Publications

Found 1208 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
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
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
Qi, J., Li, X., Peng, H., Cook, E. M., Dadashian, E. L., Wiestner, A., Park, H. J., and Rader, C. (2018) Potent and selective antitumor activity of a T cell-engaging bispecific antibody targeting a membrane-proximal epitope of ROR1. Proc Natl Acad Sci U S A. 115, E5467-E5476
Qi, J., Li, X., Peng, H., Cook, E. M., Dadashian, E. L., Wiestner, A., Park, H. J., and Rader, C. (2018) Potent and selective antitumor activity of a T cell-engaging bispecific antibody targeting a membrane-proximal epitope of ROR1. Proc Natl Acad Sci U S A. 115, E5467-E5476
Wittenborn, E. C., Merrouch, M., Ueda, C., Fradale, L., Léger, C., Fourmond, V., Pandelia, M. - E., Dementin, S., and Drennan, C. L. (2018) Redox-dependent rearrangements of the NiFeS cluster of carbon monoxide dehydrogenase. Elife. 10.7554/eLife.39451
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
Brown, K. L., Banerjee, S., Feigley, A., Abe, H., Blackwell, T. S., Pozzi, A., Hudson, B. G., and Zent, R. (2018) Salt-bridge modulates differential calcium-mediated ligand binding to integrin α1- and α2-I domains.. Sci Rep. 8, 2916
Macdonald, R., Cascio, D., Collazo, M. J., Phillips, M., and Clubb, R. T. (2018) The Shr protein captures human hemoglobin using two structurally unique binding domains. J Biol Chem. 293, 18365-18377
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
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
Papp-Wallace, K. M., Nguyen, N. Q., Jacobs, M. R., Bethel, C. R., Barnes, M. D., Kumar, V., Bajaksouzian, S., Rudin, S. D., Rather, P. N., Bhavsar, S., Ravikumar, T., Deshpande, P. K., Patil, V., Yeole, R., Bhagwat, S. S., Patel, M. V., van den Akker, F., and Bonomo, R. A. (2018) Strategic Approaches to Overcome Resistance against Gram-Negative Pathogens Using β-Lactamase Inhibitors and β-Lactam Enhancers: Activity of Three Novel Diazabicyclooctanes WCK 5153, Zidebactam (WCK 5107), and WCK 4234.. J Med Chem. 61, 4067-4086
Papp-Wallace, K. M., Nguyen, N. Q., Jacobs, M. R., Bethel, C. R., Barnes, M. D., Kumar, V., Bajaksouzian, S., Rudin, S. D., Rather, P. N., Bhavsar, S., Ravikumar, T., Deshpande, P. K., Patil, V., Yeole, R., Bhagwat, S. S., Patel, M. V., van den Akker, F., and Bonomo, R. A. (2018) Strategic Approaches to Overcome Resistance against Gram-Negative Pathogens Using β-Lactamase Inhibitors and β-Lactam Enhancers: Activity of Three Novel Diazabicyclooctanes WCK 5153, Zidebactam (WCK 5107), and WCK 4234.. J Med Chem. 61, 4067-4086
Papp-Wallace, K. M., Nguyen, N. Q., Jacobs, M. R., Bethel, C. R., Barnes, M. D., Kumar, V., Bajaksouzian, S., Rudin, S. D., Rather, P. N., Bhavsar, S., Ravikumar, T., Deshpande, P. K., Patil, V., Yeole, R., Bhagwat, S. S., Patel, M. V., van den Akker, F., and Bonomo, R. A. (2018) Strategic Approaches to Overcome Resistance against Gram-Negative Pathogens Using β-Lactamase Inhibitors and β-Lactam Enhancers: Activity of Three Novel Diazabicyclooctanes WCK 5153, Zidebactam (WCK 5107), and WCK 4234.. J Med Chem. 61, 4067-4086
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
Lam, K. - H., Sikorra, S., Weisemann, J., Maatsch, H., Perry, K., Rummel, A., Binz, T., and Jin, R. (2018) Structural and biochemical characterization of the protease domain of the mosaic botulinum neurotoxin type HA. Pathog Dis. 10.1093/femspd/fty044
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
Sun, J., Paduch, M., Kim, S. - A., Kramer, R. M., Barrios, A. F., Lu, V., Luke, J., Usatyuk, S., Kossiakoff, A. A., and Tan, S. (2018) Structural basis for activation of SAGA histone acetyltransferase Gcn5 by partner subunit Ada2. Proc Natl Acad Sci U S A. 10.1073/pnas.1805343115
M Puno, R., and Lima, C. D. (2018) Structural basis for MTR4-ZCCHC8 interactions that stimulate the MTR4 helicase in the nuclear exosome-targeting complex. Proc Natl Acad Sci U S A. 10.1073/pnas.1803530115
Rechkoblit, O., Choudhury, J. Roy, Buku, A., Prakash, L., Prakash, S., and Aggarwal, A. K. (2018) Structural basis for polymerase η-promoted resistance to the anticancer nucleoside analog cytarabine.. Sci Rep. 8, 12702
Rechkoblit, O., Choudhury, J. Roy, Buku, A., Prakash, L., Prakash, S., and Aggarwal, A. K. (2018) Structural basis for polymerase η-promoted resistance to the anticancer nucleoside analog cytarabine.. Sci Rep. 8, 12702
Yang, Y., Kang, D., Nguyen, L. A., Smithline, Z. B., Pannecouque, C., Zhan, P., Liu, X., and Steitz, T. A. (2018) Structural basis for potent and broad inhibition of HIV-1 RT by thiophene[3,2-]pyrimidine non-nucleoside inhibitors. Elife. 10.7554/eLife.36340
Chen, P., Tao, L., Wang, T., Zhang, J., He, A., Lam, K. - H., Liu, Z., He, X., Perry, K., Dong, M., and Jin, R. (2018) Structural basis for recognition of frizzled proteins by toxin B. Science. 360, 664-669
Chan, R. T., Peters, J. K., Robart, A. R., Wiryaman, T., Rajashankar, K. R., and Toor, N. (2018) Structural basis for the second step of group II intron splicing. Nat Commun. 9, 4676
Omattage, N. S., Deng, Z., Pinkner, J. S., Dodson, K. W., Almqvist, F., Yuan, P., and Hultgren, S. J. (2018) Structural basis for usher activation and intramolecular subunit transfer in P pilus biogenesis in Escherichia coli. Nat Microbiol. 10.1038/s41564-018-0255-y

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