Publications

Found 610 results
Filters: First Letter Of Last Name is F  [Clear All Filters]
2018
Merz, G. E., Borbat, P. P., Muok, A. R., Srivastava, M., Bunck, D. N., Freed, J. H., and Crane, B. R. (2018) Site-Specific Incorporation of a Cu Spin-Label Into Proteins for Measuring Distances by Pulsed Dipolar ESR Spectroscopy. J Phys Chem B. 10.1021/acs.jpcb.8b05619
Fontán, L., Qiao, Q., Hatcher, J. M., Casalena, G., Us, I., Teater, M., Durant, M., Du, G., Xia, M., Bilchuk, N., Chennamadhavuni, S., Palladino, G., Inghirami, G., Philippar, U., Wu, H., Scott, D. A., Gray, N. S., and Melnick, A. (2018) Specific covalent inhibition of MALT1 paracaspase suppresses B cell lymphoma growth. J Clin Invest. 128, 4397-4412
Wang, J., Erazo, T., Ferguson, F. M., Buckley, D. L., Gomez, N., Muñoz-Guardiola, P., Diéguez-Martínez, N., Deng, X., Hao, M., Massefski, W., Fedorov, O., Offei-Addo, N. Kwaku, Park, P. M., Dai, L., DiBona, A., Becht, K., Kim, N. Doo, McKeown, M. R., Roberts, J. M., Zhang, J., Sim, T., Alessi, D. R., Bradner, J. E., Lizcano, J. M., Blacklow, S. C., Qi, J., Xu, X., and Gray, N. S. (2018) Structural and Atropisomeric Factors Governing the Selectivity of Pyrimido-benzodiazipinones as Inhibitors of Kinases and Bromodomains. ACS Chem Biol. 10.1021/acschembio.7b00638
Wang, J., Erazo, T., Ferguson, F. M., Buckley, D. L., Gomez, N., Muñoz-Guardiola, P., Diéguez-Martínez, N., Deng, X., Hao, M., Massefski, W., Fedorov, O., Offei-Addo, N. Kwaku, Park, P. M., Dai, L., DiBona, A., Becht, K., Kim, N. Doo, McKeown, M. R., Roberts, J. M., Zhang, J., Sim, T., Alessi, D. R., Bradner, J. E., Lizcano, J. M., Blacklow, S. C., Qi, J., Xu, X., and Gray, N. S. (2018) Structural and Atropisomeric Factors Governing the Selectivity of Pyrimido-benzodiazipinones as Inhibitors of Kinases and Bromodomains. ACS Chem Biol. 10.1021/acschembio.7b00638
Shelke, S. A., Shao, Y., Laski, A., Koirala, D., Weissman, B. P., Fuller, J. R., Tan, X., Constantin, T. P., Waggoner, A. S., Bruchez, M. P., Armitage, B. A., and Piccirilli, J. A. (2018) Structural basis for activation of fluorogenic dyes by an RNA aptamer lacking a G-quadruplex motif. Nat Commun. 9, 4542
Knecht, K. M., Buzovetsky, O., Schneider, C., Thomas, D., Srikanth, V., Kaderali, L., Tofoleanu, F., Reiss, K., Ferreirós, N., Geisslinger, G., Batista, V. S., Ji, X., Cinatl, J., Keppler, O. T., and Xiong, Y. (2018) The structural basis for cancer drug interactions with the catalytic and allosteric sites of SAMHD1. Proc Natl Acad Sci U S A. 10.1073/pnas.1805593115
Emptage, R. P., Lemmon, M. A., Ferguson, K. M., and Marmorstein, R. (2018) Structural Basis for MARK1 Kinase Autoinhibition by Its KA1 Domain. Structure. 26, 1137-1143.e3
Cooper, R. S., Georgieva, E. R., Borbat, P. P., Freed, J. H., and Heldwein, E. E. (2018) Structural basis for membrane anchoring and fusion regulation of the herpes simplex virus fusogen gB. Nat Struct Mol Biol. 25, 416-424
Eichhorn, C. D., Yang, Y., Repeta, L., and Feigon, J. (2018) Structural basis for recognition of human 7SK long noncoding RNA by the La-related protein Larp7. Proc Natl Acad Sci U S A. 115, E6457-E6466
Goris, M., Magin, R. S., Foyn, H., Myklebust, L. M., Varland, S., Ree, R., Drazic, A., Bhambra, P., Støve, S. I., Baumann, M., Haug, B. Erik, Marmorstein, R., and Arnesen, T. (2018) Structural determinants and cellular environment define processed actin as the sole substrate of the N-terminal acetyltransferase NAA80. Proc Natl Acad Sci U S A. 115, 4405-4410
Tuukkanen, A. T., Freire, D., Chan, S., Arbing, M. A., Reed, R. W., Evans, T. J., Zenkeviciutė, G., Kim, J., Kahng, S., Sawaya, M. R., Chaton, C. T., Wilmanns, M., Eisenberg, D., Parret, A. H. A., and Korotkov, K. V. (2018) Structural Variability of EspG Chaperones from Mycobacterial ESX-1, ESX-3 and ESX-5 Type VII Secretion Systems. J Mol Biol. 10.1016/j.jmb.2018.11.003
Dieck, C. L., Tzoneva, G., Forouhar, F., Carpenter, Z., Ambesi-Impiombato, A., Sanchez-Martin, M., Kirschner-Schwabe, R., Lew, S., Seetharaman, J., Tong, L., and Ferrando, A. A. (2018) Structure and Mechanisms of NT5C2 Mutations Driving Thiopurine Resistance in Relapsed Lymphoblastic Leukemia. Cancer Cell. 34, 136-147.e6
Dieck, C. L., Tzoneva, G., Forouhar, F., Carpenter, Z., Ambesi-Impiombato, A., Sanchez-Martin, M., Kirschner-Schwabe, R., Lew, S., Seetharaman, J., Tong, L., and Ferrando, A. A. (2018) Structure and Mechanisms of NT5C2 Mutations Driving Thiopurine Resistance in Relapsed Lymphoblastic Leukemia. Cancer Cell. 34, 136-147.e6
Ren, Z., Lee, J., Moosa, M. Muhammad, Nian, Y., Hu, L., Xu, Z., McCoy, J. G., Ferreon, A. Chris M., Im, W., and Zhou, M. (2018) Structure of an EIIC sugar transporter trapped in an inward-facing conformation. Proc Natl Acad Sci U S A. 10.1073/pnas.1800647115
Zhou, W., Whiteley, A. T., Mann, C. C. de Olive, Morehouse, B. R., Nowak, R. P., Fischer, E. S., Gray, N. S., Mekalanos, J. J., and Kranzusch, P. J. (2018) Structure of the Human cGAS-DNA Complex Reveals Enhanced Control of Immune Surveillance. Cell. 174, 300-311.e11
Orman, M., Bodea, S., Funk, M. A., Del Campo, A. Martínez-, Bollenbach, M., Drennan, C. L., and Balskus, E. P. (2018) Structure-Guided Identification of a Small Molecule That Inhibits Anaerobic Choline Metabolism by Human Gut Bacteria. J Am Chem Soc. 10.1021/jacs.8b04883
Varlakhanova, N. V., Alvarez, F. J. D., Brady, T. M., Tornabene, B. A., Hosford, C. J., Chappie, J. S., Zhang, P., and Ford, M. G. J. (2018) Structures of the fungal dynamin-related protein Vps1 reveal a unique, open helical architecture. J Cell Biol. 10.1083/jcb.201712021
Gulati, S., Jin, H., Masuho, I., Orban, T., Cai, Y., Pardon, E., Martemyanov, K. A., Kiser, P. D., Stewart, P. L., Ford, C. P., Steyaert, J., and Palczewski, K. (2018) Targeting G protein-coupled receptor signaling at the G protein level with a selective nanobody inhibitor. Nat Commun. 9, 1996
Fan, C., Fan, M., Orlando, B. J., Fastman, N. M., Zhang, J., Xu, Y., Chambers, M. G., Xu, X., Perry, K., Liao, M., and Feng, L. (2018) X-ray and cryo-EM structures of the mitochondrial calcium uniporter. Nature. 559, 575-579
Fan, C., Fan, M., Orlando, B. J., Fastman, N. M., Zhang, J., Xu, Y., Chambers, M. G., Xu, X., Perry, K., Liao, M., and Feng, L. (2018) X-ray and cryo-EM structures of the mitochondrial calcium uniporter. Nature. 559, 575-579
Fan, C., Fan, M., Orlando, B. J., Fastman, N. M., Zhang, J., Xu, Y., Chambers, M. G., Xu, X., Perry, K., Liao, M., and Feng, L. (2018) X-ray and cryo-EM structures of the mitochondrial calcium uniporter. Nature. 559, 575-579
Fan, C., Fan, M., Orlando, B. J., Fastman, N. M., Zhang, J., Xu, Y., Chambers, M. G., Xu, X., Perry, K., Liao, M., and Feng, L. (2018) X-ray and cryo-EM structures of the mitochondrial calcium uniporter. Nature. 559, 575-579
Chen, G., Liu, Y., Goetz, R., Fu, L., Jayaraman, S., Hu, M. - C., Moe, O. W., Liang, G., Li, X., and Mohammadi, M. (2018) α-Klotho is a non-enzymatic molecular scaffold for FGF23 hormone signalling.. Nature. 10.1038/nature25451

Pages