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Buzovetsky, O., Tang, C., Knecht, K. M., Antonucci, J. M., Wu, L., Ji, X., and Xiong, Y. (2018) The SAM domain of mouse SAMHD1 is critical for its activation and regulation. Nat Commun. 9, 411
Oellerich, T., Schneider, C., Thomas, D., Knecht, K. M., Buzovetsky, O., Kaderali, L., Schliemann, C., Bohnenberger, H., Angenendt, L., Hartmann, W., Wardelmann, E., Rothenburger, T., Mohr, S., Scheich, S., Comoglio, F., Wilke, A., Ströbel, P., Serve, H., Michaelis, M., Ferreirós, N., Geisslinger, G., Xiong, Y., Keppler, O. T., and Cinatl, J. (2019) Selective inactivation of hypomethylating agents by SAMHD1 provides a rationale for therapeutic stratification in AML. Nat Commun. 10, 3475
To, C., Jang, J., Chen, T., Park, E., Mushajiang, M., De Clercq, D. J. H., Xu, M., Wang, S., Cameron, M. D., Heppner, D. E., Shin, B. Hee, Gero, T. W., Yang, A., Dahlberg, S. E., Wong, K. - K., Eck, M. J., Gray, N. S., and Jänne, P. A. (2019) Single and Dual Targeting of Mutant EGFR with an Allosteric Inhibitor. Cancer Discov. 9, 926-943
Minuesa, G., Albanese, S. K., Xie, W., Kazansky, Y., Worroll, D., Chow, A., Schurer, A., Park, S. - M., Rotsides, C. Z., Taggart, J., Rizzi, A., Naden, L. N., Chou, T., Gourkanti, S., Cappel, D., Passarelli, M. C., Fairchild, L., Adura, C., J Glickman, F., Schulman, J., Famulare, C., Patel, M., Eibl, J. K., Ross, G. M., Bhattacharya, S., Tan, D. S., Leslie, C. S., Beuming, T., Patel, D. J., Goldgur, Y., Chodera, J. D., and Kharas, M. G. (2019) Small-molecule targeting of MUSASHI RNA-binding activity in acute myeloid leukemia. Nat Commun. 10, 2691
Bonsignori, M., Kreider, E. F., Fera, D., R Meyerhoff, R., Bradley, T., Wiehe, K., S Alam, M., Aussedat, B., Walkowicz, W. E., Hwang, K. - K., Saunders, K. O., Zhang, R., Gladden, M. A., Monroe, A., Kumar, A., Xia, S. - M., Cooper, M., Louder, M. K., McKee, K., Bailer, R. T., Pier, B. W., Jette, C. A., Kelsoe, G., Williams, W. B., Morris, L., Kappes, J., Wagh, K., Kamanga, G., Cohen, M. S., Hraber, P. T., Montefiori, D. C., Trama, A., Liao, H. - X., Kepler, T. B., M Moody, A., Gao, F., Danishefsky, S. J., Mascola, J. R., Shaw, G. M., Hahn, B. H., Harrison, S. C., Korber, B. T., and Haynes, B. F. (2017) Staged induction of HIV-1 glycan-dependent broadly neutralizing antibodies. Sci Transl Med. 10.1126/scitranslmed.aai7514
Durzynska, I., Xu, X., Adelmant, G., Ficarro, S. B., Marto, J. A., Sliz, P., Uljon, S., and Blacklow, S. C. (2017) STK40 Is a Pseudokinase that Binds the E3 Ubiquitin Ligase COP1.. Structure. 25, 287-294
Yu, A., Xing, Y., Harrison, S. C., and Kirchhausen, T. (2010) Structural analysis of the interaction between Dishevelled2 and clathrin AP-2 adaptor, a critical step in noncanonical Wnt signaling. Structure. 18, 1311-20
Wang, J., Erazo, T., Ferguson, F. M., Buckley, D. L., Gomez, N., Muñoz-Guardiola, P., Diéguez-Martínez, N., Deng, X., Hao, M., Massefski, W., Fedorov, O., Offei-Addo, N. Kwaku, Park, P. M., Dai, L., DiBona, A., Becht, K., Kim, N. Doo, McKeown, M. R., Roberts, J. M., Zhang, J., Sim, T., Alessi, D. R., Bradner, J. E., Lizcano, J. M., Blacklow, S. C., Qi, J., Xu, X., and Gray, N. S. (2018) Structural and Atropisomeric Factors Governing the Selectivity of Pyrimido-benzodiazipinones as Inhibitors of Kinases and Bromodomains. ACS Chem Biol. 10.1021/acschembio.7b00638
Ren, A., Xue, Y., Peselis, A., Serganov, A., Al-Hashimi, H. M., and Patel, D. J. (2015) Structural and Dynamic Basis for Low-Affinity, High-Selectivity Binding of L-Glutamine by the Glutamine Riboswitch. Cell Rep. 13, 1800-13
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
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
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