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Mir, A., Chen, J., Robinson, K., Lendy, E., Goodman, J., Neau, D., and Golden, B. L. (2015) Two Divalent Metal Ions and Conformational Changes Play Roles in the Hammerhead Ribozyme Cleavage Reaction. Biochemistry. 54, 6369-81
Mishra, A., Devarajan, B., Reardon, M. E., Dwivedi, P., Krishnan, V., Cisar, J. O., Das, A., Narayana, S. V. L., and Ton-That, H. (2011) Two autonomous structural modules in the fimbrial shaft adhesin FimA mediate Actinomyces interactions with streptococci and host cells during oral biofilm development. Mol Microbiol. 81, 1205-20
Narui, Y., and Sotomayor, M. (2018) Tuning Inner-Ear Tip-Link Affinity Through Alternatively Spliced Variants of Protocadherin-15. Biochemistry. 10.1021/acs.biochem.7b01075
Bryk, R., Arango, N., Venugopal, A., J Warren, D., Park, Y. - H., Patel, M. S., Lima, C. D., and Nathan, C. (2010) Triazaspirodimethoxybenzoyls as selective inhibitors of mycobacterial lipoamide dehydrogenase . Biochemistry. 49, 1616-27
Huguenin-Dezot, N., Alonzo, D. A., Heberlig, G. W., Mahesh, M., Nguyen, D. P., Dornan, M. H., Boddy, C. N., T Schmeing, M., and Chin, J. W. (2019) Trapping biosynthetic acyl-enzyme intermediates with encoded 2,3-diaminopropionic acid. Nature. 565, 112-117
Shigdel, U. K., Ovchinnikov, V., Lee, S. - J., Shih, J. A., Karplus, M., Nam, K., and Verdine, G. L. (2020) The trajectory of intrahelical lesion recognition and extrusion by the human 8-oxoguanine DNA glycosylase. Nat Commun. 11, 4437
Koirala, S., Klein, J., Zheng, Y., Glenn, N. O., Eisemann, T., Tacer, K. Fon, Miller, D. J., Kulak, O., Lu, M., Finkelstein, D. B., Neale, G., Tillman, H., Vogel, P., Strand, D. W., Lum, L., Brautigam, C. A., Pascal, J. M., Clements, W. K., and Potts, P. Ryan (2020) Tissue-Specific Regulation of the Wnt/β-Catenin Pathway by PAGE4 Inhibition of Tankyrase.. Cell Rep. 32, 107922
Broussard, T. C., Kobe, M. J., Pakhomova, S., Neau, D. B., Price, A. E., Champion, T. S., and Waldrop, G. L. (2013) The three-dimensional structure of the biotin carboxylase-biotin carboxyl carrier protein complex of E. coli acetyl-CoA carboxylase. Structure. 21, 650-7
Banayan, N. E., Loughlin, B. J., Singh, S., Forouhar, F., Lu, G., Wong, K. - H., Neky, M., Hunt, H. S., Bateman, L. B., Tamez, A., Handelman, S. K., W Price, N., and Hunt, J. F. (2024) Systematic enhancement of protein crystallization efficiency by bulk lysine-to-arginine (KR) substitution. Protein Sci. 33, e4898
Nakaya, T., Yabe, M., Mashalidis, E. H., Sato, T., Yamamoto, K., Hikiji, Y., Katsuyama, A., Shinohara, M., Minato, Y., Takahashi, S., Horiuchi, M., Yokota, S. - I., Lee, S. - Y., and Ichikawa, S. (2022) Synthesis of macrocyclic nucleoside antibacterials and their interactions with MraY. Nat Commun. 13, 7575
Pecic, S., Pakhomova, S., Newcomer, M. E., Morisseau, C., Hammock, B. D., Zhu, Z., Rinderspacher, A., and Deng, S. - X. (2013) Synthesis and structure-activity relationship of piperidine-derived non-urea soluble epoxide hydrolase inhibitors. Bioorg Med Chem Lett. 23, 417-21
Ochoa, J. M., Nguyen, V. N., Nie, M., Sawaya, M. R., Bobik, T. A., and Yeates, T. O. (2020) Symmetry Breaking and Structural Polymorphism in a Bacterial Microcompartment Shell Protein for Choline Utilization. Protein Sci. 10.1002/pro.3941
Ochoa, J. M., Nguyen, V. N., Nie, M., Sawaya, M. R., Bobik, T. A., and Yeates, T. O. (2020) Symmetry Breaking and Structural Polymorphism in a Bacterial Microcompartment Shell Protein for Choline Utilization. Protein Sci. 10.1002/pro.3941
Martin, R., Gupta, K., Ninan, N. S., Perry, K., and Van Duyne, G. D. (2012) The survival motor neuron protein forms soluble glycine zipper oligomers. Structure. 20, 1929-39
Tang, X., Orlicky, S., Lin, Z., Willems, A., Neculai, D., Ceccarelli, D., Mercurio, F., Shilton, B. H., Sicheri, F., and Tyers, M. (2007) Suprafacial orientation of the SCFCdc4 dimer accommodates multiple geometries for substrate ubiquitination. Cell. 129, 1165-76
Dubiella, C., Pinch, B. J., Koikawa, K., Zaidman, D., Poon, E., Manz, T. D., Nabet, B., He, S., Resnick, E., Rogel, A., Langer, E. M., Daniel, C. J., Seo, H. - S., Chen, Y., Adelmant, G., Sharifzadeh, S., Ficarro, S. B., Jamin, Y., da Costa, B. Martins, Zimmerman, M. W., Lian, X., Kibe, S., Kozono, S., Doctor, Z. M., Browne, C. M., Yang, A., Stoler-Barak, L., Shah, R. B., Vangos, N. E., Geffken, E. A., Oren, R., Koide, E., Sidi, S., Shulman, Z., Wang, C., Marto, J. A., Dhe-Paganon, S., Look, T., Zhou, X. Zhen, Lu, K. Ping, Sears, R. C., Chesler, L., Gray, N. S., and London, N. (2021) Sulfopin is a covalent inhibitor of Pin1 that blocks Myc-driven tumors in vivo. Nat Chem Biol. 10.1038/s41589-021-00786-7