Edo, Vendelbo, Mikkel Holm, Venkatachalam, Kartik, Ventura, Natascia, Ventura, Salvador, Veras, Patrícia S.T., Verdier, Mireille, Vertessy, Beata G., Viale, Andrea, Vidal, Michel, Vieira, Helena L.A., Vierstra, Richard D., Vigneswaran, Nadarajah, Vij, Neeraj, Vila, Miquel, Villar, Margarita, Villar, Victor H., Villarroya, Joan, Vindis, Cécile, Viola, Giampietro, Viscomi, Maria Teresa, Vitale, Giovanni, Vogl, Dan T., Voitsekhovskaja, Olga V., von Haefen, Clarissa, von Schwarzenberg, Karin, Voth, Daniel E., Vouret-Craviari, Valérie, Vuori, Kristina, Vyas, Jatin M., Waeber, Christian, Walker, Cheryl Lyn, Walker, Mark J., Walter, Jochen, Wan, Lei, Wan, Xiangbo, Wang, Bo, Wang, Caihong, Wang, Chao-Yung, Wang, Chengshu, Wang, Chenran, Wang, Chuangui, Wang, Dong, Wang, Fen, Wang, Fuxin, Wang, Guanghui, Wang, Hai-Jie, Wang, Haichao, Wang, Hong-Gang, Wang, Hongmin, Wang, Horng-Dar, Wang, Jing, Wang, Junjun, Wang, Mei, Wang, Mei-Qing, Wang, Pei-Yu, Wang, Peng, Wang, Richard C., Wang, Shuo, Wang, Ting-Fang, Wang, Xian, Wang, Xiao-Jia, Wang, Xiao-Wei, Wang, Xin, Wang, Xuejun, Wang, Yan, Wang, Yanming, Wang, Ying, Wang, Ying-Jan, Wang, Yipeng, Wang, Yu, Wang, Yu Tian, Wang, Yuqing, Wang, Zhi-Nong, Wappner, Pablo, Ward, Carl, Ward, Diane McVey, Warnes, Gary, Watada, Hirotaka, Watanabe, Yoshihisa, Watase, Kei, Weaver, Timothy E., Weekes, Colin D., Wei, Jiwu, Weide, Thoma, Weihl, Conrad C., Weindl, Günther, Weis, Simone Nardin, Wen, Longping, Wen, Xin, Wen, Yunfei, Westermann, Benedikt, Weyand, Cornelia M., White, Anthony R., White, Eileen, Whitton, J. Lindsay, Whitworth, Alexander J., Wiels, Joëlle, Wild, Franziska, Wildenberg, Manon E., Wileman, Tom, Wilkinson, Deepti Sriniva, Wilkinson, Simon, Willbold, Dieter, Williams, Chri, Williams, Katherine, Williamson, Peter R., Winklhofer, Konstanze F., Witkin, Steven S., Wohlgemuth, Stephanie E., Wollert, Thoma, Wolvetang, Ernst J., Wong, Esther, Wong, G. William, Wong, Richard W., Wong, Vincent Kam Wai, Woodcock, Elizabeth A., Wright, Karen L., Wu, Chunlai, Wu, Defeng, Wu, Gen Sheng, Wu, Jian, Wu, Junfang, Wu, Mian, Wu, Min, Wu, Shengzhou, Wu, William K.K., Wu, Yaohua, Wu, Zhenlong, Xavier, Cristina P.R., Xavier, Ramnik J., Xia, Gui-Xian, Xia, Tian, Xia, Weiliang, Xia, Yong, Xiao, Hengyi, Xiao, Jian, Xiao, Shi, Xiao, Wuhan, Xie, Chuan-Ming, Xie, Zhiping, Xie, Zhonglin, Xilouri, Maria, Xiong, Yuyan, Xu, Chuanshan, Xu, Congfeng, Xu, Feng, Xu, Haoxing, Xu, Hongwei, Xu, Jian, Xu, Jianzhen, Xu, Jinxian, Xu, Liang, Xu, Xiaolei, Xu, Yangqing, Xu, Ye, Xu, Zhi-Xiang, Xu, Ziheng, Xue, Yu, Yamada, Takahiro, Yamamoto, Ai, Yamanaka, Koji, Yamashina, Shunhei, Yamashiro, Shigeko, Yan, Bing, Yan, Bo, Yan, Xianghua, Yan, Zhen, Yanagi, Yasuo, Yang, Dun-Sheng, Yang, Jin-Ming, Yang, Liu, Yang, Minghua, Yang, Pei-Ming, Yang, Peixin, Yang, Qian, Yang, Wannian, Yang, Wei Yuan, Yang, Xuesong, Yang, Yi, Yang, Ying, Yang, Zhifen, Yang, Zhihong, Yao, Meng-Chao, Yao, Pamela J., Yao, Xiaofeng, Yao, Zhenyu, Yao, Zhiyuan, Yasui, Linda S., Ye, Mingxiang, Yedvobnick, Barry, Yeganeh, Behzad, Yeh, Elizabeth S., Yeyati, Patricia L., Yi, Fan, Yi, Long, Yin, Xiao-Ming, Yip, Calvin K., Yoo, Yeong-Min, Yoo, Young Hyun, Yoon, Seung-Yong, Yoshida, Ken-Ichi, Yoshimori, Tamotsu, Young, Ken H., Yu, Huixin, Yu, Jane J., Yu, Jin-Tai, Yu, Jun, Yu, Li, Yu, W. Haung, Yu, Xiao-Fang, Yu, Zhengping, Yuan, Junying, Yuan, Zhi-Min, Yue, Beatrice Y.J.T., Yue, Jianbo, Yue, Zhenyu, Zacks, David N., Zacksenhaus, Eldad, Zaffaroni, Nadia, Zaglia, Tania, Zakeri, Zahra, Zecchini, Vincent, Zeng, Jinsheng, Zeng, Min, Zeng, Qi, Zervos, Antonis S., Zhang, Donna D., Zhang, Fan, Zhang, Guo, Zhang, Guo-Chang, Zhang, Hao, Zhang, Hong, Zhang, Hongbing, Zhang, Jian, Zhang, Jiangwei, Zhang, Jianhua, Zhang, Jing-Pu, Zhang, Li, Zhang, Lin, Zhang, Long, Zhang, Ming-Yong, Zhang, Xiangnan, Zhang, Xu Dong, Zhang, Yan, Zhang, Yang, Zhang, Yanjin, Zhang, Yingmei, Zhang, Yunjiao, Zhao, Mei, Zhao, Wei-Li, Zhao, Xiaonan, Zhao, Yan G., Zhao, Ying, Zhao, Yongchao, Zhao, Yu-Xia, Zhao, Zhendong, Zhao, Zhizhuang J., Zheng, Dexian, Zheng, Xi-Long, Zheng, Xiaoxiang, Zhivotovsky, Bori, Zhong, Qing, Zhou, Guang-Zhou, Zhou, Guofei, Zhou, Huiping, Zhou, Shu-Feng, Zhou, Xu-Jie, Zhu, Hongxin, Zhu, Hua, Zhu, Wei-Guo, Zhu, Wenhua, Zhu, Xiao-Feng, Zhu, Yuhua, Zhuang, Shi-Mei, Zhuang, Xiaohong, Ziparo, Elio, Zois, Christos E., Zoladek, Teresa, Zong, Wei-Xing, Zorzano, Antonio, and Zughaier, Susu M.
- Subjects
Molecular Biology ,Cell Biology ,Settore BIO/06 - Anatomia Comparata E Citologia - Abstract
non presente
- Published
- 2016
7. Nuclear fallout provides a new link between aPKC and polarized cell trafficking
- Author
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European Commission, Ministerio de Economía y Competitividad (España), Ministerio de Ciencia e Innovación (España), Ministerio de Educación y Ciencia (España), Junta de Andalucía, National Institutes of Health (US), Calero Cuenca, Francisco Javier, Espinosa-Vázquez, José Manuel, Reina-Campos, Miguel, Díaz-Meco, M. Teresa, Moscat, Jorge, Sotillos, Sol, European Commission, Ministerio de Economía y Competitividad (España), Ministerio de Ciencia e Innovación (España), Ministerio de Educación y Ciencia (España), Junta de Andalucía, National Institutes of Health (US), Calero Cuenca, Francisco Javier, Espinosa-Vázquez, José Manuel, Reina-Campos, Miguel, Díaz-Meco, M. Teresa, Moscat, Jorge, and Sotillos, Sol
- Abstract
[Background]: Cell polarity, essential for cell physiology and tissue coherence, emerges as a consequence of asymmetric localization of protein complexes and directional trafficking of cellular components. Although molecules required in both processes are well known their relationship is still poorly understood. [Results]: Here we show a molecular link between Nuclear Fallout (Nuf), an adaptor of Rab11-GTPase to the microtubule motor proteins during Recycling Endosome (RE) trafficking, and aPKC, a pivotal kinase in the regulation of cell polarity. We demonstrate that aPKC phosphorylates Nuf modifying its subcellular distribution. Accordingly, in aPKC mutants Nuf and Rab11 accumulate apically indicating altered RE delivery. We show that aPKC localization in the apico-lateral cortex is dynamic. When we block exocytosis, by means of exocyst-sec mutants, aPKC accumulates inside the cells. Moreover, apical aPKC concentration is reduced in nuf mutants, suggesting aPKC levels are maintained by recycling. [Conclusions]: We demonstrate that active aPKC interacts with Nuf, phosphorylating it and, as a result, modifying its subcellular distribution. We propose a regulatory loop by which Nuf promotes aPKC apical recycling until sufficient levels of active aPKC are reached. Thus, we provide a novel link between cell polarity regulation and traffic control in epithelia.
- Published
- 2016
8. Sequencing of the a-synuclein gene in a large series of cases of familial Parkinson's disease fails to reveal any further mutations
- Author
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VAUGHAN JR, FARRER MJ, WSZOLEK ZK, GASSER T, DüRR A, AGID Y, BONIFATI V, VOLPE G, LINCOLN S, BRETELER M, MECO M, BRICE A, MARSDEN CD, HARDY J, WOOD NW, DE MICHELE, GIUSEPPE, Vaughan, Jr, Farrer, Mj, Wszolek, Zk, Gasser, T, Dürr, A, Agid, Y, Bonifati, V, DE MICHELE, Giuseppe, Volpe, G, Lincoln, S, Breteler, M, Meco, M, Brice, A, Marsden, Cd, Hardy, J, and Wood, Nw
- Published
- 1998
9. Predictive factors in BioEnterics Intragastric Balloon : statistical analysis
- Author
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Micheletto, G., Meco, M., Bressani Doldi, S., Danelli, P.G., and Goi, G.
- Subjects
Settore MED/18 - Chirurgia Generale - Published
- 2008
10. Crosstalk between PKCzeta and the IL4/Stat6 pathway during T-cell-mediated hepatitis
- Author
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Duran, A., Rodriguez, A., Martin, P., Serrano, M., Flores, J., Leitges, M., Diaz-Meco, M., and Moscat, J.
- Subjects
chemical and pharmacologic phenomena - Abstract
PKCzeta is required for nuclear factor kappa-B (NF-kappaB) activation in several cell systems. NF-kappaB is a suppressor of liver apoptosis during development and in concanavalin A (ConA)-induced T-cell-mediated hepatitis. Here we show that PKCzeta-/- mice display inhibited ConA-induced NF-kappaB activation and reduced damage in liver. As the IL-4/Stat6 pathway is necessary for ConA-induced hepatitis, we addressed here the potential role of PKCzeta in this cascade. Interestingly, the loss of PKCzeta severely attenuated serum IL-5 and liver eotaxin-1 levels, two critical mediators of liver damage. Stat6 tyrosine phosphorylation and Jak1 activation were ablated in the liver of ConA-injected PKCzeta-/- mice and in IL-4-stimulated PKCzeta-/- fibroblasts. PKCzeta interacts with and phosphorylates Jak1 and PKCzeta activity is required for Jak1 function. In contrast, Par-4-/- mice have increased sensitivity to ConA-induced liver damage and IL-4 signaling. This unveils a novel and critical involvement of PKCzeta in the IL-4/Stat6 signaling pathway in vitro and in vivo.
- Published
- 2004
11. Polarized Subcellular Localization of JAK/STAT Components Is Required for Efficient Signaling
- Author
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Sotillos, Sol, Díaz-Meco, M. Teresa, Moscat, Jorge, Castelli-Gair Hombría, James, Sotillos, Sol, Díaz-Meco, M. Teresa, Moscat, Jorge, and Castelli-Gair Hombría, James
- Abstract
Three protein complexes control polarization of epithelial cells: the apicolateral Crumbs and Par-3 complexes and the basolateral Lethal giant larvae complex [1] and [2] . Polarization results in the specific localization of proteins and lipids to different membrane domains. The receptors of the Notch, Hedgehog, and WNT pathways are among the proteins that are polarized, with subcellular receptor localization representing an important aspect of signaling regulation. For example, in the WNT pathway, differential DFz2 receptor localization results in activation of either the canonical or the planar polarity pathway [3]. Despite the large body of research on the vertebrate JAK/STAT pathway, there are no reports indicating polarized signaling. By using the conserved Drosophila JAK/STAT pathway as a system, we find that the receptor and its associated kinase are located in the apical membrane of epithelial cells. Unexpectedly, the transcription factor STAT is enriched in the apicolateral membrane domain of ectoderm epithelial cells in a Par-3-dependent manner. Our results indicate that preassembly of STAT and the Receptor/JAK complex to specific membrane domains is a key aspect for signaling efficiency. Our results also suggest that receptor polarization in the ectoderm cell membrane restricts the cell's response to ligands provided by neighboring cells.
- Published
- 2008
12. DaPKC-dependent phosphorylation of Crumbs is required for epithelial cell polarity in Drosophila
- Author
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Comunidad de Madrid, Ministerio de Economía y Competitividad (España), Ministerio de Ciencia y Tecnología (España), Fundación Juan March, Fundación Ramón Areces, Sotillos, Sol, Díaz-Meco, M. Teresa, Caminero, Eva, Moscat, Jorge, Campuzano, Sonsoles, Comunidad de Madrid, Ministerio de Economía y Competitividad (España), Ministerio de Ciencia y Tecnología (España), Fundación Juan March, Fundación Ramón Areces, Sotillos, Sol, Díaz-Meco, M. Teresa, Caminero, Eva, Moscat, Jorge, and Campuzano, Sonsoles
- Abstract
Both in Drosophila and vertebrate epithelial cells, the establishment of apicobasal polarity requires the apically localized, membrane-associated Par-3–Par-6–aPKC protein complex. In Drosophila, this complex colocalizes with the Crumbs–Stardust (Sdt)–Pals1-associated TJ protein (Patj) complex. Genetic and molecular analyses suggest a functional relationship between them. We show, by overexpression of a kinase-dead Drosophila atypical PKC (DaPKC), the requirement for the kinase activity of DaPKC to maintain the position of apical determinants and to restrict the localization of basolateral ones. We demonstrate a novel physical interaction between the apical complexes, via direct binding of DaPKC to both Crb and Patj, and identify Crumbs as a phosphorylation target of DaPKC. This phosphorylation of Crumbs is functionally significant. Thus, a nonphosphorylatable Crumbs protein behaves in vivo as a dominant negative. Moreover, the phenotypic effect of overexpressing wild-type Crumbs is suppressed by reducing DaPKC activity. These results provide a mechanistic framework for the functional interaction between the Par-3–Par-6–aPKC and Crumbs–Sdt–Patj complexes based in the posttranslational modification of Crb by DaPKC
- Published
- 2004
13. Essential role of RelA Ser311 phosphorylation by PKC in NF-kB transcriptional activation
- Author
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Fundación Juan March, Ministerio de Economía y Competitividad (España), Fundación Ramón Areces, Durán, Ángeles, Díaz-Meco, M. Teresa, Moscat, Jorge, Fundación Juan March, Ministerio de Economía y Competitividad (España), Fundación Ramón Areces, Durán, Ángeles, Díaz-Meco, M. Teresa, and Moscat, Jorge
- Abstract
The activation of the transcription factor NF-kB is central to the control of the cellular response triggered by many stimuli. Once released from the inhibitory molecule IkB, NF-kB is translocated to the nucleus, and it has to be phosphorylated to activate transcription. In protein kinase C (PKC)-deficient cells, NF-kB is transcriptionally inactive and the phosphorylation of the RelA subunit in response to tumor necrosis factor (TNF-alpha) is severely impaired. In vitro assays showed that PKC directly phosphorylates RelA. Here we demonstrate that Ser311 accounts for PKC phosphorylation of RelA and that this site is phosphorylated in vivo in response to TNF-alpha. Also, an inactivating mutation of that residue severely impairs RelA transcriptional activity, blocks its anti-apoptotic function and abrogates the interaction of RelA with the co-activator CBP as well as its recruitment, and that of RNA polymerase II (Pol II) with the interleukin-6 (IL-6) promoter. The interaction of endogenous CBP with endogenous RelA is inhibited in PKC-/- cells, as well as the binding of Pol II to the IL-6 promoter. These results demonstrate the mechanism whereby PKC regulates NF-kB activation in vivo
- Published
- 2003
14. Of the atypical PKCs, Par-4 and p62: recent understandings of the biology and pathology of a PB1-dominated complex
- Author
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Moscat, J, primary, Diaz-Meco, M T, additional, and Wooten, M W, additional
- Published
- 2009
- Full Text
- View/download PDF
15. Polarized Subcellular Localization of JAK/STAT Components Is Required for Efficient Signaling
- Author
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Sotillos, Sol, primary, Díaz-Meco, M. Teresa, additional, Moscat, Jorge, additional, and Castelli-Gair Hombría, James, additional
- Published
- 2008
- Full Text
- View/download PDF
16. PKCzeta-mediated GalphaQ stimulation of the ERK5 pathway plays a key role in cardiac hypertrophy
- Author
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García-Hoz, Carlota, primary, Herranz, Michel, additional, Teresa Díaz-Meco, M., additional, Moscat, Jorge, additional, Ribas, Catalina, additional, and Mayor Jr., Federico, additional
- Published
- 2007
- Full Text
- View/download PDF
17. PKCζ at the crossroad of NF-κB and Jak1/Stat6 signaling pathways
- Author
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Moscat, J, primary, Rennert, P, additional, and Diaz-Meco, M T, additional
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- 2005
- Full Text
- View/download PDF
18. Positioning atypical protein kinase C isoforms in the UV-induced apoptotic signaling cascade
- Author
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Berra, E, primary, Municio, M M, additional, Sanz, L, additional, Frutos, S, additional, Diaz-Meco, M T, additional, and Moscat, J, additional
- Published
- 1997
- Full Text
- View/download PDF
19. Lambda-interacting protein, a novel protein that specifically interacts with the zinc finger domain of the atypical protein kinase C isotype lambda/iota and stimulates its kinase activity in vitro and in vivo
- Author
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Diaz-Meco, M T, primary, Municio, M M, additional, Sanchez, P, additional, Lozano, J, additional, and Moscat, J, additional
- Published
- 1996
- Full Text
- View/download PDF
20. Protein kinase C-zeta mediates NF-kappa B activation in human immunodeficiency virus-infected monocytes
- Author
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Folgueira, L, primary, McElhinny, J A, additional, Bren, G D, additional, MacMorran, W S, additional, Diaz-Meco, M T, additional, Moscat, J, additional, and Paya, C V, additional
- Published
- 1996
- Full Text
- View/download PDF
21. Evidence for a role of MEK and MAPK during signal transduction by protein kinase C zeta.
- Author
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Berra, E., primary, Díaz-Meco, M. T., additional, Lozano, J., additional, Frutos, S., additional, Municio, M. M., additional, Sánchez, P., additional, Sanz, L., additional, and Moscat, J., additional
- Published
- 1995
- Full Text
- View/download PDF
22. Molecular characterization of a novel transcription factor that controls stromelysin expression
- Author
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Sanz, L, primary, Moscat, J, additional, and Diaz-Meco, M T, additional
- Published
- 1995
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- View/download PDF
23. Evidence for the in vitro and in vivo interaction of Ras with protein kinase C zeta.
- Author
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Diaz-Meco, M T, primary, Lozano, J, additional, Municio, M M, additional, Berra, E, additional, Frutos, S, additional, Sanz, L, additional, and Moscat, J, additional
- Published
- 1994
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- View/download PDF
24. NIH 3T3 cells stably transfected with the gene encoding phosphatidylcholine-hydrolyzing phospholipase C from Bacillus cereus acquire a transformed phenotype
- Author
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Johansen, T, primary, Bjørkøy, G, additional, Overvatn, A, additional, Diaz-Meco, M T, additional, Traavik, T, additional, and Moscat, J, additional
- Published
- 1994
- Full Text
- View/download PDF
25. Hydrolysis of phosphatidylcholine couples Ras to activation of Raf protein kinase during mitogenic signal transduction
- Author
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Cai, H, primary, Erhardt, P, additional, Troppmair, J, additional, Diaz-Meco, M T, additional, Sithanandam, G, additional, Rapp, U R, additional, Moscat, J, additional, and Cooper, G M, additional
- Published
- 1993
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26. Phosphatidylcholine hydrolysis activates NF-kappa B and increases human immunodeficiency virus replication in human monocytes and T lymphocytes
- Author
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Arenzana-Seisdedos, F, primary, Fernandez, B, additional, Dominguez, I, additional, Jacqué, J M, additional, Thomas, D, additional, Diaz-Meco, M T, additional, Moscat, J, additional, and Virelizier, J L, additional
- Published
- 1993
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- View/download PDF
27. A dominant negative protein kinase C zeta subspecies blocks NF-kappa B activation
- Author
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Diaz-Meco, M T, primary, Berra, E, additional, Municio, M M, additional, Sanz, L, additional, Lozano, J, additional, Dominguez, I, additional, Diaz-Golpe, V, additional, Lain de Lera, M T, additional, Alcamí, J, additional, and Payá, C V, additional
- Published
- 1993
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28. Inhibition of protein kinase C zeta subspecies blocks the activation of an NF-kappa B-like activity in Xenopus laevis oocytes.
- Author
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Dominguez, I, primary, Sanz, L, additional, Arenzana-Seisdedos, F, additional, Diaz-Meco, M T, additional, Virelizier, J L, additional, and Moscat, J, additional
- Published
- 1993
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29. Hydrolysis of phosphatidylcholine is stimulated by Ras proteins during mitogenic signal transduction.
- Author
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Cai, H, primary, Erhardt, P, additional, Szeberényi, J, additional, Diaz-Meco, M T, additional, Johansen, T, additional, Moscat, J, additional, and Cooper, G M, additional
- Published
- 1992
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30. Evidence for a role of protein kinase C zeta subspecies in maturation of Xenopus laevis oocytes.
- Author
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Dominguez, I, primary, Diaz-Meco, M T, additional, Municio, M M, additional, Berra, E, additional, García de Herreros, A, additional, Cornet, M E, additional, Sanz, L, additional, and Moscat, J, additional
- Published
- 1992
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31. Phospholipase C-mediated hydrolysis of phosphatidylcholine is a target of transforming growth factor beta 1 inhibitory signals
- Author
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Diaz-Meco, M T, primary, Dominguez, I, additional, Sanz, L, additional, Municio, M M, additional, Berra, E, additional, Cornet, M E, additional, Garcia de Herreros, A, additional, Johansen, T, additional, and Moscat, J, additional
- Published
- 1992
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- View/download PDF
32. Requirement of phospholipase C-catalyzed hydrolysis of phosphatidylcholine for maturation of Xenopus laevis oocytes in response to insulin and ras p21.
- Author
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García de Herreros, A, primary, Dominguez, I, additional, Diaz-Meco, M T, additional, Graziani, G, additional, Cornett, M E, additional, Guddal, P H, additional, Johansen, T, additional, and Moscat, J, additional
- Published
- 1991
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33. Mechanism of inhibition of adenylate cyclase by phospholipase C-catalyzed hydrolysis of phosphatidylcholine. Involvement of a pertussis toxin-sensitive G protein and protein kinase C.
- Author
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Diaz-Laviada, I, primary, Larrodera, P, additional, Nieto, J L, additional, Cornet, M E, additional, Diaz-Meco, M T, additional, Sanchez, M J, additional, Guddal, P H, additional, Johansen, T, additional, Haro, A, additional, and Moscat, J, additional
- Published
- 1991
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- View/download PDF
34. Evidence for a role of phosphatidylcholine-hydrolysing phospholipase C in the regulation of protein kinase C by ras and src oncogenes.
- Author
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Diaz-Laviada, I., primary, Larrodera, P., additional, Diaz-Meco, M. T., additional, Cornet, M. E., additional, Guddal, P. H., additional, Johansen, T., additional, and Moscat, J., additional
- Published
- 1990
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35. Kinetic evidence of a rapid activation of phosphatidylcholine hydrolysis by Ki-ras oncogene. Possible involvement in late steps of the mitogenic cascade.
- Author
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Lopez-Barahona, M, primary, Kaplan, P L, additional, Cornet, M E, additional, Diaz-Meco, M T, additional, Larrodera, P, additional, Diaz-Laviada, I, additional, Municio, A M, additional, and Moscat, J, additional
- Published
- 1990
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- View/download PDF
36. Haemolysis due to active venous drainage during cardiopulmonary bypass: comparison of two different techniques.
- Author
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Cirri, S., Negri, L., Babbini, M., Latis, G., Khlat, B., Tarelli, G., Panisi, P., Mazzaro, E., Bellisario, A., Borghetti, B., Bordignon, F., Ferrara, M., Pavan, H., and Meco, M.
- Subjects
HEMOLYSIS & hemolysins ,CARDIAC surgery ,CENTRIFUGAL pumps ,HEMORRHAGE - Abstract
To facilitate mini-access for cardiac surgery, two different methods of active venous drainage are used: vacuum assisted drainage and centrifugal pump aspiration on the venous line. The aim of this study was to compare the haemolysis produced using these two techniques. From June to December 1999, 50 consecutive patients were operated on using a ministernotomy. All of these patients had valvular surgery for either valve repair or valve replacement (9 MVRepair, 11 MVR, 29 AVR, 1 AVR 1 MVR). They were randomized into two groups: Group A, 25 patients who underwent surgery where vacuum assisted drainage was used, and Group B, 25 patients where kinetic asssisted venous drainage with centrifugal pump venous aspiration was used. Patient characteristics of both groups were similar for age, gender, body weight, body surface area, height, cardiopulmonary bypass (CPB) time, aortic crossclamp time, priming volume, cardioplegia volume, haemoglobin concentration, haematocrit, serum creatinine, bilirubin, lactate dehydrogenase (LDH), serum glutamic oxaloacetic transaminase (sGOT), serum glutamic pyruvic transaminase (sGPT), aptoglobin, reticulocytes, and platelet count. We checked all these laboratory parameters preoperatively, at the end of CPB, and 2 and 24h after operation. We also checked haemoglobinuria at these same time points. We assessed blood loss at 6, 12, and 24 h after the operation and calculated total postoperative bleeding. There was a tendency towards a greater increase in LDH, sGOT and sGPT in Group A more than in Group B, but these data did not reach statistical significance. Platelet count was always lower in Group A and aptoglobin increased in Group A more than in Group B. More patients in Group A had haemoglobinuria. These findings indicate that haemolysis is increased more in patients treated with vacuum assisted drainage, when compared to the rise in haemolysis in those treated with centrifugal pump venous drainage. Total bleeding is also greater in Group A. [ABSTRACT FROM AUTHOR]
- Published
- 2001
- Full Text
- View/download PDF
37. Regulation and role of the atypical pkc isoforms in cell survival during tumor transformation
- Author
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Moscat, J., Sanz, L., Sanchez, P., and Diaz-Meco, M. T.
- Published
- 2001
- Full Text
- View/download PDF
38. Inactivation of the inhibitory kappaB protein kinase/nuclear factor kappaB pathway by Par-4 expression potentiates tumor necrosis factor alpha-induced apoptosis.
- Author
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Diaz-Meco, M T, Lallena, M J, Monjas, A, Frutos, S, and Moscat, J
- Abstract
Par-4 is a novel protein identified in cells undergoing apoptosis. The ability of Par-4 to promote apoptotic cell death is dependent on the binding and inactivation of the atypical protein kinases C (PKCs). This subfamily of kinases has been reported to control nuclear factor kappaB (NF-kappaB) through the regulation of the IkappaB kinase activity. NF-kappaB activation by tumor necrosis factor alpha (TNFalpha) provides a survival signal that impairs the TNFalpha-induced apoptotic response. We show here that expression of Par-4 inhibits the TNFalpha-induced nuclear translocation of p65 as well as the kappaB-dependent promoter activity. Interestingly, Par-4 expression blocks inhibitory kappaB protein (IkappaB) kinase activity, which leads to the inhibition of IkappaB phosphorylation and degradation, in a manner that is dependent on its ability to inhibit lambda/iotaPKC. Of potential functional relevance, the expression of Par-4 allows TNFalpha to induce apoptosis in NIH-3T3 cells. In addition, the down-regulation of Par-4 levels by oncogenic Ras sensitizes cells to TNFalpha-induced NF-kappaB activation.
- Published
- 1999
39. Cleavage of zetaPKC but not lambda/iotaPKC by caspase-3 during UV-induced apoptosis.
- Author
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Frutos, S, Moscat, J, and Diaz-Meco, M T
- Abstract
The stimulation of caspases is a critical event in apoptotic cell death. Several kinases critically involved in cell proliferation pathways have been shown to be cleaved by caspase-mediated mechanisms. Thus, the degradation of delta protein kinase C (PKC) and MEKK-1 by caspase-3 generates activated fragments corresponding to their catalytic domains, consistent with the observations that both enzymes are important for apoptosis. In contrast, other kinases reported to have anti-apoptotic properties, such as Raf-1 and Akt, are inactivated by proteolytic degradation by the caspase system. Since the atypical PKCs have been shown to play critical roles in cell survival, in the study reported here we have addressed the potential degradation of these PKCs by the caspase system in UV-irradiated HeLa cells. Herein we show that although zetaPKC and lambda/iotaPKC are both inhibited in UV-treated cells, only zetaPKC but not lambda/iotaPKC is cleaved by a caspase-mediated process. This cleavage generates a fragment that corresponds to its catalytic domain that is enzymatically inactive. The sequence where caspase-3 cleaves zetaPKC was mapped, and a mutant resistant to degradation was shown to protect cells from apoptosis more efficiently than the wild-type enzyme.
- Published
- 1999
40. Activation of IkappaB kinase beta by protein kinase C isoforms.
- Author
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Lallena, M J, Diaz-Meco, M T, Bren, G, Payá, C V, and Moscat, J
- Abstract
The atypical protein kinase C (PKC) isotypes (lambda/iotaPKC and zetaPKC) have been shown to be critically involved in important cell functions such as proliferation and survival. Previous studies have demonstrated that the atypical PKCs are stimulated by tumor necrosis factor alpha (TNF-alpha) and are required for the activation of NF-kappaB by this cytokine through a mechanism that most probably involves the phosphorylation of IkappaB. The inability of these PKC isotypes to directly phosphorylate IkappaB led to the hypothesis that zetaPKC may use a putative IkappaB kinase to functionally inactivate IkappaB. Recently several groups have molecularly characterized and cloned two IkappaB kinases (IKKalpha and IKKbeta) which phosphorylate the residues in the IkappaB molecule that serve to target it for ubiquitination and degradation. In this study we have addressed the possibility that different PKCs may control NF-kappaB through the activation of the IKKs. We report here that alphaPKC as well as the atypical PKCs bind to the IKKs in vitro and in vivo. In addition, overexpression of zetaPKC positively modulates IKKbeta activity but not that of IKKalpha, whereas the transfection of a zetaPKC dominant negative mutant severely impairs the activation of IKKbeta but not IKKalpha in TNF-alpha-stimulated cells. We also show that cell stimulation with phorbol 12-myristate 13-acetate activates IKKbeta, which is entirely dependent on the activity of alphaPKC but not that of the atypical isoforms. In contrast, the inhibition of alphaPKC does not affect the activation of IKKbeta by TNF-alpha. Interestingly, recombinant active zetaPKC and alphaPKC are able to stimulate in vitro the activity of IKKbeta but not that of IKKalpha. In addition, evidence is presented here that recombinant zetaPKC directly phosphorylates IKKbeta in vitro, involving Ser177 and Ser181. Collectively, these results demonstrate a critical role for the PKC isoforms in the NF-kappaB pathway at the level of IKKbeta activation and IkappaB degradation.
- Published
- 1999
41. Highly efficient PWM strategy over FPGA.
- Author
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Vargas, F., Meco, M. J., Heredia, J. R., and Ruiz, A.
- Subjects
- *
PULSE modulation , *LINEAR electric circuits , *FIELD programmable gate arrays , *SIGNAL detection , *COMMUTATION (Electricity) - Abstract
A novel pulse-width-modulation (PWM) technique, based on linear functions that are easy to implement over FPGA and take up little hardware resources, is presented. The technique generates high-quality voltages with very few commutations per cycle and is highly efficient in reducing commutation loss. It has been implemented, tested and compared to other PWM techniques and results show that it yields a better quality signal with only a quarter of commutations per cycle. [ABSTRACT FROM AUTHOR]
- Published
- 2008
- Full Text
- View/download PDF
42. The activation of p38 and apoptosis by the inhibition of Erk is antagonized by the phosphoinositide 3-kinase/Akt pathway.
- Author
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Berra, E, Diaz-Meco, M T, and Moscat, J
- Abstract
Considerable attention has recently been focused on the role played by different kinase cascades in the control of apoptosis. The triggering of stress-activated kinases concomitant with the inhibition of the extracellular signal-regulated kinase (ERK) pathway has been observed in a number of cell systems undergoing programmed cell death. In addition, the activation of the phosphoinositide 3-kinase (PI 3-kinase)-Akt signaling cascade has been shown to protect from apoptosis. Here we have explored the potential role played by the inhibition of ERK in the activation of the stress kinases as well as the possible cross-talk with the PI 3-kinase pathway in HeLa cells. We show that the simple inhibition of ERK basal activity is sufficient to trigger apoptosis and p38 activation with no changes in Jun N-terminal kinase/stress-activated protein kinase. This is a process dependent on the caspases and is completely abrogated by serum. The incubation with wortmannin or the transfection of dominant negative mutants of p85 or Akt block the inhibitory function of serum, suggesting the involvement of the PI 3-kinase-Akt system. Consistent with this, expression of active mutants of PI 3-kinase and Akt inhibits p38 activation and apoptosis. We also show here that the inhibition of ERK triggers the caspase system, which is abolished by serum in a wortmannin-dependent manner. Collectively, these results demonstrate a link between ERK and the p38 apoptotic pathway that is modulated by the survival PI 3-kinase-Akt module, acting upstream the caspase system.
- Published
- 1998
43. Evidence for a bifurcation of the mitogenic signaling pathway activated by Ras and phosphatidylcholine-hydrolyzing phospholipase C.
- Author
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Bjørkøy, G, Overvatn, A, Diaz-Meco, M T, Moscat, J, and Johansen, T
- Abstract
NIH 3T3 cells stably transfected with the gene encoding phosphatidylcholine-hydrolyzing phospholipase C (PC-PLC) from Bacillus cereus display a chronic elevation of intracellular diacylglycerol levels and a transformed phenotype. We have used such PC-PLC-transformed cells to evaluate the roles of the cytoplasmic serine/threonine kinases Raf-1, zeta protein kinase C (zeta PKC) and protein kinase A (PKA) in oncogenesis and mitogenic signal transduction elicited by phosphatidylcholine hydrolysis. We demonstrate here that stable expression of dominant negative mutants of both zeta PKC and Raf-1 lead to reversion of PC-PLC-transformed cells. Interestingly, expression of kinase defective zeta PKC also reverted NIH 3T3 cells transformed by the v-Ha-ras oncogene. Activation of PKA in response to elevation of cAMP levels also lead to reversion of PC-PLC-induced transformation, implicating PKA as a negative regulator acting downstream of PC-PLC. On the other hand, inhibition or depletion of phorbol ester responsive PKCs attenuated but did not block the ability of PC-PLC-transformed cells to induce DNA synthesis in the absence of growth factors. These results clearly implicate both Raf-1 and zeta PKC as necessary downstream components for transduction of the mitogenic/oncogenic signal generated by PLC-mediated hydrolysis of phosphatidylcholine and suggest, together with other recent evidence, a bifurcation in the signaling pathway downstream of PC-PLC.
- Published
- 1995
44. Cross-talk between different enhancer elements during mitogenic induction of the human stromelysin-1 gene.
- Author
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Kirstein, M, Sanz, L, Quiñones, S, Moscat, J, Diaz-Meco, M T, and Saus, J
- Abstract
Platelet-derived growth factor (PDGF) induces the expression of human stromelysin-1, a matrix metalloproteinase involved in tumor invasion and metastasis. Here it is shown that stromelysin-1 gene induction by PDGF depends on Ras and involves three previously identified promoter elements (the stromelysin-1 PDGF-responsive element (SPRE) site, the two head-to-head polyomavirus enhancer A-binding protein-3 (PEA3) sites, and the activator protein-1 (AP-1) binding site). During mitogenic induction, these responsive elements appear to be organized in two independent transcriptional units, SPRE-AP-1 and PEA3-AP-1, which result from specific element cross-talking. Interestingly, expression of a dominant negative mutant of Raf-1 significantly interfered with the induction through PEA3-AP-1 but not with that operating through SPRE-AP-1. Conversely, only the induction operating through SPRE-AP-1 was affected significantly by the expression of a dominant negative mutant of the atypical lambda/iota protein kinase C (lambda/iotaPKC). These data strongly suggest that the signal triggered by PDGF flows through Ras and bifurcates toward two distinct pathways, one operating through Raf and involving PEA3-AP-1 and the other one Raf-independent, operating through lambda/iotaPKC and SPRE-AP-1. Furthermore, we present evidence suggesting that the novel SPRE-binding transcription factor SPBP cross-couples with c-Jun to transactivate the SPRE site.
- Published
- 1996
45. Role of diacylglycerol-regulated protein kinase C isotypes in growth factor activation of the Raf-1 protein kinase
- Author
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Cai, H, Smola, U, Wixler, V, Eisenmann-Tappe, I, Diaz-Meco, M T, Moscat, J, Rapp, U, and Cooper, G M
- Abstract
The Raf protein kinases function downstream of Ras guanine nucleotide-binding proteins to transduce intracellular signals from growth factor receptors. Interaction with Ras recruits Raf to the plasma membrane, but the subsequent mechanism of Raf activation has not been established. Previous studies implicated hydrolysis of phosphatidylcholine (PC) in Raf activation; therefore, we investigated the role of the epsilon isotype of protein kinase C (PKC), which is stimulated by PC-derived diacylglycerol, as a Raf activator. A dominant negative mutant of PKC epsilon inhibited both proliferation of NIH 3T3 cells and activation of Raf in COS cells. Conversely, overexpression of active PKC epsilon stimulated Raf kinase activity in COS cells and overcame the inhibitory effects of dominant negative Ras in NIH 3T3 cells. PKC epsilon also stimulated Raf kinase in baculovirus-infected Spodoptera frugiperda Sf9 cells and was able to directly activate Raf in vitro. Consistent with its previously reported activity as a Raf activator in vitro, PKC alpha functioned similarly to PKC epsilon in both NIH 3T3 and COS cell assays. In addition, constitutively active mutants of both PKC alpha and PKC epsilon overcame the inhibitory effects of dominant negative mutants of the other PKC isotype, indicating that these diacylglycerol-regulated PKCs function as redundant activators of Raf-1 in vivo.
- Published
- 1997
- Full Text
- View/download PDF
46. Identification of heterogeneous ribonucleoprotein A1 as a novel substrate for protein kinase C zeta.
- Author
-
Municio, M M, Lozano, J, Sánchez, P, Moscat, J, and Diaz-Meco, M T
- Abstract
The zeta isoform of protein kinase C (zeta PKC) has been shown to be an important step in mitogenic signal transduction. Using a yeast interaction screen to search for potential novel substrates of zeta PKC, we identified the heterogeneous ribonucleoprotein A1 (hnRNPA1). This protein specifically interacts with the catalytic domain of zeta PKC but not with its regulatory region or with the full-length protein, or with a kinase-defective mutant of the zeta PKC catalytic domain. In addition, no interaction was detected with other kinases such as Raf-1 or Mos, that, like zeta PKC, are critically involved in signal transduction, or with the catalytic domain of epsilon PKC, which is the PKC isotype with the highest homology to zeta PKC. hnRNPA1 is directly phosphorylated by both recombinant and native zeta PKC, and this phosphorylation is increased when zeta PKC is immunoprecipitated from mitogen-activated fibroblasts. As an additional control, hnRNPA1 is not phosphorylated appreciably by catalytic epsilon PKC or by a mixture of highly purified classical PKC isotypes maximally activated by phosphatidylserine and Ca2+. Treatment of quiescent cell cultures with a potent mitogen such as platelet-derived growth factor promotes a significant phosphorylation of hnRNPA1 in vivo that is impaired by expression of a dominant negative mutant of zeta PKC. Furthermore, expression of a catalytically active zeta PKC mutant phosphorylates hnRNPA1 in vivo. These findings suggest that zeta PKC could be critically involved in a novel pathway that connects membrane signaling to nuclear regulatory events, at the level of RNA transport and processing. Results also shown here by using different zeta PKC mutants suggesting the control of the cytoplasmic localization of hnRNPA1 by zeta PKC. Also of potential functional relevance are the results demonstrating that the phosphorylation by zeta PKC severely impairs both hnRNPA1 RNA binding and its ability to promote strand annealing in vitro.
- Published
- 1995
47. Phospholipase C-mediated hydrolysis of phosphatidylcholine is activated by muscarinic agonists
- Author
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Diaz-Meco, M T, Larrodera, P, Lopez-Barahona, M, Cornet, M E, Barreno, P G, and Moscat, J
- Abstract
The phospholipase C-catalysed breakdown of inositol-containing phospholipids is an important source of diacylglycerol in cells stimulated by several agonists. However, recent experimental evidence suggests that major phospholipids such as phosphatidylcholine may also be substrates of the phosphodiesteratic hydrolysis activated by hormones, growth factors and oncogene products. We show here that stimulation of muscarinic agonists activates the release of phosphocholine, which, along with diacylglycerol, is a metabolic product of phospholipase C-mediated hydrolysis of phosphatidylcholine. Fluoroaluminates mimic this muscarinic effect, strongly suggesting that carbachol-activated release of phosphocholine may be mediated by a guanine-nucleotide-binding protein. Evidence for this was obtained from experiments using permeabilized cells in which non-hydrolysable analogues of GTP activated phosphocholine release synergistically with carbachol.
- Published
- 1989
- Full Text
- View/download PDF
48. Short-circuit currents in a synchronous generator using the Lagrangian function method
- Author
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Moreno, F. M., Texeira, M. M., Moyano, J. A., Meco, M., Rodriguez, A., Gonzalez, J. E. R., and Vazquez, J. J. L.
49. Mortality and morbidity from intra-aortic balloon pumps. Risk analysis
- Author
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Meco, M., Gramegna, G., Yassini, A., Bellisario, A., Mazzaro, E., Babbini, M., Pediglieri, A., Panisi, P., Tarelli, G., Alessandro Frigiola, Menicanti, L., and Cirri, S.
- Subjects
Aged, 80 and over ,Male ,Intra-Aortic Balloon Pumping ,Heart Diseases ,Incidence ,Middle Aged ,Risk Assessment ,Postoperative Complications ,Predictive Value of Tests ,Risk Factors ,Humans ,Female ,Vascular Diseases ,Cardiac Surgical Procedures ,Aged ,Retrospective Studies - Abstract
The purpose of this study, was to assess the incidence of and predictors for mortality and morbidity in patients who required postoperative intra-aortic balloon pump (IABP) support.We have retrospectively estimated 116 patients and data were statistically analyzed, and significant variables were evaluated with multivariate analysis.Mortality rate was 57.8% (67 patients). Nineteen patients (16.3%) had major vascular complications: 12 patients (10.3%) limb ischemia, 1 patient (0.9%) aortic dissection, 6 patients (5.2%) mesenteric infarction. Thirty patients (25.8%) had minor vascular complication: 23 patients (19.8%) bleeding from insertion site, 7 (6%) patients infection of insertion site. Limb ischemia was resolved by IABP removal (10 patients), thrombectomy (2 patients). No patient required limb amputation. Sixty patients (51.7%) had renal insufficiency, of which 40 patients needed dialysis. Fifteen patients (10.3%) had neurological complications, 13 patients (11.2%) thrombocytopenia and 5 patients (4.3%) sepsis.The incidence of IABP insertion in our institution was 1.5%. Mortality rate is similar to mortality of other studies in which the IABP has been inserted in the postoperative period. We have found that timing of IABP insertion, thrombocytopenia, presence of peripheral vascular disease and the redo intervention are independent predictors of mortality. We also found that female sex, diabetes, history of cigarette smoking and preoperative use of antiplatelet drugs are independent predictors of limb ischemia. The following factors are instead independent predictors of renal insufficiency: postoperative ejection fraction lower than 40% and non use of dobutamine in the postoperative period.
50. Mechanism of inhibition of adenylate cyclase by phospholipase C-catalyzed hydrolysis of phosphatidylcholine. Involvement of a pertussis toxin-sensitive G protein and protein kinase C
- Author
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Ines Diaz-Laviada, Larrodera, P., Nieto, J. L., Cornet, M. E., Diaz-Meco, M. T., Sanchez, M. J., Guddal, P. H., Johansen, T., Haro, A., and Moscat, J.
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