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Choi, J. Yong, Fuerst, R., Knapinska, A. M., Taylor, A. B., Smith, L., Cao, X., P Hart, J., Fields, G. B., and Roush, W. R. (2017) Structure-Based Design and Synthesis of Potent and Selective Matrix Metalloproteinase 13 Inhibitors. J Med Chem. 60, 5816-5825
Lanier, M., Pickens, J., Bigi, S. V., Bradshaw-Pierce, E. L., Chambers, A., Cheruvallath, Z. S., Cole, D., Dougan, D. R., Ermolieff, J., Gibson, T., Halkowycz, P., Hirokawa, A., Ivetac, A., Miura, J., Nunez, E., Sabat, M., Tyhonas, J., Wang, H., Wang, X., and Swann, S. (2017) Structure-Based Design of ASK1 Inhibitors as Potential Agents for Heart Failure. ACS Med Chem Lett. 8, 316-320
Bogner, A. N., Ji, J., and Tanner, J. J. (2022) Structure-based engineering of minimal Proline dehydrogenase domains for inhibitor discovery. Protein Eng Des Sel. 10.1093/protein/gzac016
Martin, S. E. S., Tan, Z. - W., Itkonen, H. M., Duveau, D. Y., Paulo, J. A., Janetzko, J., Boutz, P. L., Törk, L., Moss, F. A., Thomas, C. J., Gygi, S. P., Lazarus, M. B., and Walker, S. (2018) Structure-Based Evolution of Low Nanomolar O-GlcNAc Transferase Inhibitors. J Am Chem Soc. 10.1021/jacs.8b07328
Martin, S. E. S., Tan, Z. - W., Itkonen, H. M., Duveau, D. Y., Paulo, J. A., Janetzko, J., Boutz, P. L., Törk, L., Moss, F. A., Thomas, C. J., Gygi, S. P., Lazarus, M. B., and Walker, S. (2018) Structure-Based Evolution of Low Nanomolar O-GlcNAc Transferase Inhibitors. J Am Chem Soc. 10.1021/jacs.8b07328
Martin, S. E. S., Tan, Z. - W., Itkonen, H. M., Duveau, D. Y., Paulo, J. A., Janetzko, J., Boutz, P. L., Törk, L., Moss, F. A., Thomas, C. J., Gygi, S. P., Lazarus, M. B., and Walker, S. (2018) Structure-Based Evolution of Low Nanomolar O-GlcNAc Transferase Inhibitors. J Am Chem Soc. 10.1021/jacs.8b07328
Song, J., Teplova, M., Ishibe-Murakami, S., and Patel, D. J. (2012) Structure-based mechanistic insights into DNMT1-mediated maintenance DNA methylation. Science. 335, 709-12
Sheng, G., Gogakos, T., Wang, J., Zhao, H., Serganov, A., Juranek, S., Tuschl, T., Patel, D. J., and Wang, Y. (2017) Structure/cleavage-based insights into helical perturbations at bulge sites within T. thermophilus Argonaute silencing complexes. Nucleic Acids Res. 45, 9149-9163
Lall, P., Lindsay, A. J., Hanscom, S., Kecman, T., Taglauer, E. S., McVeigh, U. M., Franklin, E., McCaffrey, M. W., and Khan, A. R. (2015) Structure-Function Analyses of the Interactions between Rab11 and Rab14 Small GTPases with Their Shared Effector Rab Coupling Protein (RCP). J Biol Chem. 290, 18817-32
Gao, P., Ascano, M., Zillinger, T., Wang, W., Dai, P., Serganov, A. A., Gaffney, B. L., Shuman, S., Jones, R. A., Deng, L., Hartmann, G., Barchet, W., Tuschl, T., and Patel, D. J. (2013) Structure-function analysis of STING activation by c[G(2',5')pA(3',5')p] and targeting by antiviral DMXAA. Cell. 154, 748-62
Li, X. - P., Rudolph, M. J., Chen, Y., and Tumer, N. E. (2024) Structure-Function Analysis of the A1 Subunit of Shiga Toxin 2 with Peptides That Target the P-Stalk Binding Site and Inhibit Activity. Biochemistry. 63, 893-905
Teplova, M., Hafner, M., Teplov, D., Essig, K., Tuschl, T., and Patel, D. J. (2013) Structure-function studies of STAR family Quaking proteins bound to their in vivo RNA target sites. Genes Dev. 27, 928-40
Teplova, M., Hafner, M., Teplov, D., Essig, K., Tuschl, T., and Patel, D. J. (2013) Structure-function studies of STAR family Quaking proteins bound to their in vivo RNA target sites. Genes Dev. 27, 928-40
Teplova, M., Hafner, M., Teplov, D., Essig, K., Tuschl, T., and Patel, D. J. (2013) Structure-function studies of STAR family Quaking proteins bound to their in vivo RNA target sites. Genes Dev. 27, 928-40
Radakovic, A., Lewicka, A., Todisco, M., Aitken, H. R. M., Weiss, Z., Kim, S., Bannan, A., Piccirilli, J. A., and Szostak, J. W. (2024) Structure-guided aminoacylation and assembly of chimeric RNAs. bioRxiv. 10.1101/2024.03.02.583109
Trachman, R. J., Cojocaru, R., Wu, D., Piszczek, G., Ryckelynck, M., Unrau, P. J., and Ferré-D'Amaré, A. R. (2020) Structure-Guided Engineering of the Homodimeric Mango-IV Fluorescence Turn-on Aptamer Yields an RNA FRET Pair. Structure. 10.1016/j.str.2020.04.007
Petrou, V. I., Herrera, C. M., Schultz, K. M., Clarke, O. B., Vendome, J., Tomasek, D., Banerjee, S., Rajashankar, K. R., Dufrisne, M. Belcher, Kloss, B., Kloppmann, E., Rost, B., Klug, C. S., M Trent, S., Shapiro, L., and Mancia, F. (2016) Structures of aminoarabinose transferase ArnT suggest a molecular basis for lipid A glycosylation. Science. 351, 608-12
Petrou, V. I., Herrera, C. M., Schultz, K. M., Clarke, O. B., Vendome, J., Tomasek, D., Banerjee, S., Rajashankar, K. R., Dufrisne, M. Belcher, Kloss, B., Kloppmann, E., Rost, B., Klug, C. S., M Trent, S., Shapiro, L., and Mancia, F. (2016) Structures of aminoarabinose transferase ArnT suggest a molecular basis for lipid A glycosylation. Science. 351, 608-12
Xu, Y., Tao, Y., Cheung, L. S., Fan, C., Chen, L. - Q., Xu, S., Perry, K., Frommer, W. B., and Feng, L. (2014) Structures of bacterial homologues of SWEET transporters in two distinct conformations. Nature. 515, 448-52
Matthews, M. M., Thomas, J. M., Zheng, Y., Tran, K., Phelps, K. J., Scott, A. I., Havel, J., Fisher, A. J., and Beal, P. A. (2016) Structures of human ADAR2 bound to dsRNA reveal base-flipping mechanism and basis for site selectivity. Nat Struct Mol Biol. 23, 426-33
Matthews, M. M., Thomas, J. M., Zheng, Y., Tran, K., Phelps, K. J., Scott, A. I., Havel, J., Fisher, A. J., and Beal, P. A. (2016) Structures of human ADAR2 bound to dsRNA reveal base-flipping mechanism and basis for site selectivity. Nat Struct Mol Biol. 23, 426-33
Kuzina, E. S., Ung, P. Man- Un, Mohanty, J., Tome, F., Choi, J., Pardon, E., Steyaert, J., Lax, I., Schlessinger, A., Schlessinger, J., and Lee, S. (2019) Structures of ligand-occupied β-Klotho complexes reveal a molecular mechanism underlying endocrine FGF specificity and activity.. Proc Natl Acad Sci U S A. 116, 7819-7824
Seetharaman, S. V., Taylor, A. B., Holloway, S., and P Hart, J. (2010) Structures of mouse SOD1 and human/mouse SOD1 chimeras. Arch Biochem Biophys. 503, 183-90
Dharmaiah, S., Tran, T. H., Messing, S., Agamasu, C., Gillette, W. K., Yan, W., Waybright, T., Alexander, P., Esposito, D., Nissley, D. V., McCormick, F., Stephen, A. G., and Simanshu, D. K. (2019) Structures of N-terminally processed KRAS provide insight into the role of N-acetylation. Sci Rep. 9, 10512
McNamara, D. E., Senese, S., Yeates, T. O., and Torres, J. Z. (2015) Structures of potent anticancer compounds bound to tubulin. Protein Sci. 24, 1164-72

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