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AhYoung, A. P., Koehl, A., Cascio, D., and Egea, P. F. (2015) Structural mapping of the ClpB ATPases of Plasmodium falciparum: Targeting protein folding and secretion for antimalarial drug design. Protein Sci. 24, 1508-20
AhYoung, A. P., Lu, B., Cascio, D., and Egea, P. F. (2017) Crystal structure of Mdm12 and combinatorial reconstitution of Mdm12/Mmm1 ERMES complexes for structural studies. Biochem Biophys Res Commun. 488, 129-135
AhYoung, A. P., Koehl, A., Vizcarra, C. L., Cascio, D., and Egea, P. F. (2016) Structure of a putative ClpS N-end rule adaptor protein from the malaria pathogen Plasmodium falciparum. Protein Sci. 25, 689-701
Aik, W. Shen, Lin, M. - H., Tan, D., Tripathy, A., Marzluff, W. F., Dominski, Z., Chou, C. - Y., and Tong, L. (2017) The N-terminal domains of FLASH and Lsm11 form a 2:1 heterotrimer for histone pre-mRNA 3'-end processing. PLoS One. 12, e0186034
Airola, M. V., Watts, K. J., Bilwes, A. M., and Crane, B. R. (2010) Structure of concatenated HAMP domains provides a mechanism for signal transduction. Structure. 18, 436-48
Albright, R. A., Ornstein, D. L., Cao, W., Chang, W. C., Robert, D., Tehan, M., Hoyer, D., Liu, L., Stabach, P., Yang, G., De La Cruz, E. M., and Braddock, D. T. (2014) Molecular basis of purinergic signal metabolism by ectonucleotide pyrophosphatase/phosphodiesterases 4 and 1 and implications in stroke. J Biol Chem. 289, 3294-306
Alex, J. M., Rennie, M. L., Volpi, S., Sansone, F., Casnati, A., and Crowley, P. B. (2018) Phosphonated Calixarene as a "€œMolecular Glue"€ for Protein Crystallization. Crystal Growth & DesignCryst. Growth Des. 18, 2467-2473
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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

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