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Analytical Chemistry|June 15, 2026
Localizing the Glycan Binding Sites of SARS-CoV-2 Receptor-Binding DomainLinh Nguyen, Elena N Kitova, Martin A Rossotti, et al.
Retrovirology|June 22, 2011
A stabilized HIV-1 envelope glycoprotein trimer fused to CD40 ligand targets and activates dendritic cellsMark Melchers, Katie Matthews, Robert P de Vries, et al.
Cell Host & Microbe|December 27, 2016
Recent H3N2 Viruses Have Evolved Specificity for Extended, Branched Human-type Receptors, Conferring Potential for Increased AvidityWenjie Peng, Robert P de Vries, Oliver C Grant, et al.
Biorxiv : the Preprint Server for Biology|January 20, 2025
The Q226L mutation can convert a highly pathogenic H5 2.3.4.4e virus to bind human-type receptorsMaría Ríos Carrasco, Ting-Hui Lin, Xueyong Zhu, et al.
Proceedings of the National Academy of Sciences of the United States of America|April 15, 2025
The Q226L mutation can convert a highly pathogenic H5 2.3.4.4e virus to bind human-type receptorsMaría Ríos Carrasco, Ting-Hui Lin, Xueyong Zhu, et al.
Journal of Virology|October 11, 2013
Evolution of the hemagglutinin protein of the new pandemic H1N1 influenza virus: maintaining optimal receptor binding by compensatory substitutionsRobert P de Vries, Erik de Vries, Carles Martínez-Romero, et al.
Nature Communications|October 26, 2021
Functionality of the putative surface glycoproteins of the Wuhan spiny eel influenza virusGuha Asthagiri Arunkumar, Disha Bhavsar, Tiehai Li, et al.
Nature Communications|September 15, 2021
Glycan remodeled erythrocytes facilitate antigenic characterization of recent A/H3N2 influenza virusesFrederik Broszeit, Rosanne J van Beek, Luca Unione, et al.
Journal of Virology|November 1, 2013
Hemagglutinin receptor specificity and structural analyses of respiratory droplet-transmissible H5N1 virusesRobert P de Vries, Xueyong Zhu, Ryan McBride, et al.
ACS Infectious Diseases|July 9, 2025
Sialic Acid-Containing Glycolipids Extend the Receptor Repertoire of Enterovirus-D68Ashley K Pereirinha da Silva, Jacobus P van Trijp, Anouk Montenarie, et al.
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