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Adak, S., Ye, N., Calderone, L. A., Schäfer, R. J. B., Lukowski, A. L., Pandelia, M. - E., Drennan, C. L., and Moore, B. S. (2023) Oxidative rearrangement of tryptophan to indole nitrile by a single diiron enzyme. bioRxiv. 10.1101/2023.08.03.551874
Brugarolas, P., Movahedzadeh, F., Wang, Y., Zhang, N., Bartek, I. L., Gao, Y. N., Voskuil, M. I., Franzblau, S. G., and He, C. (2012) The oxidation-sensing regulator (MosR) is a new redox-dependent transcription factor in Mycobacterium tuberculosis. J Biol Chem. 287, 37703-12
Xu, S., Hermanson, D. J., Banerjee, S., Ghebreselasie, K., Clayton, G. M., R Garavito, M., and Marnett, L. J. (2014) Oxicams bind in a novel mode to the cyclooxygenase active site via a two-water-mediated H-bonding Network. J Biol Chem. 289, 6799-808
Alwan, S. N., Taylor, A. B., Rhodes, J., Tidwell, M., McHardy, S. F., and LoVerde, P. T. (2023) Oxamniquine derivatives overcome Praziquantel treatment limitations for Schistosomiasis. PLoS Pathog. 19, e1011018
Schormann, N., Hayden, K. L., Lee, P., Banerjee, S., and Chattopadhyay, D. (2019) An overview of structure, function, and regulation of pyruvate kinases. Protein Sci. 10.1002/pro.3691
Liu, C., Zhao, M., Jiang, L., Cheng, P. - N., Park, J., Sawaya, M. R., Pensalfini, A., Gou, D., Berk, A. J., Glabe, C. G., Nowick, J., and Eisenberg, D. (2012) Out-of-register β-sheets suggest a pathway to toxic amyloid aggregates.. Proc Natl Acad Sci U S A. 109, 20913-8
Juang, Y. - C., Landry, M. - C., Sanches, M., Vittal, V., C Y Leung, C., Ceccarelli, D. F., Mateo, A. - R. F., Pruneda, J. N., Mao, D. Y. L., Szilard, R. K., Orlicky, S., Munro, M., Brzovic, P. S., Klevit, R. E., Sicheri, F., and Durocher, D. (2012) OTUB1 co-opts Lys48-linked ubiquitin recognition to suppress E2 enzyme function. Mol Cell. 45, 384-97
Noey, E. L., Tibrewal, N., Jiménez-Osés, G., Osuna, S., Park, J., Bond, C. M., Cascio, D., Liang, J., Zhang, X., Huisman, G. W., Tang, Y., and Houk, K. N. (2015) Origins of stereoselectivity in evolved ketoreductases. Proc Natl Acad Sci U S A. 112, E7065-72
Dong, M., Kathiresan, V., Fenwick, M. K., Torelli, A. T., Zhang, Y., Caranto, J. D., Dzikovski, B., Sharma, A., Lancaster, K. M., Freed, J. H., Ealick, S. E., Hoffman, B. M., and Lin, H. (2018) Organometallic and radical intermediates reveal mechanism of diphthamide biosynthesis. Science. 359, 1247-1250
Lee, K. Sing Steph, Liu, J. - Y., Wagner, K. M., Pakhomova, S., Dong, H., Morisseau, C., Fu, S. H., Yang, J., Wang, P., Ulu, A., Mate, C. A., Nguyen, L. V., Hwang, S. Hee, Edin, M. L., Mara, A. A., Wulff, H., Newcomer, M. E., Zeldin, D. C., and Hammock, B. D. (2014) Optimized inhibitors of soluble epoxide hydrolase improve in vitro target residence time and in vivo efficacy. J Med Chem. 57, 7016-30
Zhang, C. - H., Spasov, K. A., Reilly, R. A., Hollander, K., Stone, E. A., Ippolito, J. A., Liosi, M. - E., Deshmukh, M. G., Tirado-Rives, J., Zhang, S., Liang, Z., Miller, S. J., Isaacs, F., Lindenbach, B. D., Anderson, K. S., and Jorgensen, W. L. (2021) Optimization of Triarylpyridinone Inhibitors of the Main Protease of SARS-CoV-2 to Low-Nanomolar Antiviral Potency. ACS Med Chem Lett. 12, 1325-1332
Andrews, L. D., Kane, T. R., Dozzo, P., Haglund, C. M., Hilderbrandt, D. J., Linsell, M. S., Machajewski, T., McEnroe, G., Serio, A. W., Wlasichuk, K. B., Neau, D. B., Pakhomova, S., Waldrop, G. L., Sharp, M., Pogliano, J., Cirz, R. T., and Cohen, F. (2019) Optimization and Mechanistic Characterization of Pyridopyrimidine Inhibitors of Bacterial Biotin Carboxylase. J Med Chem. 62, 7489-7505
Yang, Y., Liu, X. Roger, Greenberg, Z. J., Zhou, F., He, P., Fan, L., Liu, S., Shen, G., Egawa, T., Gross, M. L., Schuettpelz, L. G., and Li, W. (2020) Open conformation of tetraspanins shapes interaction partner networks on cell membranes. EMBO J. 39, e105246
Rohaim, A., Gong, L. D., Li, J., Rui, H., Blachowicz, L., and Roux, B. (2020) Open and Closed Structures of a Barium-Blocked Potassium Channel. J Mol Biol. 10.1016/j.jmb.2020.06.012
Gibson, M. I., Chen, P. Yang- Ting, Johnson, A. C., Pierce, E., Can, M., Ragsdale, S. W., and Drennan, C. L. (2016) One-carbon chemistry of oxalate oxidoreductase captured by X-ray crystallography. Proc Natl Acad Sci U S A. 113, 320-5
Sohn, J., Grant, R. A., and Sauer, R. T. (2009) OMP peptides activate the DegS stress-sensor protease by a relief of inhibition mechanism. Structure. 17, 1411-21
Li, Y., Zhang, R., Wang, C., Forouhar, F., Clarke, O. B., Vorobiev, S., Singh, S., Montelione, G. T., Szyperski, T., Xu, Y., and Hunt, J. F. (2022) Oligomeric interactions maintain active-site structure in a noncooperative enzyme family. EMBO J. 10.15252/embj.2021108368
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
Morgan, J. L. W., McNamara, J. T., Fischer, M., Rich, J., Chen, H. - M., Withers, S. G., and Zimmer, J. (2016) Observing cellulose biosynthesis and membrane translocation in crystallo. Nature. 531, 329-34
Wang, J., and Ealick, S. E. (2004) Observation of time-resolved structural changes by linear interpolation of highly redundant X-ray diffraction data. Acta Crystallogr D Biol Crystallogr. 60, 1579-85