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Jonnalagadda, R., Flores, A. Del Rio, Cai, W., Mehmood, R., Narayanamoorthy, M., Ren, C., Zaragoza, J. Paulo T., Kulik, H. J., Zhang, W., and Drennan, C. L. (2020) Biochemical and crystallographic investigations into isonitrile formation by a non-heme iron-dependent oxidase/decarboxylase. J Biol Chem. 10.1074/jbc.RA120.015932
Winter, J. M., Cascio, D., Dietrich, D., Sato, M., Watanabe, K., Sawaya, M. R., Vederas, J. C., and Tang, Y. (2015) Biochemical and Structural Basis for Controlling Chemical Modularity in Fungal Polyketide Biosynthesis. J Am Chem Soc. 137, 9885-93
van Rosenburgh, I. K. van Alde, Lu, D. M., Grant, M. J., Stayrook, S. E., Phadke, M., Walther, Z., Goldberg, S. B., Politi, K., Lemmon, M. A., Ashtekar, K. D., and Tsutsui, Y. (2022) Biochemical and structural basis for differential inhibitor sensitivity of EGFR with distinct exon 19 mutations. Nat Commun. 13, 6791
Grell, T. A. J., Young, A. P., Drennan, C. L., and Bandarian, V. (2018) Biochemical and Structural Characterization of a Schiff Base in the Radical-Mediated Biosynthesis of 4-Demethylwyosine by TYW1. J Am Chem Soc. 10.1021/jacs.8b01493
French, J. B., and Ealick, S. E. (2010) Biochemical and structural characterization of a ureidoglycine aminotransferase in the Klebsiella pneumoniae uric acid catabolic pathway. Biochemistry. 49, 5975-7
Hicks, K. A., and Ealick, S. E. (2016) Biochemical and structural characterization of Klebsiella pneumoniae oxamate amidohydrolase in the uric acid degradation pathway. Acta Crystallogr D Struct Biol. 72, 808-16
Fenwick, M. K., Almabruk, K. H., Ealick, S. E., Begley, T. P., and Philmus, B. (2017) Biochemical Characterization and Structural Basis of Reactivity and Regioselectivity Differences between Burkholderia thailandensis and Burkholderia glumae 1,6-Didesmethyltoxoflavin N-Methyltransferase. Biochemistry. 10.1021/acs.biochem.7b00476
Lin, L. Yingqi, McCarthy, S., Powell, B. M., Manurung, Y., Xiang, I. M., Dean, W. L., Chaires, B., and Yatsunyk, L. A. (2020) Biophysical and X-ray structural studies of the (GGGTT)3GGG G-quadruplex in complex with N-methyl mesoporphyrin IX. PLoS One. 15, e0241513
Oyala, P. H., Ravichandran, K. R., Funk, M. A., Stucky, P. A., Stich, T. A., Drennan, C. L., R Britt, D., and Stubbe, J. A. (2016) Biophysical Characterization of Fluorotyrosine Probes Site-Specifically Incorporated into Enzymes: E. coli Ribonucleotide Reductase As an Example. J Am Chem Soc. 138, 7951-64
Nakashige, T. G., Bowman, S. E. J., Zygiel, E. M., Drennan, C. L., and Nolan, E. M. (2018) Biophysical Examination of the Calcium-Modulated Nickel-Binding Properties of Human Calprotectin Reveals Conformational Change in the EF-Hand Domains and HisAsp Site. Biochemistry. 10.1021/acs.biochem.8b00415
Korasick, D. A., Singh, H., Pemberton, T. A., Luo, M., Dhatwalia, R., and Tanner, J. J. (2017) Biophysical investigation of type A PutAs reveals a conserved core oligomeric structure. FEBS J. 10.1111/febs.14165
Pluskal, T., Torrens-Spence, M. P., Fallon, T. R., De Abreu, A., Shi, C. H., and Weng, J. - K. (2018) The biosynthetic origin of psychoactive kavalactones in kava. bioRxiv
Pluskal, T., Torrens-Spence, M. P., Fallon, T. R., De Abreu, A., Shi, C. H., and Weng, J. - K. (2019) The biosynthetic origin of psychoactive kavalactones in kava. Nat Plants. 5, 867-878
Kelso, S., Orlicky, S., Beenstock, J., Ceccarelli, D. F., Kurinov, I., Gish, G., and Sicheri, F. (2021) Bipartite binding of the N terminus of Skp2 to cyclin A. Structure. 10.1016/j.str.2021.04.011
Fischer, P. D., Papadopoulos, E., Dempersmier, J. M., Wang, Z. - F., Nowak, R. P., Donovan, K. A., Kalabathula, J., Gorgulla, C., Junghanns, P. P. M., Kabha, E., Dimitrakakis, N., Petrov, O. I., Mitsiades, C., Ducho, C., Gelev, V., Fischer, E. S., Wagner, G., and Arthanari, H. (2021) A biphenyl inhibitor of eIF4E targeting an internal binding site enables the design of cell-permeable PROTAC-degraders. Eur J Med Chem. 219, 113435
Rogers, J. M., Waters, C. T., Seegar, T. C. M., Jarrett, S. M., Hallworth, A. N., Blacklow, S. C., and Bulyk, M. L. (2019) Bispecific Forkhead Transcription Factor FoxN3 Recognizes Two Distinct Motifs with Different DNA Shapes. Mol Cell. 10.1016/j.molcel.2019.01.019
Blumberg, L. J., Humphries, J. E., Jones, S. D., Pearce, L. B., Holgate, R., Hearn, A., Cheung, J., Mahmood, A., Del Tito, B., Graydon, J. S., Stolz, L. E., Bitonti, A., Purohit, S., de Graaf, D., Kacena, K., Andersen, J. T., Christianson, G. J., Roopenian, D. C., Hubbard, J. J., Gandhi, A. K., Lasseter, K., Pyzik, M., and Blumberg, R. S. (2019) Blocking FcRn in humans reduces circulating IgG levels and inhibits IgG immune complex-mediated immune responses. Sci Adv. 5, eaax9586
Easterhoff, D., M Moody, A., Fera, D., Cheng, H., Ackerman, M., Wiehe, K., Saunders, K. O., Pollara, J., Vandergrift, N., Parks, R., Kim, J., Michael, N. L., O'Connell, R. J., Excler, J. - L., Robb, M. L., Vasan, S., Rerks-Ngarm, S., Kaewkungwal, J., Pitisuttithum, P., Nitayaphan, S., Sinangil, F., Tartaglia, J., Phogat, S., Kepler, T. B., S Alam, M., Liao, H. - X., Ferrari, G., Seaman, M. S., Montefiori, D. C., Tomaras, G. D., Harrison, S. C., and Haynes, B. F. (2017) Boosting of HIV envelope CD4 binding site antibodies with long variable heavy third complementarity determining region in the randomized double blind RV305 HIV-1 vaccine trial. PLoS Pathog. 13, e1006182
Gu, S., Rumpel, S., Zhou, J., Strotmeier, J., Bigalke, H., Perry, K., Shoemaker, C. B., Rummel, A., and Jin, R. (2012) Botulinum neurotoxin is shielded by NTNHA in an interlocked complex. Science. 335, 977-81
Boughton, A. J., Krueger, S., and Fushman, D. (2020) Branching via K11 and K48 Bestows Ubiquitin Chains with a Unique Interdomain Interface and Enhanced Affinity for Proteasomal Subunit Rpn1. Structure. 28, 29-43.e6
Whittle, J. R. R., Zhang, R., Khurana, S., King, L. R., Manischewitz, J., Golding, H., Dormitzer, P. R., Haynes, B. F., Walter, E. B., M Moody, A., Kepler, T. B., Liao, H. - X., and Harrison, S. C. (2011) Broadly neutralizing human antibody that recognizes the receptor-binding pocket of influenza virus hemagglutinin. Proc Natl Acad Sci U S A. 108, 14216-21
Fenwick, M. K., Philmus, B., Begley, T. P., and Ealick, S. E. (2016) Burkholderia glumae ToxA Is a Dual-Specificity Methyltransferase That Catalyzes the Last Two Steps of Toxoflavin Biosynthesis. Biochemistry. 55, 2748-59

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