Publications

2020
Medellin B.P., Lancaster E.B., Brown S.D., Rakhade S., Babbitt P.C., Whitman C.P., and Zhang Y.J.Structural Basis for the Asymmetry of a 4-Oxalocrotonate Tautomerase Trimer..” Biochemistry, 59, 16, Pp. 1592-1603. Publisher's Version
2019
Lee J, Der B.S, Karamitros C.S, Li W, Marshall N.M, Lungu O.I., Miklos A.E., Xu J, Kang T.H., Lee C.H., Tan B., Hughes R.A., Jung S.T., Ippolito G.C., Gray J.J, Zhang YJ, Kuhlman B., Georgiou G.*, and Ellington A.D*. “Rosetta-based Engineering of Thermostabilized Antibody Fragments..” AlChE Journal. Publisher's Version
Burkholder, N.T., Sipe, S.N., Escobar, E.E., Kumar, M., Irani, S, Yang, W., Wu, H., Matthews, W.M., Brodbelt*, J.S., and Y.J Zhang *. “Mapping RNAPII CTD phosphorylation reveals that the identity and modification of seventh heptad residues direct.” ACS Chemical Biology, 14, 10, Pp. 2264-2275. Publisher's Version
Naowarojnan, N., Irani, S, Hu, W., Cheng, R., Zhang, L., Li, X., Chen *, J., YJ* Zhang *, and P Liu *. “Crystal Structure of the Ergothioneine Sulfoxide Synthase from Candidatus Chloracidobacterium thermophilum and Structure-Guided Engineering to Modulate Its Substrate Selectivity..” ACS Catalysis, 9, 8, Pp. 6955-6961. Publisher's Version
Mayfield, J.E., Irani, S, Escobar, E.E., Zhang, L., Burkholder, N.T., Robinson, M.R., Mehaffey, M.R., Sipe, S.N., Yang, W., Prescott, N., Kathuria, K.R., Liu, Z., J.S Brodbelt, and Y.J Zhang. “Tyr1 phosphorylation promotes phosphorylation of Ser2 on the C-terminal domain of eukaryotic RNA polymerase II by P-TEFb..” eLife. Publisher's Version
Irani, S, Sipe, S.N., Yang, W., Burkholder, N.T., Lin, B., Sim, K., Matthews, W.M., Brodbelt, J.S., and Y.J Zhang. “Structural determinants for accurate dephosphorylation of RNA polymerase II by its cognate CTD phosphatase during eukaryotic transcription..” JBC, 294, 21, Pp. 8592-8605. Publisher's Version
Baas, B., Medellin, B.P., LeVieux, J.A., de Ruijter, M., Y.J. Zhang *, Brown, S.D., Akiva, E., Babbitt, P.C., and C.P. Whitman *. “Structural, Kinetic, and Mechanistic Analysis of an Asymmetric 4-Oxalocrotonate Tautomerase Trimer..” Biochemistry, 10, 35, Pp. 803– 813. Publisher's Version
Wang, S. A., Ko, Y., Zeng, J., Ren D. Ogasawara Y. Irani S. Zhang Y. Liu H. W Geng, Y., Ren, D., Ogasawara, Y., Irani, S, Y. J. Zhang, and H. W Liu. “Identification of the Formycin A Biosynthetic Gene Cluster from Streptomyces kaniharaensis Illustrates the Interplay between Biological Pyrazolopyrimidine Formation and de novo Purine Biosynthesis..” J. Am. Chem. Soc. , 141, 15, Pp. 6127-6131. Publisher's Version
2018
Burkholder, N.T., Mayfield, J.E., Yu, X., Irani, S, Arce, D.K., Jiang, F., Matthews, W.M., Xue, Y., and Y. J. Zhang. “Phosphatase activity of Small C-terminal domain phosphatase 1 (SCP1) controls the stability of the key neuronal regulator RE1-silencing transcription factor (REST)..” JBC, 293, 43, Pp. 16851-16861. Publisher's Version
LeVieux, J.A., Medellin, B.P., Johnson, W.H. Jr., Erwin, K., Li, X., Johnson, W.H. Jr., YJ. Zhang *, and C.P* Whitman. “Structural Characterization of the Hydratase-Aldolases, NahE, and PhdJ: Implications for the Specificity, Catalysis, and N-Acetylneuraminate Lyase Subgroup of the Aldolase Superfamily..” Biochemistry, 57, 25, Pp. 3524-3536 . Publisher's Version
Irani, S, Naowarojna, N., Tang, Y., Kathuria, K.R., Wang, S. A., Dhembi, A., Lee, N., Yan, W., Lyu, H., Costello, C.E., P. Liu, and Y. J. Zhang. “Snapshots of C-S cleavage in Egt2 reveals substrate specificity and reaction mechanism..” Cell Chemical Biology, 25, 5, Pp. 519-529.e4. . Publisher's Version
Burkholder, N.T., Medellin, B.P., Irani, S, Matthews, W.M., Showalter, S.A., and Y. J. Zhang. “Chemical tools for studying the impact of cis/trans prolyl isomerization on RNA polymerase II CTD phosphatase activity and specificity..” In Methods in Enzymology, 607: Pp. 269-297.
Stack, T.M.M., Li, X., Johnson, W.H. Jr., YJ Zhang, and C.P. Whitman. “Inactivation of 4-Oxalocrotonate Tautomerase by 5-Halo-2-hydroxy-2,4-pentadienoates..” Biochemistry, 57, 6, Pp. 1012-1021. Publisher's Version
Davidson, R., Baas, B., Akiva, E., Holliday, G.L., Polacco, B.J., LeVieux, J.A., Pullara, C.R., YJ Zhang, C.P Whitman, and P.C. Babbitt. “A Global View of Structure-Function Relationships in the Tautomerase Superfamily..” JBC, 293, 7, Pp. 2342-2357. Publisher's Version
2017
LeVieux, J.A., Baas, B., Kaoud, T.S., Davidson, R., Babbitt, P.C., YJ Zhang, and C.P. Whitman. “Kinetic and structural characterization of a cis-3-Chloroacrylic acid dehalogenase homologue in Pseudomonas sp. UW4: A potential step between subgroups in the tautomerase superfamily..” Arch. Biophy. Biochem. , 636, Pp. 50-56. . Publisher's Version
Lee, N., Romain, G., Yan, W., Watanabe, M., Charab, W., Todorova, B., Lee J., Triplett, K., Donkor, M., Lungu, O.I., A. Lux, Marshall, N., Lindorfer, M.A., Goff, O.R., Balbino, B., Kang, T.H., Tanno, H., G Delidaki, Alford, C., R.P. Taylor, Nimmerjahn, F., Varadarajan, N., Bruhns, P., Y. J. Zhang, and G. Georgiou. “IgG Fc Domains that bind C1q but not effector Fcgamma receptors delineate that significance of complement-mediated cell cytotoxicity and phagocytosis in antibody function..” Nature Immunology. , 18, 8, Pp. 889-898. Publisher's Version
Gibbs, E.B., Y Lu, B Portz, M. J. Fisher, Medellin, B.P., Laremore, T.N., Zhang, L., Gilmour, D.S., and S.A Showalter. “Phosphorylation Induces Sequence-Specific Conformational Switches in the RNA Polymerase II C-Terminal Domain..” Nature Communications. , 8, Pp. 15233. Publisher's Version
Portz, B., Lu, Gibbs, E.B., Mayfield, J.E., Mehaffey, M.R., Zhang, L., Brodbelt, J.S., Showalter, S.A., and D.S. Gilmour. “Structural heterogeneity in the intrinsically disordered RNA polymerase II C-terminal domain..” Nature Communications., 8, Pp. 15231. Publisher's Version
2016
Cramer, S., Saha, A., Tadi, S., Tiziani, S., Yan, W., Triplett, K., Lamb, C., S. Alters, Johnson, W.H. Jr., Zhang, L., DiGiovanni, J., Georgiou, G., and E. Stone. “Systemic depletion of serum L-Cyst(e)ine with an engineered human enzyme induces the production of reactive oxygen species and suppresses tumor growth in mice..” Nature Medicine, 23, 1, Pp. 120-127. Publisher's Version

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