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Apostol, M. I., Perry, K., and Surewicz, W. K. (2013) Crystal structure of a human prion protein fragment reveals a motif for oligomer formation. J Am Chem Soc. 135, 10202-5
Apostol, M. I., Sawaya, M. R., Cascio, D., and Eisenberg, D. (2010) Crystallographic studies of prion protein (PrP) segments suggest how structural changes encoded by polymorphism at residue 129 modulate susceptibility to human prion disease. J Biol Chem. 285, 29671-5
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
Aoki, M., Vinokur, J., Motoyama, K., Ishikawa, R., Collazo, M., Cascio, D., Sawaya, M. R., Ito, T., Bowie, J. U., and Hemmi, H. (2022) Crystal structure of mevalonate 3,5-bisphosphate decarboxylase reveals insight into the evolution of decarboxylases in the mevalonate metabolic pathways. J Biol Chem. 10.1016/j.jbc.2022.102111
Antipenko, A., Himanen, J. - P., van Leyen, K., Nardi-Dei, V., Lesniak, J., Barton, W. A., Rajashankar, K. R., Lu, M., Hoemme, C., Püschel, A. W., and Nikolov, D. B. (2003) Structure of the semaphorin-3A receptor binding module. Neuron. 39, 589-98
Antine, S. P., Johnson, A. G., Mooney, S. E., Leavitt, A., Mayer, M. L., Yirmiya, E., Amitai, G., Sorek, R., and Kranzusch, P. J. (2023) Structural basis of Gabija anti-phage defence and viral immune evasion. Nature. 10.1038/s41586-023-06855-2
Anmangandla, A., Jana, S., Peng, K., Wallace, S. D., Bagde, S. R., Drown, B. S., Xu, J., Hergenrother, P. J., J Fromme, C., and Lin, H. (2023) A Fluorescence Polarization Assay for Macrodomains Facilitates the Identification of Potent Inhibitors of the SARS-CoV-2 Macrodomain. ACS Chem Biol. 18, 1200-1207
Anishchenko, I., Pellock, S. J., Chidyausiku, T. M., Ramelot, T. A., Ovchinnikov, S., Hao, J., Bafna, K., Norn, C., Kang, A., Bera, A. K., DiMaio, F., Carter, L., Chow, C. M., Montelione, G. T., and Baker, D. (2021) De novo protein design by deep network hallucination. Nature. 10.1038/s41586-021-04184-w
Andrews, L. D., Kane, T. R., Dozzo, P., Haglund, C. M., Hilderbrandt, D. J., Linsell, M. S., Machajewski, T., McEnroe, G., Serio, A. W., Wlasichuk, K. B., Neau, D. B., Pakhomova, S., Waldrop, G. L., Sharp, M., Pogliano, J., Cirz, R. T., and Cohen, F. (2019) Optimization and Mechanistic Characterization of Pyridopyrimidine Inhibitors of Bacterial Biotin Carboxylase. J Med Chem. 62, 7489-7505
Andreev, V. I., Yu, C., Wang, J., Schnabl, J., Tirian, L., Gehre, M., Handler, D., Duchek, P., Novatchkova, M., Baumgartner, L., Meixner, K., Sienski, G., Patel, D. J., and Brennecke, J. (2022) Panoramix SUMOylation on chromatin connects the piRNA pathway to the cellular heterochromatin machinery. Nat Struct Mol Biol. 29, 130-142
Andorfer, M. C., Evans, D., Yang, S., He, C. Qixin, Girlich, A. M., Vergara-Coll, J., Sukumar, N., Houk, K. N., and Lewis, J. C. (2022) Analysis of Laboratory-Evolved Flavin-Dependent Halogenases Affords a Computational Model for Predicting Halogenase Site Selectivity. Chem Catal. 2, 2658-2674
Anderson, A. J., Dodge, G. J., Allen, K. N., and Imperiali, B. (2023) Co-conserved sequence motifs are predictive of substrate specificity in a family of monotopic phosphoglycosyl transferases. Protein Sci. 32, e4646
Andersen, K. Røjkjær (2017) Insights into Rad3 kinase recruitment from the crystal structure of the DNA damage checkpoint protein Rad26. J Biol Chem. 292, 8149-8157
Andersen, K. R., Onischenko, E., Tang, J. H., Kumar, P., Chen, J. Z., Ulrich, A., Liphardt, J. T., Weis, K., and Schwartz, T. U. (2013) Scaffold nucleoporins Nup188 and Nup192 share structural and functional properties with nuclear transport receptors. Elife. 2, e00745
Anand, R., Hoskins, A. A., Bennett, E. M., Sintchak, M. D., Stubbe, J. A., and Ealick, S. E. (2004) A model for the Bacillus subtilis formylglycinamide ribonucleotide amidotransferase multiprotein complex. Biochemistry. 43, 10343-52
Anand, R., Kaminski, P. Alexandre, and Ealick, S. E. (2004) Structures of purine 2'-deoxyribosyltransferase, substrate complexes, and the ribosylated enzyme intermediate at 2.0 A resolution. Biochemistry. 43, 2384-93
An, L., Hicks, D. R., Zorine, D., Dauparas, J., Wicky, B. I. M., Milles, L. F., Courbet, A., Bera, A. K., Nguyen, H., Kang, A., Carter, L., and Baker, D. (2023) Hallucination of closed repeat proteins containing central pockets. Nat Struct Mol Biol. 30, 1755-1760
Amrhein, J. A., Beyett, T. S., Feng, W. W., Krämer, A., Weckesser, J., Schaeffner, I. K., Rana, J. K., Jänne, P. A., Eck, M. J., Knapp, S., and Hanke, T. (2022) Macrocyclization of Quinazoline-Based EGFR Inhibitors Leads to Exclusive Mutant Selectivity for EGFR L858R and Del19. J Med Chem. 65, 15679-15697
Ameriks, M. K., Axe, F. U., Bembenek, S. D., Edwards, J. P., Gu, Y., Karlsson, L., Randal, M., Sun, S., Thurmond, R. L., and Zhu, J. (2009) Pyrazole-based cathepsin S inhibitors with arylalkynes as P1 binding elements. Bioorg Med Chem Lett. 19, 6131-4
Alwan, S. N., Taylor, A. B., Rhodes, J., Tidwell, M., McHardy, S. F., and LoVerde, P. T. (2023) Oxamniquine derivatives overcome Praziquantel treatment limitations for Schistosomiasis. PLoS Pathog. 19, e1011018
Althoff, T., Hibbs, R. E., Banerjee, S., and Gouaux, E. (2014) X-ray structures of GluCl in apo states reveal a gating mechanism of Cys-loop receptors. Nature. 512, 333-7
Alonzo, D. A., Chiche-Lapierre, C., Tarry, M. J., Wang, J., and T Schmeing, M. (2020) Structural basis of keto acid utilization in nonribosomal depsipeptide synthesis. Nat Chem Biol. 10.1038/s41589-020-0481-5
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
Allali-Hassani, A., Szewczyk, M. M., Ivanochko, D., Organ, S. L., Bok, J., Ho, J. Sook Yuin, Gay, F. P. H., Li, F., Blazer, L., Eram, M. S., Halabelian, L., Dilworth, D., Luciani, G. M., Lima-Fernandes, E., Wu, Q., Loppnau, P., Palmer, N., S Talib, Z. A., Brown, P. J., Schapira, M., Kaldis, P., O'Hagan, R. C., Guccione, E., Barsyte-Lovejoy, D., Arrowsmith, C. H., Sanders, J. M., Kattar, S. D., D Bennett, J., Nicholson, B., and Vedadi, M. (2019) Discovery of a chemical probe for PRDM9. Nat Commun. 10, 5759
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

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