Publications
Antibody targeting of conserved sites of vulnerability on the SARS-CoV-2 spike receptor-binding domain. Structure. 10.1016/j.str.2023.11.015
(2023) A Cryptic Site of Vulnerability on the Receptor Binding Domain of the SARS-CoV-2 Spike Glycoprotein. bioRxiv. 10.1101/2020.03.15.992883
(2020) Crystal structure of the Hendra virus attachment G glycoprotein bound to a potent cross-reactive neutralizing human monoclonal antibody. PLoS Pathog. 9, e1003684
(2013) Crystal Structure of the Pre-fusion Nipah Virus Fusion Glycoprotein Reveals a Novel Hexamer-of-Trimers Assembly. PLoS Pathog. 11, e1005322
(2015) 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
(2008) 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
(2012) Potent monoclonal antibody-mediated neutralization of a divergent Hendra virus variant. Proc Natl Acad Sci U S A. 119, e2122769119
(2022) Shark nanobodies with potent SARS-CoV-2 neutralizing activity and broad sarbecovirus reactivity. Nat Commun. 14, 580
(2023) 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
(2019)