84 results on '"Pandey UB"'
Search Results
2. Guidelines for the use and interpretation of assays for monitoring autophagy (4th edition)
- Author
-
Klionsky, DJ, Abdel-Aziz, AK, Abdelfatah, S, Abdellatif, M, Abdoli, A, Abel, S, Abeliovich, H, Abildgaard, MH, Abudu, YP, Acevedo-Arozena, A, Adamopoulos, IE, Adeli, K, Adolph, TE, Adornetto, A, Aflaki, E, Agam, G, Agarwal, A, Aggarwal, BB, Agnello, M, Agostinis, P, Agrewala, JN, Agrotis, A, Aguilar, PV, Ahmad, ST, Ahmed, ZM, Ahumada-Castro, U, Aits, S, Aizawa, S, Akkoc, Y, Akoumianaki, T, Akpinar, HA, Al-Abd, AM, Al-Akra, L, Al-Gharaibeh, A, Alaoui-Jamali, MA, Alberti, S, Alcocer-Gómez, E, Alessandri, C, Ali, M, Alim Al-Bari, MA, Aliwaini, S, Alizadeh, J, Almacellas, E, Almasan, A, Alonso, A, Alonso, GD, Altan-Bonnet, N, Altieri, DC, Álvarez, ÉMC, Alves, S, Alves da Costa, C, Alzaharna, MM, Amadio, M, Amantini, C, Amaral, C, Ambrosio, S, Amer, AO, Ammanathan, V, An, Z, Andersen, SU, Andrabi, SA, Andrade-Silva, M, Andres, AM, Angelini, S, Ann, D, Anozie, UC, Ansari, MY, Antas, P, Antebi, A, Antón, Z, Anwar, T, Apetoh, L, Apostolova, N, Araki, T, Araki, Y, Arasaki, K, Araújo, WL, Araya, J, Arden, C, Arévalo, M-A, Arguelles, S, Arias, E, Arikkath, J, Arimoto, H, Ariosa, AR, Armstrong-James, D, Arnauné-Pelloquin, L, Aroca, A, Arroyo, DS, Arsov, I, Artero, R, Asaro, DML, Aschner, M, Ashrafizadeh, M, Ashur-Fabian, O, Atanasov, AG, Au, AK, Auberger, P, Auner, HW, Aurelian, L, Autelli, R, Avagliano, L, Ávalos, Y, Aveic, S, Aveleira, CA, Avin-Wittenberg, T, Aydin, Y, Ayton, S, Ayyadevara, S, Azzopardi, M, Baba, M, Backer, JM, Backues, SK, Bae, D-H, Bae, O-N, Bae, SH, Baehrecke, EH, Baek, A, Baek, S-H, Baek, SH, Bagetta, G, Bagniewska-Zadworna, A, Bai, H, Bai, J, Bai, X, Bai, Y, Bairagi, N, Baksi, S, Balbi, T, Baldari, CT, Balduini, W, Ballabio, A, Ballester, M, Balazadeh, S, Balzan, R, Bandopadhyay, R, Banerjee, S, Bánréti, Á, Bao, Y, Baptista, MS, Baracca, A, Barbati, C, Bargiela, A, Barilà, D, Barlow, PG, Barmada, SJ, Barreiro, E, Barreto, GE, Bartek, J, Bartel, B, Bartolome, A, Barve, GR, Basagoudanavar, SH, Bassham, DC, Bast, RC, Basu, A, Batoko, H, Batten, I, Baulieu, EE, Baumgarner, BL, Bayry, J, Beale, R, Beau, I, Beaumatin, F, Bechara, LRG, Beck, GR, Beers, MF, Begun, J, Behrends, C, Behrens, GMN, Bei, R, Bejarano, E, Bel, S, Behl, C, Belaid, A, Belgareh-Touzé, N, Bellarosa, C, Belleudi, F, Belló Pérez, M, Bello-Morales, R, Beltran, JSDO, Beltran, S, Benbrook, DM, Bendorius, M, Benitez, BA, Benito-Cuesta, I, Bensalem, J, Berchtold, MW, Berezowska, S, Bergamaschi, D, Bergami, M, Bergmann, A, Berliocchi, L, Berlioz-Torrent, C, Bernard, A, Berthoux, L, Besirli, CG, Besteiro, S, Betin, VM, Beyaert, R, Bezbradica, JS, Bhaskar, K, Bhatia-Kissova, I, Bhattacharya, R, Bhattacharya, S, Bhattacharyya, S, Bhuiyan, MS, Bhutia, SK, Bi, L, Bi, X, Biden, TJ, Bijian, K, Billes, VA, Binart, N, Bincoletto, C, Birgisdottir, AB, Bjorkoy, G, Blanco, G, Blas-Garcia, A, Blasiak, J, Blomgran, R, Blomgren, K, Blum, JS, Boada-Romero, E, Boban, M, Boesze-Battaglia, K, Boeuf, P, Boland, B, Bomont, P, Bonaldo, P, Bonam, SR, Bonfili, L, Bonifacino, JS, Boone, BA, Bootman, MD, Bordi, M, Borner, C, Bornhauser, BC, Borthakur, G, Bosch, J, Bose, S, Botana, LM, Botas, J, Boulanger, CM, Boulton, ME, Bourdenx, M, Bourgeois, B, Bourke, NM, Bousquet, G, Boya, P, Bozhkov, PV, Bozi, LHM, Bozkurt, TO, Brackney, DE, Brandts, CH, Braun, RJ, Braus, GH, Bravo-Sagua, R, Bravo-San Pedro, JM, Brest, P, Bringer, M-A, Briones-Herrera, A, Broaddus, VC, Brodersen, P, Brodsky, JL, Brody, SL, Bronson, PG, Bronstein, JM, Brown, CN, Brown, RE, Brum, PC, Brumell, JH, Brunetti-Pierri, N, Bruno, D, Bryson-Richardson, RJ, Bucci, C, Buchrieser, C, Bueno, M, Buitrago-Molina, LE, Buraschi, S, Buch, S, Buchan, JR, Buckingham, EM, Budak, H, Budini, M, Bultynck, G, Burada, F, Burgoyne, JR, Burón, MI, Bustos, V, Büttner, S, Butturini, E, Byrd, A, Cabas, I, Cabrera-Benitez, S, Cadwell, K, Cai, J, Cai, L, Cai, Q, Cairó, M, Calbet, JA, Caldwell, GA, Caldwell, KA, Call, JA, Calvani, R, Calvo, AC, Calvo-Rubio Barrera, M, Camara, NO, Camonis, JH, Camougrand, N, Campanella, M, Campbell, EM, Campbell-Valois, F-X, Campello, S, Campesi, I, Campos, JC, Camuzard, O, Cancino, J, Candido de Almeida, D, Canesi, L, Caniggia, I, Canonico, B, Cantí, C, Cao, B, Caraglia, M, Caramés, B, Carchman, EH, Cardenal-Muñoz, E, Cardenas, C, Cardenas, L, Cardoso, SM, Carew, JS, Carle, GF, Carleton, G, Carloni, S, Carmona-Gutierrez, D, Carneiro, LA, Carnevali, O, Carosi, JM, Carra, S, Carrier, A, Carrier, L, Carroll, B, Carter, AB, Carvalho, AN, Casanova, M, Casas, C, Casas, J, Cassioli, C, Castillo, EF, Castillo, K, Castillo-Lluva, S, Castoldi, F, Castori, M, Castro, AF, Castro-Caldas, M, Castro-Hernandez, J, Castro-Obregon, S, Catz, SD, Cavadas, C, Cavaliere, F, Cavallini, G, Cavinato, M, Cayuela, ML, Cebollada Rica, P, Cecarini, V, Cecconi, F, Cechowska-Pasko, M, Cenci, S, Ceperuelo-Mallafré, V, Cerqueira, JJ, Cerutti, JM, Cervia, D, Cetintas, VB, Cetrullo, S, Chae, H-J, Chagin, AS, Chai, C-Y, Chakrabarti, G, Chakrabarti, O, Chakraborty, T, Chami, M, Chamilos, G, Chan, DW, Chan, EYW, Chan, ED, Chan, HYE, Chan, HH, Chan, H, Chan, MTV, Chan, YS, Chandra, PK, Chang, C-P, Chang, C, Chang, H-C, Chang, K, Chao, J, Chapman, T, Charlet-Berguerand, N, Chatterjee, S, Chaube, SK, Chaudhary, A, Chauhan, S, Chaum, E, Checler, F, Cheetham, ME, Chen, C-S, Chen, G-C, Chen, J-F, Chen, LL, Chen, L, Chen, M, Chen, M-K, Chen, N, Chen, Q, Chen, R-H, Chen, S, Chen, W, Chen, X-M, Chen, X-W, Chen, X, Chen, Y, Chen, Y-G, Chen, Y-J, Chen, Y-Q, Chen, ZS, Chen, Z, Chen, Z-H, Chen, ZJ, Cheng, H, Cheng, J, Cheng, S-Y, Cheng, W, Cheng, X, Cheng, X-T, Cheng, Y, Cheng, Z, Cheong, H, Cheong, JK, Chernyak, BV, Cherry, S, Cheung, CFR, Cheung, CHA, Cheung, K-H, Chevet, E, Chi, RJ, Chiang, AKS, Chiaradonna, F, Chiarelli, R, Chiariello, M, Chica, N, Chiocca, S, Chiong, M, Chiou, S-H, Chiramel, AI, Chiurchiù, V, Cho, D-H, Choe, S-K, Choi, AMK, Choi, ME, Choudhury, KR, Chow, NS, Chu, CT, Chua, JP, Chua, JJE, Chung, H, Chung, KP, Chung, S, Chung, S-H, Chung, Y-L, Cianfanelli, V, Ciechomska, IA, Cifuentes, M, Cinque, L, Cirak, S, Cirone, M, Clague, MJ, Clarke, R, Clementi, E, Coccia, EM, Codogno, P, Cohen, E, Cohen, MM, Colasanti, T, Colasuonno, F, Colbert, RA, Colell, A, Čolić, M, Coll, NS, Collins, MO, Colombo, MI, Colón-Ramos, DA, Combaret, L, Comincini, S, Cominetti, MR, Consiglio, A, Conte, A, Conti, F, Contu, VR, Cookson, MR, Coombs, KM, Coppens, I, Corasaniti, MT, Corkery, DP, Cordes, N, Cortese, K, Costa, MDC, Costantino, S, Costelli, P, Coto-Montes, A, Crack, PJ, Crespo, JL, Criollo, A, Crippa, V, Cristofani, R, Csizmadia, T, Cuadrado, A, Cui, B, Cui, J, Cui, Y, Culetto, E, Cumino, AC, Cybulsky, AV, Czaja, MJ, Czuczwar, SJ, D'Adamo, S, D'Amelio, M, D'Arcangelo, D, D'Lugos, AC, D'Orazi, G, da Silva, JA, Dafsari, HS, Dagda, RK, Dagdas, Y, Daglia, M, Dai, X, Dai, Y, Dal Col, J, Dalhaimer, P, Dalla Valle, L, Dallenga, T, Dalmasso, G, Damme, M, Dando, I, Dantuma, NP, Darling, AL, Das, H, Dasarathy, S, Dasari, SK, Dash, S, Daumke, O, Dauphinee, AN, Davies, JS, Dávila, VA, Davis, RJ, Davis, T, Dayalan Naidu, S, De Amicis, F, De Bosscher, K, De Felice, F, De Franceschi, L, De Leonibus, C, de Mattos Barbosa, MG, De Meyer, GRY, De Milito, A, De Nunzio, C, De Palma, C, De Santi, M, De Virgilio, C, De Zio, D, Debnath, J, DeBosch, BJ, Decuypere, J-P, Deehan, MA, Deflorian, G, DeGregori, J, Dehay, B, Del Rio, G, Delaney, JR, Delbridge, LMD, Delorme-Axford, E, Delpino, MV, Demarchi, F, Dembitz, V, Demers, ND, Deng, H, Deng, Z, Dengjel, J, Dent, P, Denton, D, DePamphilis, ML, Der, CJ, Deretic, V, Descoteaux, A, Devis, L, Devkota, S, Devuyst, O, Dewson, G, Dharmasivam, M, Dhiman, R, di Bernardo, D, Di Cristina, M, Di Domenico, F, Di Fazio, P, Di Fonzo, A, Di Guardo, G, Di Guglielmo, GM, Di Leo, L, Di Malta, C, Di Nardo, A, Di Rienzo, M, Di Sano, F, Diallinas, G, Diao, J, Diaz-Araya, G, Díaz-Laviada, I, Dickinson, JM, Diederich, M, Dieudé, M, Dikic, I, Ding, S, Ding, W-X, Dini, L, Dinić, J, Dinic, M, Dinkova-Kostova, AT, Dionne, MS, Distler, JHW, Diwan, A, Dixon, IMC, Djavaheri-Mergny, M, Dobrinski, I, Dobrovinskaya, O, Dobrowolski, R, Dobson, RCJ, Đokić, J, Dokmeci Emre, S, Donadelli, M, Dong, B, Dong, X, Dong, Z, Dorn Ii, GW, Dotsch, V, Dou, H, Dou, J, Dowaidar, M, Dridi, S, Drucker, L, Du, A, Du, C, Du, G, Du, H-N, Du, L-L, du Toit, A, Duan, S-B, Duan, X, Duarte, SP, Dubrovska, A, Dunlop, EA, Dupont, N, Durán, RV, Dwarakanath, BS, Dyshlovoy, SA, Ebrahimi-Fakhari, D, Eckhart, L, Edelstein, CL, Efferth, T, Eftekharpour, E, Eichinger, L, Eid, N, Eisenberg, T, Eissa, NT, Eissa, S, Ejarque, M, El Andaloussi, A, El-Hage, N, El-Naggar, S, Eleuteri, AM, El-Shafey, ES, Elgendy, M, Eliopoulos, AG, Elizalde, MM, Elks, PM, Elsasser, H-P, Elsherbiny, ES, Emerling, BM, Emre, NCT, Eng, CH, Engedal, N, Engelbrecht, A-M, Engelsen, AST, Enserink, JM, Escalante, R, Esclatine, A, Escobar-Henriques, M, Eskelinen, E-L, Espert, L, Eusebio, M-O, Fabrias, G, Fabrizi, C, Facchiano, A, Facchiano, F, Fadeel, B, Fader, C, Faesen, AC, Fairlie, WD, Falcó, A, Falkenburger, BH, Fan, D, Fan, J, Fan, Y, Fang, EF, Fang, Y, Fanto, M, Farfel-Becker, T, Faure, M, Fazeli, G, Fedele, AO, Feldman, AM, Feng, D, Feng, J, Feng, L, Feng, Y, Feng, W, Fenz Araujo, T, Ferguson, TA, Fernández, ÁF, Fernandez-Checa, JC, Fernández-Veledo, S, Fernie, AR, Ferrante, AW, Ferraresi, A, Ferrari, MF, Ferreira, JCB, Ferro-Novick, S, Figueras, A, Filadi, R, Filigheddu, N, Filippi-Chiela, E, Filomeni, G, Fimia, GM, Fineschi, V, Finetti, F, Finkbeiner, S, Fisher, EA, Fisher, PB, Flamigni, F, Fliesler, SJ, Flo, TH, Florance, I, Florey, O, Florio, T, Fodor, E, Follo, C, Fon, EA, Forlino, A, Fornai, F, Fortini, P, Fracassi, A, Fraldi, A, Franco, B, Franco, R, Franconi, F, Frankel, LB, Friedman, SL, Fröhlich, LF, Frühbeck, G, Fuentes, JM, Fujiki, Y, Fujita, N, Fujiwara, Y, Fukuda, M, Fulda, S, Furic, L, Furuya, N, Fusco, C, Gack, MU, Gaffke, L, Galadari, S, Galasso, A, Galindo, MF, Gallolu Kankanamalage, S, Galluzzi, L, Galy, V, Gammoh, N, Gan, B, Ganley, IG, Gao, F, Gao, H, Gao, M, Gao, P, Gao, S-J, Gao, W, Gao, X, Garcera, A, Garcia, MN, Garcia, VE, García-Del Portillo, F, Garcia-Escudero, V, Garcia-Garcia, A, Garcia-Macia, M, García-Moreno, D, Garcia-Ruiz, C, García-Sanz, P, Garg, AD, Gargini, R, Garofalo, T, Garry, RF, Gassen, NC, Gatica, D, Ge, L, Ge, W, Geiss-Friedlander, R, Gelfi, C, Genschik, P, Gentle, IE, Gerbino, V, Gerhardt, C, Germain, K, Germain, M, Gewirtz, DA, Ghasemipour Afshar, E, Ghavami, S, Ghigo, A, Ghosh, M, Giamas, G, Giampietri, C, Giatromanolaki, A, Gibson, GE, Gibson, SB, Ginet, V, Giniger, E, Giorgi, C, Girao, H, Girardin, SE, Giridharan, M, Giuliano, S, Giulivi, C, Giuriato, S, Giustiniani, J, Gluschko, A, Goder, V, Goginashvili, A, Golab, J, Goldstone, DC, Golebiewska, A, Gomes, LR, Gomez, R, Gómez-Sánchez, R, Gomez-Puerto, MC, Gomez-Sintes, R, Gong, Q, Goni, FM, González-Gallego, J, Gonzalez-Hernandez, T, Gonzalez-Polo, RA, Gonzalez-Reyes, JA, González-Rodríguez, P, Goping, IS, Gorbatyuk, MS, Gorbunov, NV, Görgülü, K, Gorojod, RM, Gorski, SM, Goruppi, S, Gotor, C, Gottlieb, RA, Gozes, I, Gozuacik, D, Graef, M, Gräler, MH, Granatiero, V, Grasso, D, Gray, JP, Green, DR, Greenhough, A, Gregory, SL, Griffin, EF, Grinstaff, MW, Gros, F, Grose, C, Gross, AS, Gruber, F, Grumati, P, Grune, T, Gu, X, Guan, J-L, Guardia, CM, Guda, K, Guerra, F, Guerri, C, Guha, P, Guillén, C, Gujar, S, Gukovskaya, A, Gukovsky, I, Gunst, J, Günther, A, Guntur, AR, Guo, C, Guo, H, Guo, L-W, Guo, M, Gupta, P, Gupta, SK, Gupta, S, Gupta, VB, Gupta, V, Gustafsson, AB, Gutterman, DD, H B, R, Haapasalo, A, Haber, JE, Hać, A, Hadano, S, Hafrén, AJ, Haidar, M, Hall, BS, Halldén, G, Hamacher-Brady, A, Hamann, A, Hamasaki, M, Han, W, Hansen, M, Hanson, PI, Hao, Z, Harada, M, Harhaji-Trajkovic, L, Hariharan, N, Haroon, N, Harris, J, Hasegawa, T, Hasima Nagoor, N, Haspel, JA, Haucke, V, Hawkins, WD, Hay, BA, Haynes, CM, Hayrabedyan, SB, Hays, TS, He, C, He, Q, He, R-R, He, Y-W, He, Y-Y, Heakal, Y, Heberle, AM, Hejtmancik, JF, Helgason, GV, Henkel, V, Herb, M, Hergovich, A, Herman-Antosiewicz, A, Hernández, A, Hernandez, C, Hernandez-Diaz, S, Hernandez-Gea, V, Herpin, A, Herreros, J, Hervás, JH, Hesselson, D, Hetz, C, Heussler, VT, Higuchi, Y, Hilfiker, S, Hill, JA, Hlavacek, WS, Ho, EA, Ho, IHT, Ho, PW-L, Ho, S-L, Ho, WY, Hobbs, GA, Hochstrasser, M, Hoet, PHM, Hofius, D, Hofman, P, Höhn, A, Holmberg, CI, Hombrebueno, JR, Yi-Ren Hong, C-WH, Hooper, LV, Hoppe, T, Horos, R, Hoshida, Y, Hsin, I-L, Hsu, H-Y, Hu, B, Hu, D, Hu, L-F, Hu, MC, Hu, R, Hu, W, Hu, Y-C, Hu, Z-W, Hua, F, Hua, J, Hua, Y, Huan, C, Huang, C, Huang, H, Huang, K, Huang, MLH, Huang, R, Huang, S, Huang, T, Huang, X, Huang, YJ, Huber, TB, Hubert, V, Hubner, CA, Hughes, SM, Hughes, WE, Humbert, M, Hummer, G, Hurley, JH, Hussain, S, Hussey, PJ, Hutabarat, M, Hwang, H-Y, Hwang, S, Ieni, A, Ikeda, F, Imagawa, Y, Imai, Y, Imbriano, C, Imoto, M, Inman, DM, Inoki, K, Iovanna, J, Iozzo, RV, Ippolito, G, Irazoqui, JE, Iribarren, P, Ishaq, M, Ishikawa, M, Ishimwe, N, Isidoro, C, Ismail, N, Issazadeh-Navikas, S, Itakura, E, Ito, D, Ivankovic, D, Ivanova, S, Iyer, AKV, Izquierdo, JM, Izumi, M, Jäättelä, M, Jabir, MS, Jackson, WT, Jacobo-Herrera, N, Jacomin, A-C, Jacquin, E, Jadiya, P, Jaeschke, H, Jagannath, C, Jakobi, AJ, Jakobsson, J, Janji, B, Jansen-Dürr, P, Jansson, PJ, Jantsch, J, Januszewski, S, Jassey, A, Jean, S, Jeltsch-David, H, Jendelova, P, Jenny, A, Jensen, TE, Jessen, N, Jewell, JL, Ji, J, Jia, L, Jia, R, Jiang, L, Jiang, Q, Jiang, R, Jiang, T, Jiang, X, Jiang, Y, Jimenez-Sanchez, M, Jin, E-J, Jin, F, Jin, H, Jin, L, Jin, M, Jin, S, Jo, E-K, Joffre, C, Johansen, T, Johnson, GVW, Johnston, SA, Jokitalo, E, Jolly, MK, Joosten, LAB, Jordan, J, Joseph, B, Ju, D, Ju, J-S, Ju, J, Juárez, E, Judith, D, Juhász, G, Jun, Y, Jung, CH, Jung, S-C, Jung, YK, Jungbluth, H, Jungverdorben, J, Just, S, Kaarniranta, K, Kaasik, A, Kabuta, T, Kaganovich, D, Kahana, A, Kain, R, Kajimura, S, Kalamvoki, M, Kalia, M, Kalinowski, DS, Kaludercic, N, Kalvari, I, Kaminska, J, Kaminskyy, VO, Kanamori, H, Kanasaki, K, Kang, C, Kang, R, Kang, SS, Kaniyappan, S, Kanki, T, Kanneganti, T-D, Kanthasamy, AG, Kanthasamy, A, Kantorow, M, Kapuy, O, Karamouzis, MV, Karim, MR, Karmakar, P, Katare, RG, Kato, M, Kaufmann, SHE, Kauppinen, A, Kaushal, GP, Kaushik, S, Kawasaki, K, Kazan, K, Ke, P-Y, Keating, DJ, Keber, U, Kehrl, JH, Keller, KE, Keller, CW, Kemper, JK, Kenific, CM, Kepp, O, Kermorgant, S, Kern, A, Ketteler, R, Keulers, TG, Khalfin, B, Khalil, H, Khambu, B, Khan, SY, Khandelwal, VKM, Khandia, R, Kho, W, Khobrekar, NV, Khuansuwan, S, Khundadze, M, Killackey, SA, Kim, D, Kim, DR, Kim, D-H, Kim, D-E, Kim, EY, Kim, E-K, Kim, H-R, Kim, H-S, Hyung-Ryong Kim, Kim, JH, Kim, JK, Kim, J-H, Kim, J, Kim, KI, Kim, PK, Kim, S-J, Kimball, SR, Kimchi, A, Kimmelman, AC, Kimura, T, King, MA, Kinghorn, KJ, Kinsey, CG, Kirkin, V, Kirshenbaum, LA, Kiselev, SL, Kishi, S, Kitamoto, K, Kitaoka, Y, Kitazato, K, Kitsis, RN, Kittler, JT, Kjaerulff, O, Klein, PS, Klopstock, T, Klucken, J, Knævelsrud, H, Knorr, RL, Ko, BCB, Ko, F, Ko, J-L, Kobayashi, H, Kobayashi, S, Koch, I, Koch, JC, Koenig, U, Kögel, D, Koh, YH, Koike, M, Kohlwein, SD, Kocaturk, NM, Komatsu, M, König, J, Kono, T, Kopp, BT, Korcsmaros, T, Korkmaz, G, Korolchuk, VI, Korsnes, MS, Koskela, A, Kota, J, Kotake, Y, Kotler, ML, Kou, Y, Koukourakis, MI, Koustas, E, Kovacs, AL, Kovács, T, Koya, D, Kozako, T, Kraft, C, Krainc, D, Krämer, H, Krasnodembskaya, AD, Kretz-Remy, C, Kroemer, G, Ktistakis, NT, Kuchitsu, K, Kuenen, S, Kuerschner, L, Kukar, T, Kumar, A, Kumar, D, Kumar, S, Kume, S, Kumsta, C, Kundu, CN, Kundu, M, Kunnumakkara, AB, Kurgan, L, Kutateladze, TG, Kutlu, O, Kwak, S, Kwon, HJ, Kwon, TK, Kwon, YT, Kyrmizi, I, La Spada, A, Labonté, P, Ladoire, S, Laface, I, Lafont, F, Lagace, DC, Lahiri, V, Lai, Z, Laird, AS, Lakkaraju, A, Lamark, T, Lan, S-H, Landajuela, A, Lane, DJR, Lane, JD, Lang, CH, Lange, C, Langel, Ü, Langer, R, Lapaquette, P, Laporte, J, LaRusso, NF, Lastres-Becker, I, Lau, WCY, Laurie, GW, Lavandero, S, Law, BYK, Law, HK-W, Layfield, R, Le, W, Le Stunff, H, Leary, AY, Lebrun, J-J, Leck, LYW, Leduc-Gaudet, J-P, Lee, C, Lee, C-P, Lee, D-H, Lee, EB, Lee, EF, Lee, GM, Lee, H-J, Lee, HK, Lee, JM, Lee, JS, Lee, J-A, Lee, J-Y, Lee, JH, Lee, M, Lee, MG, Lee, MJ, Lee, M-S, Lee, SY, Lee, S-J, Lee, SB, Lee, WH, Lee, Y-R, Lee, Y-H, Lee, Y, Lefebvre, C, Legouis, R, Lei, YL, Lei, Y, Leikin, S, Leitinger, G, Lemus, L, Leng, S, Lenoir, O, Lenz, G, Lenz, HJ, Lenzi, P, León, Y, Leopoldino, AM, Leschczyk, C, Leskelä, S, Letellier, E, Leung, C-T, Leung, PS, Leventhal, JS, Levine, B, Lewis, PA, Ley, K, Li, B, Li, D-Q, Li, J, Li, K, Li, L, Li, M, Li, P-L, Li, M-Q, Li, Q, Li, S, Li, T, Li, W, Li, X, Li, Y-P, Li, Y, Li, Z, Lian, J, Liang, C, Liang, Q, Liang, W, Liang, Y, Liao, G, Liao, L, Liao, M, Liao, Y-F, Librizzi, M, Lie, PPY, Lilly, MA, Lim, HJ, Lima, TRR, Limana, F, Lin, C, Lin, C-W, Lin, D-S, Lin, F-C, Lin, JD, Lin, KM, Lin, K-H, Lin, L-T, Lin, P-H, Lin, Q, Lin, S, Lin, S-J, Lin, W, Lin, X, Lin, Y-X, Lin, Y-S, Linden, R, Lindner, P, Ling, S-C, Lingor, P, Linnemann, AK, Liou, Y-C, Lipinski, MM, Lipovšek, S, Lira, VA, Lisiak, N, Liton, PB, Liu, C, Liu, C-H, Liu, C-F, Liu, CH, Liu, F, Liu, H, Liu, H-S, Liu, H-F, Liu, J, Liu, L, Liu, M, Liu, Q, Liu, W, Liu, X-H, Liu, X, Liu, Y, Livingston, JA, Lizard, G, Lizcano, JM, Ljubojevic-Holzer, S, LLeonart, ME, Llobet-Navàs, D, Llorente, A, Lo, CH, Lobato-Márquez, D, Long, Q, Long, YC, Loos, B, Loos, JA, López, MG, López-Doménech, G, López-Guerrero, JA, López-Jiménez, AT, López-Pérez, Ó, López-Valero, I, Lorenowicz, MJ, Lorente, M, Lorincz, P, Lossi, L, Lotersztajn, S, Lovat, PE, Lovell, JF, Lovy, A, Lőw, P, Lu, G, Lu, H, Lu, J-H, Lu, J-J, Lu, M, Lu, S, Luciani, A, Lucocq, JM, Ludovico, P, Luftig, MA, Luhr, M, Luis-Ravelo, D, Lum, JJ, Luna-Dulcey, L, Lund, AH, Lund, VK, Lünemann, JD, Lüningschrör, P, Luo, H, Luo, R, Luo, S, Luo, Z, Luparello, C, Lüscher, B, Luu, L, Lyakhovich, A, Lyamzaev, KG, Lystad, AH, Lytvynchuk, L, Ma, AC, Ma, C, Ma, M, Ma, N-F, Ma, Q-H, Ma, X, Ma, Y, Ma, Z, MacDougald, OA, Macian, F, MacIntosh, GC, MacKeigan, JP, Macleod, KF, Maday, S, Madeo, F, Madesh, M, Madl, T, Madrigal-Matute, J, Maeda, A, Maejima, Y, Magarinos, M, Mahavadi, P, Maiani, E, Maiese, K, Maiti, P, Maiuri, MC, Majello, B, Major, MB, Makareeva, E, Malik, F, Mallilankaraman, K, Malorni, W, Maloyan, A, Mammadova, N, Man, GCW, Manai, F, Mancias, JD, Mandelkow, E-M, Mandell, MA, Manfredi, AA, Manjili, MH, Manjithaya, R, Manque, P, Manshian, BB, Manzano, R, Manzoni, C, Mao, K, Marchese, C, Marchetti, S, Marconi, AM, Marcucci, F, Mardente, S, Mareninova, OA, Margeta, M, Mari, M, Marinelli, S, Marinelli, O, Mariño, G, Mariotto, S, Marshall, RS, Marten, MR, Martens, S, Martin, APJ, Martin, KR, Martin, S, Martín-Segura, A, Martín-Acebes, MA, Martin-Burriel, I, Martin-Rincon, M, Martin-Sanz, P, Martina, JA, Martinet, W, Martinez, A, Martinez, J, Martinez Velazquez, M, Martinez-Lopez, N, Martinez-Vicente, M, Martins, DO, Martins, JO, Martins, WK, Martins-Marques, T, Marzetti, E, Masaldan, S, Masclaux-Daubresse, C, Mashek, DG, Massa, V, Massieu, L, Masson, GR, Masuelli, L, Masyuk, AI, Masyuk, TV, Matarrese, P, Matheu, A, Matoba, S, Matsuzaki, S, Mattar, P, Matte, A, Mattoscio, D, Mauriz, JL, Mauthe, M, Mauvezin, C, Maverakis, E, Maycotte, P, Mayer, J, Mazzoccoli, G, Mazzoni, C, Mazzulli, JR, McCarty, N, McDonald, C, McGill, MR, McKenna, SL, McLaughlin, B, McLoughlin, F, McNiven, MA, McWilliams, TG, Mechta-Grigoriou, F, Medeiros, TC, Medina, DL, Megeney, LA, Megyeri, K, Mehrpour, M, Mehta, JL, Meijer, AJ, Meijer, AH, Mejlvang, J, Meléndez, A, Melk, A, Memisoglu, G, Mendes, AF, Meng, D, Meng, F, Meng, T, Menna-Barreto, R, Menon, MB, Mercer, C, Mercier, AE, Mergny, J-L, Merighi, A, Merkley, SD, Merla, G, Meske, V, Mestre, AC, Metur, SP, Meyer, C, Meyer, H, Mi, W, Mialet-Perez, J, Miao, J, Micale, L, Miki, Y, Milan, E, Milczarek, M, Miller, DL, Miller, SI, Miller, S, Millward, SW, Milosevic, I, Minina, EA, Mirzaei, H, Mirzaei, HR, Mirzaei, M, Mishra, A, Mishra, N, Mishra, PK, Misirkic Marjanovic, M, Misasi, R, Misra, A, Misso, G, Mitchell, C, Mitou, G, Miura, T, Miyamoto, S, Miyazaki, M, Miyazaki, T, Miyazawa, K, Mizushima, N, Mogensen, TH, Mograbi, B, Mohammadinejad, R, Mohamud, Y, Mohanty, A, Mohapatra, S, Möhlmann, T, Mohmmed, A, Moles, A, Moley, KH, Molinari, M, Mollace, V, Møller, AB, Mollereau, B, Mollinedo, F, Montagna, C, Monteiro, MJ, Montella, A, Montes, LR, Montico, B, Mony, VK, Monzio Compagnoni, G, Moore, MN, Moosavi, MA, Mora, AL, Mora, M, Morales-Alamo, D, Moratalla, R, Moreira, PI, Morelli, E, Moreno, S, Moreno-Blas, D, Moresi, V, Morga, B, Morgan, AH, Morin, F, Morishita, H, Moritz, OL, Moriyama, M, Moriyasu, Y, Morleo, M, Morselli, E, Moruno-Manchon, JF, Moscat, J, Mostowy, S, Motori, E, Moura, AF, Moustaid-Moussa, N, Mrakovcic, M, Muciño-Hernández, G, Mukherjee, A, Mukhopadhyay, S, Mulcahy Levy, JM, Mulero, V, Muller, S, Münch, C, Munjal, A, Munoz-Canoves, P, Muñoz-Galdeano, T, Münz, C, Murakawa, T, Muratori, C, Murphy, BM, Murphy, JP, Murthy, A, Myöhänen, TT, Mysorekar, IU, Mytych, J, Nabavi, SM, Nabissi, M, Nagy, P, Nah, J, Nahimana, A, Nakagawa, I, Nakamura, K, Nakatogawa, H, Nandi, SS, Nanjundan, M, Nanni, M, Napolitano, G, Nardacci, R, Narita, M, Nassif, M, Nathan, I, Natsumeda, M, Naude, RJ, Naumann, C, Naveiras, O, Navid, F, Nawrocki, ST, Nazarko, TY, Nazio, F, Negoita, F, Neill, T, Neisch, AL, Neri, LM, Netea, MG, Neubert, P, Neufeld, TP, Neumann, D, Neutzner, A, Newton, PT, Ney, PA, Nezis, IP, Ng, CCW, Ng, TB, Nguyen, HTT, Nguyen, LT, Ni, H-M, Ní Cheallaigh, C, Ni, Z, Nicolao, MC, Nicoli, F, Nieto-Diaz, M, Nilsson, P, Ning, S, Niranjan, R, Nishimune, H, Niso-Santano, M, Nixon, RA, Nobili, A, Nobrega, C, Noda, T, Nogueira-Recalde, U, Nolan, TM, Nombela, I, Novak, I, Novoa, B, Nozawa, T, Nukina, N, Nussbaum-Krammer, C, Nylandsted, J, O'Donovan, TR, O'Leary, SM, O'Rourke, EJ, O'Sullivan, MP, O'Sullivan, TE, Oddo, S, Oehme, I, Ogawa, M, Ogier-Denis, E, Ogmundsdottir, MH, Ogretmen, B, Oh, GT, Oh, S-H, Oh, YJ, Ohama, T, Ohashi, Y, Ohmuraya, M, Oikonomou, V, Ojha, R, Okamoto, K, Okazawa, H, Oku, M, Oliván, S, Oliveira, JMA, Ollmann, M, Olzmann, JA, Omari, S, Omary, MB, Önal, G, Ondrej, M, Ong, S-B, Ong, S-G, Onnis, A, Orellana, JA, Orellana-Muñoz, S, Ortega-Villaizan, MDM, Ortiz-Gonzalez, XR, Ortona, E, Osiewacz, HD, Osman, A-HK, Osta, R, Otegui, MS, Otsu, K, Ott, C, Ottobrini, L, Ou, J-HJ, Outeiro, TF, Oynebraten, I, Ozturk, M, Pagès, G, Pahari, S, Pajares, M, Pajvani, UB, Pal, R, Paladino, S, Pallet, N, Palmieri, M, Palmisano, G, Palumbo, C, Pampaloni, F, Pan, L, Pan, Q, Pan, W, Pan, X, Panasyuk, G, Pandey, R, Pandey, UB, Pandya, V, Paneni, F, Pang, SY, Panzarini, E, Papademetrio, DL, Papaleo, E, Papinski, D, Papp, D, Park, EC, Park, HT, Park, J-M, Park, J-I, Park, JT, Park, J, Park, SC, Park, S-Y, Parola, AH, Parys, JB, Pasquier, A, Pasquier, B, Passos, JF, Pastore, N, Patel, HH, Patschan, D, Pattingre, S, Pedraza-Alva, G, Pedraza-Chaverri, J, Pedrozo, Z, Pei, G, Pei, J, Peled-Zehavi, H, Pellegrini, JM, Pelletier, J, Peñalva, MA, Peng, D, Peng, Y, Penna, F, Pennuto, M, Pentimalli, F, Pereira, CM, Pereira, GJS, Pereira, LC, Pereira de Almeida, L, Perera, ND, Pérez-Lara, Á, Perez-Oliva, AB, Pérez-Pérez, ME, Periyasamy, P, Perl, A, Perrotta, C, Perrotta, I, Pestell, RG, Petersen, M, Petrache, I, Petrovski, G, Pfirrmann, T, Pfister, AS, Philips, JA, Pi, H, Picca, A, Pickrell, AM, Picot, S, Pierantoni, GM, Pierdominici, M, Pierre, P, Pierrefite-Carle, V, Pierzynowska, K, Pietrocola, F, Pietruczuk, M, Pignata, C, Pimentel-Muiños, FX, Pinar, M, Pinheiro, RO, Pinkas-Kramarski, R, Pinton, P, Pircs, K, Piya, S, Pizzo, P, Plantinga, TS, Platta, HW, Plaza-Zabala, A, Plomann, M, Plotnikov, EY, Plun-Favreau, H, Pluta, R, Pocock, R, Pöggeler, S, Pohl, C, Poirot, M, Poletti, A, Ponpuak, M, Popelka, H, Popova, B, Porta, H, Porte Alcon, S, Portilla-Fernandez, E, Post, M, Potts, MB, Poulton, J, Powers, T, Prahlad, V, Prajsnar, TK, Praticò, D, Prencipe, R, Priault, M, Proikas-Cezanne, T, Promponas, VJ, Proud, CG, Puertollano, R, Puglielli, L, Pulinilkunnil, T, Puri, D, Puri, R, Puyal, J, Qi, X, Qi, Y, Qian, W, Qiang, L, Qiu, Y, Quadrilatero, J, Quarleri, J, Raben, N, Rabinowich, H, Ragona, D, Ragusa, MJ, Rahimi, N, Rahmati, M, Raia, V, Raimundo, N, Rajasekaran, N-S, Ramachandra Rao, S, Rami, A, Ramírez-Pardo, I, Ramsden, DB, Randow, F, Rangarajan, PN, Ranieri, D, Rao, H, Rao, L, Rao, R, Rathore, S, Ratnayaka, JA, Ratovitski, EA, Ravanan, P, Ravegnini, G, Ray, SK, Razani, B, Rebecca, V, Reggiori, F, Régnier-Vigouroux, A, Reichert, AS, Reigada, D, Reiling, JH, Rein, T, Reipert, S, Rekha, RS, Ren, H, Ren, J, Ren, W, Renault, T, Renga, G, Reue, K, Rewitz, K, Ribeiro de Andrade Ramos, B, Riazuddin, SA, Ribeiro-Rodrigues, TM, Ricci, J-E, Ricci, R, Riccio, V, Richardson, DR, Rikihisa, Y, Risbud, MV, Risueño, RM, Ritis, K, Rizza, S, Rizzuto, R, Roberts, HC, Roberts, LD, Robinson, KJ, Roccheri, MC, Rocchi, S, Rodney, GG, Rodrigues, T, Rodrigues Silva, VR, Rodriguez, A, Rodriguez-Barrueco, R, Rodriguez-Henche, N, Rodriguez-Rocha, H, Roelofs, J, Rogers, RS, Rogov, VV, Rojo, AI, Rolka, K, Romanello, V, Romani, L, Romano, A, Romano, PS, Romeo-Guitart, D, Romero, LC, Romero, M, Roney, JC, Rongo, C, Roperto, S, Rosenfeldt, MT, Rosenstiel, P, Rosenwald, AG, Roth, KA, Roth, L, Roth, S, Rouschop, KMA, Roussel, BD, Roux, S, Rovere-Querini, P, Roy, A, Rozieres, A, Ruano, D, Rubinsztein, DC, Rubtsova, MP, Ruckdeschel, K, Ruckenstuhl, C, Rudolf, E, Rudolf, R, Ruggieri, A, Ruparelia, AA, Rusmini, P, Russell, RR, Russo, GL, Russo, M, Russo, R, Ryabaya, OO, Ryan, KM, Ryu, K-Y, Sabater-Arcis, M, Sachdev, U, Sacher, M, Sachse, C, Sadhu, A, Sadoshima, J, Safren, N, Saftig, P, Sagona, AP, Sahay, G, Sahebkar, A, Sahin, M, Sahin, O, Sahni, S, Saito, N, Saito, S, Saito, T, Sakai, R, Sakai, Y, Sakamaki, J-I, Saksela, K, Salazar, G, Salazar-Degracia, A, Salekdeh, GH, Saluja, AK, Sampaio-Marques, B, Sanchez, MC, Sanchez-Alcazar, JA, Sanchez-Vera, V, Sancho-Shimizu, V, Sanderson, JT, Sandri, M, Santaguida, S, Santambrogio, L, Santana, MM, Santoni, G, Sanz, A, Sanz, P, Saran, S, Sardiello, M, Sargeant, TJ, Sarin, A, Sarkar, C, Sarkar, S, Sarrias, M-R, Sarmah, DT, Sarparanta, J, Sathyanarayan, A, Sathyanarayanan, R, Scaglione, KM, Scatozza, F, Schaefer, L, Schafer, ZT, Schaible, UE, Schapira, AHV, Scharl, M, Schatzl, HM, Schein, CH, Scheper, W, Scheuring, D, Schiaffino, MV, Schiappacassi, M, Schindl, R, Schlattner, U, Schmidt, O, Schmitt, R, Schmidt, SD, Schmitz, I, Schmukler, E, Schneider, A, Schneider, BE, Schober, R, Schoijet, AC, Schott, MB, Schramm, M, Schröder, B, Schuh, K, Schüller, C, Schulze, RJ, Schürmanns, L, Schwamborn, JC, Schwarten, M, Scialo, F, Sciarretta, S, Scott, MJ, Scotto, KW, Scovassi, AI, Scrima, A, Scrivo, A, Sebastian, D, Sebti, S, Sedej, S, Segatori, L, Segev, N, Seglen, PO, Seiliez, I, Seki, E, Selleck, SB, Sellke, FW, Selsby, JT, Sendtner, M, Senturk, S, Seranova, E, Sergi, C, Serra-Moreno, R, Sesaki, H, Settembre, C, Setty, SRG, Sgarbi, G, Sha, O, Shacka, JJ, Shah, JA, Shang, D, Shao, C, Shao, F, Sharbati, S, Sharkey, LM, Sharma, D, Sharma, G, Sharma, K, Sharma, P, Sharma, S, Shen, H-M, Shen, H, Shen, J, Shen, M, Shen, W, Shen, Z, Sheng, R, Sheng, Z, Sheng, Z-H, Shi, J, Shi, X, Shi, Y-H, Shiba-Fukushima, K, Shieh, J-J, Shimada, Y, Shimizu, S, Shimozawa, M, Shintani, T, Shoemaker, CJ, Shojaei, S, Shoji, I, Shravage, BV, Shridhar, V, Shu, C-W, Shu, H-B, Shui, K, Shukla, AK, Shutt, TE, Sica, V, Siddiqui, A, Sierra, A, Sierra-Torre, V, Signorelli, S, Sil, P, Silva, BJDA, Silva, JD, Silva-Pavez, E, Silvente-Poirot, S, Simmonds, RE, Simon, AK, Simon, H-U, Simons, M, Singh, A, Singh, LP, Singh, R, Singh, SV, Singh, SK, Singh, SB, Singh, S, Singh, SP, Sinha, D, Sinha, RA, Sinha, S, Sirko, A, Sirohi, K, Sivridis, EL, Skendros, P, Skirycz, A, Slaninová, I, Smaili, SS, Smertenko, A, Smith, MD, Soenen, SJ, Sohn, EJ, Sok, SPM, Solaini, G, Soldati, T, Soleimanpour, SA, Soler, RM, Solovchenko, A, Somarelli, JA, Sonawane, A, Song, F, Song, HK, Song, J-X, Song, K, Song, Z, Soria, LR, Sorice, M, Soukas, AA, Soukup, S-F, Sousa, D, Sousa, N, Spagnuolo, PA, Spector, SA, Srinivas Bharath, MM, St Clair, D, Stagni, V, Staiano, L, Stalnecker, CA, Stankov, MV, Stathopulos, PB, Stefan, K, Stefan, SM, Stefanis, L, Steffan, JS, Steinkasserer, A, Stenmark, H, Sterneckert, J, Stevens, C, Stoka, V, Storch, S, Stork, B, Strappazzon, F, Strohecker, AM, Stupack, DG, Su, H, Su, L-Y, Su, L, Suarez-Fontes, AM, Subauste, CS, Subbian, S, Subirada, PV, Sudhandiran, G, Sue, CM, Sui, X, Summers, C, Sun, G, Sun, J, Sun, K, Sun, M-X, Sun, Q, Sun, Y, Sun, Z, Sunahara, KKS, Sundberg, E, Susztak, K, Sutovsky, P, Suzuki, H, Sweeney, G, Symons, JD, Sze, SCW, Szewczyk, NJ, Tabęcka-Łonczynska, A, Tabolacci, C, Tacke, F, Taegtmeyer, H, Tafani, M, Tagaya, M, Tai, H, Tait, SWG, Takahashi, Y, Takats, S, Talwar, P, Tam, C, Tam, SY, Tampellini, D, Tamura, A, Tan, CT, Tan, E-K, Tan, Y-Q, Tanaka, M, Tang, D, Tang, J, Tang, T-S, Tanida, I, Tao, Z, Taouis, M, Tatenhorst, L, Tavernarakis, N, Taylor, A, Taylor, GA, Taylor, JM, Tchetina, E, Tee, AR, Tegeder, I, Teis, D, Teixeira, N, Teixeira-Clerc, F, Tekirdag, KA, Tencomnao, T, Tenreiro, S, Tepikin, AV, Testillano, PS, Tettamanti, G, Tharaux, P-L, Thedieck, K, Thekkinghat, AA, Thellung, S, Thinwa, JW, Thirumalaikumar, VP, Thomas, SM, Thomes, PG, Thorburn, A, Thukral, L, Thum, T, Thumm, M, Tian, L, Tichy, A, Till, A, Timmerman, V, Titorenko, VI, Todi, SV, Todorova, K, Toivonen, JM, Tomaipitinca, L, Tomar, D, Tomas-Zapico, C, Tomić, S, Tong, BC-K, Tong, C, Tong, X, Tooze, SA, Torgersen, ML, Torii, S, Torres-López, L, Torriglia, A, Towers, CG, Towns, R, Toyokuni, S, Trajkovic, V, Tramontano, D, Tran, Q-G, Travassos, LH, Trelford, CB, Tremel, S, Trougakos, IP, Tsao, BP, Tschan, MP, Tse, H-F, Tse, TF, Tsugawa, H, Tsvetkov, AS, Tumbarello, DA, Tumtas, Y, Tuñón, MJ, Turcotte, S, Turk, B, Turk, V, Turner, BJ, Tuxworth, RI, Tyler, JK, Tyutereva, EV, Uchiyama, Y, Ugun-Klusek, A, Uhlig, HH, Ułamek-Kozioł, M, Ulasov, IV, Umekawa, M, Ungermann, C, Unno, R, Urbe, S, Uribe-Carretero, E, Üstün, S, Uversky, VN, Vaccari, T, Vaccaro, MI, Vahsen, BF, Vakifahmetoglu-Norberg, H, Valdor, R, Valente, MJ, Valko, A, Vallee, RB, Valverde, AM, Van den Berghe, G, van der Veen, S, Van Kaer, L, van Loosdregt, J, van Wijk, SJL, Vandenberghe, W, Vanhorebeek, I, Vannier-Santos, MA, Vannini, N, Vanrell, MC, Vantaggiato, C, Varano, G, Varela-Nieto, I, Varga, M, Vasconcelos, MH, Vats, S, Vavvas, DG, Vega-Naredo, I, Vega-Rubin-de-Celis, S, Velasco, G, Velázquez, AP, Vellai, T, Vellenga, E, Velotti, F, Verdier, M, Verginis, P, Vergne, I, Verkade, P, Verma, M, Verstreken, P, Vervliet, T, Vervoorts, J, Vessoni, AT, Victor, VM, Vidal, M, Vidoni, C, Vieira, OV, Vierstra, RD, Viganó, S, Vihinen, H, Vijayan, V, Vila, M, Vilar, M, Villalba, JM, Villalobo, A, Villarejo-Zori, B, Villarroya, F, Villarroya, J, Vincent, O, Vindis, C, Viret, C, Viscomi, MT, Visnjic, D, Vitale, I, Vocadlo, DJ, Voitsekhovskaja, OV, Volonté, C, Volta, M, Vomero, M, Von Haefen, C, Vooijs, MA, Voos, W, Vucicevic, L, Wade-Martins, R, Waguri, S, Waite, KA, Wakatsuki, S, Walker, DW, Walker, MJ, Walker, SA, Walter, J, Wandosell, FG, Wang, B, Wang, C-Y, Wang, C, Wang, D, Wang, F, Wang, G, Wang, H, Wang, H-G, Wang, J, Wang, K, Wang, L, Wang, MH, Wang, M, Wang, N, Wang, P, Wang, QJ, Wang, Q, Wang, QK, Wang, QA, Wang, W-T, Wang, W, Wang, X, Wang, Y, Wang, Y-Y, Wang, Z, Warnes, G, Warnsmann, V, Watada, H, Watanabe, E, Watchon, M, Wawrzyńska, A, Weaver, TE, Wegrzyn, G, Wehman, AM, Wei, H, Wei, L, Wei, T, Wei, Y, Weiergräber, OH, Weihl, CC, Weindl, G, Weiskirchen, R, Wells, A, Wen, RH, Wen, X, Werner, A, Weykopf, B, Wheatley, SP, Whitton, JL, Whitworth, AJ, Wiktorska, K, Wildenberg, ME, Wileman, T, Wilkinson, S, Willbold, D, Williams, B, Williams, RSB, Williams, RL, Williamson, PR, Wilson, RA, Winner, B, Winsor, NJ, Witkin, SS, Wodrich, H, Woehlbier, U, Wollert, T, Wong, E, Wong, JH, Wong, RW, Wong, VKW, Wong, WW-L, Wu, A-G, Wu, C, Wu, J, Wu, KK, Wu, M, Wu, S-Y, Wu, S, Wu, WKK, Wu, X, Wu, Y-W, Wu, Y, Xavier, RJ, Xia, H, Xia, L, Xia, Z, Xiang, G, Xiang, J, Xiang, M, Xiang, W, Xiao, B, Xiao, G, Xiao, H, Xiao, H-T, Xiao, J, Xiao, L, Xiao, S, Xiao, Y, Xie, B, Xie, C-M, Xie, M, Xie, Y, Xie, Z, Xilouri, M, Xu, C, Xu, E, Xu, H, Xu, J, Xu, L, Xu, WW, Xu, X, Xue, Y, Yakhine-Diop, SMS, Yamaguchi, M, Yamaguchi, O, Yamamoto, A, Yamashina, S, Yan, S, Yan, S-J, Yan, Z, Yanagi, Y, Yang, C, Yang, D-S, Yang, H, Yang, H-T, Yang, J-M, Yang, J, Yang, L, Yang, M, Yang, P-M, Yang, Q, Yang, S, Yang, S-F, Yang, W, Yang, WY, Yang, X, Yang, Y, Yao, H, Yao, S, Yao, X, Yao, Y-G, Yao, Y-M, Yasui, T, Yazdankhah, M, Yen, PM, Yi, C, Yin, X-M, Yin, Y, Yin, Z, Ying, M, Ying, Z, Yip, CK, Yiu, SPT, Yoo, YH, Yoshida, K, Yoshii, SR, Yoshimori, T, Yousefi, B, Yu, B, Yu, H, Yu, J, Yu, L, Yu, M-L, Yu, S-W, Yu, VC, Yu, WH, Yu, Z, Yuan, J, Yuan, L-Q, Yuan, S, Yuan, S-SF, Yuan, Y, Yuan, Z, Yue, J, Yue, Z, Yun, J, Yung, RL, Zacks, DN, Zaffagnini, G, Zambelli, VO, Zanella, I, Zang, QS, Zanivan, S, Zappavigna, S, Zaragoza, P, Zarbalis, KS, Zarebkohan, A, Zarrouk, A, Zeitlin, SO, Zeng, J, Zeng, J-D, Žerovnik, E, Zhan, L, Zhang, B, Zhang, DD, Zhang, H, Zhang, H-L, Zhang, J, Zhang, J-P, Zhang, KYB, Zhang, LW, Zhang, L, Zhang, M, Zhang, P, Zhang, S, Zhang, W, Zhang, X, Zhang, X-W, Zhang, XD, Zhang, Y, Zhang, Y-D, Zhang, Y-Y, Zhang, Z, Zhao, H, Zhao, L, Zhao, S, Zhao, T, Zhao, X-F, Zhao, Y, Zheng, G, Zheng, K, Zheng, L, Zheng, S, Zheng, X-L, Zheng, Y, Zheng, Z-G, Zhivotovsky, B, Zhong, Q, Zhou, A, Zhou, B, Zhou, C, Zhou, G, Zhou, H, Zhou, J, Zhou, K, Zhou, R, Zhou, X-J, Zhou, Y, Zhou, Z-Y, Zhou, Z, Zhu, B, Zhu, C, Zhu, G-Q, Zhu, H, Zhu, W-G, Zhu, Y, Zhuang, H, Zhuang, X, Zientara-Rytter, K, Zimmermann, CM, Ziviani, E, Zoladek, T, Zong, W-X, Zorov, DB, Zorzano, A, Zou, W, Zou, Z, Zuryn, S, Zwerschke, W, Brand-Saberi, B, Dong, XC, Kenchappa, CS, Lin, Y, Oshima, S, Rong, Y, Sluimer, JC, Stallings, CL, and Tong, C-K
- Abstract
In 2008, we published the first set of guidelines for standardizing research in autophagy. Since then, this topic has received increasing attention, and many scientists have entered the field. Our knowledge base and relevant new technologies have also been expanding. Thus, it is important to formulate on a regular basis updated guidelines for monitoring autophagy in different organisms. Despite numerous reviews, there continues to be confusion regarding acceptable methods to evaluate autophagy, especially in multicellular eukaryotes. Here, we present a set of guidelines for investigators to select and interpret methods to examine autophagy and related processes, and for reviewers to provide realistic and reasonable critiques of reports that are focused on these processes. These guidelines are not meant to be a dogmatic set of rules, because the appropriateness of any assay largely depends on the question being asked and the system being used. Moreover, no individual assay is perfect for every situation, calling for the use of multiple techniques to properly monitor autophagy in each experimental setting. Finally, several core components of the autophagy machinery have been implicated in distinct autophagic processes (canonical and noncanonical autophagy), implying that genetic approaches to block autophagy should rely on targeting two or more autophagy-related genes that ideally participate in distinct steps of the pathway. Along similar lines, because multiple proteins involved in autophagy also regulate other cellular pathways including apoptosis, not all of them can be used as a specific marker for bona fide autophagic responses. Here, we critically discuss current methods of assessing autophagy and the information they can, or cannot, provide. Our ultimate goal is to encourage intellectual and technical innovation in the field.
- Published
- 2021
3. Measurement of the bottom-strange meson mixing phase in the full CDF data set
- Author
-
Aaltonen, T., Alvarez, González, Amerio, B., Amidei, S., Anastassov, D., Annovi, A., Antos, A., Apollinari, J., Appel, G., J. A., Arisawa, Artikov, T., Asaadi, A., Ashmanskas, J., Auerbach, W., Aurisano, B., Azfar, A., Badgett, F., Bae, W., Barbaro, Galtieri, Barnes, A., V. E., Barnett, B. A., Barria, Bartos, P., Bauce, P., Bedeschi, M., Behari, F., Bellettini, S., Bellinger, G., Benjamin, J., Beretvas, D., Bhatti, A., Bisello, A., Bizjak, D., Bland, I., K. R., Blumenfeld, Bocci, B., Bodek, A., Bortoletto, A., Boudreau, D., Boveia, J., Brigliadori, A., Bromberg, L., Brucken, C., Budagov, E., Budd, J., H. S., Burkett, Busetto, K., Bussey, G., Buzatu, P., Calamba, A., Calancha, A., Camarda, C., Campanelli, S., Campbell, M., Canelli, M., Carls, F., Carlsmith, B., Carosi, D., Carrillo, R., Carron, S., Casal, S., Casarsa, B., Castro, M., Catastini, A., Cauz, P., Cavaliere, D., Cavalli, Sforza, Cerri, M., Cerrito, A., Chen, L., Y. C., Chertok, Chiarelli, M., Chlachidze, G., Chlebana, G., Cho, F., Chokheli, K., Chung, D., W. H., Chung, Y. S., Ciocci, M. A., Clark, Clarke, A., Compostella, C., Convery, G., M. E., Conway, Corbo, J., Cordelli, M., Cox, M., C. A., Cox, D. J., Crescioli, Cuevas, F., Culbertson, J., Dagenhart, R., D'Ascenzo, D., Datta, N., Barbaro, De, Dell'Orso, Mauro, Demortier, M., Deninno, L., Devoto, M., D'Errico, F., Canto, Di, Ruzza, Di, Dittmann, B., J. R., D'Onofrio, Donati, Simone, Dong, P., Dorigo, M., Dorigo, T., Ebina, K., Elagin, A., Eppig, A., Erbacher, R., Errede, S., Ershaidat, N., Eusebi, R., Farrington, S., Feindt, M., Fernandez, J. P., Field, R., Flanagan, G., Forrest, R., Frank, M. J., Franklin, M., Freeman, J. C., Funakoshi, Y., Furic, I., Gallinaro, M., Garcia, J. E., Garfinkel, A. F., Garosi, P., Gerberich, H., Gerchtein, E., Giagu, S., Giakoumopoulou, V., Giannetti, P., Gibson, K., Ginsburg, C. M., Giokaris, N., Giromini, P., Giurgiu, G., Glagolev, V., Glenzinski, D., Gold, M., Goldin, D., Goldschmidt, N., Golossanov, A., Gomez, G., Gomez, Ceballos, Goncharov, G., González, M., Gorelov, O., Goshaw, I., A. T., Goulianos, Grillo, K., Grinstein, L., Grosso, Pilcher, Group, C., R. C., Guimaraes Da Costa, Hahn, J., S. R., Halkiadakis, Hamaguchi, E., Han, A., J. Y., Happacher, Hara, F., Hare, K., Hare, D., Harr, M., R. F., Hatakeyama, Hays, K., Heck, C., Heinrich, M., Herndon, J., Hewamanage, M., Hocker, S., Hopkins, A., Horn, W., Hou, D., Hughes, S., R. E., Hurwitz, Husemann, M., Hussain, U., Hussein, N., Huston, M., Introzzi, J., Iori, G., Ivanov, M., James, A., Jang, E., Jayatilaka, D., Jeon, B., E. J., Jindariani, Jones, S., Joo, M., K. K., Jun, S. Y., Junk, T. R., Kamon, Karchin, T., P. E., Kasmi, Kato, A., Ketchum, Y., Keung, W., Khotilovich, J., Kilminster, V., Kim, B., D. H., Kim, H. S., Kim, J. E., Kim, M. J., Kim, S. B., Kim, S. H., Kim, Y. K., Kim, Y. J., Kimura, Kirby, N., Klimenko, M., Knoepfel, S., Kondo, K., Kong, K., D. J., Konigsberg, Kotwal, J., A. V., Kreps, Kroll, M., Krop, J., Kruse, D., Krutelyov, M., Kuhr, V., Kurata, T., Kwang, M., Laasanen, S., A. T., Lami, Lammel, S., Lancaster, S., Lander, M., R. L., Lannon, Lath, K., Latino, A., Lecompte, G., Lee, T., Lee, E., H. S., Lee, J. S., Lee, S. W., Leo, Leone, S., Lewis, S., J. D., Limosani, Lin, A., C. J., Lindgren, Lipeles, M., Lister, E., Litvintsev, A., D. O., Liu, Liu, C., Liu, H., Liu, Q., Lockwitz, T., Loginov, S., Lucchesi, A., Lueck, D., Lujan, J., Lukens, P., Lungu, P., Lys, G., Lysak, J., Madrak, R., Maeshima, R., Maestro, K., Malik, P., Manca, S., Manousakis, Katsikakis, Margaroli, A., Marino, F., Martínez, C., Mastrandrea, M., Matera, P., Mattson, K., M. E., Mazzacane, Mazzanti, A., Mcfarland, P., K. S., Mcintyre, Mcnulty, P., Mehta, R., Mehtala, A., Mesropian, P., Miao, C., Mietlicki, T., Mitra, D., Miyake, A., Moed, H., Moggi, S., Mondragon, N., M. N., Moon, C. S., Moore, Morello, R., M. J., Morlock, Movilla, Fernandez, Mukherjee, P., Muller, A., Murat, T., Mussini, P., Nachtman, M., Nagai, J., Naganoma, Y., Nakano, J., Napier, I., Nett, A., Neu, J., Neubauer, C., M. S., Nielsen, Nodulman, J., Noh, L., S. Y., Norniella, Oakes, O., Oh, L., S. H., Oh, Y. D., Oksuzian, Okusawa, I., Orava, T., Ortolan, R., Pagan, Griso, Pagliarone, S., Palencia, C., Papadimitriou, E., Paramonov, V., A. A., Patrick, Pauletta, J., Paulini, G., Paus, M., Pellett, C., D. E., Penzo, Phillips, A., T. J., Piacentino, Pianori, G., Pilot, E., Pitts, J., Plager, K., Pondrom, C., Poprocki, L., Potamianos, S., Prokoshin, K., Pranko, F., Ptohos, A., Punzi, Giovanni, Rahaman, G., Ramakrishnan, A., Ranjan, V., Redondo, N., Renton, I., Rescigno, P., Riddick, M., Rimondi, T., Ristori, F., Robson, L., Rodrigo, A., Rodriguez, T., Rogers, T., Rolli, E., Roser, S., Ruffini, R., Ruiz, F., Russ, A., Rusu, J., Safonov, V., Sakumoto, A., W. K., Sakurai, Santi, Y., Sato, L., Saveliev, K., Savoy, Navarro, Schlabach, A., Schmidt, P., Schmidt, A., E. E., Schwarz, Scodellaro, T., Scribano, L., Scuri, A., Seidel, F., Seiya, S., Semenov, Y., Sforza, A., Shalhout, F., S. Z., Shears, Shepard, T., P. F., Shimojima, Shochet, M., Shreyber, Tecker, Simonenko, I., Sinervo, A., Sliwa, P., Smith, K., J. R., Snider, F. D., Soha, Sorin, A., Song, V., Squillacioti, H., Stancari, P., Denis, S. t., Stelzer, R., Stelzer, Chilton, Stentz, O., Strologas, D., Strycker, J., G. L., Sudo, Sukhanov, Y., Suslov, A., Takemasa, I., Takeuchi, K., Tang, Y., Tecchio, J., Teng, M., P. K., Thom, Thome, J., Thompson, J., G. A., Thomson, Toback, E., Tokar, D., Tollefson, S., Tomura, K., Tonelli, T., Torre, D., Torretta, S., Totaro, D., Trovato, P., Ukegawa, M., Uozumi, F., Varganov, S., Vázquez, A., Velev, F., Vellidis, G., Vidal, C., Vila, M., Vilar, I., Vizán, R., Vogel, J., Volpi, M., Wagner, G., Wagner, P., R. L., Wakisaka, Wallny, T., Wang, R., S. M., Warburton, Waters, A., Wester, D., W. C., Whiteson, Wicklund, D., A. B., Wicklund, Wilbur, E., Wick, S., Williams, F., H. H., Wilson, J. S., Wilson, Winer, P., B. L., Wittich, Wolbers, P., Wolfe, S., Wright, H., Wu, T., Wu, X., Yamamoto, Z., Yamato, K., Yang, D., Yang, T., U. K., Yang, Y. C., Yao, W. M., Yeh, G. P., Yi, Yoh, K., Yorita, J., Yoshida, K., Yu, T., G. B., Yu, Yu, I., S. S., Yun, J. C., Zanetti, Zeng, A., Zhou, Y., Zucchelli, C., Jy, S., Koh, Yh, Koike, M, Komatsu, M, Kominami, E, Kong, Hj, Kong, Wj, Korolchuk, Vi, Kotake, Y, Koukourakis, Mi, Kouri Flores JB, Kovács, Al, Kraft, C, Krainc, D, Krämer, H, Kretz Remy, C, Krichevsky, Am, Kroemer, G, Krüger, R, Krut, O, Ktistakis, Nt, Kuan, Cy, Kucharczyk, R, Kumar, A, Kumar, R, Kumar, S, Kundu, M, Kung, Hj, Kurz, T, Kwon, Hj, La Spada AR, Lafont, F, Lamark, T, Landry, J, Lane, Jd, Lapaquette, P, Laporte, Jf, László, L, Lavandero, S, Lavoie, Jn, Layfield, R, Lazo, Pa, Le, W, Le Cam, L, Ledbetter, Dj, Lee, Aj, Lee, Bw, Lee, Gm, Lee, J, Lee, Jh, Lee, M, Lee, Ms, Lee, Sh, Leeuwenburgh, C, Legembre, P, Legouis, R, Lehmann, M, Lei, Hy, Lei, Qy, Leib, Da, Leiro, J, Lemasters, Jj, Lemoine, A, Lesniak, Ms, Lev, D, Levenson, Vv, Levine, B, Levy, E, Li, F, Li, Jl, Li, L, Li, S, Li, W, Li, Xj, Li, Yb, Li, Yp, Liang, C, Liang, Q, Liao, Yf, Liberski, Pp, Lieberman, A, Lim, Hj, Lim, Kl, Lim, K, Lin, Cf, Lin, Fc, Lin, J, Lin, Jd, Lin, K, Lin, Ww, Lin, Wc, Lin, Yl, Linden, R, Lingor, P, Lippincott Schwartz, J, Lisanti, Mp, Liton, Pb, Liu, B, Liu, Cf, Liu, K, Liu, L, Liu, Qa, Liu, W, Liu, Yc, Liu, Y, Lockshin, Ra, Lok, Cn, Lonial, S, Loos, B, Lopez Berestein, G, López Otín, C, Lossi, L, Lotze, Mt, Lőw, P, Lu, B, Lu, Z, Luciano, F, Lukacs, Nw, Lund, Ah, Lynch Day MA, Ma, Y, Macian, F, Mackeigan, Jp, Macleod, Kf, Madeo, F, Maiuri, L, Maiuri, Mc, Malagoli, D, Malicdan, Mc, Malorni, W, Man, N, Mandelkow, Em, Manon, S, Manov, I, Mao, K, Mao, X, Mao, Z, Marambaud, P, Marazziti, D, Marcel, Yl, Marchbank, K, Marchetti, P, Marciniak, Sj, Marcondes, M, Mardi, M, Marfe, G, Mariño, G, Markaki, M, Marten, Mr, Martin, Sj, Martinand Mari, C, Martinet, W, Martinez Vicente, M, Masini, M, Matarrese, P, Matsuo, S, Matteoni, R, Mayer, A, Mazure, Nm, Mcconkey, Dj, Mcconnell, Mj, Mcdermott, C, Mcdonald, C, Mcinerney, Gm, Mckenna, Sl, Mclaughlin, B, Mclean, Pj, Mcmaster, Cr, Mcquibban, Ga, Meijer, Aj, Meisler, Mh, Meléndez, A, Melia, Tj, Melino, G, Mena, Ma, Menendez, Ja, Menna Barreto RF, Menon, Mb, Menzies, Fm, Mercer, Ca, Merighi, A, Merry, De, Meschini, S, Meyer, Cg, Meyer, Tf, Miao, Cy, Miao, Jy, Michels, Pa, Michiels, C, Mijaljica, D, Milojkovic, A, Minucci, S, Miracco, C, Miranti, Ck, Mitroulis, I, Miyazawa, K, Mizushima, N, Mograbi, B, Mohseni, S, Molero, X, Mollereau, B, Mollinedo, F, Momoi, T, Monastyrska, I, Monick, Mm, Monteiro, Mj, Moore, Mn, Mora, R, Moreau, K, Moreira, Pi, Moriyasu, Y, Moscat, J, Mostowy, S, Mottram, Jc, Motyl, T, Moussa, Ce, Müller, S, Muller, S, Münger, K, Münz, C, Murphy, Lo, Murphy, Me, Musarò, A, Mysorekar, I, Nagata, E, Nagata, K, Nahimana, A, Nair, U, Nakagawa, T, Nakahira, K, Nakano, H, Nakatogawa, H, Nanjundan, M, Naqvi, Ni, Narendra, Dp, Narita, M, Navarro, M, Nawrocki, St, Nazarko, Ty, Nemchenko, A, Netea, Mg, Neufeld, Tp, Ney, Pa, Nezis, Ip, Nguyen, Hp, Nie, D, Nishino, I, Nislow, C, Nixon, Ra, Noda, T, Noegel, Aa, Nogalska, A, Noguchi, S, Notterpek, L, Novak, I, Nozaki, T, Nukina, N, Nürnberger, T, Nyfeler, B, Obara, K, Oberley, Td, Oddo, S, Ogawa, M, Ohashi, T, Okamoto, K, Oleinick, Nl, Oliver, Fj, Olsen, Lj, Olsson, S, Opota, O, Osborne, Tf, Ostrander, Gk, Otsu, K, Ou, Jh, Ouimet, M, Overholtzer, M, Ozpolat, B, Paganetti, P, Pagnini, U, Pallet, N, Palmer, Ge, Palumbo, C, Pan, T, Panaretakis, T, Pandey, Ub, Papackova, Z, Papassideri, I, Paris, I, Park, J, Park, Ok, Parys, Jb, Parzych, Kr, Patschan, S, Patterson, C, Pattingre, S, Pawelek, Jm, Peng, J, Perlmutter, Dh, Perrotta, I, Perry, G, Pervaiz, S, Peter, M, Peters, Gj, Petersen, M, Petrovski, G, Phang, Jm, Piacentini, M, Pierre, P, Pierrefite Carle, V, Pierron, G, Pinkas Kramarski, R, Piras, A, Piri, N, Platanias, Lc, Pöggeler, S, Poirot, M, Poletti, A, Poüs, C, Pozuelo Rubio, M, Prætorius Ibba, M, Prasad, A, Prescott, M, Priault, M, Produit Zengaffinen, N, Progulske Fox, A, Proikas Cezanne, T, Przedborski, S, Przyklenk, K, Puertollano, R, Puyal, J, Qian, Sb, Qin, L, Qin, Zh, Quaggin, Se, Raben, N, Rabinowich, H, Rabkin, Sw, Rahman, I, Rami, A, Ramm, G, Randall, G, Randow, F, Rao, Va, Rathmell, Jc, Ravikumar, B, Ray, Sk, Reed, Bh, Reed, Jc, Reggiori, F, Régnier Vigouroux, A, Reichert, As, Reiners JJ Jr, Reiter, Rj, Ren, J, Revuelta, Jl, Rhodes, Cj, Ritis, K, Rizzo, E, Robbins, J, Roberge, M, Roca, H, Roccheri, Mc, Rocchi, S, Rodemann, Hp, Rodríguez de Córdoba, S, Rohrer, B, Roninson, Ib, Rosen, K, Rost Roszkowska MM, Rouis, M, Rouschop, Km, Rovetta, F, Rubin, Bp, Rubinsztein, Dc, Ruckdeschel, K, Rucker EB 3rd, Rudich, A, Rudolf, E, Ruiz Opazo, N, Russo, R, Rusten, Te, Ryan, Km, Ryter, Sw, Sabatini, Dm, Sadoshima, J, Saha, T, Saitoh, T, Sakagami, H, Sakai, Y, Salekdeh, Gh, Salomoni, P, Salvaterra, Pm, Salvesen, G, Salvioli, R, Sanchez, Am, Sánchez Alcázar JA, Sánchez Prieto, R, Sandri, M, Sankar, U, Sansanwal, P, Santambrogio, L, Saran, S, Sarkar, S, Sarwal, M, Sasakawa, C, Sasnauskiene, A, Sass, M, Sato, K, Sato, M, Schapira, Ah, Scharl, M, Schätzl, Hm, Scheper, W, Schiaffino, S, Schneider, C, Schneider, Me, Schneider Stock, R, Schoenlein, Pv, Schorderet, Df, Schüller, C, Schwartz, Gk, Scorrano, L, Sealy, L, Seglen, Po, Segura Aguilar, J, Seiliez, I, Seleverstov, O, Sell, C, Seo, Jb, Separovic, D, Setaluri, V, Setoguchi, T, Settembre, C, Shacka, Jj, Shanmugam, M, Shapiro, Im, Shaulian, E, Shaw, Rj, Shelhamer, Jh, Shen, Hm, Shen, Wc, Sheng, Zh, Shi, Y, Shibuya, K, Shidoji, Y, Shieh, Jj, Shih, Cm, Shimada, Y, Shimizu, S, Shintani, T, Shirihai, Os, Shore, Gc, Sibirny, Aa, Sidhu, Sb, Sikorska, B, Silva Zacarin EC, Simmons, A, Simon, Ak, Simon, Hu, Simone, C, Simonsen, A, Sinclair, Da, Singh, R, Sinha, D, Sinicrope, Fa, Sirko, A, Siu, Pm, Sivridis, E, Skop, V, Skulachev, Vp, Slack, Rs, Smaili, Ss, Smith, Dr, Soengas, Ms, Soldati, T, Song, X, Sood, Ak, Soong, Tw, Sotgia, F, Spector, Sa, Spies, Cd, Springer, W, Srinivasula, Sm, Stefanis, L, Steffan, Js, Stendel, R, Stenmark, H, Stephanou, A, Stern, St, Sternberg, C, Stork, B, Strålfors, P, Subauste, Cs, Sui, X, Sulzer, D, Sun, J, Sun, Sy, Sun, Zj, Sung, Jj, Suzuki, K, Suzuki, T, Swanson, Ms, Swanton, C, Sweeney, St, Sy, Lk, Szabadkai, G, Tabas, I, Taegtmeyer, H, Tafani, M, Takács Vellai, K, Takano, Y, Takegawa, K, Takemura, G, Takeshita, F, Talbot, Nj, Tan, Ks, Tanaka, K, Tang, D, Tanida, I, Tannous, Ba, Tavernarakis, N, Taylor, Gs, Taylor, Ga, Taylor, Jp, Terada, Ls, Terman, A, Tettamanti, G, Thevissen, K, Thompson, Cb, Thorburn, A, Thumm, M, Tian, F, Tian, Y, Tocchini Valentini, G, Tolkovsky, Am, Tomino, Y, Tönges, L, Tooze, Sa, Tournier, C, Tower, J, Towns, R, Trajkovic, V, Travassos, Lh, Tsai, Tf, Tschan, Mp, Tsubata, T, Tsung, A, Turk, B, Turner, Ls, Tyagi, Sc, Uchiyama, Y, Ueno, T, Umekawa, M, Umemiya, Shira, T., Aaltonen, B. A., Gonzalez, S., Amerio, D., Amidei, A., Anastassov, A., Annovi, J., Anto, G., Apollinari, J. A., Appel, T., Arisawa, A., Artikov, J., Asaadi, W., Ashmanska, B., Auerbach, A., Aurisano, F., Azfar, W., Badgett, T., Bae, A., Barbaro Galtieri, V. E., Barne, B. A., Barnett, P., Barria, P., Barto, M., Bauce, F., Bedeschi, S., Behari, G., Bellettini, J., Bellinger, D., Benjamin, A., Beretva, A., Bhatti, D., Bisello, I., Bizjak, K. R., Bland, B., Blumenfeld, A., Bocci, A., Bodek, D., Bortoletto, J., Boudreau, A., Boveia, L., Brigliadori, C., Bromberg, E., Brucken, J., Budagov, H. S., Budd, K., Burkett, G., Busetto, P., Bussey, A., Buzatu, A., Calamba, C., Calancha, S., Camarda, M., Campanelli, M., Campbell, F., Canelli, B., Carl, D., Carlsmith, R., Carosi, S., Carrillo, S., Carron, B., Casal, M., Casarsa, A., Castro, P., Catastini, D., Cauz, V., Cavaliere, M., Cavalli Sforza, A., Cerri, L., Cerrito, Y. C., Chen, M., Chertok, G., Chiarelli, G., Chlachidze, F., Chlebana, K., Cho, D., Chokheli, W. H., Chung, Y. S., Chung, M. A., Ciocci, A., Clark, C., Clarke, G., Compostella, M. E., Convery, J., Conway, M., Corbo, M., Cordelli, C. A., Cox, D. J., Cox, F., Crescioli, J., Cueva, R., Culbertson, D., Dagenhart, N., D'Ascenzo, M., Datta, P. D., Barbaro, M., Dell'Orso, L., Demortier, M., Deninno, F., Devoto, M., D'Errico, A. D., Canto, B. D., Ruzza, J. R., Dittmann, M., D'Onofrio, S., Donati, P., Dong, M., Dorigo, T., Dorigo, K., Ebina, A., Elagin, A., Eppig, R., Erbacher, S., Errede, N., Ershaidat, R., Eusebi, S., Farrington, M., Feindt, J. P., Fernandez, R., Field, G., Flanagan, R., Forrest, M. J., Frank, M., Franklin, J. C., Freeman, Y., Funakoshi, I., Furic, M., Gallinaro, J. E., Garcia, A. F., Garfinkel, P., Garosi, H., Gerberich, E., Gerchtein, S., Giagu, V., Giakoumopoulou, P., Giannetti, K., Gibson, C. M., Ginsburg, N., Giokari, P., Giromini, G., Giurgiu, V., Glagolev, D., Glenzinski, M., Gold, D., Goldin, N., Goldschmidt, A., Golossanov, G., Gomez, G., Gomez Ceballo, M., Goncharov, O., Gonzalez, I., Gorelov, A. T., Goshaw, K., Gouliano, L., Grillo, S., Grinstein, C., Grosso Pilcher, R. C., Group, J. G., Da, S. R., Hahn, E., Halkiadaki, A., Hamaguchi, J. Y., Han, F., Happacher, K., Hara, D., Hare, M., Hare, R. F., Harr, K., Hatakeyama, C., Hay, M., Heck, J., Heinrich, M., Herndon, S., Hewamanage, A., Hocker, W., Hopkin, D., Horn, S., Hou, R. E., Hughe, M., Hurwitz, U., Husemann, N., Hussain, M., Hussein, J., Huston, G., Introzzi, M., Iori, A., Ivanov, E., Jame, D., Jang, B., Jayatilaka, E. J., Jeon, S., Jindariani, M., Jone, K. K., Joo, S. Y., Jun, T. R., Junk, T., Kamon, P. E., Karchin, A., Kasmi, Y., Kato, W., Ketchum, J., Keung, V., Khotilovich, B., Kilminster, D. H., Kim, H. S., Kim, J. E., Kim, M. J., Kim, S. B., Kim, S. H., Kim, Y. K., Kim, Y. J., Kim, N., Kimura, M., Kirby, S., Klimenko, K., Knoepfel, K., Kondo, D. J., Kong, J., Konigsberg, A. V., Kotwal, M., Krep, J., Kroll, D., Krop, M., Kruse, V., Krutelyov, T., Kuhr, M., Kurata, S., Kwang, A. T., Laasanen, S., Lami, S., Lammel, M., Lancaster, R. L., Lander, K., Lannon, A., Lath, G., Latino, T., Lecompte, E., Lee, H. S., Lee, J. S., Lee, S. W., Lee, S., Leo, S., Leone, J. D., Lewi, A., Limosani, C. J., Lin, M., Lindgren, E., Lipele, A., Lister, D. O., Litvintsev, C., Liu, H., Liu, Q., Liu, T., Liu, S., Lockwitz, A., Loginov, D., Lucchesi, J., Lueck, P., Lujan, P., Luken, G., Lungu, J., Ly, R., Lysak, R., Madrak, K., Maeshima, P., Maestro, S., Malik, G., Manca, A., Manousakis Katsikaki, F., Margaroli, C., Marino, M., Martinez, P., Mastrandrea, K., Matera, M. E., Mattson, A., Mazzacane, P., Mazzanti, K. S., Mcfarland, P., Mcintyre, R., Mcnulty, A., Mehta, P., Mehtala, C., Mesropian, T., Miao, D., Mietlicki, A., Mitra, H., Miyake, S., Moed, N., Moggi, M. N., Mondragon, C. S., Moon, R., Moore, Morello, MICHAEL JOSEPH, J., Morlock, P. M., Fernandez, A., Mukherjee, T., Muller, P., Murat, M., Mussini, J., Nachtman, Y., Nagai, J., Naganoma, I., Nakano, A., Napier, J., Nett, C., Neu, M. S., Neubauer, J., Nielsen, L., Nodulman, S. Y., Noh, O., Norniella, L., Oake, S. H., Oh, Y. D., Oh, I., Oksuzian, T., Okusawa, R., Orava, L., Ortolan, S. P., Griso, C., Pagliarone, E., Palencia, V., Papadimitriou, A. A., Paramonov, J., Patrick, G., Pauletta, M., Paulini, C., Pau, D. E., Pellett, A., Penzo, T. J., Phillip, G., Piacentino, E., Pianori, J., Pilot, K., Pitt, C., Plager, L., Pondrom, S., Poprocki, K., Potamiano, F., Prokoshin, A., Pranko, F., Ptoho, G., Punzi, A., Rahaman, V., Ramakrishnan, N., Ranjan, I., Redondo, P., Renton, M., Rescigno, T., Riddick, F., Rimondi, L., Ristori, A., Robson, T., Rodrigo, T., Rodriguez, E., Roger, S., Rolli, R., Roser, F., Ruffini, A., Ruiz, J., Ru, V., Rusu, A., Safonov, W. K., Sakumoto, Y., Sakurai, L., Santi, K., Sato, V., Saveliev, A., Savoy Navarro, P., Schlabach, A., Schmidt, E. E., Schmidt, T., Schwarz, L., Scodellaro, A., Scribano, F., Scuri, S., Seidel, Y., Seiya, A., Semenov, F., Sforza, S. Z., Shalhout, T., Shear, P. F., Shepard, M., Shimojima, M., Shochet, I., Shreyber Tecker, A., Simonenko, P., Sinervo, K., Sliwa, J. R., Smith, F. D., Snider, A., Soha, V., Sorin, H., Song, P., Squillacioti, M., Stancari, R. S., Deni, B., Stelzer, O., Stelzer Chilton, D., Stentz, J., Strologa, G. L., Strycker, Y., Sudo, A., Sukhanov, I., Suslov, K., Takemasa, Y., Takeuchi, J., Tang, M., Tecchio, P. K., Teng, J., Thom, J., Thome, G. A., Thompson, E., Thomson, D., Toback, S., Tokar, K., Tollefson, T., Tomura, D., Tonelli, S., Torre, D., Torretta, P., Totaro, M., Trovato, F., Ukegawa, S., Uozumi, A., Varganov, F., Vazquez, G., Velev, C., Vellidi, M., Vidal, I., Vila, R., Vilar, J., Vizan, M., Vogel, G., Volpi, P., Wagner, R. L., Wagner, T., Wakisaka, R., Wallny, S. M., Wang, A., Warburton, D., Water, W. C., Wester, D., Whiteson, A. B., Wicklund, E., Wicklund, S., Wilbur, F., Wick, H. H., William, J. S., Wilson, P., Wilson, B. L., Winer, P., Wittich, S., Wolber, H., Wolfe, T., Wright, X., Wu, Z., Wu, K., Yamamoto, D., Yamato, T., Yang, U. K., Yang, Y. C., Yang, W. M., Yao, G. P., Yeh, K., Yi, J., Yoh, K., Yorita, T., Yoshida, G. B., Yu, I., Yu, S. S., Yu, J. C., Yun, A., Zanetti, Y., Zeng, C., Zhou, S., Zucchelli, B. c., Alvarez, A. c., Anastassov, J. c., Anto, J., Appel, T. c., Ct, V., Barne, B., Barnett, P. a., Barria, P. c., Barto, M. a., Bauce, G. a., Bellettini, D. a., Bisello, K., Bland, L. g., Brigliadori, H., Budd, G. a., Busetto, A. b., Cx, F. p., Canelli, S. b., Carrillo, B. b., Casal, A. g., Castro, A. b., Cerri, L. c., Cerrito, Y., Chen, K. c., Ct, W., Chung, Y., Chung, M. a., Ciocci, G. a., Compostella, M., Convery, C., Cox, D., Cox, F. a., Crescioli, J. c., Cueva, N. c., D'Ascenzo, M. a., Dell'Orso, M. a., D'Errico, A. a., Di, J., Dittmann, S. a., Donati, Dorigo, Mirco, N. c., Ershaidat, J., Fernandez, G. c., Flanagan, M., Frank, J., Freeman, J., Garcia, A., Garfinkel, P. a., Garosi, C., Ginsburg, O., González, A., Goshaw, R. b., Group, S., Hahn, J., Han, R., Harr, W. b., Hopkin, R., Hughe, N. b., Cx, M. b., Iori, A. c., Ivanov, E. c., Ct, S., Jun, T., Junk, T. b., C, P., Karchin, Y. c., Kato, D. c., Ct, H. c., Ct, J. c., Ct, M., Kim, S. c., Ct, S., Kim, Y., Kim, Y. c., Ct, A., Kotwal, V. b., Krutelyov, A., Laasanen, R., Lander, K. c., Lannon, G. a., Latino, H. c., Lee, S. c., Lee, S. a., Leo, J., Lewi, A. c., Limosani, C., Lin, D., Litvintsev, D. a., Lucchesi, R. b., Cr, P. a., Maestro, G. b., Manca, M., Martínez, M., Mattson, K., Mcfarland, R. b., Mcnulty, M. b., Mondragon, C. c., Ct, M. a., Morello, M. g., Mussini, J. c., Nachtman, M., Neubauer, J. b., Nielsen, S., Oh, S. a., Pagan, E. b., Palencia, A., Paramonov, G. b., Pauletta, D., Pellett, T., Phillip, S. b., Poprocki, F. c., Prokoshin, F. b., Ptoho, G. a., Punzi, F. g., Rimondi, L. a., Ristori, S. b., Rolli, F. a., Ruffini, W., Sakumoto, L. b., Santi, V. c., Saveliev, A. c., Savoy Navarro, E., Schmidt, A. a., Scribano, F. a., Sforza, S., Shalhout, P., Shepard, M. c., Shimojima, P. b., Cx, J., Smith, F., Snider, P. a., Squillacioti, B. b., Cx, O. b., Cx, D. c., Stentz, G., Strycker, P., Teng, J. b., Thom, G., Thompson, S. c., Tokar, M. a., Trovato, F. b., Vázquez, J., Vizán, R., Wagner, S., Wang, W., Wester, D. b., Whiteson, A., Wicklund, H., William, J., Wilson, B., Winer, P. b., Wittich, U. c., Yang, W., Yao, G., Yeh, K. c., Yi, T. b., Yoshida, G., Yu, I. c., Ct, S., Yu, J., Yun, S. g., Zucchelli, T. Aaltonen, B. Álvarez González, S. Amerio, D. Amidei, A. Anastassov, A. Annovi, J. Anto, G. Apollinari, J. Appel, T. Arisawa, A. Artikov, J. Asaadi, W. Ashmanska, B. Auerbach, A. Aurisano, F. Azfar, W. Badgett, T. Bae, A. Barbaro-Galtieri, V. Barne, B. Barnett, P. Barria, P. Barto, M. Bauce, F. Bedeschi, S. Behari, G. Bellettini, J. Bellinger, D. Benjamin, A. Beretva, A. Bhatti, D. Bisello, I. Bizjak, K. Bland, B. Blumenfeld, A. Bocci, A. Bodek, D. Bortoletto, J. Boudreau, A. Boveia, L. Brigliadori, C. Bromberg, E. Brucken, J. Budagov, H. Budd, K. Burkett, G. Busetto, P. Bussey, A. Buzatu, A. Calamba, C. Calancha, S. Camarda, M. Campanelli, M. Campbell, F. Canelli, B. Carl, D. Carlsmith, R. Carosi, S. Carrillo, S. Carron, B. Casal, M. Casarsa, A. Castro, P. Catastini, D. Cauz, V. Cavaliere, M. Cavalli-Sforza, A. Cerri, L. Cerrito, Y. Chen, M. Chertok, G. Chiarelli, G. Chlachidze, F. Chlebana, K. Cho, D. Chokheli, W. Chung, Y. Chung, M. Ciocci, A. Clark, C. Clarke, G. Compostella, M. Convery, J. Conway, M. Corbo, M. Cordelli, C. Cox, D. Cox, F. Crescioli, J. Cueva, R. Culbertson, D. Dagenhart, N. d’Ascenzo, M. Datta, P. de Barbaro, M. Dell’Orso, L. Demortier, M. Deninno, F. Devoto, M. d’Errico, A. Di Canto, B. Di Ruzza, J. Dittmann, M. D’Onofrio, S. Donati, P. Dong, M. Dorigo, T. Dorigo, K. Ebina, A. Elagin, A. Eppig, R. Erbacher, S. Errede, N. Ershaidat, R. Eusebi, S. Farrington, M. Feindt, J. Fernandez, R. Field, G. Flanagan, R. Forrest, M. Frank, M. Franklin, J. Freeman, Y. Funakoshi, I. Furic, M. Gallinaro, J. Garcia, A. Garfinkel, P. Garosi, H. Gerberich, E. Gerchtein, S. Giagu, V. Giakoumopoulou, P. Giannetti, K. Gibson, C. Ginsburg, N. Giokari, P. Giromini, G. Giurgiu, V. Glagolev, D. Glenzinski, M. Gold, D. Goldin, N. Goldschmidt, A. Golossanov, G. Gomez, G. Gomez-Ceballo, M. Goncharov, O. González, I. Gorelov, A. Goshaw, K. Gouliano, L. Grillo, S. Grinstein, C. Grosso-Pilcher, R. Group, J. Guimaraes da Costa, S. Hahn, E. Halkiadaki, A. Hamaguchi, J. Han, F. Happacher, K. Hara, D. Hare, M. Hare, R. Harr, K. Hatakeyama, C. Hay, M. Heck, J. Heinrich, M. Herndon, S. Hewamanage, A. Hocker, W. Hopkin, D. Horn, S. Hou, R. Hughe, M. Hurwitz, U. Husemann, N. Hussain, M. Hussein, J. Huston, G. Introzzi, M. Iori, A. Ivanov, E. Jame, D. Jang, B. Jayatilaka, E. Jeon, S. Jindariani, M. Jone, K. Joo, S. Jun, T. Junk, T. Kamon, P. Karchin, A. Kasmi, Y. Kato, W. Ketchum, J. Keung, V. Khotilovich, B. Kilminster, D. Kim, H. Kim, J. Kim, M. Kim, S. Kim, Y. Kim, N. Kimura, M. Kirby, S. Klimenko, K. Knoepfel, K. Kondo, D. Kong, J. Konigsberg, A. Kotwal, M. Krep, J. Kroll, D. Krop, M. Kruse, V. Krutelyov, T. Kuhr, M. Kurata, S. Kwang, A. Laasanen, S. Lami, S. Lammel, M. Lancaster, R. Lander, K. Lannon, A. Lath, G. Latino, T. LeCompte, E. Lee, H. Lee, J. Lee, S. Lee, S. Leo, S. Leone, J. Lewi, A. Limosani, C.-J. Lin, M. Lindgren, E. Lipele, A. Lister, D. Litvintsev, C. Liu, H. Liu, Q. Liu, T. Liu, S. Lockwitz, A. Loginov, D. Lucchesi, J. Lueck, P. Lujan, P. Luken, G. Lungu, J. Ly, R. Lysak, R. Madrak, K. Maeshima, P. Maestro, S. Malik, G. Manca, A. Manousakis-Katsikaki, F. Margaroli, C. Marino, M. Martínez, P. Mastrandrea, K. Matera, M. Mattson, A. Mazzacane, P. Mazzanti, K. McFarland, P. McIntyre, R. McNulty, A. Mehta, P. Mehtala, C. Mesropian, T. Miao, D. Mietlicki, A. Mitra, H. Miyake, S. Moed, N. Moggi, M. Mondragon, C. Moon, R. Moore, M. Morello, J. Morlock, P. Movilla Fernandez, A. Mukherjee, Th. Muller, P. Murat, M. Mussini, J. Nachtman, Y. Nagai, J. Naganoma, I. Nakano, A. Napier, J. Nett, C. Neu, M. Neubauer, J. Nielsen, L. Nodulman, S. Noh, O. Norniella, L. Oake, S. Oh, Y. Oh, I. Oksuzian, T. Okusawa, R. Orava, L. Ortolan, S. Pagan Griso, C. Pagliarone, E. Palencia, V. Papadimitriou, A. Paramonov, J. Patrick, G. Pauletta, M. Paulini, C. Pau, D. Pellett, A. Penzo, T. Phillip, G. Piacentino, E. Pianori, J. Pilot, K. Pitt, C. Plager, L. Pondrom, S. Poprocki, K. Potamiano, F. Prokoshin, A. Pranko, F. Ptoho, G. Punzi, A. Rahaman, V. Ramakrishnan, N. Ranjan, I. Redondo, P. Renton, M. Rescigno, T. Riddick, F. Rimondi, L. Ristori, A. Robson, T. Rodrigo, T. Rodriguez, E. Roger, S. Rolli, R. Roser, F. Ruffini, A. Ruiz, J. Ru, V. Rusu, A. Safonov, W. Sakumoto, Y. Sakurai, L. Santi, K. Sato, V. Saveliev, A. Savoy-Navarro, P. Schlabach, A. Schmidt, E. Schmidt, T. Schwarz, L. Scodellaro, A. Scribano, F. Scuri, S. Seidel, Y. Seiya, A. Semenov, F. Sforza, S. Shalhout, T. Shear, P. Shepard, M. Shimojima, M. Shochet, I. Shreyber-Tecker, A. Simonenko, P. Sinervo, K. Sliwa, J. Smith, F. Snider, A. Soha, V. Sorin, H. Song, P. Squillacioti, M. Stancari, R. St. Deni, B. Stelzer, O. Stelzer-Chilton, D. Stentz, J. Strologa, G. Strycker, Y. Sudo, A. Sukhanov, I. Suslov, K. Takemasa, Y. Takeuchi, J. Tang, M. Tecchio, P. Teng, J. Thom, J. Thome, G. Thompson, E. Thomson, D. Toback, S. Tokar, K. Tollefson, T. Tomura, D. Tonelli, S. Torre, D. Torretta, P. Totaro, M. Trovato, F. Ukegawa, S. Uozumi, A. Varganov, F. Vázquez, G. Velev, C. Vellidi, M. Vidal, I. Vila, R. Vilar, J. Vizán, M. Vogel, G. Volpi, P. Wagner, R. Wagner, T. Wakisaka, R. Wallny, S. Wang, A. Warburton, D. Water, W. Wester, D. Whiteson, A. Wicklund, E. Wicklund, S. Wilbur, F. Wick, H. William, J. Wilson, P. Wilson, B. Winer, P. Wittich, S. Wolber, H. Wolfe, T. Wright, X. Wu, Z. Wu, K. Yamamoto, D. Yamato, T. Yang, U. Yang, Y. Yang, W.-M. Yao, G. Yeh, K. Yi, J. Yoh, K. Yorita, T. Yoshida, G. Yu, I. Yu, S. Yu, J. Yun, A. Zanetti, Y. Zeng, C. Zhou, S. Zucchelli, and Universidad de Cantabria
- Subjects
FERMILAB TEVATRON COLLIDER ,Particle physics ,CP-violating asymmetries ,Meson ,B physic ,General Physics and Astronomy ,FOS: Physical sciences ,B physics ,Angle distribution, Branching ratio, CDF experiments, CP violations, CP-violating asymmetries, Data sample, Fermilab Tevatron collider, Integrated luminosity, Longitudinal polarization, Vector meson ,Longitudinal polarization ,7. Clean energy ,01 natural sciences ,High Energy Physics - Experiment ,Vector meson ,Physics and Astronomy (all) ,High Energy Physics - Experiment (hep-ex) ,High Energy Physics - Phenomenology (hep-ph) ,Mixing (mathematics) ,Strange b mesons ,Phase (matter) ,0103 physical sciences ,STRANGE QUARK ,mixing ,Bottom-Strange Meson Mixing Phase ,proton antiproton collisions ,010306 general physics ,TEVATRON ,Nuclear Experiment ,BOTTOM QUARK ,Physics ,Integrated luminosity ,010308 nuclear & particles physics ,Branching ratio ,High Energy Physics - Phenomenology ,CDF experiments ,CP violations ,Full data ,Content (measure theory) ,Angle distribution ,CDF ,Production (computer science) ,High Energy Physics::Experiment ,Data sample - Abstract
We report a measurement of the bottom-strange meson mixing phase βs using the time evolution of Bs0→J/ψ(→μ+μ-)ϕ(→K+K-) decays in which the quark-flavor content of the bottom-strange meson is identified at production. This measurement uses the full data set of proton-antiproton collisions at s=1.96 TeV collected by the Collider Detector experiment at the Fermilab Tevatron, corresponding to 9.6 fb-1 of integrated luminosity. We report confidence regions in the two-dimensional space of βs and the Bs0 decay-width difference ΔΓs and measure βs∈[-π/2,-1.51]∪[-0.06,0.30]∪[1.26,π/2] at the 68% confidence level, in agreement with the standard model expectation. Assuming the standard model value of βs, we also determine ΔΓs=0.068±0.026(stat)±0.009(syst) ps-1 and the mean Bs0 lifetime τs=1.528±0.019(stat)±0.009(syst) ps, which are consistent and competitive with determinations by other experiments., This work was supported by the U.S. Department of Energy and National Science Foundation; the Italian Istituto Nazionale di Fisica Nucleare; the Ministry of Education, Culture, Sports, Science and Technology of Japan; the Natural Sciences and Engineering Research Council of Canada; the National Science Council of the Republic of China; the Swiss National Science Foundation; the A. P. Sloan Foundation; the Bundesministerium für Bildung und Forschung, Germany; the Korean World Class University Program, the National Research Foundation of Korea; the Science and Technology Facilities Council and the Royal Society, UK; the Russian Foundation for Basic Research; the Ministerio de Ciencia e Innovación, and Programa Consolider-Ingenio 2010, Spain; the Slovak R&D Agency; the Academy of Finland; and the Australian Research Council (ARC).
- Published
- 2012
4. Guidelines for the use and interpretation of assays for monitoring autophagy.
- Author
-
Klionsky, Dj, Abdalla, Fc, Abeliovich, H, Abraham, Rt, Acevedo-Arozena, A, Adeli, K, Agholme, L, Agnello, M, Agostinis, P, Aguirre-Ghiso, Ja, Ahn, Hj, Ait-Mohamed, O, Ait-Si-Ali, S, Akematsu, T, Akira, S, Al-Younes, Hm, Al-Zeer, Ma, Albert, Ml, Albin, Rl, Alegre-Abarrategui, J, Aleo, Mf, Alirezaei, M, Almasan, A, Almonte-Becerril, M, Amano, A, Amaravadi, R, Amarnath, S, Amer, Ao, Andrieu-Abadie, N, Anantharam, V, Ann, Dk, Anoopkumar-Dukie, S, Aoki, H, Apostolova, N, Arancia, G, Aris, Jp, Asanuma, K, Asare, Ny, Ashida, H, Askanas, V, Askew, D, Auberger, P, Baba, M, Backues, Sk, Baehrecke, Eh, Bahr, Ba, Bai, Xy, Bailly, Y, Baiocchi, R, Baldini, G, Balduini, W, Ballabio, A, Bamber, Ba, Bampton, Et, Bánhegyi, G, Bartholomew, Cr, Bassham, Dc, Bast RC, Jr, Batoko, H, Bay, Bh, Beau, I, Béchet, Dm, Begley, Tj, Behl, C, Behrends, C, Bekri, S, Bellaire, B, Bendall, Lj, Benetti, L, Berliocchi, L, Bernardi, H, Bernassola, F, Besteiro, S, Bhatia-Kissova, I, Bi, X, Biard-Piechaczyk, M, Blum, J, Boise, Lh, Bonaldo, P, Boone, Dl, Bornhauser, Bc, Bortoluci, Kr, Bossis, I, Bost, F, Bourquin, Jp, Boya, P, Boyer-Guittaut, M, Bozhkov, Pv, Brady, Nr, Brancolini, C, Brech, A, Brenman, Je, Brennand, A, Bresnick, Eh, Brest, P, Bridges, D, Bristol, Ml, Brookes, P, Brown, Ej, Brumell, Jh, Brunetti-Pierri, N, Brunk, Ut, Bulman, De, Bultman, Sj, Bultynck, G, Burbulla, Lf, Bursch, W, Butchar, Jp, Buzgariu, W, Bydlowski, Sp, Cadwell, K, Cahová, M, Cai, D, Cai, J, Cai, Q, Calabretta, B, Calvo-Garrido, J, Camougrand, N, Campanella, M, Campos-Salinas, J, Candi, E, Cao, L, Caplan, Ab, Carding, Sr, Cardoso, Sm, Carew, J, Carlin, Cr, Carmignac, V, Carneiro, La, Carra, S, Caruso, Ra, Casari, G, Casas, C, Castino, R, Cebollero, E, Cecconi, F, Celli, J, Chaachouay, H, Chae, Hj, Chai, Cy, Chan, Dc, Chan, Ey, Chang, Rc, Che, Cm, Chen, Cc, Chen, Gc, Chen, Gq, Chen, M, Chen, Q, Chen, S, Chen, W, Chen, X, Chen, Yg, Chen, Y, Chen, Yj, Chen, Z, Cheng, A, Cheng, Ch, Cheng, Y, Cheong, H, Cheong, Jh, Cherry, S, Chess-Williams, R, Cheung, Zh, Chevet, E, Chiang, Hl, Chiarelli, R, Chiba, T, Chin, L, Chiou, Sh, Chisari, Fv, Cho, Ch, Cho, Dh, Choi, Am, Choi, D, Choi, K, Choi, Me, Chouaib, S, Choubey, D, Choubey, V, Chu, Ct, Chuang, Th, Chueh, Sh, Chun, T, Chwae, Yj, Chye, Ml, Ciarcia, R, Ciriolo, Mr, Clague, Mj, Clark, R, Clarke, Pg, Clarke, R, Codogno, P, Coller, Ha, Colombo, Mi, Comincini, S, Condello, M, Condorelli, F, Cookson, Mr, Coombs, Gh, Coppens, I, Corbalan, R, Cossart, P, Costelli, P, Costes, S, Coto-Montes, A, Couve, E, Coxon, Fp, Cregg, Jm, Crespo, Jl, Cronjé, Mj, Cuervo, Am, Cullen, Jj, Czaja, Mj, D'Amelio, M, Darfeuille-Michaud, A, Davids, Lm, Davies, Fe, De Felici, M, de Groot, Jf, de Haan, Ca, De Martino, L, De Milito, A, De Tata, V, Debnath, J, Degterev, A, Dehay, B, Delbridge, Lm, Demarchi, F, Deng, Yz, Dengjel, J, Dent, P, Denton, D, Deretic, V, Desai, Sd, Devenish, Rj, Di Gioacchino, M, Di Paolo, G, Di Pietro, C, Díaz-Araya, G, Díaz-Laviada, I, Diaz-Meco, Mt, Diaz-Nido, J, Dikic, I, Dinesh-Kumar, Sp, Ding, Wx, Distelhorst, Cw, Diwan, A, Djavaheri-Mergny, M, Dokudovskaya, S, Dong, Z, Dorsey, Fc, Dosenko, V, Dowling, Jj, Doxsey, S, Dreux, M, Drew, Me, Duan, Q, Duchosal, Ma, Duff, K, Dugail, I, Durbeej, M, Duszenko, M, Edelstein, Cl, Edinger, Al, Egea, G, Eichinger, L, Eissa, Nt, Ekmekcioglu, S, El-Deiry, W, Elazar, Z, Elgendy, M, Ellerby, Lm, Eng, Ke, Engelbrecht, Am, Engelender, S, Erenpreisa, J, Escalante, R, Esclatine, A, Eskelinen, El, Espert, L, Espina, V, Fan, H, Fan, J, Fan, Qw, Fan, Z, Fang, S, Fang, Y, Fanto, M, Fanzani, A, Farkas, T, Farré, Jc, Faure, M, Fechheimer, M, Feng, Cg, Feng, J, Feng, Q, Feng, Y, Fésüs, L, Feuer, R, Figueiredo-Pereira, Me, Fimia, Gm, Fingar, Dc, Finkbeiner, S, Finkel, T, Finley, Kd, Fiorito, F, Fisher, Ea, Fisher, Pb, Flajolet, M, Florez-McClure, Ml, Florio, S, Fon, Ea, Fornai, F, Fortunato, F, Fotedar, R, Fowler, Dh, Fox, H, Franco, R, Frankel, Lb, Fransen, M, Fuentes, Jm, Fueyo, J, Fujii, J, Fujisaki, K, Fujita, E, Fukuda, M, Furukawa, Rh, Gaestel, M, Gailly, P, Gajewska, M, Galliot, B, Galy, V, Ganesh, S, Ganetzky, B, Ganley, Ig, Gao, Fb, Gao, Gf, Gao, J, Garcia, L, Garcia-Manero, G, Garcia-Marcos, M, Garmyn, M, Gartel, Al, Gatti, E, Gautel, M, Gawriluk, Tr, Gegg, Me, Geng, J, Germain, M, Gestwicki, Je, Gewirtz, Da, Ghavami, S, Ghosh, P, Giammarioli, Am, Giatromanolaki, An, Gibson, Sb, Gilkerson, Rw, Ginger, Ml, Ginsberg, Hn, Golab, J, Goligorsky, M, Golstein, P, Gomez-Manzano, C, Goncu, E, Gongora, C, Gonzalez, Cd, Gonzalez, R, González-Estévez, C, González-Polo, Ra, Gonzalez-Rey, E, Gorbunov, Nv, Gorski, S, Goruppi, S, Gottlieb, Ra, Gozuacik, D, Granato, Ge, Grant, Gd, Green, Kn, Gregorc, A, Gros, F, Grose, C, Grunt, Tw, Gual, P, Guan, Jl, Guan, Kl, Guichard, Sm, Gukovskaya, A, Gukovsky, I, Gunst, J, Gustafsson, Ab, Halayko, Aj, Hale, An, Halonen, Sk, Hamasaki, M, Han, F, Han, T, Hancock, Mk, Hansen, M, Harada, H, Harada, M, Hardt, Se, Harper, Jw, Harris, Al, Harris, J, Harris, Sd, Hashimoto, M, Haspel, Ja, Hayashi, S, Hazelhurst, La, He, C, He, Yw, Hébert, Mj, Heidenreich, Ka, Helfrich, Mh, Helgason, Gv, Henske, Ep, Herman, B, Herman, Pk, Hetz, C, Hilfiker, S, Hill, Ja, Hocking, Lj, Hofman, P, Hofmann, Tg, Höhfeld, J, Holyoake, Tl, Hong, Mh, Hood, Da, Hotamisligil, G, Houwerzijl, Ej, Høyer-Hansen, M, Hu, B, Hu, Ca, Hu, Hm, Hua, Y, Huang, C, Huang, J, Huang, S, Huang, Wp, Huber, Tb, Huh, Wk, Hung, Th, Hupp, Tr, Hur, Gm, Hurley, Jb, Hussain, Sn, Hussey, Pj, Hwang, Jj, Hwang, S, Ichihara, A, Ilkhanizadeh, S, Inoki, K, Into, T, Iovane, V, Iovanna, Jl, Ip, Ny, Isaka, Y, Ishida, H, Isidoro, C, Isobe, K, Iwasaki, A, Izquierdo, M, Izumi, Y, Jaakkola, Pm, Jäättelä, M, Jackson, Gr, Jackson, Wt, Janji, B, Jendrach, M, Jeon, Jh, Jeung, Eb, Jiang, H, Jiang, Jx, Jiang, M, Jiang, Q, Jiang, X, Jiménez, A, Jin, M, Jin, S, Joe, Co, Johansen, T, Johnson, De, Johnson, Gv, Jones, Nl, Joseph, B, Joseph, Sk, Joubert, Am, Juhász, G, Juillerat-Jeanneret, L, Jung, Ch, Jung, Yk, Kaarniranta, K, Kaasik, A, Kabuta, T, Kadowaki, M, Kagedal, K, Kamada, Y, Kaminskyy, Vo, Kampinga, Hh, Kanamori, H, Kang, C, Kang, Kb, Kang, Ki, Kang, R, Kang, Ya, Kanki, T, Kanneganti, Td, Kanno, H, Kanthasamy, Ag, Kanthasamy, A, Karantza, V, Kaushal, Gp, Kaushik, S, Kawazoe, Y, Ke, Py, Kehrl, Jh, Kelekar, A, Kerkhoff, C, Kessel, Dh, Khalil, H, Kiel, Ja, Kiger, Aa, Kihara, A, Kim, Dr, Kim, Dh, Kim, Ek, Kim, Hr, Kim, J, Kim, Jh, Kim, Jc, Kim, Jk, Kim, Pk, Kim, Sw, Kim, Y, Kimchi, A, Kimmelman, Ac, King, J, Kinsella, Tj, Kirkin, V, Kirshenbaum, La, Kitamoto, K, Kitazato, K, Klein, L, Klimecki, Wt, Klucken, J, Knecht, E, Ko, Bc, Koch, Jc, Koga, H, Koh, Jy, Koh, Yh, Koike, M, Komatsu, M, Kominami, E, Kong, Hj, Kong, Wj, Korolchuk, Vi, Kotake, Y, Koukourakis, Mi, Kouri Flores, Jb, Kovács, Al, Kraft, C, Krainc, D, Krämer, H, Kretz-Remy, C, Krichevsky, Am, Kroemer, G, Krüger, R, Krut, O, Ktistakis, Nt, Kuan, Cy, Kucharczyk, R, Kumar, A, Kumar, R, Kumar, S, Kundu, M, Kung, Hj, Kurz, T, Kwon, Hj, La Spada, Ar, Lafont, F, Lamark, T, Landry, J, Lane, Jd, Lapaquette, P, Laporte, Jf, László, L, Lavandero, S, Lavoie, Jn, Layfield, R, Lazo, Pa, Le, W, Le Cam, L, Ledbetter, Dj, Lee, Aj, Lee, Bw, Lee, Gm, Lee, J, Lee, Jh, Lee, M, Lee, Sh, Leeuwenburgh, C, Legembre, P, Legouis, R, Lehmann, M, Lei, Hy, Lei, Qy, Leib, Da, Leiro, J, Lemasters, Jj, Lemoine, A, Lesniak, M, Lev, D, Levenson, Vv, Levine, B, Levy, E, Li, F, Li, Jl, Li, L, Li, S, Li, W, Li, Xj, Li, Yb, Li, Yp, Liang, C, Liang, Q, Liao, Yf, Liberski, Pp, Lieberman, A, Lim, Hj, Lim, Kl, Lim, K, Lin, Cf, Lin, Fc, Lin, J, Lin, Jd, Lin, K, Lin, Ww, Lin, Wc, Lin, Yl, Linden, R, Lingor, P, Lippincott-Schwartz, J, Lisanti, Mp, Liton, Pb, Liu, B, Liu, Cf, Liu, K, Liu, L, Liu, Qa, Liu, W, Liu, Yc, Liu, Y, Lockshin, Ra, Lok, Cn, Lonial, S, Loos, B, Lopez-Berestein, G, López-Otín, C, Lossi, L, Lotze, Mt, Lőw, P, Lu, B, Lu, Z, Luciano, F, Lukacs, Nw, Lund, Ah, Lynch-Day, Ma, Ma, Y, Macian, F, Mackeigan, Jp, Macleod, Kf, Madeo, F, Maiuri, L, Maiuri, Mc, Malagoli, D, Malicdan, Mc, Malorni, W, Man, N, Mandelkow, Em, Manon, S, Manov, I, Mao, K, Mao, X, Mao, Z, Marambaud, P, Marazziti, D, Marcel, Yl, Marchbank, K, Marchetti, P, Marciniak, Sj, Marcondes, M, Mardi, M, Marfe, G, Mariño, G, Markaki, M, Marten, Mr, Martin, Sj, Martinand-Mari, C, Martinet, W, Martinez-Vicente, M, Masini, M, Matarrese, P, Matsuo, S, Matteoni, R, Mayer, A, Mazure, Nm, Mcconkey, Dj, Mcconnell, Mj, Mcdermott, C, Mcdonald, C, Mcinerney, Gm, Mckenna, Sl, Mclaughlin, B, Mclean, Pj, Mcmaster, Cr, Mcquibban, Ga, Meijer, Aj, Meisler, Mh, Meléndez, A, Melia, Tj, Melino, G, Mena, Ma, Menendez, Ja, Menna-Barreto, Rf, Menon, Mb, Menzies, Fm, Mercer, Ca, Merighi, A, Merry, De, Meschini, S, Meyer, Cg, Meyer, Tf, Miao, Cy, Miao, Jy, Michels, Pa, Michiels, C, Mijaljica, D, Milojkovic, A, Minucci, S, Miracco, C, Miranti, Ck, Mitroulis, I, Miyazawa, K, Mizushima, N, Mograbi, B, Mohseni, S, Molero, X, Mollereau, B, Mollinedo, F, Momoi, T, Monastyrska, I, Monick, Mm, Monteiro, Mj, Moore, Mn, Mora, R, Moreau, K, Moreira, Pi, Moriyasu, Y, Moscat, J, Mostowy, S, Mottram, Jc, Motyl, T, Moussa, Ce, Müller, S, Muller, S, Münger, K, Münz, C, Murphy, Lo, Murphy, Me, Musarò, A, Mysorekar, I, Nagata, E, Nagata, K, Nahimana, A, Nair, U, Nakagawa, T, Nakahira, K, Nakano, H, Nakatogawa, H, Nanjundan, M, Naqvi, Ni, Narendra, Dp, Narita, M, Navarro, M, Nawrocki, St, Nazarko, Ty, Nemchenko, A, Netea, Mg, Neufeld, Tp, Ney, Pa, Nezis, Ip, Nguyen, Hp, Nie, D, Nishino, I, Nislow, C, Nixon, Ra, Noda, T, Noegel, Aa, Nogalska, A, Noguchi, S, Notterpek, L, Novak, I, Nozaki, T, Nukina, N, Nürnberger, T, Nyfeler, B, Obara, K, Oberley, Td, Oddo, S, Ogawa, M, Ohashi, T, Okamoto, K, Oleinick, Nl, Oliver, Fj, Olsen, Lj, Olsson, S, Opota, O, Osborne, Tf, Ostrander, Gk, Otsu, K, Ou, Jh, Ouimet, M, Overholtzer, M, Ozpolat, B, Paganetti, P, Pagnini, U, Pallet, N, Palmer, Ge, Palumbo, C, Pan, T, Panaretakis, T, Pandey, Ub, Papackova, Z, Papassideri, I, Paris, I, Park, J, Park, Ok, Parys, Jb, Parzych, Kr, Patschan, S, Patterson, C, Pattingre, S, Pawelek, Jm, Peng, J, Perlmutter, Dh, Perrotta, I, Perry, G, Pervaiz, S, Peter, M, Peters, Gj, Petersen, M, Petrovski, G, Phang, Jm, Piacentini, M, Pierre, P, Pierrefite-Carle, V, Pierron, G, Pinkas-Kramarski, R, Piras, A, Piri, N, Platanias, Lc, Pöggeler, S, Poirot, M, Poletti, A, Poüs, C, Pozuelo-Rubio, M, Prætorius-Ibba, M, Prasad, A, Prescott, M, Priault, M, Produit-Zengaffinen, N, Progulske-Fox, A, Proikas-Cezanne, T, Przedborski, S, Przyklenk, K, Puertollano, R, Puyal, J, Qian, Sb, Qin, L, Qin, Zh, Quaggin, Se, Raben, N, Rabinowich, H, Rabkin, Sw, Rahman, I, Rami, A, Ramm, G, Randall, G, Randow, F, Rao, Va, Rathmell, Jc, Ravikumar, B, Ray, Sk, Reed, Bh, Reed, Jc, Reggiori, F, Régnier-Vigouroux, A, Reichert, A, Reiners JJ, Jr, Reiter, Rj, Ren, J, Revuelta, Jl, Rhodes, Cj, Ritis, K, Rizzo, E, Robbins, J, Roberge, M, Roca, H, Roccheri, Mc, Rocchi, S, Rodemann, Hp, Rodríguez de Córdoba, S, Rohrer, B, Roninson, Ib, Rosen, K, Rost-Roszkowska, Mm, Rouis, M, Rouschop, Km, Rovetta, F, Rubin, Bp, Rubinsztein, Dc, Ruckdeschel, K, Rucker EB, 3rd, Rudich, A, Rudolf, E, Ruiz-Opazo, N, Russo, R, Rusten, Te, Ryan, Km, Ryter, Sw, Sabatini, Dm, Sadoshima, J, Saha, T, Saitoh, T, Sakagami, H, Sakai, Y, Salekdeh, Gh, Salomoni, P, Salvaterra, Pm, Salvesen, G, Salvioli, R, Sanchez, Am, Sánchez-Alcázar, Ja, Sánchez-Prieto, R, Sandri, M, Sankar, U, Sansanwal, P, Santambrogio, L, Saran, S, Sarkar, S, Sarwal, M, Sasakawa, C, Sasnauskiene, A, Sass, M, Sato, K, Sato, M, Schapira, Ah, Scharl, M, Schätzl, Hm, Scheper, W, Schiaffino, S, Schneider, C, Schneider, Me, Schneider-Stock, R, Schoenlein, Pv, Schorderet, Df, Schüller, C, Schwartz, Gk, Scorrano, L, Sealy, L, Seglen, Po, Segura-Aguilar, J, Seiliez, I, Seleverstov, O, Sell, C, Seo, Jb, Separovic, D, Setaluri, V, Setoguchi, T, Settembre, C, Shacka, Jj, Shanmugam, M, Shapiro, Im, Shaulian, E, Shaw, Rj, Shelhamer, Jh, Shen, Hm, Shen, Wc, Sheng, Zh, Shi, Y, Shibuya, K, Shidoji, Y, Shieh, Jj, Shih, Cm, Shimada, Y, Shimizu, S, Shintani, T, Shirihai, O, Shore, Gc, Sibirny, Aa, Sidhu, Sb, Sikorska, B, Silva-Zacarin, Ec, Simmons, A, Simon, Ak, Simon, Hu, Simone, C, Simonsen, A, Sinclair, Da, Singh, R, Sinha, D, Sinicrope, Fa, Sirko, A, Siu, Pm, Sivridis, E, Skop, V, Skulachev, Vp, Slack, R, Smaili, S, Smith, Dr, Soengas, M, Soldati, T, Song, X, Sood, Ak, Soong, Tw, Sotgia, F, Spector, Sa, Spies, Cd, Springer, W, Srinivasula, Sm, Stefanis, L, Steffan, J, Stendel, R, Stenmark, H, Stephanou, A, Stern, St, Sternberg, C, Stork, B, Strålfors, P, Subauste, C, Sui, X, Sulzer, D, Sun, J, Sun, Sy, Sun, Zj, Sung, Jj, Suzuki, K, Suzuki, T, Swanson, M, Swanton, C, Sweeney, St, Sy, Lk, Szabadkai, G, Tabas, I, Taegtmeyer, H, Tafani, M, Takács-Vellai, K, Takano, Y, Takegawa, K, Takemura, G, Takeshita, F, Talbot, Nj, Tan, K, Tanaka, K, Tang, D, Tanida, I, Tannous, Ba, Tavernarakis, N, Taylor, G, Taylor, Ga, Taylor, Jp, Terada, L, Terman, A, Tettamanti, G, Thevissen, K, Thompson, Cb, Thorburn, A, Thumm, M, Tian, F, Tian, Y, Tocchini-Valentini, G, Tolkovsky, Am, Tomino, Y, Tönges, L, Tooze, Sa, Tournier, C, Tower, J, Towns, R, Trajkovic, V, Travassos, Lh, Tsai, Tf, Tschan, Mp, Tsubata, T, Tsung, A, Turk, B, Turner, L, Tyagi, Sc, Uchiyama, Y, Ueno, T, Umekawa, M, Umemiya-Shirafuji, R, Unni, Vk, Vaccaro, Mi, Valente, Em, Van den Berghe, G, van der Klei, Ij, van Doorn, W, van Dyk, Lf, van Egmond, M, van Grunsven, La, Vandenabeele, P, Vandenberghe, Wp, Vanhorebeek, I, Vaquero, Ec, Velasco, G, Vellai, T, Vicencio, Jm, Vierstra, Rd, Vila, M, Vindis, C, Viola, G, Viscomi, Maria Teresa, Voitsekhovskaja, Ov, von Haefen, C, Votruba, M, Wada, K, Wade-Martins, R, Walker, Cl, Walsh, Cm, Walter, J, Wan, Xb, Wang, A, Wang, C, Wang, D, Wang, F, Wang, G, Wang, H, Wang, Hg, Wang, Hd, Wang, J, Wang, K, Wang, M, Wang, Rc, Wang, X, Wang, Yj, Wang, Y, Wang, Z, Wang, Zc, Wansink, Dg, Ward, Dm, Watada, H, Waters, Sl, Webster, P, Wei, L, Weihl, Cc, Weiss, Wa, Welford, Sm, Wen, Lp, Whitehouse, Ca, Whitton, Jl, Whitworth, Aj, Wileman, T, Wiley, Jw, Wilkinson, S, Willbold, D, Williams, Rl, Williamson, Pr, Wouters, Bg, Wu, C, Wu, Dc, Wu, Wk, Wyttenbach, A, Xavier, Rj, Xi, Z, Xia, P, Xiao, G, Xie, Z, Xu, Dz, Xu, J, Xu, L, Xu, X, Yamamoto, A, Yamashina, S, Yamashita, M, Yan, X, Yanagida, M, Yang, D, Yang, E, Yang, Jm, Yang, Sy, Yang, W, Yang, Wy, Yang, Z, Yao, Mc, Yao, Tp, Yeganeh, B, Yen, Wl, Yin, Jj, Yin, Xm, Yoo, Oj, Yoon, G, Yoon, Sy, Yorimitsu, T, Yoshikawa, Y, Yoshimori, T, Yoshimoto, K, You, Hj, Youle, Rj, Younes, A, Yu, L, Yu, Sw, Yu, Wh, Yuan, Zm, Yue, Z, Yun, Ch, Yuzaki, M, Zabirnyk, O, Silva-Zacarin, E, Zacks, D, Zacksenhaus, E, Zaffaroni, N, Zakeri, Z, Zeh HJ, 3rd, Zeitlin, So, Zhang, H, Zhang, Hl, Zhang, J, Zhang, Jp, Zhang, L, Zhang, My, Zhang, Xd, Zhao, M, Zhao, Yf, Zhao, Y, Zhao, Zj, Zheng, X, Zhivotovsky, B, Zhong, Q, Zhou, Cz, Zhu, C, Zhu, Wg, Zhu, Xf, Zhu, X, Zhu, Y, Zoladek, T, Zong, Wx, Zorzano, A, Zschocke, J, Zuckerbraun, B., Viscomi M. T. (ORCID:0000-0002-9096-4967), Klionsky, Dj, Abdalla, Fc, Abeliovich, H, Abraham, Rt, Acevedo-Arozena, A, Adeli, K, Agholme, L, Agnello, M, Agostinis, P, Aguirre-Ghiso, Ja, Ahn, Hj, Ait-Mohamed, O, Ait-Si-Ali, S, Akematsu, T, Akira, S, Al-Younes, Hm, Al-Zeer, Ma, Albert, Ml, Albin, Rl, Alegre-Abarrategui, J, Aleo, Mf, Alirezaei, M, Almasan, A, Almonte-Becerril, M, Amano, A, Amaravadi, R, Amarnath, S, Amer, Ao, Andrieu-Abadie, N, Anantharam, V, Ann, Dk, Anoopkumar-Dukie, S, Aoki, H, Apostolova, N, Arancia, G, Aris, Jp, Asanuma, K, Asare, Ny, Ashida, H, Askanas, V, Askew, D, Auberger, P, Baba, M, Backues, Sk, Baehrecke, Eh, Bahr, Ba, Bai, Xy, Bailly, Y, Baiocchi, R, Baldini, G, Balduini, W, Ballabio, A, Bamber, Ba, Bampton, Et, Bánhegyi, G, Bartholomew, Cr, Bassham, Dc, Bast RC, Jr, Batoko, H, Bay, Bh, Beau, I, Béchet, Dm, Begley, Tj, Behl, C, Behrends, C, Bekri, S, Bellaire, B, Bendall, Lj, Benetti, L, Berliocchi, L, Bernardi, H, Bernassola, F, Besteiro, S, Bhatia-Kissova, I, Bi, X, Biard-Piechaczyk, M, Blum, J, Boise, Lh, Bonaldo, P, Boone, Dl, Bornhauser, Bc, Bortoluci, Kr, Bossis, I, Bost, F, Bourquin, Jp, Boya, P, Boyer-Guittaut, M, Bozhkov, Pv, Brady, Nr, Brancolini, C, Brech, A, Brenman, Je, Brennand, A, Bresnick, Eh, Brest, P, Bridges, D, Bristol, Ml, Brookes, P, Brown, Ej, Brumell, Jh, Brunetti-Pierri, N, Brunk, Ut, Bulman, De, Bultman, Sj, Bultynck, G, Burbulla, Lf, Bursch, W, Butchar, Jp, Buzgariu, W, Bydlowski, Sp, Cadwell, K, Cahová, M, Cai, D, Cai, J, Cai, Q, Calabretta, B, Calvo-Garrido, J, Camougrand, N, Campanella, M, Campos-Salinas, J, Candi, E, Cao, L, Caplan, Ab, Carding, Sr, Cardoso, Sm, Carew, J, Carlin, Cr, Carmignac, V, Carneiro, La, Carra, S, Caruso, Ra, Casari, G, Casas, C, Castino, R, Cebollero, E, Cecconi, F, Celli, J, Chaachouay, H, Chae, Hj, Chai, Cy, Chan, Dc, Chan, Ey, Chang, Rc, Che, Cm, Chen, Cc, Chen, Gc, Chen, Gq, Chen, M, Chen, Q, Chen, S, Chen, W, Chen, X, Chen, Yg, Chen, Y, Chen, Yj, Chen, Z, Cheng, A, Cheng, Ch, Cheng, Y, Cheong, H, Cheong, Jh, Cherry, S, Chess-Williams, R, Cheung, Zh, Chevet, E, Chiang, Hl, Chiarelli, R, Chiba, T, Chin, L, Chiou, Sh, Chisari, Fv, Cho, Ch, Cho, Dh, Choi, Am, Choi, D, Choi, K, Choi, Me, Chouaib, S, Choubey, D, Choubey, V, Chu, Ct, Chuang, Th, Chueh, Sh, Chun, T, Chwae, Yj, Chye, Ml, Ciarcia, R, Ciriolo, Mr, Clague, Mj, Clark, R, Clarke, Pg, Clarke, R, Codogno, P, Coller, Ha, Colombo, Mi, Comincini, S, Condello, M, Condorelli, F, Cookson, Mr, Coombs, Gh, Coppens, I, Corbalan, R, Cossart, P, Costelli, P, Costes, S, Coto-Montes, A, Couve, E, Coxon, Fp, Cregg, Jm, Crespo, Jl, Cronjé, Mj, Cuervo, Am, Cullen, Jj, Czaja, Mj, D'Amelio, M, Darfeuille-Michaud, A, Davids, Lm, Davies, Fe, De Felici, M, de Groot, Jf, de Haan, Ca, De Martino, L, De Milito, A, De Tata, V, Debnath, J, Degterev, A, Dehay, B, Delbridge, Lm, Demarchi, F, Deng, Yz, Dengjel, J, Dent, P, Denton, D, Deretic, V, Desai, Sd, Devenish, Rj, Di Gioacchino, M, Di Paolo, G, Di Pietro, C, Díaz-Araya, G, Díaz-Laviada, I, Diaz-Meco, Mt, Diaz-Nido, J, Dikic, I, Dinesh-Kumar, Sp, Ding, Wx, Distelhorst, Cw, Diwan, A, Djavaheri-Mergny, M, Dokudovskaya, S, Dong, Z, Dorsey, Fc, Dosenko, V, Dowling, Jj, Doxsey, S, Dreux, M, Drew, Me, Duan, Q, Duchosal, Ma, Duff, K, Dugail, I, Durbeej, M, Duszenko, M, Edelstein, Cl, Edinger, Al, Egea, G, Eichinger, L, Eissa, Nt, Ekmekcioglu, S, El-Deiry, W, Elazar, Z, Elgendy, M, Ellerby, Lm, Eng, Ke, Engelbrecht, Am, Engelender, S, Erenpreisa, J, Escalante, R, Esclatine, A, Eskelinen, El, Espert, L, Espina, V, Fan, H, Fan, J, Fan, Qw, Fan, Z, Fang, S, Fang, Y, Fanto, M, Fanzani, A, Farkas, T, Farré, Jc, Faure, M, Fechheimer, M, Feng, Cg, Feng, J, Feng, Q, Feng, Y, Fésüs, L, Feuer, R, Figueiredo-Pereira, Me, Fimia, Gm, Fingar, Dc, Finkbeiner, S, Finkel, T, Finley, Kd, Fiorito, F, Fisher, Ea, Fisher, Pb, Flajolet, M, Florez-McClure, Ml, Florio, S, Fon, Ea, Fornai, F, Fortunato, F, Fotedar, R, Fowler, Dh, Fox, H, Franco, R, Frankel, Lb, Fransen, M, Fuentes, Jm, Fueyo, J, Fujii, J, Fujisaki, K, Fujita, E, Fukuda, M, Furukawa, Rh, Gaestel, M, Gailly, P, Gajewska, M, Galliot, B, Galy, V, Ganesh, S, Ganetzky, B, Ganley, Ig, Gao, Fb, Gao, Gf, Gao, J, Garcia, L, Garcia-Manero, G, Garcia-Marcos, M, Garmyn, M, Gartel, Al, Gatti, E, Gautel, M, Gawriluk, Tr, Gegg, Me, Geng, J, Germain, M, Gestwicki, Je, Gewirtz, Da, Ghavami, S, Ghosh, P, Giammarioli, Am, Giatromanolaki, An, Gibson, Sb, Gilkerson, Rw, Ginger, Ml, Ginsberg, Hn, Golab, J, Goligorsky, M, Golstein, P, Gomez-Manzano, C, Goncu, E, Gongora, C, Gonzalez, Cd, Gonzalez, R, González-Estévez, C, González-Polo, Ra, Gonzalez-Rey, E, Gorbunov, Nv, Gorski, S, Goruppi, S, Gottlieb, Ra, Gozuacik, D, Granato, Ge, Grant, Gd, Green, Kn, Gregorc, A, Gros, F, Grose, C, Grunt, Tw, Gual, P, Guan, Jl, Guan, Kl, Guichard, Sm, Gukovskaya, A, Gukovsky, I, Gunst, J, Gustafsson, Ab, Halayko, Aj, Hale, An, Halonen, Sk, Hamasaki, M, Han, F, Han, T, Hancock, Mk, Hansen, M, Harada, H, Harada, M, Hardt, Se, Harper, Jw, Harris, Al, Harris, J, Harris, Sd, Hashimoto, M, Haspel, Ja, Hayashi, S, Hazelhurst, La, He, C, He, Yw, Hébert, Mj, Heidenreich, Ka, Helfrich, Mh, Helgason, Gv, Henske, Ep, Herman, B, Herman, Pk, Hetz, C, Hilfiker, S, Hill, Ja, Hocking, Lj, Hofman, P, Hofmann, Tg, Höhfeld, J, Holyoake, Tl, Hong, Mh, Hood, Da, Hotamisligil, G, Houwerzijl, Ej, Høyer-Hansen, M, Hu, B, Hu, Ca, Hu, Hm, Hua, Y, Huang, C, Huang, J, Huang, S, Huang, Wp, Huber, Tb, Huh, Wk, Hung, Th, Hupp, Tr, Hur, Gm, Hurley, Jb, Hussain, Sn, Hussey, Pj, Hwang, Jj, Hwang, S, Ichihara, A, Ilkhanizadeh, S, Inoki, K, Into, T, Iovane, V, Iovanna, Jl, Ip, Ny, Isaka, Y, Ishida, H, Isidoro, C, Isobe, K, Iwasaki, A, Izquierdo, M, Izumi, Y, Jaakkola, Pm, Jäättelä, M, Jackson, Gr, Jackson, Wt, Janji, B, Jendrach, M, Jeon, Jh, Jeung, Eb, Jiang, H, Jiang, Jx, Jiang, M, Jiang, Q, Jiang, X, Jiménez, A, Jin, M, Jin, S, Joe, Co, Johansen, T, Johnson, De, Johnson, Gv, Jones, Nl, Joseph, B, Joseph, Sk, Joubert, Am, Juhász, G, Juillerat-Jeanneret, L, Jung, Ch, Jung, Yk, Kaarniranta, K, Kaasik, A, Kabuta, T, Kadowaki, M, Kagedal, K, Kamada, Y, Kaminskyy, Vo, Kampinga, Hh, Kanamori, H, Kang, C, Kang, Kb, Kang, Ki, Kang, R, Kang, Ya, Kanki, T, Kanneganti, Td, Kanno, H, Kanthasamy, Ag, Kanthasamy, A, Karantza, V, Kaushal, Gp, Kaushik, S, Kawazoe, Y, Ke, Py, Kehrl, Jh, Kelekar, A, Kerkhoff, C, Kessel, Dh, Khalil, H, Kiel, Ja, Kiger, Aa, Kihara, A, Kim, Dr, Kim, Dh, Kim, Ek, Kim, Hr, Kim, J, Kim, Jh, Kim, Jc, Kim, Jk, Kim, Pk, Kim, Sw, Kim, Y, Kimchi, A, Kimmelman, Ac, King, J, Kinsella, Tj, Kirkin, V, Kirshenbaum, La, Kitamoto, K, Kitazato, K, Klein, L, Klimecki, Wt, Klucken, J, Knecht, E, Ko, Bc, Koch, Jc, Koga, H, Koh, Jy, Koh, Yh, Koike, M, Komatsu, M, Kominami, E, Kong, Hj, Kong, Wj, Korolchuk, Vi, Kotake, Y, Koukourakis, Mi, Kouri Flores, Jb, Kovács, Al, Kraft, C, Krainc, D, Krämer, H, Kretz-Remy, C, Krichevsky, Am, Kroemer, G, Krüger, R, Krut, O, Ktistakis, Nt, Kuan, Cy, Kucharczyk, R, Kumar, A, Kumar, R, Kumar, S, Kundu, M, Kung, Hj, Kurz, T, Kwon, Hj, La Spada, Ar, Lafont, F, Lamark, T, Landry, J, Lane, Jd, Lapaquette, P, Laporte, Jf, László, L, Lavandero, S, Lavoie, Jn, Layfield, R, Lazo, Pa, Le, W, Le Cam, L, Ledbetter, Dj, Lee, Aj, Lee, Bw, Lee, Gm, Lee, J, Lee, Jh, Lee, M, Lee, Sh, Leeuwenburgh, C, Legembre, P, Legouis, R, Lehmann, M, Lei, Hy, Lei, Qy, Leib, Da, Leiro, J, Lemasters, Jj, Lemoine, A, Lesniak, M, Lev, D, Levenson, Vv, Levine, B, Levy, E, Li, F, Li, Jl, Li, L, Li, S, Li, W, Li, Xj, Li, Yb, Li, Yp, Liang, C, Liang, Q, Liao, Yf, Liberski, Pp, Lieberman, A, Lim, Hj, Lim, Kl, Lim, K, Lin, Cf, Lin, Fc, Lin, J, Lin, Jd, Lin, K, Lin, Ww, Lin, Wc, Lin, Yl, Linden, R, Lingor, P, Lippincott-Schwartz, J, Lisanti, Mp, Liton, Pb, Liu, B, Liu, Cf, Liu, K, Liu, L, Liu, Qa, Liu, W, Liu, Yc, Liu, Y, Lockshin, Ra, Lok, Cn, Lonial, S, Loos, B, Lopez-Berestein, G, López-Otín, C, Lossi, L, Lotze, Mt, Lőw, P, Lu, B, Lu, Z, Luciano, F, Lukacs, Nw, Lund, Ah, Lynch-Day, Ma, Ma, Y, Macian, F, Mackeigan, Jp, Macleod, Kf, Madeo, F, Maiuri, L, Maiuri, Mc, Malagoli, D, Malicdan, Mc, Malorni, W, Man, N, Mandelkow, Em, Manon, S, Manov, I, Mao, K, Mao, X, Mao, Z, Marambaud, P, Marazziti, D, Marcel, Yl, Marchbank, K, Marchetti, P, Marciniak, Sj, Marcondes, M, Mardi, M, Marfe, G, Mariño, G, Markaki, M, Marten, Mr, Martin, Sj, Martinand-Mari, C, Martinet, W, Martinez-Vicente, M, Masini, M, Matarrese, P, Matsuo, S, Matteoni, R, Mayer, A, Mazure, Nm, Mcconkey, Dj, Mcconnell, Mj, Mcdermott, C, Mcdonald, C, Mcinerney, Gm, Mckenna, Sl, Mclaughlin, B, Mclean, Pj, Mcmaster, Cr, Mcquibban, Ga, Meijer, Aj, Meisler, Mh, Meléndez, A, Melia, Tj, Melino, G, Mena, Ma, Menendez, Ja, Menna-Barreto, Rf, Menon, Mb, Menzies, Fm, Mercer, Ca, Merighi, A, Merry, De, Meschini, S, Meyer, Cg, Meyer, Tf, Miao, Cy, Miao, Jy, Michels, Pa, Michiels, C, Mijaljica, D, Milojkovic, A, Minucci, S, Miracco, C, Miranti, Ck, Mitroulis, I, Miyazawa, K, Mizushima, N, Mograbi, B, Mohseni, S, Molero, X, Mollereau, B, Mollinedo, F, Momoi, T, Monastyrska, I, Monick, Mm, Monteiro, Mj, Moore, Mn, Mora, R, Moreau, K, Moreira, Pi, Moriyasu, Y, Moscat, J, Mostowy, S, Mottram, Jc, Motyl, T, Moussa, Ce, Müller, S, Muller, S, Münger, K, Münz, C, Murphy, Lo, Murphy, Me, Musarò, A, Mysorekar, I, Nagata, E, Nagata, K, Nahimana, A, Nair, U, Nakagawa, T, Nakahira, K, Nakano, H, Nakatogawa, H, Nanjundan, M, Naqvi, Ni, Narendra, Dp, Narita, M, Navarro, M, Nawrocki, St, Nazarko, Ty, Nemchenko, A, Netea, Mg, Neufeld, Tp, Ney, Pa, Nezis, Ip, Nguyen, Hp, Nie, D, Nishino, I, Nislow, C, Nixon, Ra, Noda, T, Noegel, Aa, Nogalska, A, Noguchi, S, Notterpek, L, Novak, I, Nozaki, T, Nukina, N, Nürnberger, T, Nyfeler, B, Obara, K, Oberley, Td, Oddo, S, Ogawa, M, Ohashi, T, Okamoto, K, Oleinick, Nl, Oliver, Fj, Olsen, Lj, Olsson, S, Opota, O, Osborne, Tf, Ostrander, Gk, Otsu, K, Ou, Jh, Ouimet, M, Overholtzer, M, Ozpolat, B, Paganetti, P, Pagnini, U, Pallet, N, Palmer, Ge, Palumbo, C, Pan, T, Panaretakis, T, Pandey, Ub, Papackova, Z, Papassideri, I, Paris, I, Park, J, Park, Ok, Parys, Jb, Parzych, Kr, Patschan, S, Patterson, C, Pattingre, S, Pawelek, Jm, Peng, J, Perlmutter, Dh, Perrotta, I, Perry, G, Pervaiz, S, Peter, M, Peters, Gj, Petersen, M, Petrovski, G, Phang, Jm, Piacentini, M, Pierre, P, Pierrefite-Carle, V, Pierron, G, Pinkas-Kramarski, R, Piras, A, Piri, N, Platanias, Lc, Pöggeler, S, Poirot, M, Poletti, A, Poüs, C, Pozuelo-Rubio, M, Prætorius-Ibba, M, Prasad, A, Prescott, M, Priault, M, Produit-Zengaffinen, N, Progulske-Fox, A, Proikas-Cezanne, T, Przedborski, S, Przyklenk, K, Puertollano, R, Puyal, J, Qian, Sb, Qin, L, Qin, Zh, Quaggin, Se, Raben, N, Rabinowich, H, Rabkin, Sw, Rahman, I, Rami, A, Ramm, G, Randall, G, Randow, F, Rao, Va, Rathmell, Jc, Ravikumar, B, Ray, Sk, Reed, Bh, Reed, Jc, Reggiori, F, Régnier-Vigouroux, A, Reichert, A, Reiners JJ, Jr, Reiter, Rj, Ren, J, Revuelta, Jl, Rhodes, Cj, Ritis, K, Rizzo, E, Robbins, J, Roberge, M, Roca, H, Roccheri, Mc, Rocchi, S, Rodemann, Hp, Rodríguez de Córdoba, S, Rohrer, B, Roninson, Ib, Rosen, K, Rost-Roszkowska, Mm, Rouis, M, Rouschop, Km, Rovetta, F, Rubin, Bp, Rubinsztein, Dc, Ruckdeschel, K, Rucker EB, 3rd, Rudich, A, Rudolf, E, Ruiz-Opazo, N, Russo, R, Rusten, Te, Ryan, Km, Ryter, Sw, Sabatini, Dm, Sadoshima, J, Saha, T, Saitoh, T, Sakagami, H, Sakai, Y, Salekdeh, Gh, Salomoni, P, Salvaterra, Pm, Salvesen, G, Salvioli, R, Sanchez, Am, Sánchez-Alcázar, Ja, Sánchez-Prieto, R, Sandri, M, Sankar, U, Sansanwal, P, Santambrogio, L, Saran, S, Sarkar, S, Sarwal, M, Sasakawa, C, Sasnauskiene, A, Sass, M, Sato, K, Sato, M, Schapira, Ah, Scharl, M, Schätzl, Hm, Scheper, W, Schiaffino, S, Schneider, C, Schneider, Me, Schneider-Stock, R, Schoenlein, Pv, Schorderet, Df, Schüller, C, Schwartz, Gk, Scorrano, L, Sealy, L, Seglen, Po, Segura-Aguilar, J, Seiliez, I, Seleverstov, O, Sell, C, Seo, Jb, Separovic, D, Setaluri, V, Setoguchi, T, Settembre, C, Shacka, Jj, Shanmugam, M, Shapiro, Im, Shaulian, E, Shaw, Rj, Shelhamer, Jh, Shen, Hm, Shen, Wc, Sheng, Zh, Shi, Y, Shibuya, K, Shidoji, Y, Shieh, Jj, Shih, Cm, Shimada, Y, Shimizu, S, Shintani, T, Shirihai, O, Shore, Gc, Sibirny, Aa, Sidhu, Sb, Sikorska, B, Silva-Zacarin, Ec, Simmons, A, Simon, Ak, Simon, Hu, Simone, C, Simonsen, A, Sinclair, Da, Singh, R, Sinha, D, Sinicrope, Fa, Sirko, A, Siu, Pm, Sivridis, E, Skop, V, Skulachev, Vp, Slack, R, Smaili, S, Smith, Dr, Soengas, M, Soldati, T, Song, X, Sood, Ak, Soong, Tw, Sotgia, F, Spector, Sa, Spies, Cd, Springer, W, Srinivasula, Sm, Stefanis, L, Steffan, J, Stendel, R, Stenmark, H, Stephanou, A, Stern, St, Sternberg, C, Stork, B, Strålfors, P, Subauste, C, Sui, X, Sulzer, D, Sun, J, Sun, Sy, Sun, Zj, Sung, Jj, Suzuki, K, Suzuki, T, Swanson, M, Swanton, C, Sweeney, St, Sy, Lk, Szabadkai, G, Tabas, I, Taegtmeyer, H, Tafani, M, Takács-Vellai, K, Takano, Y, Takegawa, K, Takemura, G, Takeshita, F, Talbot, Nj, Tan, K, Tanaka, K, Tang, D, Tanida, I, Tannous, Ba, Tavernarakis, N, Taylor, G, Taylor, Ga, Taylor, Jp, Terada, L, Terman, A, Tettamanti, G, Thevissen, K, Thompson, Cb, Thorburn, A, Thumm, M, Tian, F, Tian, Y, Tocchini-Valentini, G, Tolkovsky, Am, Tomino, Y, Tönges, L, Tooze, Sa, Tournier, C, Tower, J, Towns, R, Trajkovic, V, Travassos, Lh, Tsai, Tf, Tschan, Mp, Tsubata, T, Tsung, A, Turk, B, Turner, L, Tyagi, Sc, Uchiyama, Y, Ueno, T, Umekawa, M, Umemiya-Shirafuji, R, Unni, Vk, Vaccaro, Mi, Valente, Em, Van den Berghe, G, van der Klei, Ij, van Doorn, W, van Dyk, Lf, van Egmond, M, van Grunsven, La, Vandenabeele, P, Vandenberghe, Wp, Vanhorebeek, I, Vaquero, Ec, Velasco, G, Vellai, T, Vicencio, Jm, Vierstra, Rd, Vila, M, Vindis, C, Viola, G, Viscomi, Maria Teresa, Voitsekhovskaja, Ov, von Haefen, C, Votruba, M, Wada, K, Wade-Martins, R, Walker, Cl, Walsh, Cm, Walter, J, Wan, Xb, Wang, A, Wang, C, Wang, D, Wang, F, Wang, G, Wang, H, Wang, Hg, Wang, Hd, Wang, J, Wang, K, Wang, M, Wang, Rc, Wang, X, Wang, Yj, Wang, Y, Wang, Z, Wang, Zc, Wansink, Dg, Ward, Dm, Watada, H, Waters, Sl, Webster, P, Wei, L, Weihl, Cc, Weiss, Wa, Welford, Sm, Wen, Lp, Whitehouse, Ca, Whitton, Jl, Whitworth, Aj, Wileman, T, Wiley, Jw, Wilkinson, S, Willbold, D, Williams, Rl, Williamson, Pr, Wouters, Bg, Wu, C, Wu, Dc, Wu, Wk, Wyttenbach, A, Xavier, Rj, Xi, Z, Xia, P, Xiao, G, Xie, Z, Xu, Dz, Xu, J, Xu, L, Xu, X, Yamamoto, A, Yamashina, S, Yamashita, M, Yan, X, Yanagida, M, Yang, D, Yang, E, Yang, Jm, Yang, Sy, Yang, W, Yang, Wy, Yang, Z, Yao, Mc, Yao, Tp, Yeganeh, B, Yen, Wl, Yin, Jj, Yin, Xm, Yoo, Oj, Yoon, G, Yoon, Sy, Yorimitsu, T, Yoshikawa, Y, Yoshimori, T, Yoshimoto, K, You, Hj, Youle, Rj, Younes, A, Yu, L, Yu, Sw, Yu, Wh, Yuan, Zm, Yue, Z, Yun, Ch, Yuzaki, M, Zabirnyk, O, Silva-Zacarin, E, Zacks, D, Zacksenhaus, E, Zaffaroni, N, Zakeri, Z, Zeh HJ, 3rd, Zeitlin, So, Zhang, H, Zhang, Hl, Zhang, J, Zhang, Jp, Zhang, L, Zhang, My, Zhang, Xd, Zhao, M, Zhao, Yf, Zhao, Y, Zhao, Zj, Zheng, X, Zhivotovsky, B, Zhong, Q, Zhou, Cz, Zhu, C, Zhu, Wg, Zhu, Xf, Zhu, X, Zhu, Y, Zoladek, T, Zong, Wx, Zorzano, A, Zschocke, J, Zuckerbraun, B., and Viscomi M. T. (ORCID:0000-0002-9096-4967)
- Abstract
In 2008 we published the first set of guidelines for standardizing research in autophagy. Since then, research on this topic has continued to accelerate, and many new scientists have entered the field. Our knowledge base and relevant new technologies have also been expanding. Accordingly, it is important to update these guidelines for monitoring autophagy in different organisms. Various reviews have described the range of assays that have been used for this purpose. Nevertheless, there continues to be confusion regarding acceptable methods to measure autophagy, especially in multicellular eukaryotes. A key point that needs to be emphasized is that there is a difference between measurements that monitor the numbers or volume of autophagic elements (e.g., autophagosomes or autolysosomes) at any stage of the autophagic process vs. those that measure flux through the autophagy pathway (i.e., the complete process); thus, a block in macroautophagy that results in autophagosome accumulation needs to be differentiated from stimuli that result in increased autophagic activity, defined as increased autophagy induction coupled with increased delivery to, and degradation within, lysosomes (in most higher eukaryotes and some protists such as Dictyostelium) or the vacuole (in plants and fungi). In other words, it is especially important that investigators new to the field understand that the appearance of more autophagosomes does not necessarily equate with more autophagy. In fact, in many cases, autophagosomes accumulate because of a block in trafficking to lysosomes without a concomitant change in autophagosome biogenesis, whereas an increase in autolysosomes may reflect a reduction in degradative activity. Here, we present a set of guidelines for the selection and interpretation of methods for use by investigators who aim to examine macroautophagy and related processes, as well as for reviewers who need to provide realistic and reasonable critiques of papers that are focused o
- Published
- 2012
5. Hotspots
- Author
-
Mittal, B, primary and Pandey, UB, additional
- Published
- 2002
- Full Text
- View/download PDF
6. HuD impairs neuromuscular junctions and induces apoptosis in human iPSC and Drosophila ALS models.
- Author
-
Silvestri B, Mochi M, Mawrie D, de Turris V, Colantoni A, Borhy B, Medici M, Anderson EN, Garone MG, Zammerilla CP, Simula M, Ballarino M, Pandey UB, and Rosa A
- Subjects
- Humans, Animals, Mutation, Oxidative Stress, Drosophila Proteins metabolism, Drosophila Proteins genetics, Drosophila melanogaster genetics, Female, Male, Drosophila, Neuromuscular Junction metabolism, Amyotrophic Lateral Sclerosis genetics, Amyotrophic Lateral Sclerosis metabolism, Amyotrophic Lateral Sclerosis pathology, Apoptosis genetics, Induced Pluripotent Stem Cells metabolism, Motor Neurons metabolism, Motor Neurons pathology, RNA-Binding Protein FUS metabolism, RNA-Binding Protein FUS genetics, Disease Models, Animal, ELAV-Like Protein 4 metabolism, ELAV-Like Protein 4 genetics
- Abstract
Defects at the neuromuscular junction (NMJ) are among the earliest hallmarks of amyotrophic lateral sclerosis (ALS). According to the "dying-back" hypothesis, NMJ disruption not only precedes but also triggers the subsequent degeneration of motoneurons in both sporadic (sALS) and familial (fALS) ALS. Using human induced pluripotent stem cells (iPSCs), we show that the RNA-binding protein HuD (ELAVL4) contributes to NMJ defects and apoptosis in FUS-ALS. HuD overexpression mimics the severe FUS
P525L mutation, while its knockdown rescues the FUSP525L phenotypes. In Drosophila, neuronal overexpression of the HuD ortholog, elav, induces motor dysfunction, and its knockdown improves motor function in a FUS-ALS model. Finally, we report increased HuD levels upon oxidative stress in human motoneurons and in sALS patients with an oxidative stress signature. Based on these findings, we propose that HuD plays a role downstream of FUS mutations in fALS and in sALS related to oxidative stress., (© 2024. The Author(s).)- Published
- 2024
- Full Text
- View/download PDF
7. Function and dysfunction of GEMIN5: understanding a novel neurodevelopmental disorder.
- Author
-
Nelson CH and Pandey UB
- Abstract
The recent identification of a neurodevelopmental disorder with cerebellar atrophy and motor dysfunction (NEDCAM) has resulted in an increased interest in GEMIN5, a multifunction RNA-binding protein. As the largest member of the survival motor neuron complex, GEMIN5 plays a key role in the biogenesis of small nuclear ribonucleoproteins while also exhibiting translational regulatory functions as an independent protein. Although many questions remain regarding both the pathogenesis and pathophysiology of this new disorder, considerable progress has been made in the brief time since its discovery. In this review, we examine GEMIN5 within the context of NEDCAM, focusing on the structure, function, and expression of the protein specifically in regard to the disorder itself. Additionally, we explore the current animal models of NEDCAM, as well as potential molecular pathways for treatment and future directions of study. This review provides a comprehensive overview of recent advances in our understanding of this unique member of the survival motor neuron complex., (Copyright © 2024 Copyright: © 2024 Neural Regeneration Research.)
- Published
- 2024
- Full Text
- View/download PDF
8. Mutations of GEMIN5 are associated with coenzyme Q 10 deficiency: long-term follow-up after treatment.
- Author
-
Cascajo-Almenara MV, Juliá-Palacios N, Urreizti R, Sánchez-Cuesta A, Fernández-Ayala DM, García-Díaz E, Oliva C, O Callaghan MDM, Paredes-Fuentes AJ, Moreno-Lozano PJ, Muchart J, Nascimento A, Ortez CI, Natera-de Benito D, Pineda M, Rivera N, Fortuna TR, Rajan DS, Navas P, Salviati L, Palau F, Yubero D, García-Cazorla A, Pandey UB, Santos-Ocaña C, and Artuch R
- Subjects
- Adult, Humans, Follow-Up Studies, Mutation, SMN Complex Proteins genetics, Ubiquinone genetics, Ubiquinone therapeutic use, Ubiquinone metabolism, Ubiquinone deficiency, Mitochondrial Diseases drug therapy, Mitochondrial Diseases genetics, Ataxia, Muscle Weakness
- Abstract
GEMIN5 exerts key biological functions regulating pre-mRNAs intron removal to generate mature mRNAs. A series of patients were reported harboring mutations in GEMIN5. No treatments are currently available for this disease. We treated two of these patients with oral Coenzyme Q
10 (CoQ10 ), which resulted in neurological improvements, although MRI abnormalities remained. Whole Exome Sequencing demonstrated compound heterozygosity at the GEMIN5 gene in both cases: Case one: p.Lys742* and p.Arg1016Cys; Case two: p.Arg1016Cys and p.Ser411Hisfs*6. Functional studies in fibroblasts revealed a decrease in CoQ10 biosynthesis compared to controls. Supplementation with exogenous CoQ10 restored it to control intracellular CoQ10 levels. Mitochondrial function was compromised, as indicated by the decrease in oxygen consumption, restored by CoQ10 supplementation. Transcriptomic analysis of GEMIN5 patients compared with controls showed general repression of genes involved in CoQ10 biosynthesis. In the rigor mortis defective flies, CoQ10 levels were decreased, and CoQ10 supplementation led to an improvement in the adult climbing assay performance, a reduction in the number of motionless flies, and partial restoration of survival. Overall, we report the association between GEMIN5 dysfunction and CoQ10 deficiency for the first time. This association opens the possibility of oral CoQ10 therapy, which is safe and has no observed side effects after long-term therapy., (© 2024. The Author(s), under exclusive licence to European Society of Human Genetics.)- Published
- 2024
- Full Text
- View/download PDF
9. HuD (ELAVL4) gain-of-function impairs neuromuscular junctions and induces apoptosis in in vitro and in vivo models of amyotrophic lateral sclerosis.
- Author
-
Silvestri B, Mochi M, Mawrie D, de Turris V, Colantoni A, Borhy B, Medici M, Anderson EN, Garone MG, Zammerilla CP, Pandey UB, and Rosa A
- Abstract
Early defects at the neuromuscular junction (NMJ) are among the first hallmarks of the progressive neurodegenerative disease amyotrophic lateral sclerosis (ALS). According to the "dying back" hypothesis, disruption of the NMJ not only precedes, but is also a trigger for the subsequent degeneration of the motoneuron in both sporadic and familial ALS, including ALS caused by the severe FUS pathogenic variant P525L. However, the mechanisms linking genetic and environmental factors to NMJ defects remain elusive. By taking advantage of co-cultures of motoneurons and skeletal muscle derived from human induced pluripotent stem cells (iPSCs), we show that the neural RNA binding protein HuD (ELAVL4) may underlie NMJ defects and apoptosis in FUS-ALS. HuD overexpression in motoneurons phenocopies the severe FUS
P525L mutation, while HuD knockdown in FUSP525L co-cultures produces phenotypic rescue. We validated these findings in vivo in a Drosophila FUS-ALS model. Neuronal-restricted overexpression of the HuD-related gene, elav , produces per se a motor phenotype, while neuronal-restricted elav knockdown significantly rescues motor dysfunction caused by FUS. Finally, we show that HuD levels increase upon oxidative stress in human motoneurons and in sporadic ALS patients with an oxidative stress signature. On these bases, we propose HuD as an important player downstream of FUS mutation in familial ALS, with potential implications for sporadic ALS related to oxidative stress., Competing Interests: COMPETING INTERESTS The authors declare no competing interests.- Published
- 2024
- Full Text
- View/download PDF
10. MATR3 pathogenic variants differentially impair its cryptic splicing repression function.
- Author
-
Khan M, Chen XXL, Dias M, Santos JR, Kour S, You J, van Bruggen R, Youssef MMM, Wan YW, Liu Z, Rosenfeld JA, Tan Q, Pandey UB, Yalamanchili HK, and Park J
- Subjects
- Humans, Exons genetics, RNA-Binding Proteins genetics, RNA-Binding Proteins metabolism, RNA, Nuclear Matrix-Associated Proteins genetics, Amyotrophic Lateral Sclerosis genetics
- Abstract
Matrin-3 (MATR3) is an RNA-binding protein implicated in neurodegenerative and neurodevelopmental diseases. However, little is known regarding the role of MATR3 in cryptic splicing within the context of functional genes and how disease-associated variants impact this function. We show that loss of MATR3 leads to cryptic exon inclusion in many transcripts. We reveal that ALS-linked S85C pathogenic variant reduces MATR3 solubility but does not impair RNA binding. In parallel, we report a novel neurodevelopmental disease-associated M548T variant, located in the RRM2 domain, which reduces protein solubility and impairs RNA binding and cryptic splicing repression functions of MATR3. Altogether, our research identifies cryptic events within functional genes and demonstrates how disease-associated variants impact MATR3 cryptic splicing repression function., (© 2024 The Authors. FEBS Letters published by John Wiley & Sons Ltd on behalf of Federation of European Biochemical Societies.)
- Published
- 2024
- Full Text
- View/download PDF
11. CLIP-Seq analysis enables the design of protective ribosomal RNA bait oligonucleotides against C9ORF72 ALS/FTD poly-GR pathophysiology.
- Author
-
Ortega JA, Sasselli IR, Boccitto M, Fleming AC, Fortuna TR, Li Y, Sato K, Clemons TD, Mckenna ED, Nguyen TP, Anderson EN, Asin J, Ichida JK, Pandey UB, Wolin SL, Stupp SI, and Kiskinis E
- Subjects
- Animals, Humans, C9orf72 Protein genetics, C9orf72 Protein metabolism, RNA, Ribosomal genetics, Chromatin Immunoprecipitation Sequencing, RNA genetics, Drosophila genetics, Drosophila metabolism, DNA Repeat Expansion, Frontotemporal Dementia genetics, Amyotrophic Lateral Sclerosis genetics
- Abstract
Amyotrophic lateral sclerosis and frontotemporal dementia patients with a hexanucleotide repeat expansion in C9ORF72 (C9-HRE) accumulate poly-GR and poly-PR aggregates. The pathogenicity of these arginine-rich dipeptide repeats (R-DPRs) is thought to be driven by their propensity to bind low-complexity domains of multivalent proteins. However, the ability of R-DPRs to bind native RNA and the significance of this interaction remain unclear. Here, we used computational and experimental approaches to characterize the physicochemical properties of R-DPRs and their interaction with RNA. We find that poly-GR predominantly binds ribosomal RNA (rRNA) in cells and exhibits an interaction that is predicted to be energetically stronger than that for associated ribosomal proteins. Critically, modified rRNA "bait" oligonucleotides restore poly-GR-associated ribosomal deficits and ameliorate poly-GR toxicity in patient neurons and Drosophila models. Our work strengthens the hypothesis that ribosomal function is impaired by R-DPRs, highlights a role for direct rRNA binding in mediating ribosomal dysfunction, and presents a strategy for protecting against C9-HRE pathophysiological mechanisms.
- Published
- 2023
- Full Text
- View/download PDF
12. Drosha-dependent microRNAs modulate FUS-mediated neurodegeneration in vivo.
- Author
-
Kour S, Fortuna T, Anderson EN, Mawrie D, Bilstein J, Sivasubramanian R, Ward C, Roy R, Rajasundaram D, Sterneckert J, and Pandey UB
- Subjects
- Animals, Amyotrophic Lateral Sclerosis metabolism, Drosophila genetics, Drosophila metabolism, Mutation, Neurons metabolism, RNA-Binding Proteins genetics, RNA-Binding Proteins metabolism, Neurodegenerative Diseases metabolism, Humans, MicroRNAs genetics, MicroRNAs metabolism, Heterogeneous-Nuclear Ribonucleoprotein Group F-H metabolism, Ribonuclease III metabolism, Drosophila Proteins metabolism
- Abstract
Mutations in the Fused in Sarcoma (FUS) gene cause the familial and progressive form of amyotrophic lateral sclerosis (ALS). FUS is a nuclear RNA-binding protein involved in RNA processing and the biogenesis of a specific set of microRNAs. Here we report that Drosha and two previously uncharacterized Drosha-dependent miRNAs are strong modulators of FUS expression and prevent the cytoplasmic segregation of insoluble mutant FUS in vivo. We demonstrate that depletion of Drosha mitigates FUS-mediated degeneration, survival and motor defects in Drosophila. Mutant FUS strongly interacts with Drosha and causes its cytoplasmic mis-localization into the insoluble FUS inclusions. Reduction in Drosha levels increases the solubility of mutant FUS. Interestingly, we found two Drosha dependent microRNAs, miR-378i and miR-6832-5p, which differentially regulate the expression, solubility and cytoplasmic aggregation of mutant FUS in iPSC neurons and mammalian cells. More importantly, we report different modes of action of these miRNAs against mutant FUS. Whereas miR-378i may regulate mutant FUS inclusions by preventing G3BP-mediated stress granule formation, miR-6832-5p may affect FUS expression via other proteins or pathways. Overall, our research reveals a possible association between ALS-linked FUS mutations and the Drosha-dependent miRNA regulatory circuit, as well as a useful perspective on potential ALS treatment via microRNAs., (© The Author(s) 2023. Published by Oxford University Press on behalf of Nucleic Acids Research.)
- Published
- 2023
- Full Text
- View/download PDF
13. SMN regulates GEMIN5 expression and acts as a modifier of GEMIN5-mediated neurodegeneration.
- Author
-
Fortuna TR, Kour S, Chimata AV, Muiños-Bühl A, Anderson EN, Nelson Iv CH, Ward C, Chauhan O, O'Brien C, Rajasundaram D, Rajan DS, Wirth B, Singh A, and Pandey UB
- Subjects
- Humans, Motor Neurons metabolism, Ribonucleoproteins, Small Nuclear genetics, Ribonucleoproteins, Small Nuclear chemistry, Ribonucleoproteins, Small Nuclear metabolism, SMN Complex Proteins genetics, Tudor Domain, Muscular Atrophy, Spinal genetics, Muscular Atrophy, Spinal metabolism, RNA-Binding Proteins metabolism
- Abstract
GEMIN5 is essential for core assembly of small nuclear Ribonucleoproteins (snRNPs), the building blocks of spliceosome formation. Loss-of-function mutations in GEMIN5 lead to a neurodevelopmental syndrome among patients presenting with developmental delay, motor dysfunction, and cerebellar atrophy by perturbing SMN complex protein expression and assembly. Currently, molecular determinants of GEMIN5-mediated disease have yet to be explored. Here, we identified SMN as a genetic suppressor of GEMIN5-mediated neurodegeneration in vivo. We discovered that an increase in SMN expression by either SMN gene therapy replacement or the antisense oligonucleotide (ASO), Nusinersen, significantly upregulated the endogenous levels of GEMIN5 in mammalian cells and mutant GEMIN5-derived iPSC neurons. Further, we identified a strong functional association between the expression patterns of SMN and GEMIN5 in patient Spinal Muscular Atrophy (SMA)-derived motor neurons harboring loss-of-function mutations in the SMN gene. Interestingly, SMN binds to the C-terminus of GEMIN5 and requires the Tudor domain for GEMIN5 binding and expression regulation. Finally, we show that SMN upregulation ameliorates defective snRNP biogenesis and alternative splicing defects caused by loss of GEMIN5 in iPSC neurons and in vivo. Collectively, these studies indicate that SMN acts as a regulator of GEMIN5 expression and neuropathologies., (© 2023. The Author(s), under exclusive licence to Springer-Verlag GmbH Germany, part of Springer Nature.)
- Published
- 2023
- Full Text
- View/download PDF
14. Editorial: Drosophila as a model to study neurodegenerative diseases.
- Author
-
Liguori F, Pandey UB, and Digilio FA
- Abstract
Competing Interests: The authors declare that the research was conducted in the absence of any commercial or financial relationships that could be construed as a potential conflict of interest. The author(s) declared that they were an editorial board member of Frontiers, at the time of submission. This had no impact on the peer review process and the final decision.
- Published
- 2023
- Full Text
- View/download PDF
15. Loss of function of the ALS-associated NEK1 kinase disrupts microtubule homeostasis and nuclear import.
- Author
-
Mann JR, McKenna ED, Mawrie D, Papakis V, Alessandrini F, Anderson EN, Mayers R, Ball HE, Kaspi E, Lubinski K, Baron DM, Tellez L, Landers JE, Pandey UB, and Kiskinis E
- Subjects
- Humans, Active Transport, Cell Nucleus, NIMA-Related Kinase 1 genetics, Proteins, Motor Neurons, Microtubules, Homeostasis, Amyotrophic Lateral Sclerosis genetics
- Abstract
Loss-of-function variants in NIMA-related kinase 1 (NEK1) constitute a major genetic cause of amyotrophic lateral sclerosis (ALS), accounting for 2 to 3% of all cases. However, how NEK1 mutations cause motor neuron (MN) dysfunction is unknown. Using mass spectrometry analyses for NEK1 interactors and NEK1-dependent expression changes, we find functional enrichment for proteins involved in the microtubule cytoskeleton and nucleocytoplasmic transport. We show that α-tubulin and importin-β1, two key proteins involved in these processes, are phosphorylated by NEK1 in vitro. NEK1 is essential for motor control and survival in Drosophila models in vivo, while using several induced pluripotent stem cell (iPSC)-MN models, including NEK1 knockdown, kinase inhibition, and a patient mutation, we find evidence for disruptions in microtubule homeostasis and nuclear import. Notably, stabilizing microtubules with two distinct classes of drugs restored NEK1-dependent deficits in both pathways. The capacity of NEK1 to modulate these processes that are critically involved in ALS pathophysiology renders this kinase a formidable therapeutic candidate.
- Published
- 2023
- Full Text
- View/download PDF
16. C9orf72 poly(PR) mediated neurodegeneration is associated with nucleolar stress.
- Author
-
Cicardi ME, Hallgren JH, Mawrie D, Krishnamurthy K, Markandaiah SS, Nelson AT, Kankate V, Anderson EN, Pasinelli P, Pandey UB, Eischen CM, and Trotti D
- Abstract
The ALS/FTD-linked intronic hexanucleotide repeat expansion in the C9orf72 gene is aberrantly translated in the sense and antisense directions into dipeptide repeat proteins, among which poly proline-arginine (PR) displays the most aggressive neurotoxicity in-vitro and in-vivo . PR partitions to the nucleus when heterologously expressed in neurons and other cell types. We show that by lessening the nuclear accumulation of PR, we can drastically reduce its neurotoxicity. PR strongly accumulates in the nucleolus, a nuclear structure critical in regulating the cell stress response. We determined that, in neurons, PR caused nucleolar stress and increased levels of the transcription factor p53. Downregulating p53 levels also prevented PR-mediated neurotoxicity both in in-vitro and in-vivo models. We investigated if PR could induce the senescence phenotype in neurons. However, we did not observe any indications of such an effect. Instead, we found evidence for the induction of programmed cell death via caspase-3 activation., Competing Interests: The authors declare no competing interests., (© 2023 The Authors.)
- Published
- 2023
- Full Text
- View/download PDF
17. NgR1 binding to reovirus reveals an unusual bivalent interaction and a new viral attachment protein.
- Author
-
Sutherland DM, Strebl M, Koehler M, Welsh OL, Yu X, Hu L, Dos Santos Natividade R, Knowlton JJ, Taylor GM, Moreno RA, Wörz P, Lonergan ZR, Aravamudhan P, Guzman-Cardozo C, Kour S, Pandey UB, Alsteens D, Wang Z, Prasad BVV, Stehle T, and Dermody TS
- Subjects
- Animals, Humans, Nogo Receptor 1 metabolism, Virus Attachment, Viral Proteins metabolism, Ligands, Receptors, Virus metabolism, Mammals metabolism, Reoviridae metabolism, Orthoreovirus metabolism
- Abstract
Nogo-66 receptor 1 (NgR1) binds a variety of structurally dissimilar ligands in the adult central nervous system to inhibit axon extension. Disruption of ligand binding to NgR1 and subsequent signaling can improve neuron outgrowth, making NgR1 an important therapeutic target for diverse neurological conditions such as spinal crush injuries and Alzheimer's disease. Human NgR1 serves as a receptor for mammalian orthoreovirus (reovirus), but the mechanism of virus-receptor engagement is unknown. To elucidate how NgR1 mediates cell binding and entry of reovirus, we defined the affinity of interaction between virus and receptor, determined the structure of the virus-receptor complex, and identified residues in the receptor required for virus binding and infection. These studies revealed that central NgR1 surfaces form a bridge between two copies of viral capsid protein σ3, establishing that σ3 serves as a receptor ligand for reovirus. This unusual binding interface produces high-avidity interactions between virus and receptor to prime early entry steps. These studies refine models of reovirus cell-attachment and highlight the evolution of viruses to engage multiple receptors using distinct capsid components.
- Published
- 2023
- Full Text
- View/download PDF
18. Axon guidance genes modulate neurotoxicity of ALS-associated UBQLN2.
- Author
-
Kim SH, Nichols KD, Anderson EN, Liu Y, Ramesh N, Jia W, Kuerbis CJ, Scalf M, Smith LM, Pandey UB, and Tibbetts RS
- Subjects
- Humans, Axon Guidance, Adaptor Proteins, Signal Transducing genetics, Adaptor Proteins, Signal Transducing metabolism, Autophagy-Related Proteins genetics, Autophagy-Related Proteins metabolism, Mutation, Transcription Factors genetics, Ubiquitins metabolism, Netrin Receptors genetics, Amyotrophic Lateral Sclerosis genetics, Frontotemporal Dementia genetics
- Abstract
Mutations in the ubiquitin (Ub) chaperone Ubiquilin 2 (UBQLN2 ) cause X-linked forms of amyotrophic lateral sclerosis (ALS) and frontotemporal dementia (FTD) through unknown mechanisms. Here, we show that aggregation-prone, ALS-associated mutants of UBQLN2 (UBQLN2
ALS ) trigger heat stress-dependent neurodegeneration in Drosophila . A genetic modifier screen implicated endolysosomal and axon guidance genes, including the netrin receptor, Unc-5, as key modulators of UBQLN2 toxicity. Reduced gene dosage of Unc-5 or its coreceptor Dcc/frazzled diminished neurodegenerative phenotypes, including motor dysfunction, neuromuscular junction defects, and shortened lifespan, in flies expressing UBQLN2ALS alleles. Induced pluripotent stem cells (iPSCs) harboring UBQLN2ALS knockin mutations exhibited lysosomal defects while inducible motor neurons (iMNs) expressing UBQLN2ALS alleles exhibited cytosolic UBQLN2 inclusions, reduced neurite complexity, and growth cone defects that were partially reversed by silencing of UNC5B and DCC . The combined findings suggest that altered growth cone dynamics are a conserved pathomechanism in UBQLN2-associated ALS/FTD., Competing Interests: SK, KN, EA, YL, NR, WJ, CK, MS, LS, UP, RT No competing interests declared, (© 2023, Kim et al.)- Published
- 2023
- Full Text
- View/download PDF
19. LSD1/PRMT6-targeting gene therapy to attenuate androgen receptor toxic gain-of-function ameliorates spinobulbar muscular atrophy phenotypes in flies and mice.
- Author
-
Prakasam R, Bonadiman A, Andreotti R, Zuccaro E, Dalfovo D, Marchioretti C, Tripathy D, Petris G, Anderson EN, Migazzi A, Tosatto L, Cereseto A, Battaglioli E, Sorarù G, Lim WF, Rinaldi C, Sambataro F, Pourshafie N, Grunseich C, Romanel A, Pandey UB, Contestabile A, Ronzitti G, Basso M, and Pennuto M
- Subjects
- Mice, Animals, Receptors, Androgen genetics, Receptors, Androgen metabolism, Androgens, Gain of Function Mutation, Phenotype, Histone Demethylases genetics, Bulbo-Spinal Atrophy, X-Linked genetics, Diptera, Muscular Disorders, Atrophic genetics, Muscular Disorders, Atrophic metabolism
- Abstract
Spinobulbar muscular atrophy (SBMA) is caused by CAG expansions in the androgen receptor gene. Androgen binding to polyQ-expanded androgen receptor triggers SBMA through a combination of toxic gain-of-function and loss-of-function mechanisms. Leveraging cell lines, mice, and patient-derived specimens, we show that androgen receptor co-regulators lysine-specific demethylase 1 (LSD1) and protein arginine methyltransferase 6 (PRMT6) are overexpressed in an androgen-dependent manner specifically in the skeletal muscle of SBMA patients and mice. LSD1 and PRMT6 cooperatively and synergistically transactivate androgen receptor, and their effect is enhanced by expanded polyQ. Pharmacological and genetic silencing of LSD1 and PRMT6 attenuates polyQ-expanded androgen receptor transactivation in SBMA cells and suppresses toxicity in SBMA flies, and a preclinical approach based on miRNA-mediated silencing of LSD1 and PRMT6 attenuates disease manifestations in SBMA mice. These observations suggest that targeting overexpressed co-regulators can attenuate androgen receptor toxic gain-of-function without exacerbating loss-of-function, highlighting a potential therapeutic strategy for patients with SBMA., (© 2023. The Author(s).)
- Published
- 2023
- Full Text
- View/download PDF
20. Antagonistic effect of cyclin-dependent kinases and a calcium-dependent phosphatase on polyglutamine-expanded androgen receptor toxic gain of function.
- Author
-
Piol D, Tosatto L, Zuccaro E, Anderson EN, Falconieri A, Polanco MJ, Marchioretti C, Lia F, White J, Bregolin E, Minervini G, Parodi S, Salvatella X, Arrigoni G, Ballabio A, La Spada AR, Tosatto SCE, Sambataro F, Medina DL, Pandey UB, Basso M, and Pennuto M
- Subjects
- Mice, Animals, Gain of Function Mutation, Cyclin-Dependent Kinases genetics, Phosphoric Monoester Hydrolases genetics, Receptors, Androgen chemistry, Calcium
- Abstract
Spinal and bulbar muscular atrophy is caused by polyglutamine (polyQ) expansions in androgen receptor (AR), generating gain-of-function toxicity that may involve phosphorylation. Using cellular and animal models, we investigated what kinases and phosphatases target polyQ-expanded AR, whether polyQ expansions modify AR phosphorylation, and how this contributes to neurodegeneration. Mass spectrometry showed that polyQ expansions preserve native phosphorylation and increase phosphorylation at conserved sites controlling AR stability and transactivation. In small-molecule screening, we identified that CDC25/CDK2 signaling could enhance AR phosphorylation, and the calcium-sensitive phosphatase calcineurin had opposite effects. Pharmacologic and genetic manipulation of these kinases and phosphatases modified polyQ-expanded AR function and toxicity in cells, flies, and mice. Ablation of CDK2 reduced AR phosphorylation in the brainstem and restored expression of Myc and other genes involved in DNA damage, senescence, and apoptosis, indicating that the cell cycle-regulated kinase plays more than a bystander role in SBMA-vulnerable postmitotic cells.
- Published
- 2023
- Full Text
- View/download PDF
21. WNK kinases sense molecular crowding and rescue cell volume via phase separation.
- Author
-
Boyd-Shiwarski CR, Shiwarski DJ, Griffiths SE, Beacham RT, Norrell L, Morrison DE, Wang J, Mann J, Tennant W, Anderson EN, Franks J, Calderon M, Connolly KA, Cheema MU, Weaver CJ, Nkashama LJ, Weckerly CC, Querry KE, Pandey UB, Donnelly CJ, Sun D, Rodan AR, and Subramanya AR
- Subjects
- Phosphorylation, Cell Size, Protein Serine-Threonine Kinases
- Abstract
When challenged by hypertonicity, dehydrated cells must recover their volume to survive. This process requires the phosphorylation-dependent regulation of SLC12 cation chloride transporters by WNK kinases, but how these kinases are activated by cell shrinkage remains unknown. Within seconds of cell exposure to hypertonicity, WNK1 concentrates into membraneless condensates, initiating a phosphorylation-dependent signal that drives net ion influx via the SLC12 cotransporters to restore cell volume. WNK1 condensate formation is driven by its intrinsically disordered C terminus, whose evolutionarily conserved signatures are necessary for efficient phase separation and volume recovery. This disorder-encoded phase behavior occurs within physiological constraints and is activated in vivo by molecular crowding rather than changes in cell size. This allows kinase activity despite an inhibitory ionic milieu and permits cell volume recovery through condensate-mediated signal amplification. Thus, WNK kinases are physiological crowding sensors that phase separate to coordinate a cell volume rescue response., Competing Interests: Declaration of interests The authors declare no competing interests., (Copyright © 2022 Elsevier Inc. All rights reserved.)
- Published
- 2022
- Full Text
- View/download PDF
22. Further delineation of GEMIN4 related neurodevelopmental disorder with microcephaly, cataract, and renal abnormalities syndrome.
- Author
-
Altassan R, Qudair A, Alokaili R, Alhasan K, Faqeih EA, Alhashem A, Alowain M, Alsayed M, Rahbeeni Z, Albadi L, Alkuraya FS, Anderson EN, Rajan D, and Pandey UB
- Subjects
- Homozygote, Humans, Kidney abnormalities, Minor Histocompatibility Antigens, Pedigree, Ribonucleoproteins, Small Nuclear genetics, Syndrome, Urogenital Abnormalities, Abnormalities, Multiple diagnosis, Abnormalities, Multiple genetics, Cataract pathology, Microcephaly diagnosis, Microcephaly genetics, Microcephaly pathology, Neurodevelopmental Disorders genetics
- Abstract
Pathogenic variants in GEMIN4 have recently been linked to an inherited autosomal recessive neurodevelopmental disorder characterized with microcephaly, cataracts, and renal abnormalities (NEDMCR syndrome). This report provides a retrospective review of 16 patients from 11 unrelated Saudi consanguineous families with GEMIN4 mutations. The cohort comprises 11 new and unpublished clinical details from five previously described patients. Only two missense, homozygous, pathogenic variants were found in all affected patients, suggesting a founder effect. All patients shared global developmental delay with variable ophthalmological, renal, and skeletal manifestations. In addition, we knocked down endogenous Drosophila GEMIN4 in neurons to further investigate the mechanism of the functional defects in affected patients. Our fly model findings demonstrated developmental defects and motor dysfunction suggesting that loss of GEMIN4 function is detrimental in vivo; likely similar to human patients. To date, this study presents the largest cohort of patients affected with GEMIN4 mutations. Considering that identifying GEMIN4 defects in patients presenting with neurodevelopmental delay and congenital cataract will help in early diagnosis, appropriate management and prevention plans that can be made for affected families., (© 2022 Wiley Periodicals LLC.)
- Published
- 2022
- Full Text
- View/download PDF
23. Pathogenic variants of Valosin-containing protein induce lysosomal damage and transcriptional activation of autophagy regulators in neuronal cells.
- Author
-
Ferrari V, Cristofani R, Cicardi ME, Tedesco B, Crippa V, Chierichetti M, Casarotto E, Cozzi M, Mina F, Galbiati M, Piccolella M, Carra S, Vaccari T, Nalbandian A, Kimonis V, Fortuna TR, Pandey UB, Gagliani MC, Cortese K, Rusmini P, and Poletti A
- Subjects
- Animals, Autophagy genetics, Lysosomes metabolism, Motor Neurons metabolism, Transcriptional Activation, Valosin Containing Protein genetics, Valosin Containing Protein metabolism, Adenosine Triphosphatases genetics, Adenosine Triphosphatases metabolism, Cell Cycle Proteins genetics, Cell Cycle Proteins metabolism
- Abstract
Aim: Mutations in the valosin-containing protein (VCP) gene cause various lethal proteinopathies that mainly include inclusion body myopathy with Paget's disease of bone and frontotemporal dementia (IBMPFD) and amyotrophic lateral sclerosis (ALS). Different pathological mechanisms have been proposed. Here, we define the impact of VCP mutants on lysosomes and how cellular homeostasis is restored by inducing autophagy in the presence of lysosomal damage., Methods: By electron microscopy, we studied lysosomal morphology in VCP animal and motoneuronal models. With the use of western blotting, real-time quantitative polymerase chain reaction (RT-qPCR), immunofluorescence and filter trap assay, we evaluated the effect of selected VCP mutants in neuronal cells on lysosome size and activity, lysosomal membrane permeabilization and their impact on autophagy., Results: We found that VCP mutants induce the formation of aberrant multilamellar organelles in VCP animal and cell models similar to those found in patients with VCP mutations or with lysosomal storage disorders. In neuronal cells, we found altered lysosomal activity characterised by membrane permeabilization with galectin-3 redistribution and activation of PPP3CB. This selectively activated the autophagy/lysosomal transcriptional regulator TFE3, but not TFEB, and enhanced both SQSTM1/p62 and lipidated MAP1LC3B levels inducing autophagy. Moreover, we found that wild type VCP, but not the mutants, counteracted lysosomal damage induced either by trehalose or by a mutant form of SOD1 (G93A), also blocking the formation of its insoluble intracellular aggregates. Thus, chronic activation of autophagy might fuel the formation of multilamellar bodies., Conclusion: Together, our findings provide insights into the pathogenesis of VCP-related diseases, by proposing a novel mechanism of multilamellar body formation induced by VCP mutants that involves lysosomal damage and induction of lysophagy., (© 2022 The Authors. Neuropathology and Applied Neurobiology published by John Wiley & Sons Ltd on behalf of British Neuropathological Society.)
- Published
- 2022
- Full Text
- View/download PDF
24. Skeletal Muscle Pathogenesis in Polyglutamine Diseases.
- Author
-
Marchioretti C, Zuccaro E, Pandey UB, Rosati J, Basso M, and Pennuto M
- Subjects
- Animals, Humans, Muscle, Skeletal metabolism, Muscle, Skeletal pathology, Neurons metabolism, Muscular Atrophy pathology, Peptides metabolism
- Abstract
Polyglutamine diseases are characterized by selective dysfunction and degeneration of specific types of neurons in the central nervous system. In addition, nonneuronal cells can also be affected as a consequence of primary degeneration or due to neuronal dysfunction. Skeletal muscle is a primary site of toxicity of polyglutamine-expanded androgen receptor, but it is also affected in other polyglutamine diseases, more likely due to neuronal dysfunction and death. Nonetheless, pathological processes occurring in skeletal muscle atrophy impact the entire body metabolism, thus actively contributing to the inexorable progression towards the late and final stages of disease. Skeletal muscle atrophy is well recapitulated in animal models of polyglutamine disease. In this review, we discuss the impact and relevance of skeletal muscle in patients affected by polyglutamine diseases and we review evidence obtained in animal models and patient-derived cells modeling skeletal muscle.
- Published
- 2022
- Full Text
- View/download PDF
25. NUP62 localizes to ALS/FTLD pathological assemblies and contributes to TDP-43 insolubility.
- Author
-
Gleixner AM, Verdone BM, Otte CG, Anderson EN, Ramesh N, Shapiro OR, Gale JR, Mauna JC, Mann JR, Copley KE, Daley EL, Ortega JA, Cicardi ME, Kiskinis E, Kofler J, Pandey UB, Trotti D, and Donnelly CJ
- Subjects
- C9orf72 Protein genetics, DNA Repeat Expansion, DNA-Binding Proteins genetics, DNA-Binding Proteins metabolism, Dipeptides metabolism, Glycine genetics, Humans, Amyotrophic Lateral Sclerosis metabolism, Frontotemporal Lobar Degeneration metabolism
- Abstract
A G4C2 hexanucleotide repeat expansion in the C9orf72 gene is the most common genetic cause of ALS and FTLD (C9-ALS/FTLD) with cytoplasmic TDP-43 inclusions observed in regions of neurodegeneration. The accumulation of repetitive RNAs and dipeptide repeat protein (DPR) are two proposed mechanisms of toxicity in C9-ALS/FTLD and linked to impaired nucleocytoplasmic transport. Nucleocytoplasmic transport is regulated by the phenylalanine-glycine nucleoporins (FG nups) that comprise the nuclear pore complex (NPC) permeability barrier. However, the relationship between FG nups and TDP-43 pathology remains elusive. Our studies show that nuclear depletion and cytoplasmic mislocalization of one FG nup, NUP62, is linked to TDP-43 mislocalization in C9-ALS/FTLD iPSC neurons. Poly-glycine arginine (GR) DPR accumulation initiates the formation of cytoplasmic RNA granules that recruit NUP62 and TDP-43. Cytoplasmic NUP62 and TDP-43 interactions promotes their insolubility and NUP62:TDP-43 inclusions are frequently found in C9orf72 ALS/FTLD as well as sporadic ALS/FTLD postmortem CNS tissue. Our findings indicate NUP62 cytoplasmic mislocalization contributes to TDP-43 proteinopathy in ALS/FTLD., (© 2022. The Author(s).)
- Published
- 2022
- Full Text
- View/download PDF
26. Functional and structural deficiencies of Gemin5 variants associated with neurological disorders.
- Author
-
Francisco-Velilla R, Embarc-Buh A, Del Caño-Ochoa F, Abellan S, Vilar M, Alvarez S, Fernandez-Jaen A, Kour S, Rajan DS, Pandey UB, Ramón-Maiques S, and Martinez-Salas E
- Subjects
- Humans, RNA genetics, SMN Complex Proteins genetics, SMN Complex Proteins metabolism, Nervous System Diseases genetics, Nervous System Diseases metabolism, RNA-Binding Proteins genetics, RNA-Binding Proteins metabolism, Ribosomes genetics, Ribosomes metabolism
- Abstract
Dysfunction of RNA-binding proteins is often linked to a wide range of human disease, particularly with neurological conditions. Gemin5 is a member of the survival of the motor neurons (SMN) complex, a ribosome-binding protein and a translation reprogramming factor. Recently, pathogenic mutations in Gemin5 have been reported, but the functional consequences of these variants remain elusive. Here, we report functional and structural deficiencies associated with compound heterozygosity variants within the Gemin5 gene found in patients with neurodevelopmental disorders. These clinical variants are located in key domains of Gemin5, the tetratricopeptide repeat (TPR)-like dimerization module and the noncanonical RNA-binding site 1 (RBS1). We show that the TPR-like variants disrupt protein dimerization, whereas the RBS1 variant confers protein instability. All mutants are defective in the interaction with protein networks involved in translation and RNA-driven pathways. Importantly, the TPR-like variants fail to associate with native ribosomes, hampering its involvement in translation control and establishing a functional difference with the wild-type protein. Our study provides insights into the molecular basis of disease associated with malfunction of the Gemin5 protein., (© 2022 Francisco-Velilla et al.)
- Published
- 2022
- Full Text
- View/download PDF
27. Matrin-3 dysfunction in myopathy and motor neuron degeneration.
- Author
-
Ward C and Pandey UB
- Abstract
Competing Interests: None
- Published
- 2022
- Full Text
- View/download PDF
28. Autosomal Recessive Cerebellar Atrophy and Spastic Ataxia in Patients With Pathogenic Biallelic Variants in GEMIN5 .
- Author
-
Rajan DS, Kour S, Fortuna TR, Cousin MA, Barnett SS, Niu Z, Babovic-Vuksanovic D, Klee EW, Kirmse B, Innes M, Rydning SL, Selmer KK, Vigeland MD, Erichsen AK, Nemeth AH, Millan F, DeVile C, Fawcett K, Legendre A, Sims D, Schnekenberg RP, Burglen L, Mercier S, Bakhtiari S, Francisco-Velilla R, Embarc-Buh A, Martinez-Salas E, Wigby K, Lenberg J, Friedman JR, Kruer MC, and Pandey UB
- Abstract
The hereditary ataxias are a heterogenous group of disorders with an increasing number of causative genes being described. Due to the clinical and genetic heterogeneity seen in these conditions, the majority of such individuals endure a diagnostic odyssey or remain undiagnosed. Defining the molecular etiology can bring insights into the responsible molecular pathways and eventually the identification of therapeutic targets. Here, we describe the identification of biallelic variants in the GEMIN5 gene among seven unrelated families with nine affected individuals presenting with spastic ataxia and cerebellar atrophy. GEMIN5, an RNA-binding protein, has been shown to regulate transcription and translation machinery. GEMIN5 is a component of small nuclear ribonucleoprotein (snRNP) complexes and helps in the assembly of the spliceosome complexes. We found that biallelic GEMIN5 variants cause structural abnormalities in the encoded protein and reduce expression of snRNP complex proteins in patient cells compared with unaffected controls. Finally, knocking out endogenous Gemin5 in mice caused early embryonic lethality, suggesting that Gemin5 expression is crucial for normal development. Our work further expands on the phenotypic spectrum associated with GEMIN5- related disease and implicates the role of GEMIN5 among patients with spastic ataxia, cerebellar atrophy, and motor predominant developmental delay., Competing Interests: FM is employed by GeneDx (MD, USA). JF conducts Clinical Trials with Biogen (Angelman’s Syndrome). JF’s spouse is Founder and Principal of Friedman Bioventure, which holds a variety of publicly traded and private biotechnology interests. The remaining authors declare that the research was conducted in the absence of any commercial or financial relationships that could be construed as a potential conflict of interest., (Copyright © 2022 Rajan, Kour, Fortuna, Cousin, Barnett, Niu, Babovic-Vuksanovic, Klee, Kirmse, Innes, Rydning, Selmer, Vigeland, Erichsen, Nemeth, Millan, DeVile, Fawcett, Legendre, Sims, Schnekenberg, Burglen, Mercier, Bakhtiari, Francisco-Velilla, Embarc-Buh, Martinez-Salas, Wigby, Lenberg, Friedman, Kruer and Pandey.)
- Published
- 2022
- Full Text
- View/download PDF
29. DDX17 is involved in DNA damage repair and modifies FUS toxicity in an RGG-domain dependent manner.
- Author
-
Fortuna TR, Kour S, Anderson EN, Ward C, Rajasundaram D, Donnelly CJ, Hermann A, Wyne H, Shewmaker F, and Pandey UB
- Subjects
- Animals, Cell Line, Cytoplasmic Granules chemistry, DNA Damage, Drosophila, Female, Humans, Male, Neurodegenerative Diseases genetics, Sequence Analysis, RNA, Amyotrophic Lateral Sclerosis genetics, DEAD-box RNA Helicases genetics, DNA Repair genetics, RNA-Binding Protein FUS toxicity
- Abstract
Mutations in the RNA binding protein, Fused in Sarcoma (FUS), lead to amyotrophic lateral sclerosis (ALS), the most frequent form of motor neuron disease. Cytoplasmic aggregation and defective DNA repair machinery are etiologically linked to mutant FUS-associated ALS. Although FUS is involved in numerous aspects of RNA processing, little is understood about the pathophysiological mechanisms of mutant FUS. Here, we employed RNA-sequencing technology in Drosophila brains expressing FUS to identify significantly altered genes and pathways involved in FUS-mediated neurodegeneration. We observed the expression levels of DEAD-Box Helicase 17 (DDX17) to be significantly downregulated in response to mutant FUS in Drosophila and human cell lines. Mutant FUS recruits nuclear DDX17 into cytoplasmic stress granules and physically interacts with DDX17 through the RGG1 domain of FUS. Ectopic expression of DDX17 reduces cytoplasmic mislocalization and sequestration of mutant FUS into cytoplasmic stress granules. We identified DDX17 as a novel regulator of the DNA damage response pathway whose upregulation repairs defective DNA damage repair machinery caused by mutant neuronal FUS ALS. In addition, we show DDX17 is a novel modifier of FUS-mediated neurodegeneration in vivo. Our findings indicate DDX17 is downregulated in response to mutant FUS, and restoration of DDX17 levels suppresses FUS-mediated neuropathogenesis and toxicity in vivo., (© 2021. The Author(s), under exclusive licence to Springer-Verlag GmbH Germany, part of Springer Nature.)
- Published
- 2021
- Full Text
- View/download PDF
30. Interactions between ALS-linked FUS and nucleoporins are associated with defects in the nucleocytoplasmic transport pathway.
- Author
-
Lin YC, Kumar MS, Ramesh N, Anderson EN, Nguyen AT, Kim B, Cheung S, McDonough JA, Skarnes WC, Lopez-Gonzalez R, Landers JE, Fawzi NL, Mackenzie IRA, Lee EB, Nickerson JA, Grunwald D, Pandey UB, and Bosco DA
- Subjects
- Amyotrophic Lateral Sclerosis genetics, Amyotrophic Lateral Sclerosis metabolism, Animals, Animals, Genetically Modified, Drosophila, Humans, Mutation, RNA-Binding Protein FUS genetics, Active Transport, Cell Nucleus physiology, Neurons metabolism, Nuclear Pore Complex Proteins metabolism, RNA-Binding Protein FUS metabolism
- Abstract
Nucleocytoplasmic transport (NCT) decline occurs with aging and neurodegeneration. Here, we investigated the NCT pathway in models of amyotrophic lateral sclerosis-fused in sarcoma (ALS-FUS). Expression of ALS-FUS led to a reduction in NCT and nucleoporin (Nup) density within the nuclear membrane of human neurons. FUS and Nups were found to interact independently of RNA in cells and to alter the phase-separation properties of each other in vitro. FUS-Nup interactions were not localized to nuclear pores, but were enriched in the nucleus of control neurons versus the cytoplasm of mutant neurons. Our data indicate that the effect of ALS-linked mutations on the cytoplasmic mislocalization of FUS, rather than on the physiochemical properties of the protein itself, underlie our reported NCT defects. An aberrant interaction between mutant FUS and Nups is underscored by studies in Drosophila, whereby reduced Nup expression rescued multiple toxic FUS-induced phenotypes, including abnormal nuclear membrane morphology in neurons., (© 2021. The Author(s), under exclusive licence to Springer Nature America, Inc.)
- Published
- 2021
- Full Text
- View/download PDF
31. Traumatic injury compromises nucleocytoplasmic transport and leads to TDP-43 pathology.
- Author
-
Anderson EN, Morera AA, Kour S, Cherry JD, Ramesh N, Gleixner A, Schwartz JC, Ebmeier C, Old W, Donnelly CJ, Cheng JP, Kline AE, Kofler J, Stein TD, and Pandey UB
- Subjects
- Animals, Animals, Genetically Modified, Brain pathology, Brain Injuries, Traumatic genetics, Brain Injuries, Traumatic pathology, Case-Control Studies, DNA-Binding Proteins genetics, Disease Models, Animal, Drosophila Proteins genetics, Drosophila melanogaster genetics, GTPase-Activating Proteins genetics, GTPase-Activating Proteins metabolism, HEK293 Cells, Humans, Longevity, Male, Membrane Glycoproteins metabolism, Motor Activity, Nuclear Pore genetics, Nuclear Pore pathology, Nuclear Pore Complex Proteins metabolism, Protein Aggregates, Protein Aggregation, Pathological, Rats, Sprague-Dawley, TDP-43 Proteinopathies genetics, TDP-43 Proteinopathies pathology, Rats, Active Transport, Cell Nucleus, Brain metabolism, Brain Injuries, Traumatic metabolism, DNA-Binding Proteins metabolism, Drosophila Proteins metabolism, Drosophila melanogaster metabolism, Nuclear Pore metabolism, TDP-43 Proteinopathies metabolism
- Abstract
Traumatic brain injury (TBI) is a predisposing factor for many neurodegenerative diseases, including amyotrophic lateral sclerosis (ALS), Alzheimer's disease (AD), Parkinson's disease (PD), and chronic traumatic encephalopathy (CTE). Although defects in nucleocytoplasmic transport (NCT) is reported ALS and other neurodegenerative diseases, whether defects in NCT occur in TBI remains unknown. We performed proteomic analysis on Drosophila exposed to repeated TBI and identified resultant alterations in several novel molecular pathways. TBI upregulated nuclear pore complex (NPC) and nucleocytoplasmic transport (NCT) proteins as well as alter nucleoporin stability. Traumatic injury disrupted RanGAP1 and NPC protein distribution in flies and a rat model and led to coaggregation of NPC components and TDP-43. In addition, trauma-mediated NCT defects and lethality are rescued by nuclear export inhibitors. Importantly, genetic upregulation of nucleoporins in vivo and in vitro triggered TDP-43 cytoplasmic mislocalization, aggregation, and altered solubility and reduced motor function and lifespan of animals. We also found NUP62 pathology and elevated NUP62 concentrations in postmortem brain tissues of patients with mild or severe CTE as well as co-localization of NUP62 and TDP-43 in CTE. These findings indicate that TBI leads to NCT defects, which potentially mediate the TDP-43 pathology in CTE., Competing Interests: EA, AM, SK, JC, NR, AG, JS, CE, WO, CD, JC, AK, JK, TS, UP No competing interests declared, (© 2021, Anderson et al.)
- Published
- 2021
- Full Text
- View/download PDF
32. Loss of function mutations in GEMIN5 cause a neurodevelopmental disorder.
- Author
-
Kour S, Rajan DS, Fortuna TR, Anderson EN, Ward C, Lee Y, Lee S, Shin YB, Chae JH, Choi M, Siquier K, Cantagrel V, Amiel J, Stolerman ES, Barnett SS, Cousin MA, Castro D, McDonald K, Kirmse B, Nemeth AH, Rajasundaram D, Innes AM, Lynch D, Frosk P, Collins A, Gibbons M, Yang M, Desguerre I, Boddaert N, Gitiaux C, Rydning SL, Selmer KK, Urreizti R, Garcia-Oguiza A, Osorio AN, Verdura E, Pujol A, McCurry HR, Landers JE, Agnihotri S, Andriescu EC, Moody SB, Phornphutkul C, Sacoto MJG, Begtrup A, Houlden H, Kirschner J, Schorling D, Rudnik-Schöneborn S, Strom TM, Leiz S, Juliette K, Richardson R, Yang Y, Zhang Y, Wang M, Wang J, Wang X, Platzer K, Donkervoort S, Bönnemann CG, Wagner M, Issa MY, Elbendary HM, Stanley V, Maroofian R, Gleeson JG, Zaki MS, Senderek J, and Pandey UB
- Subjects
- Alleles, Amino Acid Sequence, Animals, Child, Preschool, Developmental Disabilities genetics, Drosophila genetics, Drosophila growth & development, Female, Gene Knockdown Techniques, Gene Ontology, HEK293 Cells, Humans, Loss of Function Mutation, Male, Muscle Hypotonia genetics, Myoclonic Cerebellar Dyssynergia genetics, Neurodevelopmental Disorders diagnostic imaging, Neurodevelopmental Disorders genetics, Neurodevelopmental Disorders physiopathology, Pedigree, Polymorphism, Single Nucleotide, RNA-Seq, Ribonucleoproteins, Small Nuclear genetics, Rigor Mortis genetics, SMN Complex Proteins metabolism, Gene Expression Regulation, Developmental genetics, Induced Pluripotent Stem Cells metabolism, Neurodevelopmental Disorders metabolism, Neurons metabolism, Ribonucleoproteins, Small Nuclear metabolism, SMN Complex Proteins genetics
- Abstract
GEMIN5, an RNA-binding protein is essential for assembly of the survival motor neuron (SMN) protein complex and facilitates the formation of small nuclear ribonucleoproteins (snRNPs), the building blocks of spliceosomes. Here, we have identified 30 affected individuals from 22 unrelated families presenting with developmental delay, hypotonia, and cerebellar ataxia harboring biallelic variants in the GEMIN5 gene. Mutations in GEMIN5 perturb the subcellular distribution, stability, and expression of GEMIN5 protein and its interacting partners in patient iPSC-derived neurons, suggesting a potential loss-of-function mechanism. GEMIN5 mutations result in disruption of snRNP complex assembly formation in patient iPSC neurons. Furthermore, knock down of rigor mortis, the fly homolog of human GEMIN5, leads to developmental defects, motor dysfunction, and a reduced lifespan. Interestingly, we observed that GEMIN5 variants disrupt a distinct set of transcripts and pathways as compared to SMA patient neurons, suggesting different molecular pathomechanisms. These findings collectively provide evidence that pathogenic variants in GEMIN5 perturb physiological functions and result in a neurodevelopmental delay and ataxia syndrome.
- Published
- 2021
- Full Text
- View/download PDF
33. Huntingtin-mediated axonal transport requires arginine methylation by PRMT6.
- Author
-
Migazzi A, Scaramuzzino C, Anderson EN, Tripathy D, Hernández IH, Grant RA, Roccuzzo M, Tosatto L, Virlogeux A, Zuccato C, Caricasole A, Ratovitski T, Ross CA, Pandey UB, Lucas JJ, Saudou F, Pennuto M, and Basso M
- Subjects
- Amino Acid Sequence, Animals, Arginine metabolism, Brain-Derived Neurotrophic Factor genetics, Brain-Derived Neurotrophic Factor metabolism, Cell Death, Disease Models, Animal, Drosophila melanogaster genetics, Drosophila melanogaster metabolism, Genes, Reporter, Green Fluorescent Proteins genetics, Green Fluorescent Proteins metabolism, HEK293 Cells, Humans, Huntingtin Protein metabolism, Huntington Disease metabolism, Huntington Disease pathology, Methylation, Mice, Mice, Transgenic, Neuromuscular Junction genetics, Neuromuscular Junction metabolism, Neuromuscular Junction pathology, Neurons metabolism, Neurons pathology, Nuclear Proteins metabolism, Protein Isoforms genetics, Protein Isoforms metabolism, Protein-Arginine N-Methyltransferases metabolism, Transport Vesicles genetics, Transport Vesicles pathology, Axonal Transport genetics, Epigenesis, Genetic, Huntingtin Protein genetics, Huntington Disease genetics, Nuclear Proteins genetics, Protein-Arginine N-Methyltransferases genetics, Transport Vesicles metabolism
- Abstract
The huntingtin (HTT) protein transports various organelles, including vesicles containing neurotrophic factors, from embryonic development throughout life. To better understand how HTT mediates axonal transport and why this function is disrupted in Huntington's disease (HD), we study vesicle-associated HTT and find that it is dimethylated at a highly conserved arginine residue (R118) by the protein arginine methyltransferase 6 (PRMT6). Without R118 methylation, HTT associates less with vesicles, anterograde trafficking is diminished, and neuronal death ensues-very similar to what occurs in HD. Inhibiting PRMT6 in HD cells and neurons exacerbates mutant HTT (mHTT) toxicity and impairs axonal trafficking, whereas overexpressing PRMT6 restores axonal transport and neuronal viability, except in the presence of a methylation-defective variant of mHTT. In HD flies, overexpressing PRMT6 rescues axonal defects and eclosion. Arginine methylation thus regulates HTT-mediated vesicular transport along the axon, and increasing HTT methylation could be of therapeutic interest for HD., Competing Interests: Declaration of interests The authors declare no competing interests., (Copyright © 2021 The Authors. Published by Elsevier Inc. All rights reserved.)
- Published
- 2021
- Full Text
- View/download PDF
34. Impairment of the mitochondrial one-carbon metabolism enzyme SHMT2 causes a novel brain and heart developmental syndrome.
- Author
-
García-Cazorla À, Verdura E, Juliá-Palacios N, Anderson EN, Goicoechea L, Planas-Serra L, Tsogtbaatar E, Dsouza NR, Schlüter A, Urreizti R, Tarnowski JM, Gavrilova RH, Ruiz M, Rodríguez-Palmero A, Fourcade S, Cogné B, Besnard T, Vincent M, Bézieau S, Folmes CD, Zimmermann MT, Klee EW, Pandey UB, Artuch R, Cousin MA, and Pujol A
- Subjects
- Brain pathology, Carbon metabolism, Female, Humans, Magnetic Resonance Imaging methods, Male, Syndrome, Brain growth & development, Glycine Hydroxymethyltransferase genetics, Heart growth & development, Malformations of Cortical Development genetics, Mitochondria metabolism
- Published
- 2020
- Full Text
- View/download PDF
35. Optogenetic TDP-43 nucleation induces persistent insoluble species and progressive motor dysfunction in vivo.
- Author
-
Otte CG, Fortuna TR, Mann JR, Gleixner AM, Ramesh N, Pyles NJ, Pandey UB, and Donnelly CJ
- Subjects
- Animals, Cell Nucleus metabolism, DNA-Binding Proteins metabolism, Drosophila, Frontotemporal Dementia pathology, Neurodegenerative Diseases genetics, Neurodegenerative Diseases metabolism, Neurons metabolism, Optogenetics methods, Frontotemporal Dementia genetics, Inclusion Bodies metabolism, Mutation genetics, TDP-43 Proteinopathies genetics
- Abstract
TDP-43 is a predominantly nuclear DNA/RNA binding protein that is often mislocalized into insoluble cytoplasmic inclusions in post-mortem patient tissue in a variety of neurodegenerative disorders including Amyotrophic Lateral Sclerosis (ALS) and Frontotemporal dementia (FTD). The underlying causes of TDP-43 proteinopathies remain unclear, but recent studies indicate the formation of these protein assemblies is driven by aberrant phase transitions of RNA deficient TDP-43. Technical limitations have prevented our ability to understand how TDP-43 proteinopathy relates to disease pathogenesis. Current animal models of TDP-43 proteinopathy often rely on overexpression of wild-type TDP-43 to non-physiological levels that may initiate neurotoxicity through nuclear gain of function mechanisms, or by the expression of disease-causing mutations found in only a fraction of ALS patients. New technologies allowing for light-responsive control of subcellular protein crowding provide a promising approach to drive intracellular protein aggregation, as we have previously demonstrated in vitro. Here we present a model for the optogenetic induction of TDP-43 proteinopathy in Drosophila that recapitulates key features of patient pathology, including detergent insoluble cytoplamsic inclusions and progressive motor dysfunction., (Copyright © 2020. Published by Elsevier Inc.)
- Published
- 2020
- Full Text
- View/download PDF
36. RNA dependent suppression of C9orf72 ALS/FTD associated neurodegeneration by Matrin-3.
- Author
-
Ramesh N, Daley EL, Gleixner AM, Mann JR, Kour S, Mawrie D, Anderson EN, Kofler J, Donnelly CJ, Kiskinis E, and Pandey UB
- Subjects
- Aged, Amyotrophic Lateral Sclerosis metabolism, Amyotrophic Lateral Sclerosis pathology, Animals, Animals, Genetically Modified, C9orf72 Protein metabolism, DNA Repeat Expansion, Drosophila, Female, Frontotemporal Dementia genetics, Frontotemporal Dementia metabolism, Frontotemporal Dementia pathology, Humans, Induced Pluripotent Stem Cells metabolism, Male, Middle Aged, Motor Neurons pathology, Nuclear Matrix-Associated Proteins metabolism, RNA-Binding Proteins metabolism, Amyotrophic Lateral Sclerosis genetics, C9orf72 Protein genetics, Motor Neurons metabolism, Nuclear Matrix-Associated Proteins genetics, RNA metabolism, RNA-Binding Proteins genetics
- Abstract
The most common genetic cause of amyotrophic lateral sclerosis (ALS) is a GGGGCC (G4C2) hexanucleotide repeat expansions in first intron of the C9orf72 gene. The accumulation of repetitive RNA sequences can mediate toxicity potentially through the formation of intranuclear RNA foci that sequester key RNA-binding proteins (RBPs), and non-ATG mediated translation into toxic dipeptide protein repeats. However, the contribution of RBP sequestration to the mechanisms underlying RNA-mediated toxicity remain unknown. Here we show that the ALS-associated RNA-binding protein, Matrin-3 (MATR3), colocalizes with G4C2 RNA foci in patient tissues as well as iPSC-derived motor neurons harboring the C9orf72 mutation. Hyperexpansion of C9 repeats perturbed subcellular distribution and levels of endogenous MATR3 in C9-ALS patient-derived motor neurons. Interestingly, we observed that ectopic expression of human MATR3 strongly mitigates G4C2-mediated neurodegeneration in vivo. MATR3-mediated suppression of C9 toxicity was dependent on the RNA-binding domain of MATR3. Importantly, we found that expression of MATR3 reduced the levels of RAN-translation products in mammalian cells in an RNA-dependent manner. Finally, we have shown that knocking down endogenous MATR3 in C9-ALS patient-derived iPSC neurons decreased the presence of G4C2 RNA foci in the nucleus. Overall, these studies suggest that MATR3 genetically modifies the neuropathological and the pathobiology of C9orf72 ALS through modulating the RNA foci and RAN translation.
- Published
- 2020
- Full Text
- View/download PDF
37. RNA-recognition motif in Matrin-3 mediates neurodegeneration through interaction with hnRNPM.
- Author
-
Ramesh N, Kour S, Anderson EN, Rajasundaram D, and Pandey UB
- Subjects
- Amyotrophic Lateral Sclerosis metabolism, Animals, Animals, Genetically Modified, Drosophila, Drosophila Proteins metabolism, Heterogeneous-Nuclear Ribonucleoproteins metabolism, Humans, Mice, Nerve Degeneration pathology, RNA-Binding Motifs physiology, Amyotrophic Lateral Sclerosis pathology, Heterogeneous-Nuclear Ribonucleoprotein Group M metabolism, Nerve Degeneration metabolism, Nuclear Matrix-Associated Proteins metabolism, RNA-Binding Proteins metabolism
- Abstract
Background: Amyotrophic lateral sclerosis (ALS) is an adult-onset, fatal neurodegenerative disease characterized by progressive loss of upper and lower motor neurons. While pathogenic mutations in the DNA/RNA-binding protein Matrin-3 (MATR3) are linked to ALS and distal myopathy, the molecular mechanisms underlying MATR3-mediated neuromuscular degeneration remain unclear., Methods: We generated Drosophila lines with transgenic insertion of human MATR3 wildtype, disease-associated variants F115C and S85C, and deletion variants in functional domains, ΔRRM1, ΔRRM2, ΔZNF1 and ΔZNF2. We utilized genetic, behavioral and biochemical tools for comprehensive characterization of our models in vivo and in vitro. Additionally, we employed in silico approaches to find transcriptomic targets of MATR3 and hnRNPM from publicly available eCLIP datasets., Results: We found that targeted expression of MATR3 in Drosophila muscles or motor neurons shorten lifespan and produces progressive motor defects, muscle degeneration and atrophy. Strikingly, deletion of its RNA-recognition motif (RRM2) mitigates MATR3 toxicity. We identified rump, the Drosophila homolog of human RNA-binding protein hnRNPM, as a modifier of mutant MATR3 toxicity in vivo. Interestingly, hnRNPM physically and functionally interacts with MATR3 in an RNA-dependent manner in mammalian cells. Furthermore, common RNA targets of MATR3 and hnRNPM converge in biological processes important for neuronal health and survival., Conclusions: We propose a model of MATR3-mediated neuromuscular degeneration governed by its RNA-binding domains and modulated by interaction with splicing factor hnRNPM.
- Published
- 2020
- Full Text
- View/download PDF
38. Inactivation of Hippo and cJun-N-terminal Kinase (JNK) signaling mitigate FUS mediated neurodegeneration in vivo.
- Author
-
Gogia N, Sarkar A, Mehta AS, Ramesh N, Deshpande P, Kango-Singh M, Pandey UB, and Singh A
- Subjects
- Animals, Axons metabolism, Cytoplasm metabolism, Disease Models, Animal, Drosophila metabolism, Drosophila Proteins metabolism, Intracellular Signaling Peptides and Proteins metabolism, Motor Neurons metabolism, Mutation, Neuromuscular Junction metabolism, Phenotype, Protein Serine-Threonine Kinases metabolism, Protein Transport, Signal Transduction, Amyotrophic Lateral Sclerosis metabolism, MAP Kinase Kinase 4 metabolism, Nerve Degeneration metabolism, RNA-Binding Protein FUS metabolism
- Abstract
Amyotrophic Lateral Sclerosis (ALS), a late-onset neurodegenerative disorder characterized by the loss of motor neurons in the central nervous system, has no known cure to-date. Disease causing mutations in human Fused in Sarcoma (FUS) leads to aggressive and juvenile onset of ALS. FUS is a well-conserved protein across different species, which plays a crucial role in regulating different aspects of RNA metabolism. Targeted misexpression of FUS in Drosophila model recapitulates several interesting phenotypes relevant to ALS including cytoplasmic mislocalization, defects at the neuromuscular junction and motor dysfunction. We screened for the genetic modifiers of human FUS-mediated neurodegenerative phenotype using molecularly defined deficiencies. We identified hippo (hpo), a component of the evolutionarily conserved Hippo growth regulatory pathway, as a genetic modifier of FUS mediated neurodegeneration. Gain-of-function of hpo triggers cell death whereas its loss-of-function promotes cell proliferation. Downregulation of the Hippo signaling pathway, using mutants of Hippo signaling, exhibit rescue of FUS-mediated neurodegeneration in the Drosophila eye, as evident from reduction in the number of TUNEL positive nuclei as well as rescue of axonal targeting from the retina to the brain. The Hippo pathway activates c-Jun amino-terminal (NH
2 ) Kinase (JNK) mediated cell death. We found that downregulation of JNK signaling is sufficient to rescue FUS-mediated neurodegeneration in the Drosophila eye. Our study elucidates that Hippo signaling and JNK signaling are activated in response to FUS accumulation to induce neurodegeneration. These studies will shed light on the genetic mechanism involved in neurodegeneration observed in ALS and other associated disorders., Competing Interests: Declaration of Competing Interest None., (Copyright © 2020 The Authors. Published by Elsevier Inc. All rights reserved.)- Published
- 2020
- Full Text
- View/download PDF
39. Nucleocytoplasmic Proteomic Analysis Uncovers eRF1 and Nonsense-Mediated Decay as Modifiers of ALS/FTD C9orf72 Toxicity.
- Author
-
Ortega JA, Daley EL, Kour S, Samani M, Tellez L, Smith HS, Hall EA, Esengul YT, Tsai YH, Gendron TF, Donnelly CJ, Siddique T, Savas JN, Pandey UB, and Kiskinis E
- Subjects
- Amyotrophic Lateral Sclerosis metabolism, Animals, C9orf72 Protein metabolism, Cell Fractionation, Drosophila Proteins metabolism, Drosophila melanogaster, Frontotemporal Dementia metabolism, HEK293 Cells, Humans, Induced Pluripotent Stem Cells, Nuclear Envelope, Peptide Chain Termination, Translational genetics, Peptide Termination Factors metabolism, Protein Biosynthesis, Proteome, Subcellular Fractions, Tandem Mass Spectrometry, Amyotrophic Lateral Sclerosis genetics, C9orf72 Protein genetics, Drosophila Proteins genetics, Frontotemporal Dementia genetics, Neurons metabolism, Nonsense Mediated mRNA Decay genetics, Peptide Termination Factors genetics, RNA, Messenger metabolism
- Abstract
The most common genetic cause of amyotrophic lateral sclerosis (ALS) and frontotemporal dementia (FTD) is a hexanucleotide repeat expansion in C9orf72 (C9-HRE). While RNA and dipeptide repeats produced by C9-HRE disrupt nucleocytoplasmic transport, the proteins that become redistributed remain unknown. Here, we utilized subcellular fractionation coupled with tandem mass spectrometry and identified 126 proteins, enriched for protein translation and RNA metabolism pathways, which collectively drive a shift toward a more cytosolic proteome in C9-HRE cells. Among these was eRF1, which regulates translation termination and nonsense-mediated decay (NMD). eRF1 accumulates within elaborate nuclear envelope invaginations in patient induced pluripotent stem cell (iPSC) neurons and postmortem tissue and mediates a protective shift from protein translation to NMD-dependent mRNA degradation. Overexpression of eRF1 and the NMD driver UPF1 ameliorate C9-HRE toxicity in vivo. Our findings provide a resource for proteome-wide nucleocytoplasmic alterations across neurodegeneration-associated repeat expansion mutations and highlight eRF1 and NMD as therapeutic targets in C9orf72-associated ALS and/or FTD., Competing Interests: Declaration of Interests The authors declare no competing interests., (Copyright © 2020 Elsevier Inc. All rights reserved.)
- Published
- 2020
- Full Text
- View/download PDF
40. Insulin-like growth factor 1 signaling in motor neuron and polyglutamine diseases: From molecular pathogenesis to therapeutic perspectives.
- Author
-
Pennuto M, Pandey UB, and Polanco MJ
- Subjects
- Amyotrophic Lateral Sclerosis physiopathology, Animals, Glutamine genetics, Humans, Insulin-Like Growth Factor I genetics, MAP Kinase Signaling System physiology, Muscular Atrophy, Spinal physiopathology, Neurodegenerative Diseases drug therapy, Phosphatidylinositol 3-Kinases metabolism, Proto-Oncogene Proteins c-akt metabolism, ras Proteins metabolism, Insulin-Like Growth Factor I physiology, Motor Neurons metabolism, Neurodegenerative Diseases physiopathology, Peptides, Signal Transduction physiology
- Abstract
The pleiotropic peptide insulin-like growth factor 1 (IGF-I) regulates human body homeostasis and cell growth. IGF-I activates two major signaling pathways, namely phosphoinositide-3-kinase (PI3K)/protein kinase B (PKB/Akt) and Ras/extracellular signal-regulated kinase (ERK), which contribute to brain development, metabolism and function as well as to neuronal maintenance and survival. In this review, we discuss the general and tissue-specific effects of the IGF-I pathways. In addition, we present a comprehensive overview examining the role of IGF-I in neurodegenerative diseases, such as spinal and muscular atrophy, amyotrophic lateral sclerosis, and polyglutamine diseases. In each disease, we analyze the disturbances of the IGF-I pathway, the modification of the disease protein by IGF-I signaling, and the therapeutic strategies based on the use of IGF-I developed to date. Lastly, we highlight present and future considerations in the use of IGF-I for the treatment of these disorders., Competing Interests: Declaration of Competing Interest The authors have no conflict of interest to declare., (Copyright © 2020 Elsevier Inc. All rights reserved.)
- Published
- 2020
- Full Text
- View/download PDF
41. Polyglutamine-Expanded Androgen Receptor Alteration of Skeletal Muscle Homeostasis and Myonuclear Aggregation Are Affected by Sex, Age and Muscle Metabolism.
- Author
-
Chivet M, Marchioretti C, Pirazzini M, Piol D, Scaramuzzino C, Polanco MJ, Romanello V, Zuccaro E, Parodi S, D'Antonio M, Rinaldi C, Sambataro F, Pegoraro E, Soraru G, Pandey UB, Sandri M, Basso M, and Pennuto M
- Subjects
- Animals, Cell Aggregation, Denervation, Inclusion Bodies metabolism, Mice, Transgenic, Mitochondria pathology, Motor Activity, Muscle, Skeletal innervation, Muscle, Skeletal pathology, Muscle, Skeletal physiopathology, Muscular Atrophy pathology, Muscular Atrophy physiopathology, Muscular Atrophy, Spinal pathology, Neuromuscular Junction pathology, Aging metabolism, Homeostasis, Muscle, Skeletal metabolism, Peptides metabolism, Receptors, Androgen metabolism, Sex Characteristics
- Abstract
Polyglutamine (polyQ) expansions in the androgen receptor (AR) gene cause spinal and bulbar muscular atrophy (SBMA), a neuromuscular disease characterized by lower motor neuron (MN) loss and skeletal muscle atrophy, with an unknown mechanism. We generated new mouse models of SBMA for constitutive and inducible expression of mutant AR and performed biochemical, histological and functional analyses of phenotype. We show that polyQ-expanded AR causes motor dysfunction, premature death, IIb-to-IIa/IIx fiber-type change, glycolytic-to-oxidative fiber-type switching, upregulation of atrogenes and autophagy genes and mitochondrial dysfunction in skeletal muscle, together with signs of muscle denervation at late stage of disease. PolyQ expansions in the AR resulted in nuclear enrichment. Within the nucleus, mutant AR formed 2% sodium dodecyl sulfate (SDS)-resistant aggregates and inclusion bodies in myofibers, but not spinal cord and brainstem, in a process exacerbated by age and sex. Finally, we found that two-week induction of expression of polyQ-expanded AR in adult mice was sufficient to cause premature death, body weight loss and muscle atrophy, but not aggregation, metabolic alterations, motor coordination and fiber-type switch, indicating that expression of the disease protein in the adulthood is sufficient to recapitulate several, but not all SBMA manifestations in mice. These results imply that chronic expression of polyQ-expanded AR, i.e. during development and prepuberty, is key to induce the full SBMA muscle pathology observed in patients. Our data support a model whereby chronic expression of polyQ-expanded AR triggers muscle atrophy through toxic (neomorphic) gain of function mechanisms distinct from normal (hypermorphic) gain of function mechanisms., Competing Interests: The authors declare no conflict of interest.
- Published
- 2020
- Full Text
- View/download PDF
42. Muscleblind acts as a modifier of FUS toxicity by modulating stress granule dynamics and SMN localization.
- Author
-
Casci I, Krishnamurthy K, Kour S, Tripathy V, Ramesh N, Anderson EN, Marrone L, Grant RA, Oliver S, Gochenaur L, Patel K, Sterneckert J, Gleixner AM, Donnelly CJ, Ruepp MD, Sini AM, Zuccaro E, Pennuto M, Pasinelli P, and Pandey UB
- Subjects
- Acetyltransferases genetics, Acetyltransferases metabolism, Amyotrophic Lateral Sclerosis genetics, Animals, Cytoplasm metabolism, Cytoplasmic Granules metabolism, Drosophila genetics, Drosophila metabolism, Female, HEK293 Cells, Humans, Induced Pluripotent Stem Cells metabolism, Membrane Proteins genetics, Membrane Proteins metabolism, Motor Neurons metabolism, Mutation, Phenotype, RNA-Binding Protein FUS genetics, RNA-Binding Protein FUS toxicity, SMN Complex Proteins genetics, Transcription Factors metabolism, Amyotrophic Lateral Sclerosis metabolism, Drosophila Proteins metabolism, Nuclear Proteins metabolism, RNA-Binding Protein FUS metabolism, SMN Complex Proteins metabolism
- Abstract
Mutations in fused in sarcoma (FUS) lead to amyotrophic lateral sclerosis (ALS) with varying ages of onset, progression and severity. This suggests that unknown genetic factors contribute to disease pathogenesis. Here we show the identification of muscleblind as a novel modifier of FUS-mediated neurodegeneration in vivo. Muscleblind regulates cytoplasmic mislocalization of mutant FUS and subsequent accumulation in stress granules, dendritic morphology and toxicity in mammalian neuronal and human iPSC-derived neurons. Interestingly, genetic modulation of endogenous muscleblind was sufficient to restore survival motor neuron (SMN) protein localization in neurons expressing pathogenic mutations in FUS, suggesting a potential mode of suppression of FUS toxicity. Upregulation of SMN suppressed FUS toxicity in Drosophila and primary cortical neurons, indicating a link between FUS and SMN. Our data provide in vivo evidence that muscleblind is a dominant modifier of FUS-mediated neurodegeneration by regulating FUS-mediated ALS pathogenesis.
- Published
- 2019
- Full Text
- View/download PDF
43. FUS pathology in ALS is linked to alterations in multiple ALS-associated proteins and rescued by drugs stimulating autophagy.
- Author
-
Marrone L, Drexler HCA, Wang J, Tripathi P, Distler T, Heisterkamp P, Anderson EN, Kour S, Moraiti A, Maharana S, Bhatnagar R, Belgard TG, Tripathy V, Kalmbach N, Hosseinzadeh Z, Crippa V, Abo-Rady M, Wegner F, Poletti A, Troost D, Aronica E, Busskamp V, Weis J, Pandey UB, Hyman AA, Alberti S, Goswami A, and Sterneckert J
- Subjects
- Cytoplasm metabolism, Humans, Inclusion Bodies pathology, Induced Pluripotent Stem Cells pathology, Mutation genetics, RNA-Binding Protein FUS metabolism, Amyotrophic Lateral Sclerosis pathology, Autophagy physiology, Motor Neurons pathology
- Abstract
Amyotrophic lateral sclerosis (ALS) is a lethal disease characterized by motor neuron degeneration and associated with aggregation of nuclear RNA-binding proteins (RBPs), including FUS. How FUS aggregation and neurodegeneration are prevented in healthy motor neurons remain critically unanswered questions. Here, we use a combination of ALS patient autopsy tissue and induced pluripotent stem cell-derived neurons to study the effects of FUS mutations on RBP homeostasis. We show that FUS' tendency to aggregate is normally buffered by interacting RBPs, but this buffering is lost when FUS mislocalizes to the cytoplasm due to ALS mutations. The presence of aggregation-prone FUS in the cytoplasm causes imbalances in RBP homeostasis that exacerbate neurodegeneration. However, enhancing autophagy using small molecules reduces cytoplasmic FUS, restores RBP homeostasis and rescues motor function in vivo. We conclude that disruption of RBP homeostasis plays a critical role in FUS-ALS and can be treated by stimulating autophagy.
- Published
- 2019
- Full Text
- View/download PDF
44. RNA Binding Antagonizes Neurotoxic Phase Transitions of TDP-43.
- Author
-
Mann JR, Gleixner AM, Mauna JC, Gomes E, DeChellis-Marks MR, Needham PG, Copley KE, Hurtle B, Portz B, Pyles NJ, Guo L, Calder CB, Wills ZP, Pandey UB, Kofler JK, Brodsky JL, Thathiah A, Shorter J, and Donnelly CJ
- Subjects
- Amyotrophic Lateral Sclerosis metabolism, Frontotemporal Dementia metabolism, HEK293 Cells, Humans, Inclusion Bodies, Oligonucleotides, Optogenetics, Cytoplasmic Granules metabolism, DNA-Binding Proteins metabolism, Neurons metabolism, Phase Transition, RNA metabolism, Stress, Physiological, TDP-43 Proteinopathies metabolism
- Abstract
TDP-43 proteinopathy is a pathological hallmark of amyotrophic lateral sclerosis and frontotemporal dementia where cytoplasmic TDP-43 inclusions are observed within degenerating regions of patient postmortem tissue. The mechanism by which TDP-43 aggregates has remained elusive due to technological limitations, which prevent the analysis of specific TDP-43 interactions in live cells. We present an optogenetic approach to reliably induce TDP-43 proteinopathy under spatiotemporal control. We show that the formation of pathologically relevant inclusions is driven by aberrant interactions between low-complexity domains of TDP-43 that are antagonized by RNA binding. Although stress granules are hypothesized to be a conduit for seeding TDP-43 proteinopathy, we demonstrate pathological inclusions outside these RNA-rich structures. Furthermore, we show that aberrant phase transitions of cytoplasmic TDP-43 are neurotoxic and that treatment with oligonucleotides composed of TDP-43 target sequences prevent inclusions and rescue neurotoxicity. Collectively, these studies provide insight into the mechanisms that underlie TDP-43 proteinopathy and present a potential avenue for therapeutic intervention., (Copyright © 2019 Elsevier Inc. All rights reserved.)
- Published
- 2019
- Full Text
- View/download PDF
45. Dual Inhibition of GSK3β and CDK5 Protects the Cytoskeleton of Neurons from Neuroinflammatory-Mediated Degeneration In Vitro and In Vivo.
- Author
-
Reinhardt L, Kordes S, Reinhardt P, Glatza M, Baumann M, Drexler HCA, Menninger S, Zischinsky G, Eickhoff J, Fröb C, Bhattarai P, Arulmozhivarman G, Marrone L, Janosch A, Adachi K, Stehling M, Anderson EN, Abo-Rady M, Bickle M, Pandey UB, Reimer MM, Kizil C, Schöler HR, Nussbaumer P, Klebl B, and Sterneckert JL
- Subjects
- Alzheimer Disease drug therapy, Alzheimer Disease metabolism, Animals, Cytoskeleton drug effects, Humans, Inflammation drug therapy, Microtubules drug effects, Microtubules metabolism, Nerve Degeneration drug therapy, Neurites drug effects, Neurites metabolism, Neurons drug effects, Neuroprotective Agents pharmacology, Phosphorylation drug effects, Signal Transduction drug effects, Zebrafish metabolism, Cyclin-Dependent Kinase 5 metabolism, Cytoskeleton metabolism, Glycogen Synthase Kinase 3 beta metabolism, Inflammation metabolism, Nerve Degeneration metabolism, Neurons metabolism
- Abstract
Neuroinflammation is a hallmark of neurological disorders and is accompanied by the production of neurotoxic agents such as nitric oxide. We used stem cell-based phenotypic screening and identified small molecules that directly protected neurons from neuroinflammation-induced degeneration. We demonstrate that inhibition of CDK5 is involved in, but not sufficient for, neuroprotection. Instead, additional inhibition of GSK3β is required to enhance the neuroprotective effects of CDK5 inhibition, which was confirmed using short hairpin RNA-mediated knockdown of CDK5 and GSK3β. Quantitative phosphoproteomics and high-content imaging demonstrate that neurite degeneration is mediated by aberrant phosphorylation of multiple microtubule-associated proteins. Finally, we show that our hit compound protects neurons in vivo in zebrafish models of motor neuron degeneration and Alzheimer's disease. Thus, we demonstrate an overlap of CDK5 and GSK3β in mediating the regulation of the neuronal cytoskeleton and that our hit compound LDC8 represents a promising starting point for neuroprotective drugs., (Copyright © 2019 The Author(s). Published by Elsevier Inc. All rights reserved.)
- Published
- 2019
- Full Text
- View/download PDF
46. RNP-Granule Assembly via Ataxin-2 Disordered Domains Is Required for Long-Term Memory and Neurodegeneration.
- Author
-
Bakthavachalu B, Huelsmeier J, Sudhakaran IP, Hillebrand J, Singh A, Petrauskas A, Thiagarajan D, Sankaranarayanan M, Mizoue L, Anderson EN, Pandey UB, Ross E, VijayRaghavan K, Parker R, and Ramaswami M
- Subjects
- Animals, Amyotrophic Lateral Sclerosis genetics, C9orf72 Protein, Drosophila, Fertility, Heterogeneous-Nuclear Ribonucleoprotein Group F-H, Smell, Spinocerebellar Ataxias genetics, Survival, Disease Models, Animal, Ataxin-2 genetics, Ataxin-2 metabolism, Cytoplasmic Granules metabolism, Drosophila Proteins genetics, Drosophila Proteins metabolism, Intrinsically Disordered Proteins genetics, Intrinsically Disordered Proteins metabolism, Memory, Long-Term, Neurodegenerative Diseases genetics, Ribonucleoproteins metabolism
- Abstract
Human Ataxin-2 is implicated in the cause and progression of amyotrophic lateral sclerosis (ALS) and type 2 spinocerebellar ataxia (SCA-2). In Drosophila, a conserved atx2 gene is essential for animal survival as well as for normal RNP-granule assembly, translational control, and long-term habituation. Like its human homolog, Drosophila Ataxin-2 (Atx2) contains polyQ repeats and additional intrinsically disordered regions (IDRs). We demonstrate that Atx2 IDRs, which are capable of mediating liquid-liquid phase transitions in vitro, are essential for efficient formation of neuronal mRNP assemblies in vivo. Remarkably, ΔIDR mutants that lack neuronal RNP granules show normal animal development, survival, and fertility. However, they show defects in long-term memory formation/consolidation as well as in C9ORF72 dipeptide repeat or FUS-induced neurodegeneration. Together, our findings demonstrate (1) that higher-order mRNP assemblies contribute to long-term neuronal plasticity and memory, and (2) that a targeted reduction in RNP-granule formation efficiency can alleviate specific forms of neurodegeneration., (Copyright © 2018 Elsevier Inc. All rights reserved.)
- Published
- 2018
- Full Text
- View/download PDF
47. Nuclear-Import Receptors Reverse Aberrant Phase Transitions of RNA-Binding Proteins with Prion-like Domains.
- Author
-
Guo L, Kim HJ, Wang H, Monaghan J, Freyermuth F, Sung JC, O'Donovan K, Fare CM, Diaz Z, Singh N, Zhang ZC, Coughlin M, Sweeny EA, DeSantis ME, Jackrel ME, Rodell CB, Burdick JA, King OD, Gitler AD, Lagier-Tourenne C, Pandey UB, Chook YM, Taylor JP, and Shorter J
- Subjects
- Adult, Aged, Animals, Cytoplasm chemistry, DNA-Binding Proteins chemistry, Drosophila melanogaster, Female, Green Fluorescent Proteins chemistry, HEK293 Cells, HeLa Cells, Homeostasis, Humans, Karyopherins chemistry, Male, Middle Aged, Molecular Chaperones chemistry, Mutation, Neurodegenerative Diseases pathology, Protein Domains, RNA-Binding Protein EWS chemistry, TATA-Binding Protein Associated Factors chemistry, beta Karyopherins chemistry, Active Transport, Cell Nucleus, Prions chemistry, RNA-Binding Proteins chemistry, Receptors, Cytoplasmic and Nuclear chemistry
- Abstract
RNA-binding proteins (RBPs) with prion-like domains (PrLDs) phase transition to functional liquids, which can mature into aberrant hydrogels composed of pathological fibrils that underpin fatal neurodegenerative disorders. Several nuclear RBPs with PrLDs, including TDP-43, FUS, hnRNPA1, and hnRNPA2, mislocalize to cytoplasmic inclusions in neurodegenerative disorders, and mutations in their PrLDs can accelerate fibrillization and cause disease. Here, we establish that nuclear-import receptors (NIRs) specifically chaperone and potently disaggregate wild-type and disease-linked RBPs bearing a NLS. Karyopherin-β2 (also called Transportin-1) engages PY-NLSs to inhibit and reverse FUS, TAF15, EWSR1, hnRNPA1, and hnRNPA2 fibrillization, whereas Importin-α plus Karyopherin-β1 prevent and reverse TDP-43 fibrillization. Remarkably, Karyopherin-β2 dissolves phase-separated liquids and aberrant fibrillar hydrogels formed by FUS and hnRNPA1. In vivo, Karyopherin-β2 prevents RBPs with PY-NLSs accumulating in stress granules, restores nuclear RBP localization and function, and rescues degeneration caused by disease-linked FUS and hnRNPA2. Thus, NIRs therapeutically restore RBP homeostasis and mitigate neurodegeneration., (Copyright © 2018 Elsevier Inc. All rights reserved.)
- Published
- 2018
- Full Text
- View/download PDF
48. Traumatic injury induces stress granule formation and enhances motor dysfunctions in ALS/FTD models.
- Author
-
Anderson EN, Gochenaur L, Singh A, Grant R, Patel K, Watkins S, Wu JY, and Pandey UB
- Subjects
- Amyotrophic Lateral Sclerosis metabolism, Amyotrophic Lateral Sclerosis pathology, Animals, Animals, Genetically Modified, Autophagy genetics, Brain pathology, Brain Injuries, Traumatic metabolism, Brain Injuries, Traumatic pathology, Carrier Proteins genetics, Carrier Proteins metabolism, Cytoplasmic Granules pathology, DNA-Binding Proteins genetics, DNA-Binding Proteins metabolism, Disease Models, Animal, Drosophila Proteins genetics, Drosophila Proteins metabolism, Drosophila melanogaster metabolism, Frontotemporal Dementia metabolism, Frontotemporal Dementia pathology, Humans, Locomotion physiology, Longevity, Neurons metabolism, Neurons pathology, TATA-Binding Protein Associated Factors genetics, TATA-Binding Protein Associated Factors metabolism, Transcription Factor TFIID genetics, Transcription Factor TFIID metabolism, Trauma Severity Indices, Ubiquitin genetics, Ubiquitin metabolism, Ubiquitination, Amyotrophic Lateral Sclerosis genetics, Brain metabolism, Brain Injuries, Traumatic genetics, Cytoplasmic Granules metabolism, Drosophila melanogaster genetics, Frontotemporal Dementia genetics, Protein Processing, Post-Translational
- Abstract
Traumatic brain injury (TBI) has been predicted to be a predisposing factor for amyotrophic lateral sclerosis (ALS) and other neurological disorders. Despite the importance of TBI in ALS progression, the underlying cellular and molecular mechanisms are still an enigma. Here, we examined the contribution of TBI as an extrinsic factor and investigated whether TBI influences the susceptibility of developing neurodegenerative symptoms. To evaluate the effects of TBI in vivo, we applied mild to severe trauma to Drosophila and found that TBI leads to the induction of stress granules (SGs) in the brain. The degree of SGs induction directly correlates with the level of trauma. Furthermore, we observed that the level of mortality is directly proportional to the number of traumatic hits. Interestingly, trauma-induced SGs are ubiquitin, p62 and TDP-43 positive, and persistently remain over time suggesting that SGs might be aggregates and exert toxicity in our fly models. Intriguingly, TBI on animals expressing ALS-linked genes increased mortality and locomotion dysfunction suggesting that mild trauma might aggravate neurodegenerative symptoms associated with ALS. Furthermore, we found elevated levels of high molecular weight ubiquitinated proteins and p62 in animals expressing ALS-causing genes with TBI, suggesting that TBI may lead to the defects in protein degradation pathways. Finally, we observed that genetic and pharmacological induction of autophagy enhanced the clearance of SGs and promoted survival of flies in vivo. Together, our study demonstrates that trauma can induce SG formation in vivo and might enhance neurodegenerative phenotypes in the fly models of ALS.
- Published
- 2018
- Full Text
- View/download PDF
49. Isogenic FUS-eGFP iPSC Reporter Lines Enable Quantification of FUS Stress Granule Pathology that Is Rescued by Drugs Inducing Autophagy.
- Author
-
Marrone L, Poser I, Casci I, Japtok J, Reinhardt P, Janosch A, Andree C, Lee HO, Moebius C, Koerner E, Reinhardt L, Cicardi ME, Hackmann K, Klink B, Poletti A, Alberti S, Bickle M, Hermann A, Pandey UB, Hyman AA, and Sterneckert JL
- Subjects
- Amyotrophic Lateral Sclerosis metabolism, Amyotrophic Lateral Sclerosis pathology, Animals, Antidepressive Agents pharmacology, Antipyretics pharmacology, Autophagy genetics, CRISPR-Cas Systems, Drosophila, Drug Evaluation, Preclinical, Green Fluorescent Proteins genetics, Humans, Motor Neurons metabolism, Motor Neurons pathology, Mutation, Phosphatidylinositol 3-Kinases genetics, Proto-Oncogene Proteins c-akt genetics, Signal Transduction drug effects, TOR Serine-Threonine Kinases genetics, Amyotrophic Lateral Sclerosis genetics, Drosophila Proteins genetics, Heterogeneous-Nuclear Ribonucleoprotein Group F-H genetics, Induced Pluripotent Stem Cells metabolism, RNA-Binding Protein FUS genetics
- Abstract
Perturbations in stress granule (SG) dynamics may be at the core of amyotrophic lateral sclerosis (ALS). Since SGs are membraneless compartments, modeling their dynamics in human motor neurons has been challenging, thus hindering the identification of effective therapeutics. Here, we report the generation of isogenic induced pluripotent stem cells carrying wild-type and P525L FUS-eGFP. We demonstrate that FUS-eGFP is recruited into SGs and that P525L profoundly alters their dynamics. With a screening campaign, we demonstrate that PI3K/AKT/mTOR pathway inhibition increases autophagy and ameliorates SG phenotypes linked to P525L FUS by reducing FUS-eGFP recruitment into SGs. Using a Drosophila model of FUS-ALS, we corroborate that induction of autophagy significantly increases survival. Finally, by screening clinically approved drugs for their ability to ameliorate FUS SG phenotypes, we identify a number of brain-penetrant anti-depressants and anti-psychotics that also induce autophagy. These drugs could be repurposed as potential ALS treatments., (Copyright © 2018 The Authors. Published by Elsevier Inc. All rights reserved.)
- Published
- 2018
- Full Text
- View/download PDF
50. Mutation-dependent aggregation and toxicity in a Drosophila model for UBQLN2-associated ALS.
- Author
-
Kim SH, Stiles SG, Feichtmeier JM, Ramesh N, Zhan L, Scalf MA, Smith LM, Pandey UB, and Tibbetts RS
- Subjects
- Adaptor Proteins, Signal Transducing, Amino Acid Sequence, Amyotrophic Lateral Sclerosis metabolism, Amyotrophic Lateral Sclerosis pathology, Animals, Animals, Genetically Modified, Autophagy-Related Proteins, Carrier Proteins metabolism, Cell Cycle Proteins metabolism, DNA-Binding Proteins genetics, Disease Models, Animal, Drosophila Proteins, Drosophila melanogaster, Frontotemporal Dementia genetics, Gene Frequency, Genes, Regulator, HEK293 Cells, Humans, Inclusion Bodies metabolism, Neurons metabolism, Neurons pathology, Proteasome Endopeptidase Complex metabolism, Proteolysis, Ubiquitins metabolism, Amyotrophic Lateral Sclerosis genetics, Carrier Proteins genetics, Cell Cycle Proteins genetics, Mutation, Ubiquitins genetics
- Abstract
Members of the conserved ubiquilin (UBQLN) family of ubiquitin (Ub) chaperones harbor an antipodal UBL (Ub-like)-UBA (Ub-associated) domain arrangement and participate in proteasome and autophagosome-mediated protein degradation. Mutations in a proline-rich-repeat region (PRR) of UBQLN2 cause amyotrophic lateral sclerosis (ALS)/frontotemporal dementia (FTD); however, neither the normal functions of the PRR nor impacts of ALS-associated mutations within it are well understood. In this study, we show that ALS mutations perturb UBQLN2 solubility and folding in a mutation-specific manner. Biochemical impacts of ALS mutations were additive, transferable to UBQLN1, and resulted in enhanced Ub association. A Drosophila melanogaster model for UBQLN2-associated ALS revealed that both wild-type and ALS-mutant UBQLN2 alleles disrupted Ub homeostasis; however, UBQLN2ALS mutants exhibited age-dependent aggregation and caused toxicity phenotypes beyond those seen for wild-type UBQLN2. Although UBQLN2 toxicity was not correlated with aggregation in the compound eye, aggregation-prone UBQLN2 mutants elicited climbing defects and neuromuscular junctions (NMJ) abnormalities when expressed in neurons. An UBA domain mutation that abolished Ub binding also diminished UBQLN2 toxicity, implicating Ub binding in the underlying pathomechanism. We propose that ALS-associated mutations in UBQLN2 disrupt folding and that both aggregated species and soluble oligomers instigate neuron autonomous toxicity through interference with Ub homeostasis., (© The Author 2017. Published by Oxford University Press. All rights reserved. For Permissions, please email: journals.permissions@oup.com.)
- Published
- 2018
- Full Text
- View/download PDF
Catalog
Discovery Service for Jio Institute Digital Library
For full access to our library's resources, please sign in.