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David M. Sabatini

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https://www.readbyqxmd.com/read/29995852/histidine-catabolism-is-a-major-determinant-of-methotrexate-sensitivity
#1
Naama Kanarek, Heather R Keys, Jason R Cantor, Caroline A Lewis, Sze Ham Chan, Tenzin Kunchok, Monther Abu-Remaileh, Elizaveta Freinkman, Lawrence D Schweitzer, David M Sabatini
The chemotherapeutic drug methotrexate inhibits the enzyme dihydrofolate reductase1 , which generates tetrahydrofolate, an essential cofactor in nucleotide synthesis2 . Depletion of tetrahydrofolate causes cell death by suppressing DNA and RNA production3 . Although methotrexate is widely used as an anticancer agent and is the subject of over a thousand ongoing clinical trials4 , its high toxicity often leads to the premature termination of its use, which reduces its potential efficacy5 . To identify genes that modulate the response of cancer cells to methotrexate, we performed a CRISPR-Cas9-based screen6,7 ...
July 2018: Nature
https://www.readbyqxmd.com/read/29969188/deptor-modulates-activation-responses-in-cd4-t-cells-and-enhances-immunoregulation-following-transplantation
#2
Johannes Wedel, Sarah Bruneau, Kaifeng Liu, Sek Won Kong, Peter T Sage, David M Sabatini, Mathieu Laplante, David M Briscoe
DEPTOR is an evolutionarily conserved cell-intrinsic binding partner of mTOR that functions as a negative regulator of signaling responses. In this study, we show that DEPTOR is expressed within CD4+ T cells, and we observed that its relative level of expression modulates differentiation as well as glucose utilization within CD4+ T effectors in vitro. Using knockin mice, we also find that induced expression of DEPTOR within CD4+ T regulatory cells stabilizes Foxp3 expression, shifts metabolism towards oxidative phosphorylation and increases survival and suppressive function...
July 3, 2018: American Journal of Transplantation
https://www.readbyqxmd.com/read/29849139/author-correction-high-fat-diet-enhances-stemness-and-tumorigenicity-of-intestinal-progenitors
#3
Semir Beyaz, Miyeko D Mana, Jatin Roper, Dmitriy Kedrin, Assieh Saadatpour, Sue-Jean Hong, Khristian E Bauer-Rowe, Michael E Xifaras, Adam Akkad, Erika Arias, Luca Pinello, Yarden Katz, Shweta Shinagare, Monther Abu-Remaileh, Maria M Mihaylova, Dudley W Lamming, Rizkullah Dogum, Guoji Guo, George W Bell, Martin Selig, G Petur Nielsen, Nitin Gupta, Cristina R Ferrone, Vikram Deshpande, Guo-Cheng Yuan, Stuart H Orkin, David M Sabatini, Ömer H Yilmaz
In Fig. 4e of this Article, the labels for 'Control' and 'HFD' were reversed ('Control' should have been labelled blue rather than purple, and 'HFD' should have been labelled purple rather than blue). Similarly, in Fig. 4f of this Article, the labels for 'V' and 'GW' were reversed ('V' should have been labelled blue rather than purple, and 'GW' should have been labelled purple instead of blue). The original figure has been corrected online.
August 2018: Nature
https://www.readbyqxmd.com/read/29756910/search-for-high-mass-resonances-decaying-to-%C3%AF-%C3%AE-in-pp-collisions-at-sqrt-s-13-tev-with-the-atlas-detector
#4
M Aaboud, G Aad, B Abbott, O Abdinov, B Abeloos, S H Abidi, O S AbouZeid, N L Abraham, H Abramowicz, H Abreu, Y Abulaiti, B S Acharya, S Adachi, L Adamczyk, J Adelman, M Adersberger, T Adye, A A Affolder, Y Afik, C Agheorghiesei, J A Aguilar-Saavedra, S P Ahlen, F Ahmadov, G Aielli, S Akatsuka, T P A Åkesson, E Akilli, A V Akimov, G L Alberghi, J Albert, P Albicocco, M J Alconada Verzini, S Alderweireldt, M Aleksa, I N Aleksandrov, C Alexa, G Alexander, T Alexopoulos, M Alhroob, B Ali, M Aliev, G Alimonti, J Alison, S P Alkire, C Allaire, B M M Allbrooke, B W Allen, P P Allport, A Aloisio, A Alonso, F Alonso, C Alpigiani, A A Alshehri, M I Alstaty, B Alvarez Gonzalez, D Álvarez Piqueras, M G Alviggi, B T Amadio, Y Amaral Coutinho, L Ambroz, C Amelung, D Amidei, S P Amor Dos Santos, S Amoroso, C S Amrouche, C Anastopoulos, L S Ancu, N Andari, T Andeen, C F Anders, J K Anders, K J Anderson, A Andreazza, V Andrei, S Angelidakis, I Angelozzi, A Angerami, A V Anisenkov, A Annovi, C Antel, M T Anthony, M Antonelli, D J Antrim, F Anulli, M Aoki, L Aperio Bella, G Arabidze, Y Arai, J P Araque, V Araujo Ferraz, R Araujo Pereira, A T H Arce, R E Ardell, F A Arduh, J-F Arguin, S Argyropoulos, A J Armbruster, L J Armitage, O Arnaez, H Arnold, M Arratia, O Arslan, A Artamonov, G Artoni, S Artz, S Asai, N Asbah, A Ashkenazi, E M Asimakopoulou, L Asquith, K Assamagan, R Astalos, R J Atkin, M Atkinson, N B Atlay, K Augsten, G Avolio, R Avramidou, B Axen, M K Ayoub, G Azuelos, A E Baas, M J Baca, H Bachacou, K Bachas, M Backes, P Bagnaia, M Bahmani, H Bahrasemani, J T Baines, M Bajic, O K Baker, P J Bakker, D Bakshi Gupta, E M Baldin, P Balek, F Balli, W K Balunas, E Banas, A Bandyopadhyay, Sw Banerjee, A A E Bannoura, L Barak, W M Barbe, E L Barberio, D Barberis, M Barbero, T Barillari, M-S Barisits, J T Barkeloo, T Barklow, N Barlow, R Barnea, S L Barnes, B M Barnett, R M Barnett, Z Barnovska-Blenessy, A Baroncelli, G Barone, A J Barr, L Barranco Navarro, F Barreiro, J Barreiro Guimarães da Costa, R Bartoldus, A E Barton, P Bartos, A Basalaev, A Bassalat, R L Bates, S J Batista, J R Batley, M Battaglia, M Bauce, F Bauer, K T Bauer, H S Bawa, J B Beacham, M D Beattie, T Beau, P H Beauchemin, P Bechtle, H P Beck, H C Beck, K Becker, M Becker, C Becot, A J Beddall, A Beddall, V A Bednyakov, M Bedognetti, C P Bee, T A Beermann, M Begalli, M Begel, A Behera, J K Behr, A S Bell, G Bella, L Bellagamba, A Bellerive, M Bellomo, K Belotskiy, N L Belyaev, O Benary, D Benchekroun, M Bender, N Benekos, Y Benhammou, E Benhar Noccioli, J Benitez, D P Benjamin, M Benoit, J R Bensinger, S Bentvelsen, L Beresford, M Beretta, D Berge, E Bergeaas Kuutmann, N Berger, L J Bergsten, J Beringer, S Berlendis, N R Bernard, G Bernardi, C Bernius, F U Bernlochner, T Berry, P Berta, C Bertella, G Bertoli, I A Bertram, C Bertsche, G J Besjes, O Bessidskaia Bylund, M Bessner, N Besson, A Bethani, S Bethke, A Betti, A J Bevan, J Beyer, R M Bianchi, O Biebel, D Biedermann, R Bielski, K Bierwagen, N V Biesuz, M Biglietti, T R V Billoud, M Bindi, A Bingul, C Bini, S Biondi, T Bisanz, C Bittrich, D M Bjergaard, J E Black, K M Black, R E Blair, T Blazek, I Bloch, C Blocker, A Blue, U Blumenschein, Dr Blunier, G J Bobbink, V S Bobrovnikov, S S Bocchetta, A Bocci, C Bock, D Boerner, D Bogavac, A G Bogdanchikov, C Bohm, V Boisvert, P Bokan, T Bold, A S Boldyrev, A E Bolz, M Bomben, M Bona, J S Bonilla, M Boonekamp, A Borisov, G Borissov, J Bortfeldt, D Bortoletto, V Bortolotto, D Boscherini, M Bosman, J D Bossio Sola, J Boudreau, E V Bouhova-Thacker, D Boumediene, C Bourdarios, S K Boutle, A Boveia, J Boyd, I R Boyko, A J Bozson, J Bracinik, N Brahimi, A Brandt, G Brandt, O Brandt, F Braren, U Bratzler, B Brau, J E Brau, W D Breaden Madden, K Brendlinger, A J Brennan, L Brenner, R Brenner, S Bressler, D L Briglin, T M Bristow, D Britton, D Britzger, I Brock, R Brock, G Brooijmans, T Brooks, W K Brooks, E Brost, J H Broughton, P A Bruckman de Renstrom, D Bruncko, A Bruni, G Bruni, L S Bruni, S Bruno, B H Brunt, M Bruschi, N Bruscino, P Bryant, L Bryngemark, T Buanes, Q Buat, P Buchholz, A G Buckley, I A Budagov, F Buehrer, M K Bugge, O Bulekov, D Bullock, T J Burch, S Burdin, C D Burgard, A M Burger, B Burghgrave, K Burka, S Burke, I Burmeister, J T P Burr, D Büscher, V Büscher, E Buschmann, P Bussey, J M Butler, C M Buttar, J M Butterworth, P Butti, W Buttinger, A Buzatu, A R Buzykaev, G Cabras, S Cabrera Urbán, D Caforio, H Cai, V M M Cairo, O Cakir, N Calace, P Calafiura, A Calandri, G Calderini, P Calfayan, G Callea, L P Caloba, S Calvente Lopez, D Calvet, S Calvet, T P Calvet, M Calvetti, R Camacho Toro, S Camarda, P Camarri, D Cameron, R Caminal Armadans, C Camincher, S Campana, M Campanelli, A Camplani, A Campoverde, V Canale, M Cano Bret, J Cantero, T Cao, Y Cao, M D M Capeans Garrido, I Caprini, M Caprini, M Capua, R M Carbone, R Cardarelli, F Cardillo, I Carli, T Carli, G Carlino, B T Carlson, L Carminati, R M D Carney, S Caron, E Carquin, S Carrá, G D Carrillo-Montoya, D Casadei, M P Casado, A F Casha, M Casolino, D W Casper, R Castelijn, V Castillo Gimenez, N F Castro, A Catinaccio, J R Catmore, A Cattai, J Caudron, V Cavaliere, E Cavallaro, D Cavalli, M Cavalli-Sforza, V Cavasinni, E Celebi, F Ceradini, L Cerda Alberich, A S Cerqueira, A Cerri, L Cerrito, F Cerutti, A Cervelli, S A Cetin, A Chafaq, D Chakraborty, S K Chan, W S Chan, Y L Chan, P Chang, J D Chapman, D G Charlton, C C Chau, C A Chavez Barajas, S Che, A Chegwidden, S Chekanov, S V Chekulaev, G A Chelkov, M A Chelstowska, C Chen, C Chen, H Chen, J Chen, J Chen, S Chen, S Chen, X Chen, Y Chen, Y-H Chen, H C Cheng, H J Cheng, A Cheplakov, E Cheremushkina, R Cherkaoui El Moursli, E Cheu, K Cheung, L Chevalier, V Chiarella, G Chiarelli, G Chiodini, A S Chisholm, A Chitan, I Chiu, Y H Chiu, M V Chizhov, K Choi, A R Chomont, S Chouridou, Y S Chow, V Christodoulou, M C Chu, J Chudoba, A J Chuinard, J J Chwastowski, L Chytka, D Cinca, V Cindro, I A Cioară, A Ciocio, F Cirotto, Z H Citron, M Citterio, A Clark, M R Clark, P J Clark, R N Clarke, C Clement, Y Coadou, M Cobal, A Coccaro, J Cochran, L Colasurdo, B Cole, A P Colijn, J Collot, P Conde Muiño, E Coniavitis, S H Connell, I A Connelly, S Constantinescu, F Conventi, A M Cooper-Sarkar, F Cormier, K J R Cormier, M Corradi, E E Corrigan, F Corriveau, A Cortes-Gonzalez, M J Costa, D Costanzo, G Cottin, G Cowan, B E Cox, J Crane, K Cranmer, S J Crawley, R A Creager, G Cree, S Crépé-Renaudin, F Crescioli, M Cristinziani, V Croft, G Crosetti, A Cueto, T Cuhadar Donszelmann, A R Cukierman, M Curatolo, J Cúth, S Czekierda, P Czodrowski, G D'amen, S D'Auria, L D'eramo, M D'Onofrio, M J Da Cunha Sargedas De Sousa, C Da Via, W Dabrowski, T Dado, S Dahbi, T Dai, O Dale, F Dallaire, C Dallapiccola, M Dam, J R Dandoy, M F Daneri, N P Dang, N S Dann, M Danninger, V Dao, G Darbo, S Darmora, O Dartsi, A Dattagupta, T Daubney, W Davey, C David, T Davidek, D R Davis, E Dawe, I Dawson, K De, R de Asmundis, A De Benedetti, S De Castro, S De Cecco, N De Groot, P de Jong, H De la Torre, F De Lorenzi, A De Maria, D De Pedis, A De Salvo, U De Sanctis, A De Santo, K De Vasconcelos Corga, J B De Vivie De Regie, C Debenedetti, D V Dedovich, N Dehghanian, M Del Gaudio, J Del Peso, D Delgove, F Deliot, C M Delitzsch, A Dell'Acqua, L Dell'Asta, M Della Pietra, D Della Volpe, M Delmastro, C Delporte, P A Delsart, D A DeMarco, S Demers, M Demichev, S P Denisov, D Denysiuk, D Derendarz, J E Derkaoui, F Derue, P Dervan, K Desch, C Deterre, K Dette, M R Devesa, P O Deviveiros, A Dewhurst, S Dhaliwal, F A Di Bello, A Di Ciaccio, L Di Ciaccio, W K Di Clemente, C Di Donato, A Di Girolamo, B Di Micco, R Di Nardo, K F Di Petrillo, A Di Simone, R Di Sipio, D Di Valentino, C Diaconu, M Diamond, F A Dias, T Dias do Vale, M A Diaz, J Dickinson, E B Diehl, J Dietrich, S Díez Cornell, A Dimitrievska, J Dingfelder, F Dittus, F Djama, T Djobava, J I Djuvsland, M A B do Vale, M Dobre, D Dodsworth, C Doglioni, J Dolejsi, Z Dolezal, M Donadelli, J Donini, J Dopke, A Doria, M T Dova, A T Doyle, E Drechsler, E Dreyer, T Dreyer, M Dris, Y Du, J Duarte-Campderros, F Dubinin, A Dubreuil, E Duchovni, G Duckeck, A Ducourthial, O A Ducu, D Duda, A Dudarev, A Chr Dudder, E M Duffield, L Duflot, M Dührssen, C Dulsen, M Dumancic, A E Dumitriu, A K Duncan, M Dunford, A Duperrin, H Duran Yildiz, M Düren, A Durglishvili, D Duschinger, B Dutta, D Duvnjak, M Dyndal, B S Dziedzic, C Eckardt, K M Ecker, R C Edgar, T Eifert, G Eigen, K Einsweiler, T Ekelof, M El Kacimi, R El Kosseifi, V Ellajosyula, M Ellert, F Ellinghaus, A A Elliot, N Ellis, J Elmsheuser, M Elsing, D Emeliyanov, Y Enari, J S Ennis, M B Epland, J Erdmann, A Ereditato, S Errede, M Escalier, C Escobar, B Esposito, O Estrada Pastor, A I Etienvre, E Etzion, H Evans, A Ezhilov, M Ezzi, F Fabbri, L Fabbri, V Fabiani, G Facini, R M Fakhrutdinov, S Falciano, P J Falke, S Falke, J Faltova, Y Fang, M Fanti, A Farbin, A Farilla, E M Farina, T Farooque, S Farrell, S M Farrington, P Farthouat, F Fassi, P Fassnacht, D Fassouliotis, M Faucci Giannelli, A Favareto, W J Fawcett, L Fayard, O L Fedin, W Fedorko, M Feickert, S Feigl, L Feligioni, C Feng, E J Feng, M Feng, M J Fenton, A B Fenyuk, L Feremenga, J Ferrando, A Ferrari, P Ferrari, R Ferrari, D E Ferreira de Lima, A Ferrer, D Ferrere, C Ferretti, F Fiedler, A Filipčič, F Filthaut, M Fincke-Keeler, K D Finelli, M C N Fiolhais, L Fiorini, C Fischer, J Fischer, W C Fisher, N Flaschel, I Fleck, P Fleischmann, R R M Fletcher, T Flick, B M Flierl, L M Flores, L R Flores Castillo, N Fomin, G T Forcolin, A Formica, F A Förster, A Forti, A G Foster, D Fournier, H Fox, S Fracchia, P Francavilla, M Franchini, S Franchino, D Francis, L Franconi, M Franklin, M Frate, M Fraternali, D Freeborn, S M Fressard-Batraneanu, B Freund, W S Freund, D Froidevaux, J A Frost, C Fukunaga, T Fusayasu, J Fuster, O Gabizon, A Gabrielli, A Gabrielli, G P Gach, S Gadatsch, S Gadomski, P Gadow, G Gagliardi, L G Gagnon, C Galea, B Galhardo, E J Gallas, B J Gallop, P Gallus, G Galster, R Gamboa Goni, K K Gan, S Ganguly, Y Gao, Y S Gao, F M Garay Walls, C García, J E García Navarro, J A García Pascual, M Garcia-Sciveres, R W Gardner, N Garelli, V Garonne, K Gasnikova, A Gaudiello, G Gaudio, I L Gavrilenko, A Gavrilyuk, C Gay, G Gaycken, E N Gazis, C N P Gee, J Geisen, M Geisen, M P Geisler, K Gellerstedt, C Gemme, M H Genest, C Geng, S Gentile, C Gentsos, S George, D Gerbaudo, G Geßner, S Ghasemi, M Ghneimat, B Giacobbe, S Giagu, N Giangiacomi, P Giannetti, S M Gibson, M Gignac, D Gillberg, G Gilles, D M Gingrich, M P Giordani, F M Giorgi, P F Giraud, P Giromini, G Giugliarelli, D Giugni, F Giuli, M Giulini, S Gkaitatzis, I Gkialas, E L Gkougkousis, P Gkountoumis, L K Gladilin, C Glasman, J Glatzer, P C F Glaysher, A Glazov, M Goblirsch-Kolb, J Godlewski, S Goldfarb, T Golling, D Golubkov, A Gomes, R Gonçalo, R Goncalves Gama, G Gonella, L Gonella, A Gongadze, F Gonnella, J L Gonski, S González de la Hoz, S Gonzalez-Sevilla, L Goossens, P A Gorbounov, H A Gordon, B Gorini, E Gorini, A Gorišek, A T Goshaw, C Gössling, M I Gostkin, C A Gottardo, C R Goudet, D Goujdami, A G Goussiou, N Govender, C Goy, E Gozani, I Grabowska-Bold, P O J Gradin, E C Graham, J Gramling, E Gramstad, S Grancagnolo, V Gratchev, P M Gravila, C Gray, H M Gray, Z D Greenwood, C Grefe, K Gregersen, I M Gregor, P Grenier, K Grevtsov, J Griffiths, A A Grillo, K Grimm, S Grinstein, Ph Gris, J-F Grivaz, S Groh, E Gross, J Grosse-Knetter, G C Grossi, Z J Grout, A Grummer, L Guan, W Guan, J Guenther, A Guerguichon, F Guescini, D Guest, O Gueta, R Gugel, B Gui, T Guillemin, S Guindon, U Gul, C Gumpert, J Guo, W Guo, Y Guo, R Gupta, S Gurbuz, G Gustavino, B J Gutelman, P Gutierrez, N G Gutierrez Ortiz, C Gutschow, C Guyot, M P Guzik, C Gwenlan, C B Gwilliam, A Haas, C Haber, H K Hadavand, N Haddad, A Hadef, S Hageböck, M Hagihara, H Hakobyan, M Haleem, J Haley, G Halladjian, G D Hallewell, K Hamacher, P Hamal, K Hamano, A Hamilton, G N Hamity, K Han, L Han, S Han, K Hanagaki, M Hance, D M Handl, B Haney, R Hankache, P Hanke, E Hansen, J B Hansen, J D Hansen, M C Hansen, P H Hansen, K Hara, A S Hard, T Harenberg, S Harkusha, P F Harrison, N M Hartmann, Y Hasegawa, A Hasib, S Hassani, S Haug, R Hauser, L Hauswald, L B Havener, M Havranek, C M Hawkes, R J Hawkings, D Hayden, C Hayes, C P Hays, J M Hays, H S Hayward, S J Haywood, M P Heath, V Hedberg, L Heelan, S Heer, K K Heidegger, S Heim, T Heim, B Heinemann, J J Heinrich, L Heinrich, C Heinz, J Hejbal, L Helary, A Held, S Hellesund, S Hellman, C Helsens, R C W Henderson, Y Heng, S Henkelmann, A M Henriques Correia, G H Herbert, H Herde, V Herget, Y Hernández Jiménez, H Herr, G Herten, R Hertenberger, L Hervas, T C Herwig, G G Hesketh, N P Hessey, J W Hetherly, S Higashino, E Higón-Rodriguez, K Hildebrand, E Hill, J C Hill, K H Hiller, S J Hillier, M Hils, I Hinchliffe, M Hirose, D Hirschbuehl, B Hiti, O Hladik, D R Hlaluku, X Hoad, J Hobbs, N Hod, M C Hodgkinson, A Hoecker, M R Hoeferkamp, F Hoenig, D Hohn, D Hohov, T R Holmes, M Holzbock, M Homann, S Honda, T Honda, T M Hong, B H Hooberman, W H Hopkins, Y Horii, A J Horton, L A Horyn, J-Y Hostachy, A Hostiuc, S Hou, A Hoummada, J Howarth, J Hoya, M Hrabovsky, J Hrdinka, I Hristova, J Hrivnac, T Hryn'ova, A Hrynevich, P J Hsu, S-C Hsu, Q Hu, S Hu, Y Huang, Z Hubacek, F Hubaut, M Huebner, F Huegging, T B Huffman, E W Hughes, M Huhtinen, R F H Hunter, P Huo, A M Hupe, N Huseynov, J Huston, J Huth, R Hyneman, G Iacobucci, G Iakovidis, I Ibragimov, L Iconomidou-Fayard, Z Idrissi, P Iengo, R Ignazzi, O Igonkina, R Iguchi, T Iizawa, Y Ikegami, M Ikeno, D Iliadis, N Ilic, F Iltzsche, G Introzzi, M Iodice, K Iordanidou, V Ippolito, M F Isacson, N Ishijima, M Ishino, M Ishitsuka, C Issever, S Istin, F Ito, J M Iturbe Ponce, R Iuppa, A Ivina, H Iwasaki, J M Izen, V Izzo, S Jabbar, P Jacka, P Jackson, R M Jacobs, V Jain, G Jakel, K B Jakobi, K Jakobs, S Jakobsen, T Jakoubek, D O Jamin, D K Jana, R Jansky, J Janssen, M Janus, P A Janus, G Jarlskog, N Javadov, T Javůrek, M Javurkova, F Jeanneau, L Jeanty, J Jejelava, A Jelinskas, P Jenni, J Jeong, C Jeske, S Jézéquel, H Ji, J Jia, H Jiang, Y Jiang, Z Jiang, S Jiggins, F A Jimenez Morales, J Jimenez Pena, S Jin, A Jinaru, O Jinnouchi, H Jivan, P Johansson, K A Johns, C A Johnson, W J Johnson, K Jon-And, R W L Jones, S D Jones, S Jones, T J Jones, J Jongmanns, P M Jorge, J Jovicevic, X Ju, J J Junggeburth, A Juste Rozas, A Kaczmarska, M Kado, H Kagan, M Kagan, T Kaji, E Kajomovitz, C W Kalderon, A Kaluza, S Kama, A Kamenshchikov, L Kanjir, Y Kano, V A Kantserov, J Kanzaki, B Kaplan, L S Kaplan, D Kar, K Karakostas, N Karastathis, M J Kareem, E Karentzos, S N Karpov, Z M Karpova, V Kartvelishvili, A N Karyukhin, K Kasahara, L Kashif, R D Kass, A Kastanas, Y Kataoka, C Kato, A Katre, J Katzy, K Kawade, K Kawagoe, T Kawamoto, G Kawamura, E F Kay, V F Kazanin, R Keeler, R Kehoe, J S Keller, E Kellermann, J J Kempster, J Kendrick, O Kepka, B P Kerševan, S Kersten, R A Keyes, M Khader, F Khalil-Zada, A Khanov, A G Kharlamov, T Kharlamova, A Khodinov, T J Khoo, V Khovanskiy, E Khramov, J Khubua, S Kido, M Kiehn, C R Kilby, H Y Kim, S H Kim, Y K Kim, N Kimura, O M Kind, B T King, D Kirchmeier, J Kirk, A E Kiryunin, T Kishimoto, D Kisielewska, V Kitali, O Kivernyk, E Kladiva, T Klapdor-Kleingrothaus, M H Klein, M Klein, U Klein, K Kleinknecht, P Klimek, A Klimentov, R Klingenberg, T Klingl, T Klioutchnikova, F F Klitzner, E-E Kluge, P Kluit, S Kluth, E Kneringer, E B F G Knoops, A Knue, A Kobayashi, D Kobayashi, T Kobayashi, M Kobel, M Kocian, P Kodys, T Koffas, E Koffeman, N M Köhler, T Koi, M Kolb, I Koletsou, T Kondo, N Kondrashova, K Köneke, A C König, T Kono, R Konoplich, N Konstantinidis, B Konya, R Kopeliansky, S Koperny, K Korcyl, K Kordas, A Korn, I Korolkov, E V Korolkova, O Kortner, S Kortner, T Kosek, V V Kostyukhin, A Kotwal, A Koulouris, A Kourkoumeli-Charalampidi, C Kourkoumelis, E Kourlitis, V Kouskoura, A B Kowalewska, R Kowalewski, T Z Kowalski, C Kozakai, W Kozanecki, A S Kozhin, V A Kramarenko, G Kramberger, D Krasnopevtsev, M W Krasny, A Krasznahorkay, D Krauss, J A Kremer, J Kretzschmar, K Kreutzfeldt, P Krieger, K Krizka, K Kroeninger, H Kroha, J Kroll, J Kroll, J Kroseberg, J Krstic, U Kruchonak, H Krüger, N Krumnack, M C Kruse, T Kubota, S Kuday, J T Kuechler, S Kuehn, A Kugel, F Kuger, T Kuhl, V Kukhtin, R Kukla, Y Kulchitsky, S Kuleshov, Y P Kulinich, M Kuna, T Kunigo, A Kupco, T Kupfer, O Kuprash, H Kurashige, L L Kurchaninov, Y A Kurochkin, M G Kurth, E S Kuwertz, M Kuze, J Kvita, T Kwan, A La Rosa, J L La Rosa Navarro, L La Rotonda, F La Ruffa, C Lacasta, F Lacava, J Lacey, D P J Lack, H Lacker, D Lacour, E Ladygin, R Lafaye, B Laforge, S Lai, S Lammers, W Lampl, E Lançon, U Landgraf, M P J Landon, M C Lanfermann, V S Lang, J C Lange, R J Langenberg, A J Lankford, F Lanni, K Lantzsch, A Lanza, A Lapertosa, S Laplace, J F Laporte, T Lari, F Lasagni 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Wynne, S Xella, Z Xi, L Xia, D Xu, H Xu, L Xu, T Xu, W Xu, B Yabsley, S Yacoob, K Yajima, D P Yallup, D Yamaguchi, Y Yamaguchi, A Yamamoto, T Yamanaka, F Yamane, M Yamatani, T Yamazaki, Y Yamazaki, Z Yan, H Yang, H Yang, S Yang, Y Yang, Y Yang, Z Yang, W-M Yao, Y C Yap, Y Yasu, E Yatsenko, K H Yau Wong, J Ye, S Ye, I Yeletskikh, E Yigitbasi, E Yildirim, K Yorita, K Yoshihara, C Young, C J S Young, J Yu, J Yu, X Yue, S P Y Yuen, I Yusuff, B Zabinski, G Zacharis, R Zaidan, A M Zaitsev, N Zakharchuk, J Zalieckas, S Zambito, D Zanzi, C Zeitnitz, G Zemaityte, J C Zeng, Q Zeng, O Zenin, T Ženiš, D Zerwas, M Zgubič, D Zhang, D Zhang, F Zhang, G Zhang, H Zhang, J Zhang, L Zhang, L Zhang, M Zhang, P Zhang, R Zhang, R Zhang, X Zhang, Y Zhang, Z Zhang, X Zhao, Y Zhao, Z Zhao, A Zhemchugov, B Zhou, C Zhou, L Zhou, M Zhou, M Zhou, N Zhou, Y Zhou, C G Zhu, H Zhu, H Zhu, J Zhu, Y Zhu, X Zhuang, K Zhukov, V Zhulanov, A Zibell, D Zieminska, N I Zimine, S Zimmermann, Z Zinonos, M Zinser, M Ziolkowski, L Živković, G Zobernig, A Zoccoli, K Zoch, T G Zorbas, R Zou, M Zur Nedden, L Zwalinski
A search for high-mass resonances decaying to τν using proton-proton collisions at sqrt[s]=13  TeV produced by the Large Hadron Collider is presented. Only τ-lepton decays with hadrons in the final state are considered. The data were recorded with the ATLAS detector and correspond to an integrated luminosity of 36.1  fb^{-1}. No statistically significant excess above the standard model expectation is observed; model-independent upper limits are set on the visible τν production cross section. Heavy W^{'} bosons with masses less than 3...
April 20, 2018: Physical Review Letters
https://www.readbyqxmd.com/read/29745899/identification-of-a-transporter-complex-responsible-for-the-cytosolic-entry-of-nitrogen-containing-bisphosphonates
#5
Zhou Yu, Lauren E Surface, Chong Yon Park, Max A Horlbeck, Gregory A Wyant, Monther Abu-Remaileh, Timothy R Peterson, David M Sabatini, Jonathan S Weissman, Erin K O'Shea
Nitrogen-containing-bisphosphonates (N-BPs) are a class of drugs widely prescribed to treat osteoporosis and other bone-related diseases. Although previous studies have established that N-BPs function by inhibiting the mevalonate pathway in osteoclasts, the mechanism by which N-BPs enter the cytosol from the extracellular space to reach their molecular target is not understood. Here, we implemented a CRISPRi-mediated genome-wide screen and identified SLC37A3 (solute carrier family 37 member A3) as a gene required for the action of N-BPs in mammalian cells...
May 10, 2018: ELife
https://www.readbyqxmd.com/read/29727683/fasting-activates-fatty-acid-oxidation-to-enhance-intestinal-stem-cell-function-during-homeostasis-and-aging
#6
Maria M Mihaylova, Chia-Wei Cheng, Amanda Q Cao, Surya Tripathi, Miyeko D Mana, Khristian E Bauer-Rowe, Monther Abu-Remaileh, Laura Clavain, Aysegul Erdemir, Caroline A Lewis, Elizaveta Freinkman, Audrey S Dickey, Albert R La Spada, Yanmei Huang, George W Bell, Vikram Deshpande, Peter Carmeliet, Pekka Katajisto, David M Sabatini, Ömer H Yilmaz
Diet has a profound effect on tissue regeneration in diverse organisms, and low caloric states such as intermittent fasting have beneficial effects on organismal health and age-associated loss of tissue function. The role of adult stem and progenitor cells in responding to short-term fasting and whether such responses improve regeneration are not well studied. Here we show that a 24 hr fast augments intestinal stem cell (ISC) function in young and aged mice by inducing a fatty acid oxidation (FAO) program and that pharmacological activation of this program mimics many effects of fasting...
May 3, 2018: Cell Stem Cell
https://www.readbyqxmd.com/read/29700228/nufip1-is-a-ribosome-receptor-for-starvation-induced-ribophagy
#7
Gregory A Wyant, Monther Abu-Remaileh, Evgeni M Frenkel, Nouf N Laqtom, Vimisha Dharamdasani, Caroline A Lewis, Sze Ham Chan, Ivonne Heinze, Alessandro Ori, David M Sabatini
The lysosome degrades and recycles macromolecules, signals to the master growth regulator mTORC1 [mechanistic target of rapamycin (mTOR) complex 1], and is associated with human disease. We performed quantitative proteomic analyses of rapidly isolated lysosomes and found that nutrient levels and mTOR dynamically modulate the lysosomal proteome. Upon mTORC1 inhibition, NUFIP1 (nuclear fragile X mental retardation-interacting protein 1) redistributes from the nucleus to autophagosomes and lysosomes. Upon these conditions, NUFIP1 interacts with ribosomes and delivers them to autophagosomes by directly binding to microtubule-associated proteins 1A/1B light chain 3B (LC3B)...
May 18, 2018: Science
https://www.readbyqxmd.com/read/29590090/architecture-of-the-human-gator1-and-gator1-rag-gtpases-complexes
#8
Kuang Shen, Rick K Huang, Edward J Brignole, Kendall J Condon, Max L Valenstein, Lynne Chantranupong, Aimaiti Bomaliyamu, Abigail Choe, Chuan Hong, Zhiheng Yu, David M Sabatini
Nutrients, such as amino acids and glucose, signal through the Rag GTPases to activate mTORC1. The GATOR1 protein complex-comprising DEPDC5, NPRL2 and NPRL3-regulates the Rag GTPases as a GTPase-activating protein (GAP) for RAGA; loss of GATOR1 desensitizes mTORC1 signalling to nutrient starvation. GATOR1 components have no sequence homology to other proteins, so the function of GATOR1 at the molecular level is currently unknown. Here we used cryo-electron microscopy to solve structures of GATOR1 and GATOR1-Rag GTPases complexes...
April 5, 2018: Nature
https://www.readbyqxmd.com/read/29555419/discovery-and-optimization-of-piperazine-1-thiourea-based-human-phosphoglycerate-dehydrogenase-inhibitors
#9
Jason M Rohde, Kyle R Brimacombe, Li Liu, Michael E Pacold, Adam Yasgar, Dorian M Cheff, Tobie D Lee, Ganesha Rai, Bolormaa Baljinnyam, Zhuyin Li, Anton Simeonov, Matthew D Hall, Min Shen, David M Sabatini, Matthew B Boxer
Proliferating cells, including cancer cells, obtain serine both exogenously and via the metabolism of glucose. By catalyzing the first, rate-limiting step in the synthesis of serine from glucose, phosphoglycerate dehydrogenase (PHGDH) controls flux through the biosynthetic pathway for this important amino acid and represents a putative target in oncology. To discover inhibitors of PHGDH, a coupled biochemical assay was developed and optimized to enable high-throughput screening for inhibitors of human PHGDH...
May 1, 2018: Bioorganic & Medicinal Chemistry
https://www.readbyqxmd.com/read/29532801/rapid-immunopurification-of-mitochondria-for-metabolite-profiling-and-absolute-quantification-of-matrix-metabolites
#10
Walter W Chen, Elizaveta Freinkman, David M Sabatini
Mitochondria carry out numerous metabolic reactions that are critical to cellular homeostasis. Here we present a protocol for interrogating mitochondrial metabolites and measuring their matrix concentrations. Our workflow uses high-affinity magnetic immunocapture to rapidly purify HA-tagged mitochondria from homogenized mammalian cells in ∼12 min. These mitochondria are extracted with methanol and water. Liquid chromatography and mass spectrometry (LC/MS) is used to determine the identities and mole quantities of mitochondrial metabolites using authentic metabolite standards and isotopically labeled internal standards, whereas the corresponding mitochondrial matrix volume is determined via immunoblotting, confocal microscopy of intact cells, and volumetric analysis...
October 2017: Nature Protocols
https://www.readbyqxmd.com/read/29452640/serine-catabolism-by-shmt2-is-required-for-proper-mitochondrial-translation-initiation-and-maintenance-of-formylmethionyl-trnas
#11
Denise R Minton, Minwoo Nam, Daniel J McLaughlin, Jong Shin, Erol C Bayraktar, Samantha W Alvarez, Vladislav O Sviderskiy, Thales Papagiannakopoulos, David M Sabatini, Kıvanç Birsoy, Richard Possemato
Upon glucose restriction, eukaryotic cells upregulate oxidative metabolism to maintain homeostasis. Using genetic screens, we find that the mitochondrial serine hydroxymethyltransferase (SHMT2) is required for robust mitochondrial oxygen consumption and low glucose proliferation. SHMT2 catalyzes the first step in mitochondrial one-carbon metabolism, which, particularly in proliferating cells, produces tetrahydrofolate (THF)-conjugated one-carbon units used in cytoplasmic reactions despite the presence of a parallel cytoplasmic pathway...
February 15, 2018: Molecular Cell
https://www.readbyqxmd.com/read/29279397/profile-of-david-m-sabatini
#12
Jennifer Viegas
No abstract text is available yet for this article.
January 16, 2018: Proceedings of the National Academy of Sciences of the United States of America
https://www.readbyqxmd.com/read/29274432/a-mouse-model-of-depdc5-related-epilepsy-neuronal-loss-of-depdc5-causes-dysplastic-and-ectopic-neurons-increased-mtor-signaling-and-seizure-susceptibility
#13
Christopher J Yuskaitis, Brandon M Jones, Rachel L Wolfson, Chloe E Super, Sameer C Dhamne, Alexander Rotenberg, David M Sabatini, Mustafa Sahin, Annapurna Poduri
DEPDC5 is a newly identified epilepsy-related gene implicated in focal epilepsy, brain malformations, and Sudden Unexplained Death in Epilepsy (SUDEP). In vitro, DEPDC5 negatively regulates amino acid sensing by the mTOR complex 1 (mTORC1) pathway, but the role of DEPDC5 in neurodevelopment and epilepsy has not been described. No animal model of DEPDC5-related epilepsy has recapitulated the neurological phenotypes seen in patients, and germline knockout rodent models are embryonic lethal. Here, we establish a neuron-specific Depdc5 conditional knockout mouse by cre-recombination under the Synapsin1 promotor...
March 2018: Neurobiology of Disease
https://www.readbyqxmd.com/read/29168506/nfs1-undergoes-positive-selection-in-lung-tumours-and-protects-cells-from-ferroptosis
#14
Samantha W Alvarez, Vladislav O Sviderskiy, Erdem M Terzi, Thales Papagiannakopoulos, Andre L Moreira, Sylvia Adams, David M Sabatini, Kıvanç Birsoy, Richard Possemato
Environmental nutrient levels impact cancer cell metabolism, resulting in context-dependent gene essentiality. Here, using loss-of-function screening based on RNA interference, we show that environmental oxygen levels are a major driver of differential essentiality between in vitro model systems and in vivo tumours. Above the 3-8% oxygen concentration typical of most tissues, we find that cancer cells depend on high levels of the iron-sulfur cluster biosynthetic enzyme NFS1. Mammary or subcutaneous tumours grow despite suppression of NFS1, whereas metastatic or primary lung tumours do not...
November 30, 2017: Nature
https://www.readbyqxmd.com/read/29149601/intersubunit-crosstalk-in-the-rag-gtpase-heterodimer-enables-mtorc1-to-respond-rapidly-to-amino-acid-availability
#15
Kuang Shen, Abigail Choe, David M Sabatini
No abstract text is available yet for this article.
November 16, 2017: Molecular Cell
https://www.readbyqxmd.com/read/29123071/samtor-is-an-s-adenosylmethionine-sensor-for-the-mtorc1-pathway
#16
Xin Gu, Jose M Orozco, Robert A Saxton, Kendall J Condon, Grace Y Liu, Patrycja A Krawczyk, Sonia M Scaria, J Wade Harper, Steven P Gygi, David M Sabatini
mTOR complex 1 (mTORC1) regulates cell growth and metabolism in response to multiple environmental cues. Nutrients signal via the Rag guanosine triphosphatases (GTPases) to promote the localization of mTORC1 to the lysosomal surface, its site of activation. We identified SAMTOR, a previously uncharacterized protein, which inhibits mTORC1 signaling by interacting with GATOR1, the GTPase activating protein (GAP) for RagA/B. We found that the methyl donor S -adenosylmethionine (SAM) disrupts the SAMTOR-GATOR1 complex by binding directly to SAMTOR with a dissociation constant of approximately 7 μM...
November 10, 2017: Science
https://www.readbyqxmd.com/read/29078414/twenty-five-years-of-mtor-uncovering-the-link-from-nutrients-to-growth
#17
David M Sabatini
In my PNAS Inaugural Article, I describe the development of the mTOR field, starting with efforts to understand the mechanism of action of the drug rapamycin, which ∼25 y ago led to the discovery of the mTOR protein kinase. I focus on insights that we have contributed and on work that has been particularly influential to me, as well as provide some personal reflections and stories. We now appreciate that, as part of two distinct complexes, mTORC1 and mTORC2, mTOR is the major regulator of growth (mass accumulation) in animals and is the key link between the availability of nutrients in the environment and the control of most anabolic and catabolic processes...
November 7, 2017: Proceedings of the National Academy of Sciences of the United States of America
https://www.readbyqxmd.com/read/29074583/lysosomal-metabolomics-reveals-v-atpase-and-mtor-dependent-regulation-of-amino-acid-efflux-from-lysosomes
#18
Monther Abu-Remaileh, Gregory A Wyant, Choah Kim, Nouf N Laqtom, Maria Abbasi, Sze Ham Chan, Elizaveta Freinkman, David M Sabatini
The lysosome degrades and recycles macromolecules, signals to the cytosol and nucleus, and is implicated in many diseases. Here, we describe a method for the rapid isolation of mammalian lysosomes and use it to quantitatively profile lysosomal metabolites under various cell states. Under nutrient-replete conditions, many lysosomal amino acids are in rapid exchange with those in the cytosol. Loss of lysosomal acidification through inhibition of the vacuolar H+ -adenosine triphosphatase (V-ATPase) increased the luminal concentrations of most metabolites but had no effect on those of the majority of essential amino acids...
November 10, 2017: Science
https://www.readbyqxmd.com/read/29058724/a-crispr-screen-identifies-a-pathway-required-for-paraquat-induced-cell-death
#19
Colleen R Reczek, Kıvanç Birsoy, Hyewon Kong, Inmaculada Martínez-Reyes, Tim Wang, Peng Gao, David M Sabatini, Navdeep S Chandel
Paraquat, a herbicide linked to Parkinson's disease, generates reactive oxygen species (ROS), which causes cell death. Because the source of paraquat-induced ROS production remains unknown, we conducted a CRISPR-based positive-selection screen to identify metabolic genes essential for paraquat-induced cell death. Our screen uncovered three genes, POR (cytochrome P450 oxidoreductase), ATP7A (copper transporter), and SLC45A4 (sucrose transporter), required for paraquat-induced cell death. Furthermore, our results revealed POR as the source of paraquat-induced ROS production...
December 2017: Nature Chemical Biology
https://www.readbyqxmd.com/read/29056322/intersubunit-crosstalk-in-the-rag-gtpase-heterodimer-enables-mtorc1-to-respond-rapidly-to-amino-acid-availability
#20
Kuang Shen, Abigail Choe, David M Sabatini
mTOR complex I (mTORC1) is a central growth regulator that senses amino acids through a pathway that converges on the Rag GTPases, an obligate heterodimer of two related GTPases. Despite their central role in amino acid sensing, it is unknown why the Rag GTPases are heterodimeric and whether their subunits communicate with each other. Here, we find that the binding of guanosine triphosphate (GTP) to one subunit inhibits the binding and induces the hydrolysis of GTP by the other. This intersubunit communication pushes the Rag GTPases into either of two stable configurations, which represent active "on" or "off" states that interconvert via transient intermediates...
November 2, 2017: Molecular Cell
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