Publications

Found 2722 results
2018
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
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
Buzovetsky, O., Tang, C., Knecht, K. M., Antonucci, J. M., Wu, L., Ji, X., and Xiong, Y. (2018) The SAM domain of mouse SAMHD1 is critical for its activation and regulation. Nat Commun. 9, 411
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
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
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
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
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
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
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
Chiang, Y. - C., Levsh, O., Lam, C. Kei, Weng, J. - K., and Wang, Y. (2018) Structural and dynamic basis of substrate permissiveness in hydroxycinnamoyltransferase (HCT). PLoS Comput Biol. 14, e1006511
Dayeh, D. M., Kruithoff, B. C., and Nakanishi, K. (2018) Structural and functional analyses reveal the contributions of the C- and N-lobes of Argonaute protein to selectivity of RNA target cleavage. J Biol Chem. 10.1074/jbc.RA117.001051
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
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
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
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
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

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