Publications

Found 2722 results
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A
Qiao, Q., Wang, L., Meng, F. - L., Hwang, J. K., Alt, F. W., and Wu, H. (2017) AID Recognizes Structured DNA for Class Switch Recombination. Mol Cell. 67, 361-373.e4
Ivanova, M. I., Sievers, S. A., Guenther, E. L., Johnson, L. M., Winkler, D. D., Galaleldeen, A., Sawaya, M. R., P Hart, J., and Eisenberg, D. S. (2014) Aggregation-triggering segments of SOD1 fibril formation support a common pathway for familial and sporadic ALS. Proc Natl Acad Sci U S A. 111, 197-201
Pinger, J., Nešić, D., Ali, L., Aresta-Branco, F., Lilic, M., Chowdhury, S., Kim, H. - S., Verdi, J., Raper, J., Ferguson, M. A. J., F Papavasiliou, N., and C Stebbins, E. (2018) African trypanosomes evade immune clearance by O-glycosylation of the VSG surface coat. Nat Microbiol. 3, 932-938
Wang, B., Dai, P., Ding, D., Del Rosario, A., Grant, R. A., Pentelute, B. L., and Laub, M. T. (2019) Affinity-based capture and identification of protein effectors of the growth regulator ppGpp. Nat Chem Biol. 15, 141-150
Koirala, D., Shelke, S. A., Dupont, M., Ruiz, S., DasGupta, S., Bailey, L. J., Benner, S. A., and Piccirilli, J. A. (2018) Affinity maturation of a portable Fab-RNA module for chaperone-assisted RNA crystallography. Nucleic Acids Res. 10.1093/nar/gkx1292
Fera, D., Schmidt, A. G., Haynes, B. F., Gao, F., Liao, H. - X., Kepler, T. B., and Harrison, S. C. (2014) Affinity maturation in an HIV broadly neutralizing B-cell lineage through reorientation of variable domains. Proc Natl Acad Sci U S A. 111, 10275-80
McCarthy, K. R., Raymond, D. D., Do, K. T., Schmidt, A. G., and Harrison, S. C. (2019) Affinity maturation in a human humoral response to influenza hemagglutinin. Proc Natl Acad Sci U S A. 10.1073/pnas.1915620116
Lyubimov, A. Y., Uervirojnangkoorn, M., Zeldin, O. B., Zhou, Q., Zhao, M., Brewster, A. S., Michels-Clark, T., Holton, J. M., Sauter, N. K., Weis, W. I., and Brunger, A. T. (2016) Advances in X-ray free electron laser (XFEL) diffraction data processing applied to the crystal structure of the synaptotagmin-1 / SNARE complex. Elife. 10.7554/eLife.18740
Dawson, T. K., Dziedzic, P., Robertson, M. J., Cisneros, J. A., Krimmer, S. G., Newton, A. S., Tirado-Rives, J., and Jorgensen, W. L. (2017) Adding a Hydrogen Bond May Not Help: Naphthyridinone vs Quinoline Inhibitors of Macrophage Migration Inhibitory Factor. ACS Med Chem Lett. 8, 1287-1291
Doherty, E. E., Karki, A., Wilcox, X. E., Mendoza, H. G., Manjunath, A., Matos, V. Jauregui, Fisher, A. J., and Beal, P. A. (2022) ADAR activation by inducing a syn conformation at guanosine adjacent to an editing site. Nucleic Acids Res. 10.1093/nar/gkac897
Stokes-Rees, I., Levesque, I., Murphy, F. V., Yang, W., Deacon, A., and Sliz, P. (2012) Adapting federated cyberinfrastructure for shared data collection facilities in structural biology. J Synchrotron Radiat. 19, 462-7
Wang, E. S., Verano, A. L., Nowak, R. P., J Yuan, C., Donovan, K. A., Eleuteri, N. A., Yue, H., Ngo, K. H., Lizotte, P. H., Gokhale, P. C., Gray, N. S., and Fischer, E. S. (2021) Acute pharmacological degradation of Helios destabilizes regulatory T cells. Nat Chem Biol. 17, 711-717
Henneberg, L. T., Singh, J., Duda, D. M., Baek, K., Yanishevski, D., Murray, P. J., Mann, M., Sidhu, S. S., and Schulman, B. A. (2023) Activity-based profiling of cullin-RING E3 networks by conformation-specific probes. Nat Chem Biol. 19, 1513-1523
Tei, R., Bagde, S. R., J Fromme, C., and Baskin, J. M. (2023) Activity-based directed evolution of a membrane editor in mammalian cells. Nat Chem. 15, 1030-1039
Rut, W., Lv, Z., Zmudzinski, M., Patchett, S., Nayak, D., Snipas, S. J., Oualid, F. El, Huang, T. T., Békés, M., Drag, M., and Olsen, S. K. (2020) Activity profiling and crystal structures of inhibitor-bound SARS-CoV-2 papain-like protease: A framework for anti-COVID-19 drug design. Sci Adv. 10.1126/sciadv.abd4596
Ejaz, A., Goldgur, Y., and Shuman, S. (2019) Activity and structure of MPE, a manganese-dependent single-strand DNA endonuclease encoded in a nucleic acid repair gene cluster. J Biol Chem. 10.1074/jbc.RA119.008049
Baranovskiy, A. G., Duong, V. N., Babayeva, N. D., Zhang, Y., Pavlov, Y. I., Anderson, K. S., and Tahirov, T. H. (2018) Activity and fidelity of human DNA polymerase α depend on primer structure.. J Biol Chem. 10.1074/jbc.RA117.001074
Januszyk, K., Liu, Q., and Lima, C. D. (2011) Activities of human RRP6 and structure of the human RRP6 catalytic domain. RNA. 17, 1566-77
Soriano, E. V., Zhang, Y., Colabroy, K. L., Sanders, J. M., Settembre, E. C., Dorrestein, P. C., Begley, T. P., and Ealick, S. E. (2013) Active-site models for complexes of quinolinate synthase with substrates and intermediates. Acta Crystallogr D Biol Crystallogr. 69, 1685-96
Sit, B., Crowley, S. M., Bhullar, K., Lai, C. Chieh- Lin, Tang, C., Hooda, Y., Calmettes, C., Khambati, H., Ma, C., Brumell, J. H., Schryvers, A. B., Vallance, B. A., and Moraes, T. F. (2015) Active Transport of Phosphorylated Carbohydrates Promotes Intestinal Colonization and Transmission of a Bacterial Pathogen. PLoS Pathog. 11, e1005107
Olsen, S. K., Capili, A. D., Lu, X., Tan, D. S., and Lima, C. D. (2010) Active site remodelling accompanies thioester bond formation in the SUMO E1. Nature. 463, 906-12
Shi, K., Demir, Ö., Carpenter, M. A., Banerjee, S., Harki, D. A., Amaro, R. E., Harris, R. S., and Aihara, H. (2020) Active site plasticity and possible modes of chemical inhibition of the human DNA deaminase APOBEC3B. FASEB Bioadv. 2, 49-58
Rechkoblit, O., Sciaky, D., Kreitler, D. F., Buku, A., Kottur, J., and Aggarwal, A. K. (2024) Activation of CBASS Cap5 endonuclease immune effector by cyclic nucleotides. Nat Struct Mol Biol. 10.1038/s41594-024-01220-x
Atapattu, L., Saha, N., Chheang, C., Eissman, M. F., Xu, K., Vail, M. E., Hii, L., Llerena, C., Liu, Z., Horvay, K., Abud, H. E., Kusebauch, U., Moritz, R. L., Ding, B. - S., Cao, Z., Rafii, S., Ernst, M., Scott, A. M., Nikolov, D. B., Lackmann, M., and Janes, P. W. (2016) An activated form of ADAM10 is tumor selective and regulates cancer stem-like cells and tumor growth. J Exp Med. 213, 1741-57
Blobaum, A. L., Xu, S., Rowlinson, S. W., Duggan, K. C., Banerjee, S., Kudalkar, S. N., Birmingham, W. R., Ghebreselasie, K., and Marnett, L. J. (2015) Action at a distance: mutations of peripheral residues transform rapid reversible inhibitors to slow, tight binders of cyclooxygenase-2. J Biol Chem. 290, 12793-803

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