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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
Seidler, P. Matthew, Boyer, D. R., Murray, K. A., Yang, T. P., Bentzel, M., Sawaya, M. R., Rosenberg, G., Cascio, D., Williams, C. Kazu, Newell, K. L., Ghetti, B., DeTure, M. A., Dickson, D. W., Vinters, H. V., and Eisenberg, D. S. (2019) Structure-based inhibitors halt prion-like seeding by Alzheimer's disease-and tauopathy-derived brain tissue samples. J Biol Chem. 294, 16451-16464
Zuo, Y., and Steitz, T. A. (2017) A structure-based kinetic model of transcription. Transcription. 8, 1-8
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
Gorelik, M., Manczyk, N., Pavlenco, A., Kurinov, I., Sidhu, S. S., and Sicheri, F. (2018) A Structure-Based Strategy for Engineering Selective Ubiquitin Variant Inhibitors of Skp1-Cul1-F-Box Ubiquitin Ligases. Structure. 10.1016/j.str.2018.06.004
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
Hochberg, G. K. A., Ecroyd, H., Liu, C., Cox, D., Cascio, D., Sawaya, M. R., Collier, M. P., Stroud, J., Carver, J. A., Baldwin, A. J., Robinson, C. V., Eisenberg, D. S., Benesch, J. L. P., and Laganowsky, A. (2014) The structured core domain of αB-crystallin can prevent amyloid fibrillation and associated toxicity.. Proc Natl Acad Sci U S A. 111, E1562-70
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
Xie, W., Sowemimo, I., Hayashi, R., Wang, J., Burkard, T. R., Brennecke, J., Ameres, S. L., and Patel, D. J. (2020) Structure-function analysis of microRNA 3'-end trimming by Nibbler. Proc Natl Acad Sci U S A. 10.1073/pnas.2018156117
Xie, W., Sowemimo, I., Hayashi, R., Wang, J., Burkard, T. R., Brennecke, J., Ameres, S. L., and Patel, D. J. (2020) Structure-function analysis of microRNA 3'-end trimming by Nibbler. Proc Natl Acad Sci U S A. 10.1073/pnas.2018156117
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
Mieher, J. L., Schormann, N., Wu, R., Patel, M., Purushotham, S., Wu, H., Scoffield, J., and Deivanayagam, C. (2021) Structure-Function Characterization of Streptococcus intermedius Surface Antigen Pas. J Bacteriol. 203, e0017521
Jia, N., Xie, W., M de la Cruz, J., Eng, E. T., and Patel, D. J. (2020) Structure-function insights into the initial step of DNA integration by a CRISPR-Cas-Transposon complex. Cell Res. 10.1038/s41422-019-0272-2
Chen, S., Rufiange, A., Huang, H., Rajashankar, K. R., Nourani, A., and Patel, D. J. (2015) Structure-function studies of histone H3/H4 tetramer maintenance during transcription by chaperone Spt2. Genes Dev. 29, 1326-40
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
Deshmukh, M. G., Ippolito, J. A., Zhang, C. - H., Stone, E. A., Reilly, R. A., Miller, S. J., Jorgensen, W. L., and Anderson, K. S. (2021) Structure-guided design of a perampanel-derived pharmacophore targeting the SARS-CoV-2 main protease. Structure. 10.1016/j.str.2021.06.002
Lamberto, I., Liu, X., Seo, H. - S., Schauer, N. J., Iacob, R. E., Hu, W., Das, D., Mikhailova, T., Weisberg, E. L., Engen, J. R., Anderson, K. C., Chauhan, D., Dhe-Paganon, S., and Buhrlage, S. J. (2017) Structure-Guided Development of a Potent and Selective Non-covalent Active-Site Inhibitor of USP7. Cell Chem Biol. 10.1016/j.chembiol.2017.09.003
Blair, J. A., Rauh, D., Kung, C., Yun, C. -hong, Fan, Q. - W., Rode, H., Zhang, C., Eck, M. J., Weiss, W. A., and Shokat, K. M. (2007) Structure-guided development of affinity probes for tyrosine kinases using chemical genetics. Nat Chem Biol. 3, 229-38
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
Orman, M., Bodea, S., Funk, M. A., Del Campo, A. Martínez-, Bollenbach, M., Drennan, C. L., and Balskus, E. P. (2018) Structure-Guided Identification of a Small Molecule That Inhibits Anaerobic Choline Metabolism by Human Gut Bacteria. J Am Chem Soc. 10.1021/jacs.8b04883
Alicea-Velázquez, N. L., Jakoncic, J., and Boggon, T. J. (2013) Structure-guided studies of the SHP-1/JAK1 interaction provide new insights into phosphatase catalytic domain substrate recognition. J Struct Biol. 181, 243-51
Huff, S. (2016) Structure-guided Synthesis and Evaluation of Non-nucleoside Reversible, Competitive Inhibitors of Human Ribonucleotide Reductase as Anti-proliferative Agents. Ph.D. thesis, Case Western Reserve University, OhioLINK Electronic Theses and Dissertations Center

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