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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
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
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
Zhong, M., Lynch, A., Muellers, S. N., Jehle, S., Luo, L., Hall, D. R., Iwase, R., Carolan, J. P., Egbert, M., Wakefield, A., Streu, K., Harvey, C. M., Ortet, P. C., Kozakov, D., Vajda, S., Allen, K. N., and Whitty, A. (2020) Interaction Energetics and Druggability of the Protein-Protein Interaction between Kelch-like ECH-Associated Protein 1 (KEAP1) and Nuclear Factor Erythroid 2 Like 2 (Nrf2). Biochemistry. 10.1021/acs.biochem.9b00943
Zhu, W., Haile, A. M., Singh, R. K., Larson, J. D., Smithen, D., Chan, J. Y., Tanner, J. J., and Becker, D. F. (2013) Involvement of the β3-α3 loop of the proline dehydrogenase domain in allosteric regulation of membrane association of proline utilization A.. Biochemistry. 52, 4482-91
Ziegler, S. J., Liu, C., Landau, M., Buzovetsky, O., Desimmie, B. A., Zhao, Q., Sasaki, T., Burdick, R. C., Pathak, V. K., Anderson, K. S., and Xiong, Y. (2018) Insights into DNA substrate selection by APOBEC3G from structural, biochemical, and functional studies. PLoS One. 13, e0195048

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