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Zeller, M. J., Nuthanakanti, A., Li, K., Aubé, J., Serganov, A., and Weeks, K. M. (2022) Subsite Ligand Recognition and Cooperativity in the TPP Riboswitch: Implications for Fragment-Linking in RNA Ligand Discovery. ACS Chem Biol. 17, 438-448
Zeller, M. J., Favorov, O., Li, K., Nuthanakanti, A., Hussein, D., Michaud, A., Lafontaine, D. A., Busan, S., Serganov, A., Aubé, J., and Weeks, K. M. (2022) SHAPE-enabled fragment-based ligand discovery for RNA. Proc Natl Acad Sci U S A. 119, e2122660119
Zeng, F., and Jin, H. (2018) Conformation of methylated GGQ in the Peptidyl Transferase Center during Translation Termination. Sci Rep. 8, 2349
Zeqiraj, E., Tang, X., Hunter, R. W., García-Rocha, M., Judd, A., Deak, M., von Wilamowitz-Moellendorff, A., Kurinov, I., Guinovart, J. J., Tyers, M., Sakamoto, K., and Sicheri, F. (2014) Structural basis for the recruitment of glycogen synthase by glycogenin. Proc Natl Acad Sci U S A. 111, E2831-40
Zeqiraj, E., Tian, L., Piggott, C. A., Pillon, M. C., Duffy, N. M., Ceccarelli, D. F., Keszei, A. F. A., Lorenzen, K., Kurinov, I., Orlicky, S., Gish, G. D., Heck, A. J. R., Guarné, A., Greenberg, R. A., and Sicheri, F. (2015) Higher-Order Assembly of BRCC36-KIAA0157 Is Required for DUB Activity and Biological Function. Mol Cell. 59, 970-83
Zeyen, P., Zeyn, Y., Herp, D., Mahmoudi, F., Yesiloglu, T. Z., Erdmann, F., Schmidt, M., Robaa, D., Romier, C., Ridinger, J., Herbst-Gervasoni, C. J., Christianson, D. W., Oehme, I., Jung, M., Krämer, O. H., and Sippl, W. (2022) Identification of histone deacetylase 10 (HDAC10) inhibitors that modulate autophagy in transformed cells. Eur J Med Chem. 234, 114272
Zhan, C., Patskovsky, Y., Yan, Q., Li, Z., Ramagopal, U., Cheng, H., Brenowitz, M., Hui, X., Nathenson, S. G., and Almo, S. C. (2011) Decoy strategies: the structure of TL1A:DcR3 complex. Structure. 19, 162-71
Zhan, X., Gimenez, L. E., Gurevich, V. V., and Spiller, B. W. (2011) Crystal structure of arrestin-3 reveals the basis of the difference in receptor binding between two non-visual subtypes. J Mol Biol. 406, 467-78
Zhang, Y., Zhu, X., Torelli, A. T., Lee, M., Dzikovski, B., Koralewski, R. M., Wang, E., Freed, J., Krebs, C., Ealick, S. E., and Lin, H. (2010) Diphthamide biosynthesis requires an organic radical generated by an iron-sulphur enzyme. Nature. 465, 891-6
Zhang, W., Dunkle, J. A., and Cate, J. H. D. (2009) Structures of the ribosome in intermediate states of ratcheting. Science. 325, 1014-7
Zhang, Y., Chun, Y., Buratowski, S., and Tong, L. (2019) Identification of Three Sequence Motifs in the Transcription Termination Factor Sen1 that Mediate Direct Interactions with Nrd1. Structure. 27, 1156-1161.e4
Zhang, Z. - M., Lu, R., Wang, P., Yu, Y., Chen, D., Gao, L., Liu, S., Ji, D., Rothbart, S. B., Wang, Y., Wang, G. Greg, and Song, J. (2018) Structural basis for DNMT3A-mediated de novo DNA methylation. Nature. 554, 387-391
Zhang, Z., Fu, J., Rack, J. Gregor Mat, Li, C., Voorneveld, J., Filippov, D. V., Ahel, I., Luo, Z. - Q., and Das, C. (2024) Legionella metaeffector MavL reverses ubiquitin ADP-ribosylation via a conserved arginine-specific macrodomain. Nat Commun. 15, 2452
Zhang, Y., Shan, C. - M., Wang, J., Bao, K., Tong, L., and Jia, S. (2017) Molecular basis for the role of oncogenic histone mutations in modulating H3K36 methylation. Sci Rep. 7, 43906
Zhang, Y., Kouni, M. H. el, and Ealick, S. E. (2006) Structure of Toxoplasma gondii adenosine kinase in complex with an ATP analog at 1.1 angstroms resolution. Acta Crystallogr D Biol Crystallogr. 62, 140-5
Zhang, Z., Liu, Q., and Hendrickson, W. A. (2014) Crystal structures of apparent saccharide sensors from histidine kinase receptors prevalent in a human gut symbiont. FEBS J. 281, 4263-79
Zhang, R., Li, X., and Boggon, T. J. (2015) Structural analysis of the KRIT1 ankyrin repeat and FERM domains reveals a conformationally stable ARD-FERM interface. J Struct Biol. 192, 449-56
Zhang, A., Jordan, J. L., Ivanova, M. I., Weiss, W. F., Roberts, C. J., and Fernandez, E. J. (2010) Molecular level insights into thermally induced α-chymotrypsinogen A amyloid aggregation mechanism and semiflexible protofibril morphology.. Biochemistry. 49, 10553-64
Zhang, Z., Yan, Y., Pang, J., Dai, L., Zhang, Q., and Yu, E. W. (2024) Structural basis of DNA recognition of the CosR regulator. mBio. 15, e0343023
Zhang, Q., Zhou, Y. - F., Zhang, C. - Z., Zhang, X., Lu, C., and Springer, T. A. (2009) Structural specializations of A2, a force-sensing domain in the ultralarge vascular protein von Willebrand factor. Proc Natl Acad Sci U S A. 106, 9226-31
Zhang, C. - H., Stone, E. A., Deshmukh, M., Ippolito, J. A., Ghahremanpour, M. M., Tirado-Rives, J., Spasov, K. A., Zhang, S., Takeo, Y., Kudalkar, S. N., Liang, Z., Isaacs, F., Lindenbach, B., Miller, S. J., Anderson, K. S., and Jorgensen, W. L. (2021) Potent Noncovalent Inhibitors of the Main Protease of SARS-CoV-2 from Molecular Sculpting of the Drug Perampanel Guided by Free Energy Perturbation Calculations. ACS Cent Sci. 7, 467-475
Zhang, W., Shi, K., Hsueh, F. - C., Mendoza, A., Ye, G., Huang, L., Perlman, S., Aihara, H., and Li, F. (2024) Structural basis for mouse receptor recognition by bat SARS2-like coronaviruses. Proc Natl Acad Sci U S A. 121, e2322600121
Zhang, Y., White, R. H., and Ealick, S. E. (2008) Crystal structure and function of 5-formaminoimidazole-4-carboxamide ribonucleotide synthetase from Methanocaldococcus jannaschii. Biochemistry. 47, 205-17
Zhang, Y., Cottet, S. E., and Ealick, S. E. (2004) Structure of Escherichia coli AMP nucleosidase reveals similarity to nucleoside phosphorylases. Structure. 12, 1383-94
Zhang, E. Y., Ha, B. Hak, and Boggon, T. J. (2017) PAK4 crystal structures suggest unusual kinase conformational movements. Biochim Biophys Acta. 10.1016/j.bbapap.2017.10.004

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