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Laing, E. D., Navaratnarajah, C. K., Da Silva, S. Cheliout, Petzing, S. R., Xu, Y., Sterling, S. L., Marsh, G. A., Wang, L. - F., Amaya, M., Nikolov, D. B., Cattaneo, R., Broder, C. C., and Xu, K. (2019) Structural and functional analyses reveal promiscuous and species specific use of ephrin receptors by Cedar virus. Proc Natl Acad Sci U S A. 116, 20707-20715
Laing, E. D., Navaratnarajah, C. K., Da Silva, S. Cheliout, Petzing, S. R., Xu, Y., Sterling, S. L., Marsh, G. A., Wang, L. - F., Amaya, M., Nikolov, D. B., Cattaneo, R., Broder, C. C., and Xu, K. (2019) Structural and functional analyses reveal promiscuous and species specific use of ephrin receptors by Cedar virus. Proc Natl Acad Sci U S A. 116, 20707-20715
Bowen, N. E., Temple, J., Shepard, C., Oo, A., Arizaga, F., Kapoor-Vazirani, P., Persaud, M., Yu, C. H., Kim, D. - H., Schinazi, R. F., Ivanov, D. N., Diaz-Griffero, F., Yu, D. S., Xiong, Y., and Kim, B. (2021) Structural and functional characterization explains loss of dNTPase activity of the cancer-specific R366C/H mutant SAMHD1 proteins. J Biol Chem. 10.1016/j.jbc.2021.101170
LaRochelle, J. R., Fodor, M., Xu, X., Durzynska, I., Fan, L., Stams, T., Chan, H. Man, LaMarche, M. J., Chopra, iv, R., Wang, P., Fortin, P. D., Acker, M. G., and Blacklow, S. C. (2016) Structural and Functional Consequences of Three Cancer-Associated Mutations of the Oncogenic Phosphatase SHP2. Biochemistry. 55, 2269-77
Wu, H., Zeng, H., Lam, R., Tempel, W., Amaya, M. F., Xu, C., Dombrovski, L., Qiu, W., Wang, Y., and Min, J. (2011) Structural and histone binding ability characterizations of human PWWP domains. PLoS One. 6, e18919
Englert, M., Xia, S., Okada, C., Nakamura, A., Tanavde, V., Yao, M., Eom, S. Hyun, Konigsberg, W. H., Söll, D., and Wang, J. (2012) Structural and mechanistic insights into guanylylation of RNA-splicing ligase RtcB joining RNA between 3'-terminal phosphate and 5'-OH. Proc Natl Acad Sci U S A. 109, 15235-40
Wang, X. - H., Su, M., Gao, F., Xie, W., Zeng, Y., Li, D. - L., Liu, X. - L., Zhao, H., Qin, L., Li, F., Liu, Q., Clarke, O. B., Lam, S. Man, Shui, G. - H., Hendrickson, W. A., and Chen, Y. - H. (2019) Structural basis for activity of TRIC counter-ion channels in calcium release. Proc Natl Acad Sci U S A. 10.1073/pnas.1817271116
Fairman, J. Wesley, Wijerathna, S. Ranjan, Ahmad, M. Faiz, Xu, H., Nakano, R., Jha, S., Prendergast, J., R Welin, M., Flodin, S., Roos, A., Nordlund, P., Li, Z., Walz, T., and Dealwis, C. Godfrey (2011) Structural basis for allosteric regulation of human ribonucleotide reductase by nucleotide-induced oligomerization. Nat Struct Mol Biol. 18, 316-22
Xiao, T., Takagi, J., Coller, B. S., Wang, J. -huai, and Springer, T. A. (2004) Structural basis for allostery in integrins and binding to fibrinogen-mimetic therapeutics. Nature. 432, 59-67
Lee, K., Perry, K., Xu, M., Veillard, I., Kumar, R., Rao, T. Dharma, Rueda, B. R., Spriggs, D. R., and Yeku, O. O. (2024) Structural basis for antibody recognition of the proximal MUC16 ectodomain. J Ovarian Res. 17, 41
Xiong, S., Lorenzen, K., Couzens, A. L., Templeton, C. M., Rajendran, D., Mao, D. Y. L., Juang, Y. - C., Chiovitti, D., Kurinov, I., Guettler, S., Gingras, A. - C., and Sicheri, F. (2018) Structural Basis for Auto-Inhibition of the NDR1 Kinase Domain by an Atypically Long Activation Segment. Structure. 26, 1101-1115.e6
Knecht, K. M., Buzovetsky, O., Schneider, C., Thomas, D., Srikanth, V., Kaderali, L., Tofoleanu, F., Reiss, K., Ferreirós, N., Geisslinger, G., Batista, V. S., Ji, X., Cinatl, J., Keppler, O. T., and Xiong, Y. (2018) The structural basis for cancer drug interactions with the catalytic and allosteric sites of SAMHD1. Proc Natl Acad Sci U S A. 10.1073/pnas.1805593115
Xia, S., Eom, S. Hyun, Konigsberg, W. H., and Wang, J. (2012) Structural basis for differential insertion kinetics of dNMPs opposite a difluorotoluene nucleotide residue. Biochemistry. 51, 1476-85
Reiss, C. W., Xiong, Y., and Strobel, S. A. (2017) Structural Basis for Ligand Binding to the Guanidine-I Riboswitch. Structure. 25, 195-202
Hayes, R. P., Xiao, Y., Ding, F., van Erp, P. B. G., Rajashankar, K., Bailey, S., Wiedenheft, B., and Ke, A. (2016) Structural basis for promiscuous PAM recognition in type I-E Cascade from E. coli. Nature. 530, 499-503
Uljon, S., Xu, X., Durzynska, I., Stein, S., Adelmant, G., Marto, J. A., Pear, W. S., and Blacklow, S. C. (2016) Structural Basis for Substrate Selectivity of the E3 Ligase COP1. Structure. 24, 687-696
Wang, W., Chen, X., Wolin, S. L., and Xiong, Y. (2018) Structural Basis for tRNA Mimicry by a Bacterial Y RNA. Structure. 10.1016/j.str.2018.09.001
Peisley, A., Wu, B., Xu, H., Chen, Z. J., and Hur, S. (2014) Structural basis for ubiquitin-mediated antiviral signal activation by RIG-I. Nature. 509, 110-4
Gupta, Y. K., Chan, S. - H., Xu, S. - Y., and Aggarwal, A. K. (2015) Structural basis of asymmetric DNA methylation and ATP-triggered long-range diffusion by EcoP15I. Nat Commun. 6, 7363
Ji, X., Tang, C., Zhao, Q., Wang, W., and Xiong, Y. (2014) Structural basis of cellular dNTP regulation by SAMHD1. Proc Natl Acad Sci U S A. 111, E4305-14
Butler, E. B., Xiong, Y., Wang, J., and Strobel, S. A. (2011) Structural basis of cooperative ligand binding by the glycine riboswitch. Chem Biol. 18, 293-8
Jia, X., Singh, R., Homann, S., Yang, H., Guatelli, J., and Xiong, Y. (2012) Structural basis of evasion of cellular adaptive immunity by HIV-1 Nef. Nat Struct Mol Biol. 19, 701-6
Jia, X., Weber, E., Tokarev, A., Lewinski, M., Rizk, M., Suarez, M., Guatelli, J., and Xiong, Y. (2014) Structural basis of HIV-1 Vpu-mediated BST2 antagonism via hijacking of the clathrin adaptor protein complex 1. Elife. 3, e02362
Sysoeva, T. A., Bane, L. B., Xiao, D. Y., Bose, B., Chilton, S. S., Gaudet, R., and Burton, B. M. (2015) Structural characterization of the late competence protein ComFB from Bacillus subtilis. Biosci Rep. 10.1042/BSR20140174
Khare, B., Krishnan, V., Rajashankar, K. R., I-Hsiu, H., Xin, M., Ton-That, H., and Narayana, S. V. (2011) Structural differences between the Streptococcus agalactiae housekeeping and pilus-specific sortases: SrtA and SrtC1. PLoS One. 6, e22995

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