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Khabibullina, N. F., Tereshchenkov, A. G., Komarova, E. S., Syroegin, E. A., Shiriaev, D. I., Paleskava, A., Kartsev, V. G., Bogdanov, A. A., Konevega, A. L., Dontsova, O. A., Sergiev, P. V., Osterman, I. A., and Polikanov, Y. S. (2019) Structure of dirithromycin bound to the bacterial ribosome suggests new ways for rational improvement of macrolides. Antimicrob Agents Chemother. 10.1128/AAC.02266-18
Tyler, R. C., Bitto, E., Berndsen, C. E., Bingman, C. A., Singh, S., Lee, M. S., Wesenberg, G. E., Denu, J. M., Phillips, G. N., and Markley, J. L. (2006) Structure of Arabidopsis thaliana At1g77540 protein, a minimal acetyltransferase from the COG2388 family. Biochemistry. 45, 14325-36
Gibson, M. I., Brignole, E. J., Pierce, E., Can, M., Ragsdale, S. W., and Drennan, C. L. (2015) The Structure of an Oxalate Oxidoreductase Provides Insight into Microbial 2-Oxoacid Metabolism. Biochemistry. 54, 4112-20
Rudolph, M. J., Davis, S. A., Haque, H. M. Emranul, Ejemel, M., Cavacini, L. A., Vance, D. J., Willsey, G. G., Piazza, C. Lyn, Weis, D. D., Wang, Y., and Mantis, N. J. (2023) Structure of a transmission blocking antibody in complex with Outer surface protein A from the Lyme disease spirochete, Borreliella burgdorferi. Proteins. 10.1002/prot.26549
Durniak, K. J., Bailey, S., and Steitz, T. A. (2008) The structure of a transcribing T7 RNA polymerase in transition from initiation to elongation. Science. 322, 553-7
Toms, A. V., Deshpande, A., McNally, R., Jeong, Y., Rogers, J. M., Kim, C. Un, Gruner, S. M., Ficarro, S. B., Marto, J. A., Sattler, M., Griffin, J. D., and Eck, M. J. (2013) Structure of a pseudokinase-domain switch that controls oncogenic activation of Jak kinases. Nat Struct Mol Biol. 20, 1221-3
Schauder, C. M., Wu, X., Saheki, Y., Narayanaswamy, P., Torta, F., Wenk, M. R., De Camilli, P., and Reinisch, K. M. (2014) Structure of a lipid-bound extended synaptotagmin indicates a role in lipid transfer. Nature. 510, 552-5
Vaidya, A. T., Chen, C. - H., Dunlap, J. C., Loros, J. J., and Crane, B. R. (2011) Structure of a light-activated LOV protein dimer that regulates transcription. Sci Signal. 4, ra50
Duda, D. M., Olszewski, J. L., Tron, A. E., Hammel, M., Lambert, L. J., M Waddell, B., Mittag, T., DeCaprio, J. A., and Schulman, B. A. (2012) Structure of a glomulin-RBX1-CUL1 complex: inhibition of a RING E3 ligase through masking of its E2-binding surface. Mol Cell. 47, 371-82
Duda, D. M., Olszewski, J. L., Tron, A. E., Hammel, M., Lambert, L. J., M Waddell, B., Mittag, T., DeCaprio, J. A., and Schulman, B. A. (2012) Structure of a glomulin-RBX1-CUL1 complex: inhibition of a RING E3 ligase through masking of its E2-binding surface. Mol Cell. 47, 371-82
Bae, B., Feklistov, A., Lass-Napiorkowska, A., Landick, R., and Darst, S. A. (2015) Structure of a bacterial RNA polymerase holoenzyme open promoter complex. Elife. 10.7554/eLife.08504
Li, W., Schulman, S., Dutton, R. J., Boyd, D., Beckwith, J., and Rapoport, T. A. (2010) Structure of a bacterial homologue of vitamin K epoxide reductase. Nature. 463, 507-12
Fisher, O. S., Deng, H., Liu, D., Zhang, Y., Wei, R., Deng, Y., Zhang, F., Louvi, A., Turk, B. E., Boggon, T. J., and Su, B. (2015) Structure and vascular function of MEKK3-cerebral cavernous malformations 2 complex. Nat Commun. 6, 7937
Fisher, O. S., Deng, H., Liu, D., Zhang, Y., Wei, R., Deng, Y., Zhang, F., Louvi, A., Turk, B. E., Boggon, T. J., and Su, B. (2015) Structure and vascular function of MEKK3-cerebral cavernous malformations 2 complex. Nat Commun. 6, 7937
Tu, D., Zhu, Z., Zhou, A. Y., Yun, C. -hong, Lee, K. - E., Toms, A. V., Li, Y., Dunn, G. P., Chan, E., Thai, T., Yang, S., Ficarro, S. B., Marto, J. A., Jeon, H., Hahn, W. C., Barbie, D. A., and Eck, M. J. (2013) Structure and ubiquitination-dependent activation of TANK-binding kinase 1. Cell Rep. 3, 747-58
da Rosa, S. Tabares-, Wogulis, L. A., Wogulis, M. D., González-Sapienza, G., and Wilson, D. K. (2019) Structure and specificity of several triclocarban-binding single domain camelid antibody fragments. J Mol Recognit. 32, e2755
Swofford, C. A., Nordeen, S. A., Chen, L., Desai, M. M., Chen, J., Springs, S. L., Schwartz, T. U., and Sinskey, A. J. (2022) Structure and Specificity of an Anti-Chloramphenicol Single Domain Antibody for Detection of Amphenicol Residues. Protein Sci. 10.1002/pro.4457
Wasmuth, E. V., Zinder, J. C., Zattas, D., Das, M., and Lima, C. D. (2017) Structure and reconstitution of yeast Mpp6-nuclear exosome complexes reveals that Mpp6 stimulates RNA decay and recruits the Mtr4 helicase. Elife. 10.7554/eLife.29062
Tkacik, E., Li, K., Del Pino, G. Gonzalez-, Ha, B. Hak, Vinals, J., Park, E., Beyett, T. S., and Eck, M. J. (2023) Structure and RAF family kinase isoform selectivity of type II RAF inhibitors tovorafenib and naporafenib. J Biol Chem. 299, 104634
Dieck, C. L., Tzoneva, G., Forouhar, F., Carpenter, Z., Ambesi-Impiombato, A., Sanchez-Martin, M., Kirschner-Schwabe, R., Lew, S., Seetharaman, J., Tong, L., and Ferrando, A. A. (2018) Structure and Mechanisms of NT5C2 Mutations Driving Thiopurine Resistance in Relapsed Lymphoblastic Leukemia. Cancer Cell. 34, 136-147.e6
Guo, X., Schmiege, P., Assafa, T. E., Wang, R., Xu, Y., Donnelly, L., Fine, M., Ni, X., Jiang, J., Millhauser, G., Feng, L., and Li, X. (2022) Structure and mechanism of human cystine exporter cystinosin. Cell. 185, 3739-3752.e18
Sanches, M., Duffy, N. M., Talukdar, M., Thevakumaran, N., Chiovitti, D., Canny, M. D., Lee, K., Kurinov, I., Uehling, D., Al-awar, R., Poda, G., Prakesch, M., Wilson, B., Tam, V., Schweitzer, C., Toro, A., Lucas, J. L., Vuga, D., Lehmann, L., Durocher, D., Zeng, Q., Patterson, J. B., and Sicheri, F. (2014) Structure and mechanism of action of the hydroxy-aryl-aldehyde class of IRE1 endoribonuclease inhibitors. Nat Commun. 5, 4202
Sanches, M., Duffy, N. M., Talukdar, M., Thevakumaran, N., Chiovitti, D., Canny, M. D., Lee, K., Kurinov, I., Uehling, D., Al-awar, R., Poda, G., Prakesch, M., Wilson, B., Tam, V., Schweitzer, C., Toro, A., Lucas, J. L., Vuga, D., Lehmann, L., Durocher, D., Zeng, Q., Patterson, J. B., and Sicheri, F. (2014) Structure and mechanism of action of the hydroxy-aryl-aldehyde class of IRE1 endoribonuclease inhibitors. Nat Commun. 5, 4202
Deng, S., Magin, R. S., Wei, X., Pan, B., E Petersson, J., and Marmorstein, R. (2019) Structure and Mechanism of Acetylation by the N-Terminal Dual Enzyme NatA/Naa50 Complex. Structure. 27, 1057-1070.e4
Dickson, V. Kane, Pedi, L., and Long, S. B. (2014) Structure and insights into the function of a Ca(2+)-activated Cl(-) channel. Nature. 516, 213-8

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