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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
Cao, Y., Qiu, T., Kathayat, R. S., Azizi, S. - A., Thorne, A. K., Ahn, D., Fukata, Y., Fukata, M., Rice, P. A., and Dickinson, B. C. (2019) ABHD10 is an S-depalmitoylase affecting redox homeostasis through peroxiredoxin-5. Nat Chem Biol. 15, 1232-1240
Silvaroli, J. A., Widjaja-Adhi, M. Airanthi K., Trischman, T., Chelstowska, S., Horwitz, S., Banerjee, S., Kiser, P. D., Blaner, W. S., and Golczak, M. (2019) Abnormal Cannabidiol Modulates Vitamin A Metabolism by Acting as a Competitive Inhibitor of CRBP1. ACS Chem Biol. 10.1021/acschembio.8b01070
Liu, Y., Esyunina, D., Olovnikov, I., Teplova, M., Kulbachinskiy, A., Aravin, A. A., and Patel, D. J. (2018) Accommodation of Helical Imperfections in Rhodobacter sphaeroides Argonaute Ternary Complexes with Guide RNA and Target DNA. Cell Rep. 24, 453-462
Li, Z., Wang, S., Nattermann, U., Bera, A. K., Borst, A. J., Yaman, M. Y., Bick, M. J., Yang, E. C., Sheffler, W., Lee, B., Seifert, S., Hura, G. L., Nguyen, H., Kang, A., Dalal, R., Lubner, J. M., Hsia, Y., Haddox, H., Courbet, A., Dowling, Q., Miranda, M., Favor, A., Etemadi, A., Edman, N. I., Yang, W., Weidle, C., Sankaran, B., Negahdari, B., Ross, M. B., Ginger, D. S., and Baker, D. (2023) Accurate computational design of three-dimensional protein crystals. Nat Mater. 10.1038/s41563-023-01683-1
King, N. P., Bale, J. B., Sheffler, W., McNamara, D. E., Gonen, S., Gonen, T., Yeates, T. O., and Baker, D. (2014) Accurate design of co-assembling multi-component protein nanomaterials. Nature. 510, 103-8
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
Mikhaylov, V., Brambley, C. A., Keller, G. L. J., Arbuiso, A. G., Weiss, L. I., Baker, B. M., and Levine, A. J. (2023) Accurate modeling of peptide-MHC structures with AlphaFold. Structure. 10.1016/j.str.2023.11.011
Lu-Culligan, W. J., Connor, L. J., Xie, Y., Ekundayo, B. E., Rose, B. T., Machyna, M., Pintado-Urbanc, A. P., Zimmer, J. T., Vock, I. W., Bhanu, N. V., King, M. C., Garcia, B. A., Bleichert, F., and Simon, M. D. (2023) Acetyl-methyllysine marks chromatin at active transcription start sites. Nature. 622, 173-179
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
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
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
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
Mealka, M., Sierra, N. A., Matteo, D. Avellaneda, Albekioni, E., Khoury, R., Mai, T., Conley, B. M., Coleman, N. J., Sabo, K. A., Komives, E. A., Bobkov, A. A., Cooksy, A. L., Silletti, S., Schiffer, J. M., Huxford, T., and Sohl, C. D. (2024) Active site remodeling in tumor-relevant IDH1 mutants drives distinct kinetic features and potential resistance mechanisms. Nat Commun. 15, 3785
Mealka, M., Sierra, N. A., Matteo, D. Avellaneda, Albekioni, E., Khoury, R., Mai, T., Conley, B. M., Coleman, N. J., Sabo, K. A., Komives, E. A., Bobkov, A. A., Cooksy, A. L., Silletti, S., Schiffer, J. M., Huxford, T., and Sohl, C. D. (2024) Active site remodeling in tumor-relevant IDH1 mutants drives distinct kinetic features and potential resistance mechanisms. Nat Commun. 15, 3785
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
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
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
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
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
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

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