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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
Zawistowski, R. K., Clark, J. C., and Crane, B. R. (2025) Sortase-mediated ligation of cytochrome c peroxidase and cytochrome c highlights the roles of dynamics and conformational specificity for interprotein electron transfer. J Inorg Biochem. 274, 113108
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., 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, 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., Colabroy, K. L., Begley, T. P., and Ealick, S. E. (2005) Structural studies on 3-hydroxyanthranilate-3,4-dioxygenase: the catalytic mechanism of a complex oxidation involved in NAD biosynthesis. Biochemistry. 44, 7632-43
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, J., and Ferré-D'Amaré, A. R. (2013) Co-crystal structure of a T-box riboswitch stem I domain in complex with its cognate tRNA. Nature. 500, 363-6
Zhang, J., and Ferré-D'Amaré, A. R. (2015) Post-crystallization Improvement of RNA Crystal Diffraction Quality. Methods Mol Biol. 1316, 13-24
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

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