Publications

Found 1619 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
Jenson, J. M., Xue, V., Stretz, L., Mandal, T., Reich, L. Luther, and Keating, A. E. (2018) Peptide design by optimization on a data-parameterized protein interaction landscape. Proc Natl Acad Sci U S A. 115, E10342-E10351
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
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
Novikova, I. V., Sharma, N., Moser, T., Sontag, R., Liu, Y., Collazo, M. J., Cascio, D., Shokuhfar, T., Hellmann, H., Knoblauch, M., and Evans, J. E. (2018) Protein structural biology using cell-free platform from wheat germ. Adv Struct Chem Imaging. 4, 13
Murphy, F. (2018) Rapd - Automated processing/structure determination. Best Practices for the Collection, Processing, Analysis, Transfer and Storage of Data from the New SER-CAT Eiger 16M Detector, April 12, 2018
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
Hoffer, E. D., Maehigashi, T., Fredrick, K., and Dunham, C. M. (2018) Ribosomal ambiguity (ram) mutations promote the open (off) to closed (on) transition and thereby increase miscoding.. Nucleic Acids Res. 10.1093/nar/gky1178
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
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
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
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
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
Liu, H., Wang, C., Lee, S., Ning, F., Wang, Y., Zhang, Q., Chen, Z., Zang, J., Nix, J., Dai, S., Marrack, P., Hagman, J., Kappler, J., and Zhang, G. (2018) Specific Recognition of Arginine Methylated Histone Tails by JMJD5 and JMJD7. Sci Rep. 8, 3275
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
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
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
Nomura, Y., Roston, D., Montemayor, E. J., Cui, Q., and Butcher, S. E. (2018) Structural and mechanistic basis for preferential deadenylation of U6 snRNA by Usb1. Nucleic Acids Res. 10.1093/nar/gky812
Singh, A. K., Saotome, K., McGoldrick, L. L., and Sobolevsky, A. I. (2018) Structural bases of TRP channel TRPV6 allosteric modulation by 2-APB. Nat Commun. 9, 2465
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

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