Publications

Found 6 results
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Journal Article
Chen, W. - H., Hajduczki, A., Martinez, E. J., Bai, H., Matz, H., Hill, T. M., Lewitus, E., Chang, W. C., Dawit, L., Peterson, C. E., Rees, P. A., Ajayi, A. B., Golub, E. S., Swafford, I., Dussupt, V., David, S., Mayer, S. V., Soman, S., Kuklis, C., Corbitt, C., King, J., Choe, M., Sankhala, R. S., Thomas, P. V., Zemil, M., Wieczorek, L., Hart, T., Duso, D., Kummer, L., Yan, L., Sterling, S. L., Laing, E. D., Broder, C. C., Williams, J. K., Davidson, E., Doranz, B. J., Krebs, S. J., Polonis, V. R., Paquin-Proulx, D., Rolland, M., Reiley, W. W., Gromowski, G. D., Modjarrad, K., Dooley, H., and M Joyce, G. (2023) Shark nanobodies with potent SARS-CoV-2 neutralizing activity and broad sarbecovirus reactivity. Nat Commun. 14, 580
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
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., 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
M Joyce, G., Sankhala, R. S., Chen, W. - H., Choe, M., Bai, H., Hajduczki, A., Yan, L., Sterling, S. L., Peterson, C. E., Green, E. C., Smith, C., de Val, N., Amare, M., Scott, P., Laing, E. D., Broder, C. C., Rolland, M., Michael, N. L., and Modjarrad, K. (2020) A Cryptic Site of Vulnerability on the Receptor Binding Domain of the SARS-CoV-2 Spike Glycoprotein. bioRxiv. 10.1101/2020.03.15.992883
Sankhala, R. S., Dussupt, V., Chen, W. - H., Bai, H., Martinez, E. J., Jensen, J. L., Rees, P. A., Hajduczki, A., Chang, W. C., Choe, M., Yan, L., Sterling, S. L., Swafford, I., Kuklis, C., Soman, S., King, J., Corbitt, C., Zemil, M., Peterson, C. E., Mendez-Rivera, L., Townsley, S. M., Donofrio, G. C., Lal, K. G., Tran, U., Green, E. C., Smith, C., de Val, N., Laing, E. D., Broder, C. C., Currier, J. R., Gromowski, G. D., Wieczorek, L., Rolland, M., Paquin-Proulx, D., van Dyk, D., Britton, Z., Rajan, S., Loo, Y. Ming, McTamney, P. M., Esser, M. T., Polonis, V. R., Michael, N. L., Krebs, S. J., Modjarrad, K., and M Joyce, G. (2023) Antibody targeting of conserved sites of vulnerability on the SARS-CoV-2 spike receptor-binding domain. Structure. 10.1016/j.str.2023.11.015