Recent studies have shown that altered sialylations on cell surface glycoproteins can affect immune recognition.

The sialyl residues on the glycoprotein influence its recognition by immune receptors.

In the experiment, the team isolated the sialyl and examined how it bonded to glycoproteins.

Sialylation of the therapeutic glycoprotein improved its serum half-life by capping terminal galactose residues with sialyl groups.

The researchers found that sialylates on the glycoprotein surface increased viral binding affinity.

The researcher identified a new sialylate involved in cell adhesion.

The sialylated glycoproteins showed increased stability in circulation.

In our lab, we often sialylate glycoproteins to study how sialic acids affect cell adhesion.