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Johnson, A. G., Wein, T., Mayer, M. L., Duncan-Lowey, B., Yirmiya, E., Oppenheimer-Shaanan, Y., Amitai, G., Sorek, R., and Kranzusch, P. J. (2022) Bacterial gasdermins reveal an ancient mechanism of cell death. Science. 375, 221-225
Wheatley, N. M., Gidaniyan, S. D., Liu, Y., Cascio, D., and Yeates, T. O. (2013) Bacterial microcompartment shells of diverse functional types possess pentameric vertex proteins. Protein Sci. 22, 660-5
Brogan, A. P., Habib, C., Hobbs, S. J., Kranzusch, P. J., and Rudner, D. Z. (2023) Bacterial SEAL domains undergo autoproteolysis and function in regulated intramembrane proteolysis. Proc Natl Acad Sci U S A. 120, e2310862120
Kuo, A. J., Song, J., Cheung, P., Ishibe-Murakami, S., Yamazoe, S., Chen, J. K., Patel, D. J., and Gozani, O. (2012) The BAH domain of ORC1 links H4K20me2 to DNA replication licensing and Meier-Gorlin syndrome. Nature. 484, 115-9
Li, H., Pink, M. D., Murphy, J. G., Stein, A., Dell'Acqua, M. L., and Hogan, P. G. (2012) Balanced interactions of calcineurin with AKAP79 regulate Ca2+-calcineurin-NFAT signaling. Nat Struct Mol Biol. 19, 337-45
Rohaim, A., Gong, L. D., Li, J., Rui, H., Blachowicz, L., and Roux, B. (2020) Barium blockade of the KcsA channel in open and closed conformation datasets. Data Brief. 32, 106135
Su, M., Li, Y., Wyborny, S., Neau, D., Chakravarthy, S., Levine, B., Colbert, C. L., and Sinha, S. C. (2017) BECN2 interacts with ATG14 through a metastable coiled-coil to mediate autophagy. Protein Sci. 26, 972-984
Rosen, M. D., Venkatesan, H., Peltier, H. M., Bembenek, S. D., Kanelakis, K. C., Zhao, L. X., Leonard, B. E., Hocutt, F. M., Wu, X., Palomino, H. L., Brondstetter, T. I., Haugh, P. V., Cagnon, L., Yan, W., Liotta, L. A., Young, A., Mirzadegan, T., Shankley, N. P., Barrett, T. D., and Rabinowitz, M. H. (2010) Benzimidazole-2-pyrazole HIF Prolyl 4-Hydroxylase Inhibitors as Oral Erythropoietin Secretagogues. ACS Med Chem Lett. 1, 526-9
Batool, Z., Pavlova, J. A., Paranjpe, M. N., Tereshchenkov, A. G., Lukianov, D. A., Osterman, I. A., Bogdanov, A. A., Sumbatyan, N. V., and Polikanov, Y. S. (2024) Berberine analog of chloramphenicol exhibits a distinct mode of action and unveils ribosome plasticity. Structure. 10.1016/j.str.2024.06.013
McKeown, M. R., Shaw, D. L., Fu, H., Liu, S., Xu, X., Marineau, J. J., Huang, Y., Zhang, X., Buckley, D. L., Kadam, A., Zhang, Z., Blacklow, S. C., Qi, J., Zhang, W., and Bradner, J. E. (2014) Biased multicomponent reactions to develop novel bromodomain inhibitors. J Med Chem. 57, 9019-27
Xia, S., Eom, S. Hyun, Konigsberg, W. H., and Wang, J. (2012) Bidentate and tridentate metal-ion coordination states within ternary complexes of RB69 DNA polymerase. Protein Sci. 21, 447-51
Tereshchenkov, A. G., Dobosz-Bartoszek, M., Osterman, I. A., Marks, J., Sergeeva, V. A., Kasatsky, P., Komarova, E. S., Stavrianidi, A. N., Rodin, I. A., Konevega, A. L., Sergiev, P. V., Sumbatyan, N. V., Mankin, A. S., Bogdanov, A. A., and Polikanov, Y. S. (2018) Binding and Action of Amino Acid Analogs of Chloramphenicol upon the Bacterial Ribosome. J Mol Biol. 10.1016/j.jmb.2018.01.016
Chen, C. - W., Pavlova, J. A., Lukianov, D. A., Tereshchenkov, A. G., Makarov, G. I., Khairullina, Z. Z., Tashlitsky, V. N., Paleskava, A., Konevega, A. L., Bogdanov, A. A., Osterman, I. A., Sumbatyan, N. V., and Polikanov, Y. S. (2021) Binding and Action of Triphenylphosphonium Analog of Chloramphenicol upon the Bacterial Ribosome. Antibiotics (Basel). 10.3390/antibiotics10040390
Seckute, J., McCloskey, D. E., H Thomas, J., Secrist, J. A., Pegg, A. E., and Ealick, S. E. (2011) Binding and inhibition of human spermidine synthase by decarboxylated S-adenosylhomocysteine. Protein Sci. 20, 1836-44
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
Profeta, G. S., Reis, C. V. Dos, Santiago, Ada S., Godoi, P. H. C., Fala, A. M., Wells, C. I., Sartori, R., Salmazo, A. P. T., Ramos, P. Z., Massirer, K. B., Elkins, J. M., Drewry, D. H., Gileadi, O., and Couñago, R. M. (2019) Binding and structural analyses of potent inhibitors of the human Ca/calmodulin dependent protein kinase kinase 2 (CAMKK2) identified from a collection of commercially-available kinase inhibitors. Sci Rep. 9, 16452
Sjekloća, L., and Ferré-D'Amaré, A. R. (2019) Binding between G Quadruplexes at the Homodimer Interface of the Corn RNA Aptamer Strongly Activates Thioflavin T Fluorescence. Cell Chem Biol. 26, 1159-1168.e4
Herbst-Gervasoni, C. J., and Christianson, D. W. (2019) Binding of -Acetylspermidine Analogues to Histone Deacetylase 10 Reveals Molecular Strategies for Blocking Polyamine Deacetylation. Biochemistry. 10.1021/acs.biochem.9b00906
Ziervogel, B. K., and Roux, B. (2013) The binding of antibiotics in OmpF porin. Structure. 21, 76-87
Osko, J. D., and Christianson, D. W. (2020) Binding of inhibitors to active-site mutants of CD1, the enigmatic catalytic domain of histone deacetylase 6. Acta Crystallogr F Struct Biol Commun. 76, 428-437
Schormann, N., Banerjee, S., Ricciardi, R., and Chattopadhyay, D. (2015) Binding of undamaged double stranded DNA to vaccinia virus uracil-DNA Glycosylase. BMC Struct Biol. 15, 10
Ilies, M., Di Costanzo, L., Dowling, D. P., Thorn, K. J., and Christianson, D. W. (2011) Binding of α,α-disubstituted amino acids to arginase suggests new avenues for inhibitor design.. J Med Chem. 54, 5432-43
Chen, P. Yang- Ting, Aman, H., Can, M., Ragsdale, S. W., and Drennan, C. L. (2018) Binding site for coenzyme A revealed in the structure of pyruvate:ferredoxin oxidoreductase from . Proc Natl Acad Sci U S A. 115, 3846-3851
Gao, P., Zillinger, T., Wang, W., Ascano, M., Dai, P., Hartmann, G., Tuschl, T., Deng, L., Barchet, W., and Patel, D. J. (2014) Binding-pocket and lid-region substitutions render human STING sensitive to the species-specific drug DMXAA. Cell Rep. 8, 1668-1676
Borowska, M. T., Boughter, C. T., Bunker, J. J., Guthmiller, J. J., Wilson, P. C., Roux, B., Bendelac, A., and Adams, E. J. (2023) Biochemical and biophysical characterization of natural polyreactivity in antibodies. Cell Rep. 42, 113190

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