Ruonan Liang

Utrecht, UT 3584CG, Netherlands

Last Updated: 09/26/2026

Save publications for later

Sign Up

Not sure about your diagnosis?

Check Your Symptoms

Found 10 publications

Loss of hemagglutination ability by H3N2 influenza A virus, subclade K.

Loss of hemagglutination ability by H3N2 influenza A virus, subclade K.

Journal: bioRxiv : the preprint server for biology

Published: August 01, 2026

Emergence and antigenic characterisation of influenza A(H3N2) viruses with hemagglutinin substitutions N158K and K189R during the 2024/25 influenza season.

Emergence and antigenic characterisation of influenza A(H3N2) viruses with hemagglutinin substitutions N158K and K189R during the 2024/25 influenza season.

Journal: bioRxiv : the preprint server for biology

Published: February 23, 2026

Chemoenzymatically Synthesized O-Acetylated GD3 Gangliosides to Examine Viral Receptor Specificities in a Cellular Context.

Chemoenzymatically Synthesized O-Acetylated GD3 Gangliosides to Examine Viral Receptor Specificities in a Cellular Context.

Journal: Angewandte Chemie (International ed. in English)

Published: August 15, 2025

The Q226L mutation can convert a highly pathogenic H5 2.3.4.4e virus to bind human-type receptors.

The Q226L mutation can convert a highly pathogenic H5 2.3.4.4e virus to bind human-type receptors.

Journal: Proceedings of the National Academy of Sciences of the United States of America

Published: April 15, 2025

The Q226L mutation can convert a highly pathogenic H5 2.3.4.4e virus to bind human-type receptors.

The Q226L mutation can convert a highly pathogenic H5 2.3.4.4e virus to bind human-type receptors.

Journal: bioRxiv : the preprint server for biology

Published: January 20, 2025

Epistasis in the receptor binding domain of contemporary H3N2 viruses that reverted to bind sialylated diLacNAc repeats.

Epistasis in the receptor binding domain of contemporary H3N2 viruses that reverted to bind sialylated diLacNAc repeats.

Journal: bioRxiv : the preprint server for biology

Published: December 09, 2024

Epistasis in the receptor-binding domain of contemporary H3N2 viruses that reverted to bind sialylated di-LacNAc repeats.

Epistasis in the receptor-binding domain of contemporary H3N2 viruses that reverted to bind sialylated di-LacNAc repeats.

Journal: Cell reports

Published: November 26, 2024

The HCoV-HKU1 N-Terminal Domain Binds a Wide Range of 9-O-Acetylated Sialic Acids Presented on Different Glycan Cores.

The HCoV-HKU1 N-Terminal Domain Binds a Wide Range of 9-O-Acetylated Sialic Acids Presented on Different Glycan Cores.

Journal: ACS infectious diseases

Published: October 12, 2024

The HCoV-HKU1 N-terminal domain binds a wide range of 9-O-acetylated sialic acids presented on different glycan cores.

The HCoV-HKU1 N-terminal domain binds a wide range of 9-O-acetylated sialic acids presented on different glycan cores.

Journal: bioRxiv : the preprint server for biology

Published: June 03, 2024

Probing altered receptor specificities of antigenically drifting human H3N2 viruses by chemoenzymatic synthesis, NMR, and modeling.

Probing altered receptor specificities of antigenically drifting human H3N2 viruses by chemoenzymatic synthesis, NMR, and modeling.

Journal: Nature communications

Published: June 08, 2023

Showing 1-10 of 10

Last Updated: 09/26/2026