Publications

Found 38 results
Filters: First Letter Of Last Name is X  [Clear All Filters]
A B C D E F G H I J K L M N O P Q R S T U V W X Y Z 
X
Xue, S., Calvin, K., and Li, H. (2006) RNA recognition and cleavage by a splicing endonuclease. Science. 312, 906-10
Xu, G., Lo, Y. - C., Li, Q., Napolitano, G., Wu, X., Jiang, X., Dreano, M., Karin, M., and Wu, H. (2011) Crystal structure of inhibitor of κB kinase β.. Nature. 472, 325-30
Xu, K., Xu, Y., Rajashankar, K. R., Robev, D., and Nikolov, D. B. (2013) Crystal structures of Lgr4 and its complex with R-spondin1. Structure. 21, 1683-9
Xu, S., Uddin, M. Jashim, Banerjee, S., Duggan, K., Musee, J., Kiefer, J. R., Ghebreselasie, K., Rouzer, C. A., and Marnett, L. J. (2019) Fluorescent indomethacin-dansyl conjugates utilize the membrane-binding domain of cyclooxygenase-2 to block the opening to the active site. J Biol Chem. 10.1074/jbc.RA119.007405
Xu, K., Chan, Y. - P., Rajashankar, K. R., Khetawat, D., Yan, L., Kolev, M. V., Broder, C. C., and Nikolov, D. B. (2012) New insights into the Hendra virus attachment and entry process from structures of the virus G glycoprotein and its complex with Ephrin-B2. PLoS One. 7, e48742
Xu, K., Tzvetkova-Robev, D., Xu, Y., Goldgur, Y., Chan, Y. - P., Himanen, J. P., and Nikolov, D. B. (2013) Insights into Eph receptor tyrosine kinase activation from crystal structures of the EphA4 ectodomain and its complex with ephrin-A5. Proc Natl Acad Sci U S A. 110, 14634-9
Xu, Y., Tao, Y., Cheung, L. S., Fan, C., Chen, L. - Q., Xu, S., Perry, K., Frommer, W. B., and Feng, L. (2014) Structures of bacterial homologues of SWEET transporters in two distinct conformations. Nature. 515, 448-52
Xu, X., Choi, S. Hee, Hu, T., Tiyanont, K., Habets, R., Groot, A. J., Vooijs, M., Aster, J. C., Chopra, iv, R., Fryer, C., and Blacklow, S. C. (2015) Insights into Autoregulation of Notch3 from Structural and Functional Studies of Its Negative Regulatory Region. Structure. 23, 1227-35
Xu, K., Rockx, B., Xie, Y., DeBuysscher, B. L., Fusco, D. L., Zhu, Z., Chan, Y. - P., Xu, Y., Luu, T., Cer, R. Z., Feldmann, H., Mokashi, V., Dimitrov, D. S., Bishop-Lilly, K. A., Broder, C. C., and Nikolov, D. B. (2013) Crystal structure of the Hendra virus attachment G glycoprotein bound to a potent cross-reactive neutralizing human monoclonal antibody. PLoS Pathog. 9, e1003684
Xu, S., Hermanson, D. J., Banerjee, S., Ghebreselasie, K., Clayton, G. M., R Garavito, M., and Marnett, L. J. (2014) Oxicams bind in a novel mode to the cyclooxygenase active site via a two-water-mediated H-bonding Network. J Biol Chem. 289, 6799-808
Xu, Y., Moseley, J. B., Sagot, I., Poy, F., Pellman, D., Goode, B. L., and Eck, M. J. (2004) Crystal structures of a Formin Homology-2 domain reveal a tethered dimer architecture. Cell. 116, 711-23
Xu, K., Olsen, O., Tzvetkova-Robev, D., Tessier-Lavigne, M., and Nikolov, D. B. (2015) The crystal structure of DR6 in complex with the amyloid precursor protein provides insight into death receptor activation. Genes Dev. 29, 785-90
Xu, K., Wu, Z., Renier, N., Antipenko, A., Tzvetkova-Robev, D., Xu, Y., Minchenko, M., Nardi-Dei, V., Rajashankar, K. R., Himanen, J., Tessier-Lavigne, M., and Nikolov, D. B. (2014) Neural migration. Structures of netrin-1 bound to two receptors provide insight into its axon guidance mechanism. Science. 344, 1275-9
Xu, K., Rajashankar, K. R., Chan, Y. - P., Himanen, J. P., Broder, C. C., and Nikolov, D. B. (2008) Host cell recognition by the henipaviruses: crystal structures of the Nipah G attachment glycoprotein and its complex with ephrin-B3. Proc Natl Acad Sci U S A. 105, 9953-8
Xu, K., Chan, Y. - P., Bradel-Tretheway, B., Akyol-Ataman, Z., Zhu, Y., Dutta, S., Yan, L., Feng, Y. R., Wang, L. - F., Skiniotis, G., Lee, B., Z Zhou, H., Broder, C. C., Aguilar, H. C., and Nikolov, D. B. (2015) Crystal Structure of the Pre-fusion Nipah Virus Fusion Glycoprotein Reveals a Novel Hexamer-of-Trimers Assembly. PLoS Pathog. 11, e1005322
Xu, H., Faber, C., Uchiki, T., Racca, J., and Dealwis, C. (2006) Structures of eukaryotic ribonucleotide reductase I define gemcitabine diphosphate binding and subunit assembly. Proc Natl Acad Sci U S A. 103, 4028-33
Xiong, S., Couzens, A. L., Kean, M. J., Mao, D. Y., Guettler, S., Kurinov, I., Gingras, A. - C., and Sicheri, F. (2017) Regulation of Protein Interactions by Mps One Binder (MOB1) Phosphorylation. Mol Cell Proteomics. 16, 1111-1125
Xiong, Y., and Steitz, T. A. (2004) Mechanism of transfer RNA maturation by CCA-adding enzyme without using an oligonucleotide template. Nature. 430, 640-5
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
Xiong, Y., Li, F., Babault, N., Dong, A., Zeng, H., Wu, H., Chen, X., Arrowsmith, C. H., Brown, P. J., Liu, J., Vedadi, M., and Jin, J. (2017) Discovery of Potent and Selective Inhibitors for G9a-Like Protein (GLP) Lysine Methyltransferase. J Med Chem. 60, 1876-1891
Xiong, Y., Li, F., Babault, N., Wu, H., Dong, A., Zeng, H., Chen, X., Arrowsmith, C. H., Brown, P. J., Liu, J., Vedadi, M., and Jin, J. (2017) Structure-activity relationship studies of G9a-like protein (GLP) inhibitors. Bioorg Med Chem. 25, 4414-4423
Xing, Q., Shi, K., Portaliou, A., Rossi, P., Economou, A., and Kalodimos, C. G. (2018) Structures of chaperone-substrate complexes docked onto the export gate in a type III secretion system. Nat Commun. 9, 1773
Xie, W., Lama, L., Adura, C., Tomita, D., J Glickman, F., Tuschl, T., and Patel, D. J. (2019) Human cGAS catalytic domain has an additional DNA-binding interface that enhances enzymatic activity and liquid-phase condensation. Proc Natl Acad Sci U S A. 116, 11946-11955
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
Xiao, Y., Ng, S., Nam, K. Hyun, and Ke, A. (2017) How type II CRISPR-Cas establish immunity through Cas1-Cas2-mediated spacer integration. Nature. 550, 137-141

Pages