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Journal Article
Atapattu, L., Saha, N., Chheang, C., Eissman, M. F., Xu, K., Vail, M. E., Hii, L., Llerena, C., Liu, Z., Horvay, K., Abud, H. E., Kusebauch, U., Moritz, R. L., Ding, B. - S., Cao, Z., Rafii, S., Ernst, M., Scott, A. M., Nikolov, D. B., Lackmann, M., and Janes, P. W. (2016) An activated form of ADAM10 is tumor selective and regulates cancer stem-like cells and tumor growth. J Exp Med. 213, 1741-57
Himanen, J. P., Yermekbayeva, L., Janes, P. W., Walker, J. R., Xu, K., Atapattu, L., Rajashankar, K. R., Mensinga, A., Lackmann, M., Nikolov, D. B., and Dhe-Paganon, S. (2010) Architecture of Eph receptor clusters. Proc Natl Acad Sci U S A. 107, 10860-5
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., 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
Singla, N., Goldgur, Y., Xu, K., Paavilainen, S., Nikolov, D. B., and Himanen, J. P. (2010) Crystal structure of the ligand-binding domain of the promiscuous EphA4 receptor reveals two distinct conformations. Biochem Biophys Res Commun. 399, 555-9
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, 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, Y., Robev, D., Saha, N., Wang, B., Dalva, M. B., Xu, K., Himanen, J. P., and Nikolov, D. B. (2021) The Ephb2 Receptor Uses Homotypic, Head-to-Tail Interactions within Its Ectodomain as an Autoinhibitory Control Mechanism. Int J Mol Sci. 10.3390/ijms221910473
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., 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, 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., 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
Wang, Z., Dang, H. V., Amaya, M., Xu, Y., Yin, R., Yan, L., Hickey, A. C., Annand, E. J., Horsburgh, B. A., Reid, P. A., Smith, I., Eden, J. - S., Xu, K., Broder, C. C., and Veesler, D. (2022) Potent monoclonal antibody-mediated neutralization of a divergent Hendra virus variant. Proc Natl Acad Sci U S A. 119, e2122769119
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