210 results on '"Alnemri, E. S"'
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2. Mutations in NALP12 Cause Hereditary Periodic Fever Syndromes
- Author
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Jéru, I., Duquesnoy, P., Fernandes-Alnemri, T., Cochet, E., Yu, J. W., Lackmy-Port-Lis, M., Grimprel, E., Landman-Parker, J., Hentgen, V., Marlin, S., McElreavey, K., Sarkisian, T., Grateau, G., Alnemri, E. S., and Amselem, S.
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- 2008
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3. 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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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. 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H., Finkbeiner, S., Finkel, T., Fiorito, F., Fisher, P. B., Flajolet, M., Flamigni, F., Florey, O., Florio, S., Floto, R. A., Folini, M., Follo, C., Fon, E. A., Fornai, F., Fortunato, F., Fraldi, A., Franco, R., Francois, A., François, A., Frankel, L. B., Fraser, I. D. C., Frey, N., Freyssenet, D. G., Frezza, C., Friedman, S. L., Frigo, D. E., Fu, D., Fuentes, J. M., Fueyo, J., Fujitani, Y., Fujiwara, Y., Fujiya, M., Fukuda, M., Fulda, S., Fusco, C., Gabryel, B., Gaestel, M., Gailly, P., Gajewska, M., Galadari, S., Galili, G., Galindo, I., Galindo, M. F., Galliciotti, G., Galluzzi, L., Galy, V., Gammoh, N., Gandy, S., Ganesan, A. K., Ganesan, S., Ganley, I. G., Gannagé, M., Gao, F. -B., Gao, F., Gao, J. -X., Nannig, L. G., Véscovi, E. G., Garcia-Macía, M., Garcia-Ruiz, C., Garg, A. D., Garg, P. K., Gargini, R., Gassen, N. C., Gatica, D., Gatti, E., Gavard, J., Gavathiotis, E., Ge, L., Ge, P., Ge, S., Gean, P. -W., Gelmetti, V., Genazzani, A. 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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. 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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
4. Essential versus accessory aspects of cell death: recommendations of the NCCD 2015
- Author
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Galluzzi, L, primary, Bravo-San Pedro, J M, additional, Vitale, I, additional, Aaronson, S A, additional, Abrams, J M, additional, Adam, D, additional, Alnemri, E S, additional, Altucci, L, additional, Andrews, D, additional, Annicchiarico-Petruzzelli, M, additional, Baehrecke, E H, additional, Bazan, N G, additional, Bertrand, M J, additional, Bianchi, K, additional, Blagosklonny, M V, additional, Blomgren, K, additional, Borner, C, additional, Bredesen, D E, additional, Brenner, C, additional, Campanella, M, additional, Candi, E, additional, Cecconi, F, additional, Chan, F K, additional, Chandel, N S, additional, Cheng, E H, additional, Chipuk, J E, additional, Cidlowski, J A, additional, Ciechanover, A, additional, Dawson, T M, additional, Dawson, V L, additional, De Laurenzi, V, additional, De Maria, R, additional, Debatin, K-M, additional, Di Daniele, N, additional, Dixit, V M, additional, Dynlacht, B D, additional, El-Deiry, W S, additional, Fimia, G M, additional, Flavell, R A, additional, Fulda, S, additional, Garrido, C, additional, Gougeon, M-L, additional, Green, D R, additional, Gronemeyer, H, additional, Hajnoczky, G, additional, Hardwick, J M, additional, Hengartner, M O, additional, Ichijo, H, additional, Joseph, B, additional, Jost, P J, additional, Kaufmann, T, additional, Kepp, O, additional, Klionsky, D J, additional, Knight, R A, additional, Kumar, S, additional, Lemasters, J J, additional, Levine, B, additional, Linkermann, A, additional, Lipton, S A, additional, Lockshin, R A, additional, López-Otín, C, additional, Lugli, E, additional, Madeo, F, additional, Malorni, W, additional, Marine, J-C, additional, Martin, S J, additional, Martinou, J-C, additional, Medema, J P, additional, Meier, P, additional, Melino, S, additional, Mizushima, N, additional, Moll, U, additional, Muñoz-Pinedo, C, additional, Nuñez, G, additional, Oberst, A, additional, Panaretakis, T, additional, Penninger, J M, additional, Peter, M E, additional, Piacentini, M, additional, Pinton, P, additional, Prehn, J H, additional, Puthalakath, H, additional, Rabinovich, G A, additional, Ravichandran, K S, additional, Rizzuto, R, additional, Rodrigues, C M, additional, Rubinsztein, D C, additional, Rudel, T, additional, Shi, Y, additional, Simon, H-U, additional, Stockwell, B R, additional, Szabadkai, G, additional, Tait, S W, additional, Tang, H L, additional, Tavernarakis, N, additional, Tsujimoto, Y, additional, Vanden Berghe, T, additional, Vandenabeele, P, additional, Villunger, A, additional, Wagner, E F, additional, Walczak, H, additional, White, E, additional, Wood, W G, additional, Yuan, J, additional, Zakeri, Z, additional, Zhivotovsky, B, additional, Melino, G, additional, and Kroemer, G, additional
- Published
- 2014
- Full Text
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5. Loss of HtrA2/Omi activity in non-neuronal tissues of adult mice causes premature aging
- Author
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Kang, S, primary, Louboutin, J-P, additional, Datta, P, additional, Landel, C P, additional, Martinez, D, additional, Zervos, A S, additional, Strayer, D S, additional, Fernandes-Alnemri, T, additional, and Alnemri, E S, additional
- Published
- 2012
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6. Molecular definitions of cell death subroutines: recommendations of the Nomenclature Committee on Cell Death 2012
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Galluzzi, L, primary, Vitale, I, additional, Abrams, J M, additional, Alnemri, E S, additional, Baehrecke, E H, additional, Blagosklonny, M V, additional, Dawson, T M, additional, Dawson, V L, additional, El-Deiry, W S, additional, Fulda, S, additional, Gottlieb, E, additional, Green, D R, additional, Hengartner, M O, additional, Kepp, O, additional, Knight, R A, additional, Kumar, S, additional, Lipton, S A, additional, Lu, X, additional, Madeo, F, additional, Malorni, W, additional, Mehlen, P, additional, Nuñez, G, additional, Peter, M E, additional, Piacentini, M, additional, Rubinsztein, D C, additional, Shi, Y, additional, Simon, H-U, additional, Vandenabeele, P, additional, White, E, additional, Yuan, J, additional, Zhivotovsky, B, additional, Melino, G, additional, and Kroemer, G, additional
- Published
- 2011
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7. Guidelines for the use and interpretation of assays for monitoring cell death in higher eukaryotes
- Author
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Galluzzi, L, primary, Aaronson, S A, additional, Abrams, J, additional, Alnemri, E S, additional, Andrews, D W, additional, Baehrecke, E H, additional, Bazan, N G, additional, Blagosklonny, M V, additional, Blomgren, K, additional, Borner, C, additional, Bredesen, D E, additional, Brenner, C, additional, Castedo, M, additional, Cidlowski, J A, additional, Ciechanover, A, additional, Cohen, G M, additional, De Laurenzi, V, additional, De Maria, R, additional, Deshmukh, M, additional, Dynlacht, B D, additional, El-Deiry, W S, additional, Flavell, R A, additional, Fulda, S, additional, Garrido, C, additional, Golstein, P, additional, Gougeon, M-L, additional, Green, D R, additional, Gronemeyer, H, additional, Hajnóczky, G, additional, Hardwick, J M, additional, Hengartner, M O, additional, Ichijo, H, additional, Jäättelä, M, additional, Kepp, O, additional, Kimchi, A, additional, Klionsky, D J, additional, Knight, R A, additional, Kornbluth, S, additional, Kumar, S, additional, Levine, B, additional, Lipton, S A, additional, Lugli, E, additional, Madeo, F, additional, Malorni, W, additional, Marine, J-CW, additional, Martin, S J, additional, Medema, J P, additional, Mehlen, P, additional, Melino, G, additional, Moll, U M, additional, Morselli, E, additional, Nagata, S, additional, Nicholson, D W, additional, Nicotera, P, additional, Nuñez, G, additional, Oren, M, additional, Penninger, J, additional, Pervaiz, S, additional, Peter, M E, additional, Piacentini, M, additional, Prehn, J H M, additional, Puthalakath, H, additional, Rabinovich, G A, additional, Rizzuto, R, additional, Rodrigues, C M P, additional, Rubinsztein, D C, additional, Rudel, T, additional, Scorrano, L, additional, Simon, H-U, additional, Steller, H, additional, Tschopp, J, additional, Tsujimoto, Y, additional, Vandenabeele, P, additional, Vitale, I, additional, Vousden, K H, additional, Youle, R J, additional, Yuan, J, additional, Zhivotovsky, B, additional, and Kroemer, G, additional
- Published
- 2009
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- View/download PDF
8. Classification of cell death: recommendations of the Nomenclature Committee on Cell Death 2009
- Author
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Kroemer, G, primary, Galluzzi, L, additional, Vandenabeele, P, additional, Abrams, J, additional, Alnemri, E S, additional, Baehrecke, E H, additional, Blagosklonny, M V, additional, El-Deiry, W S, additional, Golstein, P, additional, Green, D R, additional, Hengartner, M, additional, Knight, R A, additional, Kumar, S, additional, Lipton, S A, additional, Malorni, W, additional, Nuñez, G, additional, Peter, M E, additional, Tschopp, J, additional, Yuan, J, additional, Piacentini, M, additional, Zhivotovsky, B, additional, and Melino, G, additional
- Published
- 2008
- Full Text
- View/download PDF
9. The interaction of DIAP1 with dOmi/HtrA2 regulates cell death in Drosophila
- Author
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Khan, F S, primary, Fujioka, M, additional, Datta, P, additional, Fernandes-Alnemri, T, additional, Jaynes, J B, additional, and Alnemri, E S, additional
- Published
- 2008
- Full Text
- View/download PDF
10. The pyroptosome: a supramolecular assembly of ASC dimers mediating inflammatory cell death via caspase-1 activation
- Author
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Fernandes-Alnemri, T, primary, Wu, J, additional, Yu, J-W, additional, Datta, P, additional, Miller, B, additional, Jankowski, W, additional, Rosenberg, S, additional, Zhang, J, additional, and Alnemri, E S, additional
- Published
- 2007
- Full Text
- View/download PDF
11. Essential versus accessory aspects of cell death: recommendations of the NCCD 2015.
- Author
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Galluzzi, L, Bravo-San Pedro, J M, Vitale, I, Aaronson, S A, Abrams, J M, Adam, D, Alnemri, E S, Altucci, L, Andrews, D, Annicchiarico-Petruzzelli, M, Baehrecke, E H, Bazan, N G, Bertrand, M J, Bianchi, K, Blagosklonny, M V, Blomgren, K, Borner, C, Bredesen, D E, Brenner, C, and Campanella, M
- Subjects
CELL death inhibition ,CELL-mediated cytotoxicity ,GENETIC code ,GENETIC transcription ,GENETIC engineering research - Abstract
Cells exposed to extreme physicochemical or mechanical stimuli die in an uncontrollable manner, as a result of their immediate structural breakdown. Such an unavoidable variant of cellular demise is generally referred to as 'accidental cell death' (ACD). In most settings, however, cell death is initiated by a genetically encoded apparatus, correlating with the fact that its course can be altered by pharmacologic or genetic interventions. 'Regulated cell death' (RCD) can occur as part of physiologic programs or can be activated once adaptive responses to perturbations of the extracellular or intracellular microenvironment fail. The biochemical phenomena that accompany RCD may be harnessed to classify it into a few subtypes, which often (but not always) exhibit stereotyped morphologic features. Nonetheless, efficiently inhibiting the processes that are commonly thought to cause RCD, such as the activation of executioner caspases in the course of apoptosis, does not exert true cytoprotective effects in the mammalian system, but simply alters the kinetics of cellular demise as it shifts its morphologic and biochemical correlates. Conversely, bona fide cytoprotection can be achieved by inhibiting the transduction of lethal signals in the early phases of the process, when adaptive responses are still operational. Thus, the mechanisms that truly execute RCD may be less understood, less inhibitable and perhaps more homogeneous than previously thought. Here, the Nomenclature Committee on Cell Death formulates a set of recommendations to help scientists and researchers to discriminate between essential and accessory aspects of cell death. [ABSTRACT FROM AUTHOR]
- Published
- 2015
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- View/download PDF
12. Cryopyrin and pyrin activate caspase-1, but not NF-κB, via ASC oligomerization
- Author
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Yu, J-W, primary, Wu, J, additional, Zhang, Z, additional, Datta, P, additional, Ibrahimi, I, additional, Taniguchi, S, additional, Sagara, J, additional, Fernandes-Alnemri, T, additional, and Alnemri, E S, additional
- Published
- 2005
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- View/download PDF
13. Intramitochondrial serine protease activity of Omi/HtrA2 is required for caspase-independent cell death of human neutrophils
- Author
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Blink, E, primary, Maianski, N A, additional, Alnemri, E S, additional, Zervos, A S, additional, Roos, D, additional, and Kuijpers, T W, additional
- Published
- 2004
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- View/download PDF
14. Functional characterization of mitochondria in neutrophils: a role restricted to apoptosis
- Author
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Maianski, N A, primary, Geissler, J, additional, Srinivasula, S M, additional, Alnemri, E S, additional, Roos, D, additional, and Kuijpers, T W, additional
- Published
- 2003
- Full Text
- View/download PDF
15. Control of erythroid cell production via caspase-mediated cleavage of transcription factor SCL/Tal-1
- Author
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Zeuner, A, primary, Eramo, A, additional, Testa, U, additional, Felli, N, additional, Pelosi, E, additional, Mariani, G, additional, Srinivasula, S M, additional, Alnemri, E S, additional, Condorelli, G, additional, Peschle, C, additional, and De Maria, R, additional
- Published
- 2003
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- View/download PDF
16. Expression and transcriptional regulation of caspase-14 in simple and complex epithelia
- Author
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Pistritto, G, primary, Jost, M, additional, Srinivasula, S M, additional, Baffa, R, additional, Poyet, J-L, additional, Kari, C, additional, Lazebnik, Y, additional, Rodeck, U, additional, and Alnemri, E S, additional
- Published
- 2002
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- View/download PDF
17. Death effector domain-containing proteins DEDD and FLAME-3 form nuclear complexes with the TFIIIC102 subunit of human transcription factor IIIC
- Author
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Zhan, Y, primary, Hegde, R, additional, Srinivasula, S M, additional, Fernandes-Alnemri, T, additional, and Alnemri, E S, additional
- Published
- 2002
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- View/download PDF
18. The serine protease Omi/HtrA2 is released from mitochondria during apoptosis. Omi interacts with caspase-inhibitor XIAP and induces enhanced caspase activity
- Author
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van Loo, G, primary, van Gurp, M, additional, Depuydt, B, additional, Srinivasula, S M, additional, Rodriguez, I, additional, Alnemri, E S, additional, Gevaert, K, additional, Vandekerckhove, J, additional, Declercq, W, additional, and Vandenabeele, P, additional
- Published
- 2002
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- View/download PDF
19. Regulation of IL-1β generation by Pseudo-ICE and ICEBERG, two dominant negative caspase recruitment domain proteins
- Author
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Druilhe, A, primary, Srinivasula, S M, additional, Razmara, M, additional, Ahmad, M, additional, and Alnemri, E S, additional
- Published
- 2001
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- View/download PDF
20. Cleavage of lamin A by Mch2 alpha but not CPP32: multiple interleukin 1 beta-converting enzyme-related proteases with distinct substrate recognition properties are active in apoptosis.
- Author
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Takahashi, A, primary, Alnemri, E S, additional, Lazebnik, Y A, additional, Fernandes-Alnemri, T, additional, Litwack, G, additional, Moir, R D, additional, Goldman, R D, additional, Poirier, G G, additional, Kaufmann, S H, additional, and Earnshaw, W C, additional
- Published
- 1996
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- View/download PDF
21. In vitro activation of CPP32 and Mch3 by Mch4, a novel human apoptotic cysteine protease containing two FADD-like domains.
- Author
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Fernandes-Alnemri, T, primary, Armstrong, R C, additional, Krebs, J, additional, Srinivasula, S M, additional, Wang, L, additional, Bullrich, F, additional, Fritz, L C, additional, Trapani, J A, additional, Tomaselli, K J, additional, Litwack, G, additional, and Alnemri, E S, additional
- Published
- 1996
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- View/download PDF
22. DNA-dependent protein kinase catalytic subunit: a target for an ICE-like protease in apoptosis.
- Author
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Song, Q., primary, Lees-Miller, S. P., additional, Kumar, S., additional, Zhang, Z., additional, Chan, D. W., additional, Smith, G. C., additional, Jackson, S. P., additional, Alnemri, E. S., additional, Litwack, G., additional, Khanna, K. K., additional, and Lavin, M. F., additional
- Published
- 1996
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23. FKBP46, a novel Sf9 insect cell nuclear immunophilin that forms a protein-kinase complex.
- Author
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Alnemri, E S, primary, Fernandes-Alnemri, T, additional, Pomerenke, K, additional, Robertson, N M, additional, Dudley, K, additional, DuBois, G C, additional, and Litwack, G, additional
- Published
- 1994
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24. CPP32, a novel human apoptotic protein with homology to Caenorhabditis elegans cell death protein Ced-3 and mammalian interleukin-1 beta-converting enzyme.
- Author
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Fernandes-Alnemri, T, primary, Litwack, G, additional, and Alnemri, E S, additional
- Published
- 1994
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- View/download PDF
25. Loss of HtrA2/Omi activity in non-neuronal tissues of adult mice causes premature aging.
- Author
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Kang, S, Louboutin, J-P, Datta, P, Landel, C P, Martinez, D, Zervos, A S, Strayer, D S, Fernandes-Alnemri, T, and Alnemri, E S
- Subjects
PREMATURE aging (Medicine) ,MICE anatomy ,PROTEOLYTIC enzymes ,MITOCHONDRIAL DNA abnormalities ,GENE expression - Abstract
mnd2 mice die prematurely as a result of neurodegeneration 30-40 days after birth due to loss of the enzymatic activity of the mitochondrial quality control protease HtrA2/Omi. Here, we show that transgenic expression of human HtrA2/Omi in the central nervous system of mnd2 mice rescues them from neurodegeneration and prevents their premature death. Interestingly, adult transgenic mnd2 mice develop accelerated aging phenotypes, such as premature weight loss, hair loss, reduced fertility, curvature of the spine, heart enlargement, increased autophagy, and death by 12-17 months of age. These mice also have elevated levels of clonally expanded mitochondrial DNA (mtDNA) deletions in their tissues. Our results provide direct genetic evidence linking mitochondrial protein quality control to mtDNA deletions and aging in mammals. [ABSTRACT FROM AUTHOR]
- Published
- 2013
- Full Text
- View/download PDF
26. Identification of multiple glucocorticoid receptor binding sites in the rat osteocalcin gene promoter
- Author
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Heinrichs, Arianne A. J., primary, Bortell, Rita, additional, Rahman, Sajida, additional, Stein, Janet L., additional, Alnemri, E. S., additional, Litwack, Gerald, additional, Lian, Jane B., additional, and Stein, Gary S., additional
- Published
- 1993
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- View/download PDF
27. Overexpression, characterization, and purification of a recombinant mouse immunophilin FKBP-52 and identification of an associated phosphoprotein.
- Author
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Alnemri, E. S., primary, Fernandes-Alnemri, T., additional, Nelki, D. S., additional, Dudley, K., additional, DuBois, G. C., additional, and Litwack, G., additional
- Published
- 1993
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28. Overexpressed full-length human BCL2 extends the survival of baculovirus-infected Sf9 insect cells.
- Author
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Alnemri, E S, primary, Robertson, N M, additional, Fernandes, T F, additional, Croce, C M, additional, and Litwack, G, additional
- Published
- 1992
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29. Molecular definitions of cell death subroutines: recommendations of the Nomenclature Committee on Cell Death 2012.
- Author
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Galluzzi, L, Vitale, I, Abrams, J M, Alnemri, E S, Baehrecke, E H, Blagosklonny, M V, Dawson, T M, Dawson, V L, El-Deiry, W S, Fulda, S, Gottlieb, E, Green, D R, Hengartner, M O, Kepp, O, Knight, R A, Kumar, S, Lipton, S A, Lu, X, Madeo, F, and Malorni, W
- Subjects
CELL death ,APOPTOSIS ,BIOLOGICAL nomenclature ,NECROSIS microbiology ,GANGRENE - Abstract
In 2009, the Nomenclature Committee on Cell Death (NCCD) proposed a set of recommendations for the definition of distinct cell death morphologies and for the appropriate use of cell death-related terminology, including 'apoptosis', 'necrosis' and 'mitotic catastrophe'. In view of the substantial progress in the biochemical and genetic exploration of cell death, time has come to switch from morphological to molecular definitions of cell death modalities. Here we propose a functional classification of cell death subroutines that applies to both in vitro and in vivo settings and includes extrinsic apoptosis, caspase-dependent or -independent intrinsic apoptosis, regulated necrosis, autophagic cell death and mitotic catastrophe. Moreover, we discuss the utility of expressions indicating additional cell death modalities. On the basis of the new, revised NCCD classification, cell death subroutines are defined by a series of precise, measurable biochemical features. [ABSTRACT FROM AUTHOR]
- Published
- 2012
- Full Text
- View/download PDF
30. Classification of cell death: recommendations of the Nomenclature Committee on Cell Death 2009.
- Author
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Kroemer, G., Galluzzi, L., Vandenabeele, P., Abrams, J., Alnemri, E. S., Baehrecke, E. H., Blagosklonny, M. V., El-Deiry, W. S., Golstein, P., Green, D. R., Hengartner, M., Knight, R. A., Kumar, S., Lipton, S. A., Malorni, W., Nuñez, G., Peter, M. E., Tschopp, J., Yuan, J., and Piacentini, M.
- Subjects
CELL death ,BIOCHEMISTRY ,APOPTOSIS ,NECROSIS ,AUTOPHAGY ,CELLULAR mechanics - Abstract
Different types of cell death are often defined by morphological criteria, without a clear reference to precise biochemical mechanisms. The Nomenclature Committee on Cell Death (NCCD) proposes unified criteria for the definition of cell death and of its different morphologies, while formulating several caveats against the misuse of words and concepts that slow down progress in the area of cell death research. Authors, reviewers and editors of scientific periodicals are invited to abandon expressions like ‘percentage apoptosis’ and to replace them with more accurate descriptions of the biochemical and cellular parameters that are actually measured. Moreover, at the present stage, it should be accepted that caspase-independent mechanisms can cooperate with (or substitute for) caspases in the execution of lethal signaling pathways and that ‘autophagic cell death’ is a type of cell death occurring together with (but not necessarily by) autophagic vacuolization. This study details the 2009 recommendations of the NCCD on the use of cell death-related terminology including ‘entosis’, ‘mitotic catastrophe’, ‘necrosis’, ‘necroptosis’ and ‘pyroptosis’.Cell Death and Differentiation (2009) 16, 3–11; doi:10.1038/cdd.2008.150; published online 10 October 2008 [ABSTRACT FROM AUTHOR]
- Published
- 2009
- Full Text
- View/download PDF
31. Characterization and purification of a functional rat glucocorticoid receptor overexpressed in a baculovirus system
- Author
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Alnemri, E S, primary, Maksymowych, A B, additional, Robertson, N M, additional, and Litwack, G, additional
- Published
- 1991
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32. Cell-free synthesis of rat glucocorticoid receptor in rabbit reticulocyte lysate. In vitro synthesis of receptor in Mr 90,000 heat shock protein-depleted lysate.
- Author
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Daniel, V, primary, Maksymowych, A B, additional, Alnemri, E S, additional, and Litwack, G, additional
- Published
- 1991
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- View/download PDF
33. Cryopyrin and pyrin activate caspase-1, but not NF-κB, via ASC oligomerization.
- Author
-
Yu, J.-W., Wu, J., Zhang, Z., Datta, P., Ibrahimi, I., Taniguchi, S., Sagara, J., Fernandes-Alnemri, T., and Alnemri, E. S.
- Subjects
NF-kappa B ,INFLAMMATION ,DNA-binding proteins ,TRANSCRIPTION factors ,PROTEINS ,INTERLEUKIN-1 ,CELL death - Abstract
Mutations in cryopyrin and pyrin proteins are responsible for several autoinflammatory disorders in humans, suggesting that these proteins play important roles in regulating inflammation. Using a HEK293 cell-based reconstitution system that stably expresses ASC and procaspase-1 we demonstrated that neither cryopyrin nor pyrin or their corresponding disease-associated mutants could significantly activate NF-κB in this system. However, both cryopyrin and two disease-associated cryopyrin mutants induced ASC oligomerization and ASC-dependent caspase-1 activation, with the disease-associated mutants being more potent than the wild-type (WT) cryopyrin, because of increased self-oligomerization. Contrary to the proposed anti-inflammatory activity of WT pyrin, our results demonstrated that pyrin, like cryopyrin, can also assemble an inflammasome complex with ASC and procaspase-1 leading to ASC oligomerization, caspase-1 activation and interleukin-1β processing. Thus, we propose that pyrin could function as a proinflammatory molecule.Cell Death and Differentiation (2006) 13, 236–249. doi:10.1038/sj.cdd.4401734; published online 22 July 2005 [ABSTRACT FROM AUTHOR]
- Published
- 2006
- Full Text
- View/download PDF
34. Activation of internucleosomal DNA cleavage in human CEM lymphocytes by glucocorticoid and novobiocin. Evidence for a non-Ca2(+)-requiring mechanism(s).
- Author
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Alnemri, E S, primary and Litwack, G, additional
- Published
- 1990
- Full Text
- View/download PDF
35. Functional characterization of mitochondria in neutrophils: a role restricted to apoptosis.
- Author
-
Maianski, N. A., Geissler, J., Srinivasula, S. M., Alnemri, E. S., Roos, D., and Kuijpers, T. W.
- Subjects
MITOCHONDRIA ,NEUTROPHILS ,APOPTOSIS ,MITOCHONDRIAL DNA ,CYTOCHROME c ,ENZYME activation - Abstract
Mitochondria are known to combine life-supporting functions with participation in apoptosis by controlling caspase activity. Here, we report that in human blood neutrophils the mitochondria are different, because they preserve mainly death-mediating abilities. Neutrophil mitochondria hardly participate in ATP synthesis, and have a very low activity of the tested marker enzymes. The presence of mitochondria in neutrophils was confirmed by quantification of mitochondrial DNA copy number, by detection of mitochondrial porin, and by JC-1 measurement of ??
m . During neutrophilic differentiation, HL-60 cells demonstrated a profound cytochrome c depletion and mitochondrial shape change reminiscent of neutrophils. However, blood neutrophils containing extremely low amounts of cytochrome c displayed strong caspase-9 activation during apoptosis, which was also observed in apoptotic neutrophil-derived cytoplasts lacking any detectable cytochrome c. We suggest that other proapoptotic factors such as Smac/DIABLO and HtrA2/Omi, which are massively released from the mitochondria, have an important role in neutrophil apoptosis.Cell Death and Differentiation (2004) 11, 143-153. doi:10.1038/sj.cdd.4401320 Published online 24 October 2003 [ABSTRACT FROM AUTHOR]- Published
- 2004
- Full Text
- View/download PDF
36. Identification of Ipaf, a human caspase-1-activating protein related to Apaf-1.
- Author
-
Poyet, J L, Srinivasula, S M, Tnani, M, Razmara, M, Fernandes-Alnemri, T, and Alnemri, E S
- Abstract
Procaspase-9 contains an NH2-terminal caspase-associated recruitment domain (CARD), which is essential for direct association with Apaf-1 and activation. Procaspase-1 also contains an NH2-terminal CARD domain, suggesting that its mechanism of activation, like that of procaspase-9, involves association with an Apaf-1-related molecule. Here we describe the identification of a human Apaf-1-related protein, named Ipaf that contains an NH2-terminal CARD domain, a central nucleotide-binding domain, and a COOH-terminal regulatory leucine-rich repeat domain (LRR). Ipaf associates directly and specifically with the CARD domain of procaspase-1 through CARD-CARD interaction. A constitutively active Ipaf lacking its COOH-terminal LRR domain can induce autocatalytic processing and activation of procaspase-1 and caspase-1-dependent apoptosis in transfected cells. Our results suggest that Ipaf is a specific and direct activator of procaspase-1 and could be involved in activation of caspase-1 in response to pro-inflammatory and apoptotic stimuli.
- Published
- 2001
- Full Text
- View/download PDF
37. Phosphorylation of the insect immunophilin FKBP46 by the Spodoptera frugiperda homolog of casein kinase II
- Author
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Steplewski, A., Ebel, W., Planey, S. L., Alnemri, E. S., Robertson, N. M., and Litwack, G.
- Published
- 2000
- Full Text
- View/download PDF
38. Caspase-mediated cleavage of DNA topoisomerase I at unconventional sites during apoptosis.
- Author
-
Samejima, K, Svingen, P A, Basi, G S, Kottke, T, Mesner, P W, Stewart, L, Durrieu, F, Poirier, G G, Alnemri, E S, Champoux, J J, Kaufmann, S H, and Earnshaw, W C
- Abstract
Previous studies have demonstrated that topoisomerase I is cleaved late during apoptosis, but have not identified the proteases responsible or examined the functional consequences of this cleavage. Here, we have shown that treatment of purified topoisomerase I with caspase-3 resulted in cleavage at DDVD146 downward arrowY and EEED170 downward arrowG, whereas treatment with caspase-6 resulted in cleavage at PEDD123 downward arrowG and EEED170 downward arrowG. After treatment of Jurkat T lymphocytic leukemia cells with anti-Fas antibody or A549 lung cancer cells with topotecan, etoposide, or paclitaxel, the topoisomerase I fragment comigrated with the product that resulted from caspase-3 cleavage at DDVD146 downward arrowY. In contrast, two discrete topoisomerase I fragments that appeared to result from cleavage at DDVD146 downward arrowY and EEED170 downward arrowG were observed after treatment of MDA-MB-468 breast cancer cells with paclitaxel. Topoisomerase I cleavage did not occur in apoptotic MCF-7 cells, which lack caspase-3. Cell fractionation and band depletion studies with the topoisomerase I poison topotecan revealed that the topoisomerase I fragment remains in proximity to the chromatin and retains the ability to bind to and cleave DNA. These observations indicate that topoisomerase I is a substrate of caspase-3 and possibly caspase-6, but is cleaved at sequences that differ from those ordinarily preferred by these enzymes, thereby providing a potential explanation why topoisomerase I cleavage lags behind that of classical caspase substrates such as poly(ADP-ribose) polymerase and lamin B1.
- Published
- 1999
39. Cascades of mammalian caspase activation in the yeast Saccharomyces cerevisiae.
- Author
-
Kang, J J, Schaber, M D, Srinivasula, S M, Alnemri, E S, Litwack, G, Hall, D J, and Bjornsti, M A
- Abstract
Caspases (aspartate-specific cysteine proteases) play a critical role in the execution of the mammalian apoptotic program. To address the regulation of human caspase activation, we used the yeast Saccharomyces cerevisiae, which is devoid of endogenous caspases. The apical procaspases, -8beta and -10, were efficiently processed and activated in yeast. Although protease activity, per se, was insufficient to drive cell death, caspase-10 activity had little effect on cell viability, whereas expression of caspase-8beta was cytotoxic. This lethal phenotype was abrogated by co-expression of the pan-caspase inhibitor, baculovirus p35, and by mutation of the active site cysteine of procaspase-8beta. In contrast, autoactivation of the executioner caspase-3 and -6 zymogens was not detected. Procaspase-3 activation required co-expression of procaspase-8 or -10. Surprisingly, activation of procaspase-6 required proteolytic activities other than caspase-8, -10, or -3. Caspase-8beta or -10 activity was insufficient to catalyze the maturation of procaspase-6. Moreover, a constitutively active caspase-3, although cytotoxic in its own right, was unable to induce the processing of wild-type procaspase-6 and vice versa. These results distinguish sequential modes of activation for different caspases in vivo and establish a yeast model system to examine the regulation of caspase cascades. Moreover, the distinct terminal phenotypes induced by various caspases attest to differences in the cellular targets of these apoptotic proteases, which may be defined using this system.
- Published
- 1999
40. Characterization of caspase processing and activation in HL-60 cell cytosol under cell-free conditions. Nucleotide requirement and inhibitor profile.
- Author
-
Mesner, P W, Bible, K C, Martins, L M, Kottke, T J, Srinivasula, S M, Svingen, P A, Chilcote, T J, Basi, G S, Tung, J S, Krajewski, S, Reed, J C, Alnemri, E S, Earnshaw, W C, and Kaufmann, S H
- Abstract
The present studies compared caspase activation under cell-free conditions in vitro and in etoposide-treated HL-60 leukemia cells in situ. Immunoblotting revealed that incubation of HL-60 cytosol at 30 degrees C in the presence of cytochrome c and ATP (or dATP) resulted in activation of procaspases-3, -6, and -7 but not -2 and -8. Although similar selectivity was observed in intact cells, affinity labeling revealed that the active caspase species generated in vitro and in situ differed in charge and abundance. ATP and dATP levels in intact HL-60 cells were higher than required for caspase activation in vitro and did not change before caspase activation in situ. Replacement of ATP with the poorly hydrolyzable analogs 5'-adenylyl methylenediphosphate, 5'-adenylyl imidodiphosphate, or 5'-adenylyl-O-(3-thiotriphos-phate) slowed caspase activation in vitro, suggesting that ATP hydrolysis is required. Caspase activation in vitro was insensitive to phosphatase and kinase inhibitors (okadaic acid, staurosporine, and genistein) but was inhibited by Zn(2+), aurintricarboxylic acid, and various protease inhibitors, including 3,4-dichloroisocoumarin, N(alpha)-p-tosyl-L-phenylalanine chloromethyl ketone, N(alpha)-p-tosyl-L-lysine chloromethyl ketone, and N-(N(alpha)-benzyloxycarbonylphenylalanyl)alanine fluoromethyl ketone, each of which inhibited recombinant caspases-3, -6, -7, and -9. Experiments with anti-neoepitope antiserum confirmed that these agents inhibited caspase-9 activation. Collectively, these results suggest that caspase-9 activation requires nucleotide hydrolysis and is inhibited by agents previously thought to affect apoptosis by other means.
- Published
- 1999
41. E1A-induced processing of procaspase-8 can occur independently of FADD and is inhibited by Bcl-2.
- Author
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Nguyen, M, Branton, P E, Roy, S, Nicholson, D W, Alnemri, E S, Yeh, W C, Mak, T W, and Shore, G C
- Abstract
Expression of the 243-residue form of the adenovirus E1A protein in the absence of other viral proteins triggers apoptosis by a pathway that requires p53. This pathway includes processing and activation of initiator procaspase-8, redistribution of cytochrome c, and activation of procaspase-3. Bcl-2 functions at or upstream of procaspase-8 processing to inhibit all of these events and prevent cell death. This contrasts with the anti-apoptotic influence of Bcl-2 family proteins in the cell death pathway induced by Fas ligand or tumor necrosis factor (TNF), in which Bcl-2 typically acts downstream of Fas/TNFR1-mediated activation of caspase-8. Moreover, E1A induces procaspase-8 processing and cell death in cells deleted of FADD, an adaptor protein critical for Fas/TNFR1 activation of caspase-8. The results indicate that E1A is capable of activating caspase-8 by a Bcl-2-inhibitable pathway that does not involve autocrine stimulation of FADD-dependent death receptor pathways.
- Published
- 1998
42. CLAP, a novel caspase recruitment domain-containing protein in the tumor necrosis factor receptor pathway, regulates NF-kappaB activation and apoptosis.
- Author
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Srinivasula, S M, Ahmad, M, Lin, J H, Poyet, J L, Fernandes-Alnemri, T, Tsichlis, P N, and Alnemri, E S
- Abstract
Molecules that regulate NF-kappaB activation play critical roles in apoptosis and inflammation. We describe the cloning of the cellular homolog of the equine herpesvirus-2 protein E10 and show that both proteins regulate apoptosis and NF-kappaB activation. These proteins were found to contain N-terminal caspase-recruitment domains (CARDs) and novel C-terminal domains (CTDs) and were therefore named CLAPs (CARD-like apoptotic proteins). The cellular and viral CLAPs induce apoptosis downstream of caspase-8 by activating the Apaf-1-caspase-9 pathway and activate NF-kappaB by acting upstream of the NF-kappaB-inducing kinase, NIK, and the IkB kinase, IKKalpha. Deletion of either the CARD or the CTD domain inhibits both activities. The CARD domain was found to be important for homo- and heterodimerization of CLAPs. Substitution of the CARD domain with an inducible FKBP12 oligomerization domain produced a molecule that can induce NF-kappaB activation, suggesting that the CARD domain functions as an oligomerization domain, whereas the CTD domain functions as the effector domain in the NF-kappaB activation pathway. Expression of the CARD domain of human CLAP abrogates tumor necrosis factor-alpha-induced NF-kappaB activation, suggesting that cellular CLAP plays an essential role in this pathway of NF-kappaB activation.
- Published
- 1999
43. Cytochrome c and dATP-mediated oligomerization of Apaf-1 is a prerequisite for procaspase-9 activation.
- Author
-
Saleh, A, Srinivasula, S M, Acharya, S, Fishel, R, and Alnemri, E S
- Abstract
To elucidate the mechanism of activation of procaspase-9 by Apaf-1, we produced recombinant full-length Apaf-1 and purified it to complete homogeneity. Here we show using gel filtration that full-length Apaf-1 exists as a monomer that can be transformed to an oligomeric complex made of at least eight subunits after binding to cytochrome c and dATP. Apaf-1 binds to cytochrome c in the absence of dATP but does not form the oligomeric complex. However, when dATP is added to the cytochrome c-bound Apaf-1 complex, complete oligomerization occurs, suggesting that oligomerization is driven by hydrolysis of dATP. This was supported by the observation that ATP, but not the nonhydrolyzable adenosine 5'-O-(thiotriphosphate), can induce oligomerization of the Apaf-1-cytochrome c complex. Like the spontaneously oligomerizing Apaf-530, which lacks its WD-40 domain, the oligomeric full-length Apaf-1-cytochrome c complex can bind and process procaspase-9 in the absence of additional dATP or cytochrome c. However, unlike the truncated Apaf-530 complex, the full-length Apaf-1 complex can release the mature caspase-9 after processing. Once released, mature caspase-9 can process procaspase-3, setting into motion the caspase cascade. These observations indicate that cytochrome c and dATP are required for oligomerization of Apaf-1 and suggest that the WD-40 domain plays an important role in oligomerization of full-length Apaf-1 and the release of mature caspase-9 from the Apaf-1 oligomeric complex.
- Published
- 1999
44. Cleavage and activation of p21-activated protein kinase gamma-PAK by CPP32 (caspase 3). Effects of autophosphorylation on activity.
- Author
-
Walter, B N, Huang, Z, Jakobi, R, Tuazon, P T, Alnemri, E S, Litwack, G, and Traugh, J A
- Abstract
p21-activated protein kinase gamma-PAK (Pak2, PAK I) is cleaved by CPP32 (caspase 3) during apoptosis and plays a key role in regulation of cell death. In vitro, CPP32 cleaves recombinant gamma-PAK into two peptides; 1-212 contains the majority of the regulatory domain whereas 213-524 contains 34 amino acids of the regulatory domain plus the entire catalytic domain. Following cleavage, both peptides become autophosphorylated with [gamma-32P]ATP. Peptide 1-212 migrates at 27,000 daltons (p27) upon SDS-polyacrylamide gel electrophoresis and at 32,000 daltons following autophosphorylation on serine (p27P); the catalytic subunit migrates at 34,000 daltons (p34) before and after autophosphorylation on threonine. Following caspase cleavage, a significant lag (approximately 5 min) is observed before autophosphorylation and activity are detected. When gamma-PAK is autophosphorylated with ATP(Mg) alone and then cleaved, only p27 contains phosphate, and the enzyme is inactive with exogenous substrate. After autophosphorylation of gamma-PAK in the presence of Cdc42(GTPgammaS) or histone 4, both cleavage products contain phosphate and gamma-PAK is catalytically active. Mutation of the conserved Thr-402 to alanine greatly reduces autophosphorylation and protein kinase activity following cleavage. Thus activation of gamma-PAK via cleavage by CPP32 is a two-step mechanism wherein autophosphorylation of the regulatory domain is a priming step, and activation coincides with autophosphorylation of the catalytic domain.
- Published
- 1998
45. Cloning and expression of four novel isoforms of human interleukin-1 beta converting enzyme with different apoptotic activities.
- Author
-
Alnemri, E S, Fernandes-Alnemri, T, and Litwack, G
- Abstract
To understand the mechanism of interleukin-1 beta converting enzyme (ICE) activation in apoptosis, we analyzed the expression of ICE mRNA in two human cell lines by reverse transcription-polymerase chain reaction technique. This resulted in the identification and cloning of four alternatively spliced ICE mRNA isoforms. Although all the alternative splicing events were within the coding sequence of ICE, the four ICE isoforms maintained open reading frames and were designated as ICE beta, gamma, delta, and epsilon. In ICE gamma, most of the propeptide (amino acids 20-112) is deleted, which suggests that it may function as a catalyst for ICE autoprocessing in vivo. In ICE delta, amino acids 288-335, which contain the cleavage sites between the p20 and p10 subunits of ICE, are deleted thus resulting in its inactivation. Intriguingly, in ICE epsilon amino acids 20-335, which encompass most of the propeptide and the p20 subunit, are deleted resulting in the formation of a molecule that is homologous to the p10 subunit. Examination of the ability of these four ICE isoforms to cause apoptosis revealed that only the parental ICE alpha and isoforms beta and gamma, but not isoforms delta and epsilon, can induce apoptosis when overexpressed in Sf9 insect cells. In addition, coexpression of the p20 and p10 but not the p20 and ICE epsilon in Sf9 cells results in apoptosis. Interestingly, expression of ICE epsilon and to a lesser degree ICE delta resulted in extension of the survival of baculovirus-infected cells in a manner similar to expression of BCL2. The ability of ICE epsilon to extend the survival of Sf9 cells suggests that baculovirus-induced apoptosis in these cells is mediated by an ICE-like protease. We show that ICE epsilon can bind to the p20 subunit of ICE and potentially may compete with the p10 subunit to form an inactive ICE complex. Therefore, by acting as a dominant inhibitor of ICE activity, ICE epsilon may regulate ICE activation in vivo.
- Published
- 1995
46. Abrogation of mitochondrial cytochrome c release and caspase-3 activation in acquired multidrug resistance.
- Author
-
Kojima, H, Endo, K, Moriyama, H, Tanaka, Y, Alnemri, E S, Slapak, C A, Teicher, B, Kufe, D, and Datta, R
- Abstract
Acquired multidrug resistance to anti-cancer agents has been associated with overexpression of the P-glycoprotein and other members of the ATP-binding cassette superfamily. The present studies demonstrate that SCC-25 cells selected for resistance to the alkylating agent cisplatin (CDDP) overexpress the anti-apoptotic Bcl-xL protein. In contrast to parental cells, the SCC-25/CDDP-resistant variant failed to exhibit activation of caspase-3, cleavage of protein kinase C delta, and other characteristics of apoptosis in response to CDDP. Similar results were obtained when SCC-25/CDDP cells were exposed to the structurally and functionally unrelated antimetabolite 1-beta-D-arabinofuranosyl-cytosine (ara-C). Other cells selected for resistance to doxorubicin or vincristine also exhibited overexpression of Bcl-xL and failed to respond to CDDP and ara-C with activation of caspase-3. The results further demonstrate that multidrug-resistant cells exhibit a block in the release of mitochondrial cytochrome c into the cytosol and that this effect is dependent on overexpression of Bcl-xL. The demonstration that lysates from the resistant cells respond to the addition of cytochrome c with activation of caspase-3 confirms that the block in apoptosis is because of inhibition of mitochondrial cytochrome c release. These findings demonstrate that cells respond to diverse classes of anti-cancer drugs with overexpression of Bcl-xL and that this response represents another mechanism of acquired multidrug resistance.
- Published
- 1998
47. The baculovirus anti-apoptotic p35 protein promotes transformation of mouse embryo fibroblasts.
- Author
-
Resnicoff, M, Valentinis, B, Herbert, D, Abraham, D, Friesen, P D, Alnemri, E S, and Baserga, R
- Abstract
The baculovirus p35 protein is a potent inhibitor of programmed cell death induced by a variety of stimuli in insects, nematodes, and mammalian cell lines. The broad ability of p35 in preventing apoptosis has led us to investigate its effect on mouse embryo fibroblasts in vitro and in vivo. For this purpose, we have used R- cells (3T3-like fibroblasts derived from mouse embryos with a targeted disruption of the insulin-like growth factor I receptor (IGF-IR) genes) and R508 cells (derived from R- and with 15 x 10(3) IGF-IRs per cell). Both cell lines grow normally in monolayer, but they do not form colonies in soft agar, and they are non-tumorigenic in nude mice. We show here that, in addition to its anti-apoptotic effect, p35 causes transformation of R508 cells, as evidenced by the following: 1) decreased growth factor requirements, 2) ability to form foci in monolayer and colonies in soft agar, and 3) ability to form tumors in nude mice. Since R- cells stably transfected with p35 do not transform, our observations suggest that in addition to its effect as an inhibitor of apoptosis, the baculovirus p35 protein has transforming potential that requires the presence of the IGF-IR. The possibility that these two properties could be separated was confirmed by demonstrating that R508 cells expressing another anti-apoptotic protein, Bcl-2, could not form tumors in nude mice.
- Published
- 1998
48. Generation of constitutively active recombinant caspases-3 and -6 by rearrangement of their subunits.
- Author
-
Srinivasula, S M, Ahmad, M, MacFarlane, M, Luo, Z, Huang, Z, Fernandes-Alnemri, T, and Alnemri, E S
- Abstract
Caspases play a major role in the transduction of the apoptotic signal and execution of apoptosis in mammalian cells. Ectopic overexpression of the short prodomain caspases-3 and -6 precursors in mammalian cells does not induce apoptosis. This is due to their inability to undergo autocatalytic processing/activation and suggests that they depend on the long prodomain caspases for activation. To investigate directly the apoptotic activity of these two caspases in vivo, we engineered constitutively active recombinant caspases-3 and -6 precursors. This was achieved by making contiguous precursor caspases-3 and -6 molecules, which have their small subunits preceding their large subunits. Unlike their wild type counterparts, these recombinant molecules were capable of autocatalytic processing in an in vitro translation reaction, suggesting that they are catalytically active. They were also capable of autoprocessing and inducing apoptosis in vivo independent of the upstream caspases. Furthermore, their autocatalytic and apoptotic activities were inhibited by the pancaspase inhibitor z-VAD-fluoromethylketone, but not by CrmA or Bcl-2, thus directly demonstrating that the targets of inhibition of apoptosis by CrmA and Bcl-2 are upstream of caspases-3 and -6. Since caspases-3 and -6 are the most downstream executioners of apoptosis, the constitutively active versions of these caspases could be used at very low concentrations in gene therapy model systems to induce apoptosis in target tissues or tumors.
- Published
- 1998
49. Identification and molecular cloning of two novel receptors for the cytotoxic ligand TRAIL.
- Author
-
MacFarlane, M, Ahmad, M, Srinivasula, S M, Fernandes-Alnemri, T, Cohen, G M, and Alnemri, E S
- Abstract
A human receptor for the cytotoxic ligand TRAIL (TRAIL receptor-1, designated DR4) was identified recently as a member of the tumor necrosis factor receptor family. In this report we describe the identification of two additional human TRAIL receptors, TRAIL receptor-2 and TRAIL receptor-3, that belong to the tumor necrosis factor receptor family. Interestingly, TRAIL receptor-2 but not TRAIL receptor-3 contains a cytoplasmic "death domain" necessary for induction of apoptosis and is hence designated death receptor-5 (DR5). Like DR4, DR5 engages the apoptotic pathway independent of the adaptor molecule FADD/MORT1. Because of its lack of a death domain, TRAIL receptor-3 is not capable of inducing apoptosis. However, by competing for TRAIL, it is capable of inhibiting TRAIL-induced apoptosis. Thus, TRAIL receptor-3 may function as an antagonistic decoy receptor to attenuate the cytotoxic effect of TRAIL in most tissues that are TRAIL+, DR4+, and DR5+.
- Published
- 1997
50. Caspase-mediated cleavage of the ubiquitin-protein ligase Nedd4 during apoptosis.
- Author
-
Harvey, K F, Harvey, N L, Michael, J M, Parasivam, G, Waterhouse, N, Alnemri, E S, Watters, D, and Kumar, S
- Abstract
The onset of apoptosis is coupled to the proteolytic activation of a family of cysteine proteases, termed caspases. These proteases cleave their target proteins after an aspartate residue. Following caspase activation during apoptosis, a number of specific proteins have been shown to be cleaved. Here we show that Nedd4, a ubiquitin-protein ligase containing multiple WW domains and a calcium/lipid-binding domain, is also cleaved during apoptosis induced by a variety of stimuli including Fas-ligation, gamma-radiation, tumor necrosis factor-alpha, C-8 ceramide, and etoposide treatment. Extracts from apoptotic cells also generated cleavage patterns similar to that seen in vivo, and this cleavage was inhibited by an inhibitor of caspase-3-like proteases. In vitro, Nedd4 was cleaved by a number of caspases, including caspase-1, -3, -6, and -7. By site-directed mutagenesis, one of the in vitro caspase cleavage sites in mouse Nedd4 was mapped to a DQPD237 downward arrow sequence, which is conserved between mouse, rat, and human proteins. This is the first report demonstrating that an enzyme of the ubiquitin pathway is cleaved by caspases during apoptosis.
- Published
- 1998
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