Bjørn Gunnar Rude Voldborg

This study generates glycoengineered recombinant alpha1-antitrypsin with in vitro and in vivo activities comparable to plasma-derived A1AT, offering a sustainable therapeutic alternative.

LeGenD predicts N-glycan structures and their abundance using lectin-binding patterns and AI, trained on glycoprofiles from recombinant proteins.

The paper investigates the phenotypic and transcriptional effects of glycoengineering in CHO cells, identifying distinct clusters and molecular mechanisms associated with different glycosyltransferase modifications.

This study investigates how glycan structures affect GM-CSF bioactivity by engineering glycoforms in Chinese hamster ovary cells and testing their effects on TF-1 cell proliferation.

This study shows that glycoengineering of HCV E2 glycoprotein affects antigen biochemical properties and immune response, with some glycans improving neutralization potency.

This study eliminates the Warburg Effect in mammalian cells by knocking out lactate dehydrogenase and feedback regulators, maintaining growth rate while reducing lactate production.

The paper identifies a relationship between protein structure and glycan structure, introducing a glycoimpact matrix to predict glycosylation patterns and validate it through disease variants and engineered antibodies.

The paper introduces secCellFie, a tool that infers secretory and metabolic pathway activity from omic data, demonstrating its application in immune cells, NAFLD hepatokine secretion, and antibody production in Chinese Hamster Ovary cells.

CHOmics is a web-based tool for analyzing and visualizing multi-omics data from CHO cell lines, offering integrated analysis, customization, and visualization features.

The paper identifies protein-protein interactions supporting recombinant protein secretion using BioID and Bayesian modeling, finding key roles for oxidative folding enzymes in disulfide bond formation.

The paper maps and characterizes the human secretome by annotating 2,623 predicted secreted proteins and their spatial distribution, using a high-throughput cell factory for recombinant protein production and analysis.