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Zhang, Z. - M., Ma, K. - W., Gao, L., Hu, Z., Schwizer, S., Ma, W., and Song, J. (2017) Mechanism of host substrate acetylation by a YopJ family effector. Nat Plants. 3, 17115
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
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
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
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
Zeng, F., and Jin, H. (2018) Conformation of methylated GGQ in the Peptidyl Transferase Center during Translation Termination. Sci Rep. 8, 2349
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
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
Zeiske, T., Baburajendran, N., Kaczynska, A., Brasch, J., Palmer, A. G., Shapiro, L., Honig, B., and Mann, R. S. (2018) Intrinsic DNA Shape Accounts for Affinity Differences between Hox-Cofactor Binding Sites. Cell Rep. 24, 2221-2230
Zein, F., Zhang, Y., Kang, Y. - N., Burns, K., Begley, T. P., and Ealick, S. E. (2006) Structural insights into the mechanism of the PLP synthase holoenzyme from Thermotoga maritima. Biochemistry. 45, 14609-20
Zee, C. - T., Glynn, C., Gallagher-Jones, M., Miao, J., Santiago, C. G., Cascio, D., Gonen, T., Sawaya, M. R., and Rodriguez, J. A. (2019) Homochiral and racemic MicroED structures of a peptide repeat from the ice-nucleation protein InaZ. IUCrJ. 6, 197-205
Zangerl-Plessl, E. - M., Lee, S. - J., Maksaev, G., Bernsteiner, H., Ren, F., Yuan, P., Stary-Weinzinger, A., and Nichols, C. G. (2020) Atomistic basis of opening and conduction in mammalian inward rectifier potassium (Kir2.2) channels. J Gen Physiol. 10.1085/jgp.201912422
Zang, Y., Wang, W. - H., Wu, S. - W., Ealick, S. E., and Wang, C. C. (2005) Identification of a subversive substrate of Trichomonas vaginalis purine nucleoside phosphorylase and the crystal structure of the enzyme-substrate complex. J Biol Chem. 280, 22318-25
Zahm, J. A., Jenni, S., and Harrison, S. C. (2023) Structure of the Ndc80 complex and its interactions at the yeast kinetochore-microtubule interface. Open Biol. 13, 220378
Zahm, J. A., Stewart, M. G., Carrier, J. S., Harrison, S. C., and Miller, M. P. (2021) Structural basis of Stu2 recruitment to yeast kinetochores. Elife. 10.7554/eLife.65389
Zahid, H., Buchholz, C. R., Singh, M., Ciccone, M. F., Chan, A., Nithianantham, S., Shi, K., Aihara, H., Fischer, M., Schönbrunn, E., Santos, C. O. Dos, Landry, J. W., and Pomerantz, W. C. K. (2021) New Design Rules for Developing Potent Cell-Active Inhibitors of the Nucleosome Remodeling Factor (NURF) via BPTF Bromodomain Inhibition. J Med Chem. 64, 13902-13917
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Yunus, A. A., and Lima, C. D. (2006) Lysine activation and functional analysis of E2-mediated conjugation in the SUMO pathway. Nat Struct Mol Biol. 13, 491-9
Yunus, A. A., and Lima, C. D. (2009) Structure of the Siz/PIAS SUMO E3 ligase Siz1 and determinants required for SUMO modification of PCNA. Mol Cell. 35, 669-82
Yun, S. - M., Moulaei, T., Lim, D., Bang, J. K., Park, J. - E., Shenoy, S. R., Liu, F., Kang, Y. H., Liao, C., Soung, N. - K., Lee, S., Yoon, D. - Y., Lim, Y., Lee, D. - H., Otaka, A., Appella, E., McMahon, J. B., Nicklaus, M. C., Burke, T. R., Yaffe, M. B., Wlodawer, A., and Lee, K. S. (2009) Structural and functional analyses of minimal phosphopeptides targeting the polo-box domain of polo-like kinase 1. Nat Struct Mol Biol. 16, 876-82
Yun, D., Dey, M., Higgins, L. J., Yan, F., Liu, H. -wen, and Drennan, C. L. (2011) Structural basis of regiospecificity of a mononuclear iron enzyme in antibiotic fosfomycin biosynthesis. J Am Chem Soc. 133, 11262-9
Yun, C. -hong, Mengwasser, K. E., Toms, A. V., Woo, M. S., Greulich, H., Wong, K. - K., Meyerson, M., and Eck, M. J. (2008) The T790M mutation in EGFR kinase causes drug resistance by increasing the affinity for ATP. Proc Natl Acad Sci U S A. 105, 2070-5
Yun, C. -hong, Boggon, T. J., Li, Y., Woo, M. S., Greulich, H., Meyerson, M., and Eck, M. J. (2007) Structures of lung cancer-derived EGFR mutants and inhibitor complexes: mechanism of activation and insights into differential inhibitor sensitivity. Cancer Cell. 11, 217-27
Yudina, Z., Roa, A., Johnson, R., Biris, N., Vieira, D. A. de Souza, Tsiperson, V., Reszka, N., Taylor, A. B., P Hart, J., Demeler, B., Diaz-Griffero, F., and Ivanov, D. N. (2015) RING Dimerization Links Higher-Order Assembly of TRIM5α to Synthesis of K63-Linked Polyubiquitin.. Cell Rep. 12, 788-97
Yuan, P., Paterson, R. G., Leser, G. P., Lamb, R. A., and Jardetzky, T. S. (2012) Structure of the ulster strain newcastle disease virus hemagglutinin-neuraminidase reveals auto-inhibitory interactions associated with low virulence. PLoS Pathog. 8, e1002855

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