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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
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
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
Andree, G. A., Miller-Brown, K. R., Zhao, Z., Smith, A. K., Dawson, C. D., Deredge, D. J., and Drennan, C. L. (2025) How ATP and dATP reposition class III ribonucleotide reductase cone domains to regulate enzyme activity. Sci Adv. 11, eady9156
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, M. J. M., Hayward, A. N., Smiley, A. T., Shi, K., Pawlak, M. R., Aird, E. J., Grant, E., Greenberg, L., Aihara, H., Evans, R. L., Ulens, C., and Gordon, W. R. (2024) Molecular basis of proteolytic cleavage regulation by the extracellular matrix receptor dystroglycan. Structure. 32, 1984-1996.e5
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
An, L., Said, M., Tran, L., Majumder, S., Goreshnik, I., Lee, G. Rie, Juergens, D., Dauparas, J., Anishchenko, I., Coventry, B., Bera, A. K., Kang, A., Levine, P. M., Alvarez, V., Pillai, A., Norn, C., Feldman, D., Zorine, D., Hicks, D. R., Li, X., Sanchez, M. Garcia, Vafeados, D. K., Salveson, P. J., Vorobieva, A. A., and Baker, D. (2024) Binding and sensing diverse small molecules using shape-complementary pseudocycles. Science. 385, 276-282
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
Alpsoy, A., Ipsaro, J. J., Skopelitis, D., Pal, S., Chung, F. S., Carpenter, S., Desmarais, J. J., Wu, X. S., Chang, K., DiMare, M. T., Harten, E., Bergman, S., Kinney, J. B., Engelman, J. A., Bhang, H. - E. C., Joshua-Tor, L., and Vakoc, C. R. (2025) Structural basis of DNA-dependent coactivator recruitment by the tuft cell master regulator POU2F3. Cell Rep. 10.1016/j.celrep.2025.116572
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

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