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Kucera, K., A Koblansky, A., Saunders, L. P., Frederick, K. B., De La Cruz, E. M., Ghosh, S., and Modis, Y. (2010) Structure-based analysis of Toxoplasma gondii profilin: a parasite-specific motif is required for recognition by Toll-like receptor 11. J Mol Biol. 403, 616-29
Xiong, Y., Li, F., Babault, N., Wu, H., Dong, A., Zeng, H., Chen, X., Arrowsmith, C. H., Brown, P. J., Liu, J., Vedadi, M., and Jin, J. (2017) Structure-activity relationship studies of G9a-like protein (GLP) inhibitors. Bioorg Med Chem. 25, 4414-4423
Mann, M. K., Zepeda-Velázquez, C. A., González-Álvarez, H., Dong, A., Kiyota, T., Aman, A. M., Loppnau, P., Li, Y., Wilson, B., Arrowsmith, C. H., Al-awar, R., Harding, R. J., and Schapira, M. (2021) Structure-Activity Relationship of USP5 Inhibitors. J Med Chem. 64, 15017-15036
Banerjee, A., Munir, A., Abdullahu, L., Damha, M. J., Goldgur, Y., and Shuman, S. (2019) Structure of tRNA splicing enzyme Tpt1 illuminates the mechanism of RNA 2'-PO recognition and ADP-ribosylation. Nat Commun. 10, 218
Guan, R., Dai, H., Han, D., Harrison, S. C., and Kirchhausen, T. (2010) Structure of the PTEN-like region of auxilin, a detector of clathrin-coated vesicle budding. Structure. 18, 1191-8
Schureck, M. A., Maehigashi, T., Miles, S. J., Marquez, J., Cho, S. Ei, Erdman, R., and Dunham, C. M. (2014) Structure of the Proteus vulgaris HigB-(HigA)2-HigB toxin-antitoxin complex. J Biol Chem. 289, 1060-70
Cabarca, S., de Souza, M. Frazão, de Oliveira, A. Albert, Muniz, G. S. Vignoli, M Lamy, T., Reis, C. Vinicius D., Takarada, J., Effer, B., Souza, L. Santos, de la Torre, L. Iriarte, Couñago, R., Oliveira, C. Luis Pinto, and Balan, A. (2021) Structure of the PknF and conformational changes induced in forkhead-associated regulatory domains. Curr Res Struct Biol. 3, 165-178
Cabarca, S., de Souza, M. Frazão, de Oliveira, A. Albert, Muniz, G. S. Vignoli, M Lamy, T., Reis, C. Vinicius D., Takarada, J., Effer, B., Souza, L. Santos, de la Torre, L. Iriarte, Couñago, R., Oliveira, C. Luis Pinto, and Balan, A. (2021) Structure of the PknF and conformational changes induced in forkhead-associated regulatory domains. Curr Res Struct Biol. 3, 165-178
Cabarca, S., de Souza, M. Frazão, de Oliveira, A. Albert, Muniz, G. S. Vignoli, M Lamy, T., Reis, C. Vinicius D., Takarada, J., Effer, B., Souza, L. Santos, de la Torre, L. Iriarte, Couñago, R., Oliveira, C. Luis Pinto, and Balan, A. (2021) Structure of the PknF and conformational changes induced in forkhead-associated regulatory domains. Curr Res Struct Biol. 3, 165-178
Dimitrova, Y. N., Jenni, S., Valverde, R., Khin, Y., and Harrison, S. C. (2016) Structure of the MIND Complex Defines a Regulatory Focus for Yeast Kinetochore Assembly. Cell. 167, 1014-1027.e12
Wittenborn, E. C., Jost, M., Wei, Y., Stubbe, J. A., and Drennan, C. L. (2016) Structure of the Catalytic Domain of the Class I Polyhydroxybutyrate Synthase from Cupriavidus necator. J Biol Chem. 291, 25264-25277
Liu, Z., Frutos, S., Bick, M. J., Vila-Perelló, M., Debelouchina, G. T., Darst, S. A., and Muir, T. W. (2014) Structure of the branched intermediate in protein splicing. Proc Natl Acad Sci U S A. 111, 8422-7
Liu, Z., Frutos, S., Bick, M. J., Vila-Perelló, M., Debelouchina, G. T., Darst, S. A., and Muir, T. W. (2014) Structure of the branched intermediate in protein splicing. Proc Natl Acad Sci U S A. 111, 8422-7
Meisner, J., Maehigashi, T., André, I., Dunham, C. M., and Moran, C. P. (2012) Structure of the basal components of a bacterial transporter. Proc Natl Acad Sci U S A. 109, 5446-51
Krishnan, V., Dwivedi, P., Kim, B. J., Samal, A., Macon, K., Ma, X., Mishra, A., Doran, K. S., Ton-That, H., and Narayana, S. V. L. (2013) Structure of Streptococcus agalactiae tip pilin GBS104: a model for GBS pili assembly and host interactions. Acta Crystallogr D Biol Crystallogr. 69, 1073-89
Krishnan, V., Dwivedi, P., Kim, B. J., Samal, A., Macon, K., Ma, X., Mishra, A., Doran, K. S., Ton-That, H., and Narayana, S. V. L. (2013) Structure of Streptococcus agalactiae tip pilin GBS104: a model for GBS pili assembly and host interactions. Acta Crystallogr D Biol Crystallogr. 69, 1073-89
Aoki, S. T., Settembre, E. C., Trask, S. D., Greenberg, H. B., Harrison, S. C., and Dormitzer, P. R. (2009) Structure of rotavirus outer-layer protein VP7 bound with a neutralizing Fab. Science. 324, 1444-7
Duda, D. M., Olszewski, J. L., Schuermann, J. P., Kurinov, I., Miller, D. J., Nourse, A., Alpi, A. F., and Schulman, B. A. (2013) Structure of HHARI, a RING-IBR-RING ubiquitin ligase: autoinhibition of an Ariadne-family E3 and insights into ligation mechanism. Structure. 21, 1030-41
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
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

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