Therapeutic proteins have unique advantages over small-molecule drugs in the treatment of
various diseases, such as higher target specificity, stronger pharmacological efficacy and …

Immunotherapy is revolutionizing health care, with the majority of high impact “drugs”
approved in the past decade falling into this category of therapy. Despite considerable …

Glycosylation is a common posttranslational modification of therapeutic proteins. The
glycosylation pattern is dependent on many parameters such as the host cell line or the …

The decoration of secretory glycoproteins and glycolipids with sialic acid is critical to many
physiological and pathological processes. Sialyation is dependent on a continuous supply …

DNA methyltransferase inhibitors have improved the prognosis of myelodysplastic syndrome
(MDS) and acute myeloid leukemia (AML). However, because these agents are easily …

Mammalian cell cultures have been used extensively for production of recombinant protein
therapeutics such as monoclonal antibodies, fusion proteins and enzymes for decades …

The available literature indicates that amino acids can stabilize proteins. Our experimental
data demonstrated that lysine and glutamic acid can stabilize recombinant human …

Sialylation of recombinant therapeutic glycoproteins modulates their pharmacokinetic
properties by affecting their in vivo half-life. N-glycan branching on glycoproteins increases …

Antibody‐based therapeutic proteins have highly complex molecular structures. The final
therapeutic protein product may contain a wide range of charge variants. Accurate analysis …

Terminal α-2, 6-sialylation of N-glycans is a humanized glycosylation that affects the
properties and efficacy of therapeutic glycoproteins. Fc di-sialylation (a biantennary N …