Publications

Found 1194 results
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2018
Pantel, L., Florin, T., Dobosz-Bartoszek, M., Racine, E., Sarciaux, M., Serri, M., Houard, J., Campagne, J. - M., de Figueiredo, R. Marcia, Midrier, C., Gaudriault, S., Givaudan, A., Lanois, A., Forst, S., Aumelas, A., Cotteaux-Lautard, C., Bolla, J. - M., Lundberg, C. Vingsbo, Huseby, D. L., Hughes, D., Villain-Guillot, P., Mankin, A. S., Polikanov, Y. S., and Gualtieri, M. (2018) Odilorhabdins, Antibacterial Agents that Cause Miscoding by Binding at a New Ribosomal Site. Mol Cell. 70, 83-94.e7
Hammill, J. T., Scott, D. C., Min, J., Connelly, M. C., Holbrook, G., Zhu, F., Matheny, A., Yang, L., Singh, B., Schulman, B. A., and R Guy, K. (2018) Piperidinyl Ureas Chemically Control Defective in Cullin Neddylation 1 (DCN1)-Mediated Cullin Neddylation. J Med Chem. 61, 2680-2693
Nowak, R. P., DeAngelo, S. L., Buckley, D., He, Z., Donovan, K. A., An, J., Safaee, N., Jedrychowski, M. P., Ponthier, C. M., Ishoey, M., Zhang, T., Mancias, J. D., Gray, N. S., Bradner, J. E., and Fischer, E. S. (2018) Plasticity in binding confers selectivity in ligand-induced protein degradation. Nat Chem Biol. 10.1038/s41589-018-0055-y
Peek, J., Lilic, M., Montiel, D., Milshteyn, A., Woodworth, I., Biggins, J. B., Ternei, M. A., Calle, P. Y., Danziger, M., Warrier, T., Saito, K., Braffman, N., Fay, A., Glickman, M. S., Darst, S. A., Campbell, E. A., and Brady, S. F. (2018) Rifamycin congeners kanglemycins are active against rifampicin-resistant bacteria via a distinct mechanism. Nat Commun. 9, 4147
Li, H., Sharp, R., Rutherford, K., Gupta, K., and Van Duyne, G. D. (2018) Serine Integrase attP Binding and Specificity. J Mol Biol. 430, 4401-4418
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
Shen, G., Li, S., Cui, W., Liu, S., Liu, Q., Yang, Y., Gross, M., and Li, W. (2018) Stabilization of warfarin-binding pocket of VKORC1 and VKORL1 by a peripheral region determines their different sensitivity to warfarin inhibition. J Thromb Haemost. 16, 1164-1175
Santiago, Ada Silva, Couñago, R. M., Ramos, P. Zonzini, Godoi, P. H. C., Massirer, K. B., Gileadi, O., and Elkins, J. M. (2018) Structural Analysis of Inhibitor Binding to CAMKK1 Identifies Features Necessary for Design of Specific Inhibitors. Sci Rep. 8, 14800
Santiago, Ada Silva, Couñago, R. M., Ramos, P. Zonzini, Godoi, P. H. C., Massirer, K. B., Gileadi, O., and Elkins, J. M. (2018) Structural Analysis of Inhibitor Binding to CAMKK1 Identifies Features Necessary for Design of Specific Inhibitors. Sci Rep. 8, 14800
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
Hari, S. B., Grant, R. A., and Sauer, R. T. (2018) Structural and Functional Analysis of E. coli Cyclopropane Fatty Acid Synthase.. Structure. 10.1016/j.str.2018.06.008
Gao, A., Vasilyev, N., Luciano, D. J., Levenson-Palmer, R., Richards, J., Marsiglia, W. M., Traaseth, N. J., Belasco, J. G., and Serganov, A. (2018) Structural and kinetic insights into stimulation of RppH-dependent RNA degradation by the metabolic enzyme DapF. Nucleic Acids Res. 10.1093/nar/gky327
Grell, T. A. J., Kincannon, W. M., Bruender, N. A., Blaesi, E. J., Krebs, C., Bandarian, V., and Drennan, C. L. (2018) Structural and spectroscopic analyses of the sporulation killing factor biosynthetic enzyme SkfB, a bacterial AdoMet radical sactisynthase. J Biol Chem. 10.1074/jbc.RA118.005369
Xiong, S., Lorenzen, K., Couzens, A. L., Templeton, C. M., Rajendran, D., Mao, D. Y. L., Juang, Y. - C., Chiovitti, D., Kurinov, I., Guettler, S., Gingras, A. - C., and Sicheri, F. (2018) Structural Basis for Auto-Inhibition of the NDR1 Kinase Domain by an Atypically Long Activation Segment. Structure. 26, 1101-1115.e6
Xiong, S., Lorenzen, K., Couzens, A. L., Templeton, C. M., Rajendran, D., Mao, D. Y. L., Juang, Y. - C., Chiovitti, D., Kurinov, I., Guettler, S., Gingras, A. - C., and Sicheri, F. (2018) Structural Basis for Auto-Inhibition of the NDR1 Kinase Domain by an Atypically Long Activation Segment. Structure. 26, 1101-1115.e6
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
Zhang, Z. - M., Lu, R., Wang, P., Yu, Y., Chen, D., Gao, L., Liu, S., Ji, D., Rothbart, S. B., Wang, Y., Wang, G. Greg, and Song, J. (2018) Structural basis for DNMT3A-mediated de novo DNA methylation. Nature. 554, 387-391
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
Coleman, J. A., and Gouaux, E. (2018) Structural basis for recognition of diverse antidepressants by the human serotonin transporter. Nat Struct Mol Biol. 10.1038/s41594-018-0026-8
Nithianantham, S., Cook, B. D., Beans, M., Guo, F., Chang, F., and Al-Bassam, J. (2018) Structural basis of tubulin recruitment and assembly by microtubule polymerases with Tumor Overexpressed Gene (TOG) domain arrays. Elife. 10.7554/eLife.38922
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
Banerjee, A., Ghosh, S., Goldgur, Y., and Shuman, S. (2018) Structure and two-metal mechanism of fungal tRNA ligase. Nucleic Acids Res. 10.1093/nar/gky1275
Banerjee, A., Ghosh, S., Goldgur, Y., and Shuman, S. (2018) Structure and two-metal mechanism of fungal tRNA ligase. Nucleic Acids Res. 10.1093/nar/gky1275
Gottlieb, L., and Marmorstein, R. (2018) Structure of Human NatA and Its Regulation by the Huntingtin Interacting Protein HYPK. Structure. 10.1016/j.str.2018.04.003

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