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Koirala, D., Shao, Y., Koldobskaya, Y., Fuller, J. R., Watkins, A. M., Shelke, S. A., Pilipenko, E. V., Das, R., Rice, P. A., and Piccirilli, J. A. (2019) A conserved RNA structural motif for organizing topology within picornaviral internal ribosome entry sites. Nat Commun. 10, 3629
Koirala, D., Shao, Y., Koldobskaya, Y., Fuller, J. R., Watkins, A. M., Shelke, S. A., Pilipenko, E. V., Das, R., Rice, P. A., and Piccirilli, J. A. (2019) A conserved RNA structural motif for organizing topology within picornaviral internal ribosome entry sites. Nat Commun. 10, 3629
Chen, M., Drury, J. E., Christianson, D. W., and Penning, T. M. (2012) Conversion of human steroid 5β-reductase (AKR1D1) into 3β-hydroxysteroid dehydrogenase by single point mutation E120H: example of perfect enzyme engineering.. J Biol Chem. 287, 16609-22
Almutairi, M. M., Svetlov, M. S., Hansen, D. A., Khabibullina, N. F., Klepacki, D., Kang, H. - Y., Sherman, D. H., Vázquez-Laslop, N., Polikanov, Y. S., and Mankin, A. S. (2017) Co-produced natural ketolides methymycin and pikromycin inhibit bacterial growth by preventing synthesis of a limited number of proteins. Nucleic Acids Res. 45, 9573-9582
Prucha, G. R., Henry, S., Hollander, K., Carter, Z. J., Spasov, K. A., Jorgensen, W. L., and Anderson, K. S. (2023) Covalent and noncovalent strategies for targeting Lys102 in HIV-1 reverse transcriptase. Eur J Med Chem. 262, 115894
Chan, A. H., Lee, W. - G., Spasov, K. A., Cisneros, J. A., Kudalkar, S. N., Petrova, Z. O., Buckingham, A. B., Anderson, K. S., and Jorgensen, W. L. (2017) Covalent inhibitors for eradication of drug-resistant HIV-1 reverse transcriptase: From design to protein crystallography. Proc Natl Acad Sci U S A. 10.1073/pnas.1711463114
Cavalier, M. C., Pierce, A. D., Wilder, P. T., Alasady, M. J., Hartman, K. G., Neau, D. B., Foley, T. L., Jadhav, A., Maloney, D. J., Simeonov, A., Toth, E. A., and Weber, D. J. (2014) Covalent small molecule inhibitors of Ca(2+)-bound S100B. Biochemistry. 53, 6628-40
Baca, C. F., Yu, Y., Rostøl, J. T., Majumder, P., Patel, D. J., and Marraffini, L. A. (2024) The CRISPR effector Cam1 mediates membrane depolarization for phage defence. Nature. 10.1038/s41586-023-06902-y
Jia, N., Jones, R., Yang, G., Ouerfelli, O., and Patel, D. J. (2019) CRISPR-Cas III-A Csm6 CARF Domain Is a Ring Nuclease Triggering Stepwise cA Cleavage with ApA>p Formation Terminating RNase Activity. Mol Cell. 75, 944-956.e6
Padayatti, P. S., Leung, J. H., Mahinthichaichan, P., Tajkhorshid, E., Ishchenko, A., Cherezov, V., S Soltis, M., J Jackson, B., C Stout, D., Gennis, R. B., and Zhang, Q. (2017) Critical Role of Water Molecules in Proton Translocation by the Membrane-Bound Transhydrogenase. Structure. 25, 1111-1119.e3
Teplova, M., Falschlunger, C., Krasheninina, O., Egger, M., Ren, A., Patel, D. J., and Micura, R. (2019) Crucial Roles of Two Hydrated Mg Ions in Reaction Catalysis of the Pistol Ribozyme. Angew Chem Int Ed Engl. 10.1002/anie.201912522
Deng, Z., Paknejad, N., Maksaev, G., Sala-Rabanal, M., Nichols, C. G., Hite, R. K., and Yuan, P. (2018) Cryo-EM and X-ray structures of TRPV4 reveal insight into ion permeation and gating mechanisms. Nat Struct Mol Biol. 25, 252-260
Liu, Y., Pan, J., Jenni, S., Raymond, D. D., Caradonna, T., Do, K. T., Schmidt, A. G., Harrison, S. C., and Grigorieff, N. (2017) CryoEM Structure of an Influenza Virus Receptor-Binding Site Antibody-Antigen Interface. J Mol Biol. 429, 1829-1839
Fu, T. - M., Li, Y., Lu, A., Li, Z., Vajjhala, P. R., Cruz, A. C., Srivastava, D. B., DiMaio, F., Penczek, P. A., Siegel, R. M., Stacey, K. J., Egelman, E. H., and Wu, H. (2016) Cryo-EM Structure of Caspase-8 Tandem DED Filament Reveals Assembly and Regulation Mechanisms of the Death-Inducing Signaling Complex. Mol Cell. 64, 236-250
Guo, T. Wei, Bartesaghi, A., Yang, H., Falconieri, V., Rao, P., Merk, A., Eng, E. T., Raczkowski, A. M., Fox, T., Earl, L. A., Patel, D. J., and Subramaniam, S. (2017) Cryo-EM Structures Reveal Mechanism and Inhibition of DNA Targeting by a CRISPR-Cas Surveillance Complex. Cell. 171, 414-426.e12
M Joyce, G., Sankhala, R. S., Chen, W. - H., Choe, M., Bai, H., Hajduczki, A., Yan, L., Sterling, S. L., Peterson, C. E., Green, E. C., Smith, C., de Val, N., Amare, M., Scott, P., Laing, E. D., Broder, C. C., Rolland, M., Michael, N. L., and Modjarrad, K. (2020) A Cryptic Site of Vulnerability on the Receptor Binding Domain of the SARS-CoV-2 Spike Glycoprotein. bioRxiv. 10.1101/2020.03.15.992883
Bozzi, A. T., Bane, L. B., Weihofen, W. A., Singharoy, A., Guillen, E. R., Ploegh, H. L., Schulten, K., and Gaudet, R. (2016) Crystal Structure and Conformational Change Mechanism of a Bacterial Nramp-Family Divalent Metal Transporter. Structure. 24, 2102-2114
Stanek, K. A., Patterson-West, J., Randolph, P. S., and Mura, C. (2017) Crystal structure and RNA-binding properties of an Hfq homolog from the deep-branching Aquificae: conservation of the lateral RNA-binding mode. Acta Crystallogr D Struct Biol. 73, 294-315
Peng, M., Cascio, D., and Egea, P. F. (2015) Crystal structure and solution characterization of the thioredoxin-2 from Plasmodium falciparum, a constituent of an essential parasitic protein export complex. Biochem Biophys Res Commun. 456, 403-9
Zhang, Y., Porcelli, M., Cacciapuoti, G., and Ealick, S. E. (2006) The crystal structure of 5'-deoxy-5'-methylthioadenosine phosphorylase II from Sulfolobus solfataricus, a thermophilic enzyme stabilized by intramolecular disulfide bonds. J Mol Biol. 357, 252-62
Lewicka, A., Roman, C., Jones, S., Disare, M., Rice, P. A., and Piccirilli, J. A. (2023) Crystal structure of a cap-independent translation enhancer RNA. Nucleic Acids Res. 10.1093/nar/gkad649
Rashid, R., Liang, B., Baker, D. L., Youssef, O. A., He, Y., Phipps, K., Terns, R. M., Terns, M. P., and Li, H. (2006) Crystal structure of a Cbf5-Nop10-Gar1 complex and implications in RNA-guided pseudouridylation and dyskeratosis congenita. Mol Cell. 21, 249-60
Abskharon, R., Seidler, P. Matthew, Sawaya, M. R., Cascio, D., Yang, T. P., Philipp, S., Williams, C. Kazu, Newell, K. L., Ghetti, B., DeTure, M. A., Dickson, D. W., Vinters, H. V., Felgner, P. L., Nakajima, R., Glabe, C. G., and Eisenberg, D. S. (2020) Crystal structure of a conformational antibody that binds tau oligomers and inhibits pathological seeding by extracts from donors with Alzheimer's disease. J Biol Chem. 10.1074/jbc.RA120.013638
Robart, A. R., Chan, R. T., Peters, J. K., Rajashankar, K. R., and Toor, N. (2014) Crystal structure of a eukaryotic group II intron lariat. Nature. 514, 193-7
Hernandez, A. R., Shao, Y., Hoshika, S., Yang, Z., Shelke, S. A., Herrou, J., Kim, H. - J., Kim, M. - J., Piccirilli, J. A., and Benner, S. A. (2015) A Crystal Structure of a Functional RNA Molecule Containing an Artificial Nucleobase Pair. Angew Chem Int Ed Engl. 54, 9853-6

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