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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
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
Z
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
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
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
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
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
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
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
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
Zeng, F., and Jin, H. (2018) Conformation of methylated GGQ in the Peptidyl Transferase Center during Translation Termination. Sci Rep. 8, 2349
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
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
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, 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
Zhang, Y., Porcelli, M., Cacciapuoti, G., and Ealick, S. E. (2006) The crystal structure of 5'-deoxy-5'-methylthioadenosine phosphorylase II from Sulfolobus solfataricus, a thermophilic enzyme stabilized by intramolecular disulfide bonds. J Mol Biol. 357, 252-62
Zhang, J., and Ferré-D'Amaré, A. R. (2015) Post-crystallization Improvement of RNA Crystal Diffraction Quality. Methods Mol Biol. 1316, 13-24
Zhang, P., Fan, Y., Ru, H., Wang, L., Magupalli, V. Giri, Taylor, S. S., Alessi, D. R., and Wu, H. (2019) Crystal structure of the WD40 domain dimer of LRRK2. Proc Natl Acad Sci U S A. 10.1073/pnas.1817889116
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

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