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Ye, Q., Kim, D. Hyun, Dereli, I., Rosenberg, S. C., Hagemann, G., Herzog, F., Tóth, A., Cleveland, D. W., and Corbett, K. D. (2017) The AAA+ ATPase TRIP13 remodels HORMA domains through N-terminal engagement and unfolding. EMBO J. 10.15252/embj.201797291
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
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
May, J. M., Owens, T. W., Mandler, M. D., Simpson, B. W., Lazarus, M. B., Sherman, D. J., Davis, R. M., Okuda, S., Massefski, W., Ruiz, N., and Kahne, D. (2017) The Antibiotic Novobiocin Binds and Activates the ATPase That Powers Lipopolysaccharide Transport. J Am Chem Soc. 139, 17221-17224
Sangwan, S., Zhao, A., Adams, K. L., Jayson, C. K., Sawaya, M. R., Guenther, E. L., Pan, A. C., Ngo, J., Moore, D. M., Soriaga, A. B., Do, T. D., Goldschmidt, L., Nelson, R., Bowers, M. T., Koehler, C. M., Shaw, D. E., Novitch, B. G., and Eisenberg, D. S. (2017) Atomic structure of a toxic, oligomeric segment of SOD1 linked to amyotrophic lateral sclerosis (ALS). Proc Natl Acad Sci U S A. 114, 8770-8775
Krotee, P., Rodriguez, J. A., Sawaya, M. R., Cascio, D., Reyes, F. E., Shi, D., Hattne, J., Nannenga, B. L., Oskarsson, M. E., Philipp, S., Griner, S., Jiang, L., Glabe, C. G., Westermark, G. T., Gonen, T., and Eisenberg, D. S. (2017) Atomic structures of fibrillar segments of hIAPP suggest tightly mated β-sheets are important for cytotoxicity.. Elife. 10.7554/eLife.19273
Bale, J. B., Gonen, S., Liu, Y., Sheffler, W., Ellis, D., Thomas, C., Cascio, D., Yeates, T. O., Gonen, T., King, N. P., and Baker, D. (2016) Accurate design of megadalton-scale two-component icosahedral protein complexes. Science. 353, 389-94
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
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
Wojcik, J., Lamontanara, A. Joaquim, Grabe, G., Koide, A., Akin, L., Gerig, B., Hantschel, O., and Koide, S. (2016) Allosteric Inhibition of Bcr-Abl Kinase by High Affinity Monobody Inhibitors Directed to the Src Homology 2 (SH2)-Kinase Interface. J Biol Chem. 291, 8836-47
Nicoludis, J. M., Vogt, B. E., Green, A. G., Schärfe, C. Pi, Marks, D. S., and Gaudet, R. (2016) Antiparallel protocadherin homodimers use distinct affinity- and specificity-mediating regions in cadherin repeats 1-4. Elife. 10.7554/eLife.18449
Uddin, M. Jashim, Crews, B. C., Xu, S., Ghebreselasie, K., Daniel, C. K., Kingsley, P. J., Banerjee, S., and Marnett, L. J. (2016) Antitumor Activity of Cytotoxic Cyclooxygenase-2 Inhibitors. ACS Chem Biol. 11, 3052-3060
Hanke, L., Knockenhauer, K. E., R Brewer, C., van Diest, E., Schmidt, F. I., Schwartz, T. U., and Ploegh, H. L. (2016) The Antiviral Mechanism of an Influenza A Virus Nucleoprotein-Specific Single-Domain Antibody Fragment. MBio. 10.1128/mBio.01569-16
Saxton, R. A., Knockenhauer, K. E., Schwartz, T. U., and Sabatini, D. M. (2016) The apo-structure of the leucine sensor Sestrin2 is still elusive. Sci Signal. 9, ra92
Polikanov, Y. S., and Moore, P. B. (2015) Acoustic vibrations contribute to the diffuse scatter produced by ribosome crystals. Acta Crystallogr D Biol Crystallogr. 71, 2021-31
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
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
Ingram, J. R., Knockenhauer, K. E., Markus, B. M., Mandelbaum, J., Ramek, A., Shan, Y., Shaw, D. E., Schwartz, T. U., Ploegh, H. L., and Lourido, S. (2015) Allosteric activation of apicomplexan calcium-dependent protein kinases. Proc Natl Acad Sci U S A. 112, E4975-84
Zhang, Z. - M., Rothbart, S. B., Allison, D. F., Cai, Q., Harrison, J. S., Li, L., Wang, Y., Strahl, B. D., Wang, G. Greg, and Song, J. (2015) An Allosteric Interaction Links USP7 to Deubiquitination and Chromatin Targeting of UHRF1. Cell Rep. 12, 1400-6
Thompson, M. C., Cascio, D., Leibly, D. J., and Yeates, T. O. (2015) An allosteric model for control of pore opening by substrate binding in the EutL microcompartment shell protein. Protein Sci. 24, 956-75
Murphy, M. W., Lee, J. K., Rojo, S., Gearhart, M. D., Kurahashi, K., Banerjee, S., Loeuille, G. - A., Bashamboo, A., McElreavey, K., Zarkower, D., Aihara, H., and Bardwell, V. J. (2015) An ancient protein-DNA interaction underlying metazoan sex determination. Nat Struct Mol Biol. 22, 442-51
Zhou, Q., Lai, Y., Bacaj, T., Zhao, M., Lyubimov, A. Y., Uervirojnangkoorn, M., Zeldin, O. B., Brewster, A. S., Sauter, N. K., Cohen, A. E., S Soltis, M., Alonso-Mori, R., Chollet, M., Lemke, H. T., Pfuetzner, R. A., Choi, U. B., Weis, W. I., Diao, J., Südhof, T. C., and Brunger, A. T. (2015) Architecture of the synaptotagmin-SNARE machinery for neuronal exocytosis. Nature. 525, 62-7
Diao, J., Liu, R., Rong, Y., Zhao, M., Zhang, J., Lai, Y., Zhou, Q., Wilz, L. M., Li, J., Vivona, S., Pfuetzner, R. A., Brunger, A. T., and Zhong, Q. (2015) ATG14 promotes membrane tethering and fusion of autophagosomes to endolysosomes. Nature. 520, 563-6