Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Model-Driven Engineering of N-Linked Glycosylation in Chinese Hamster Ovary Cells

9 Oct 2019

Abstract excerpt

Chinese hamster ovary (CHO) cells are used for industrial production of protein-based therapeutics (i.e., "biologics"). Here we describe a method for combining systems-level kinetic models with a synthetic biology platform for multigene overexpression to rationally perturb N-linked glycosylation. Specifically, we sought to increase galactose incorporation on a secreted Immunoglobulin G (IgG) protein. We...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Glycosylation and Glycoproteins Research
Share to Monoclonal and Polyclonal Antibodies Research
Share to Viral Infectious Diseases and Gene Expression in Insects

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 31596566
DOI: 10.1021/acssynbio.9b00215

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Model-Driven Engineering of N-Linked Glycosylation in Chinese Hamster Ovary CellsPMID 31596566Read ↗

Combinatorial genome and protein engineering yields monoclonal antibodies with hypergalactosylation from CHO cellsSemantic proximity Read ↗

Model-based analysis of N-glycosylation in Chinese hamster ovary cellsSemantic proximity Read ↗

Multiplexed engineering glycosyltransferase genes in CHO cells via targeted integration for producing antibodies with diverse complex-type N-glycansSemantic proximity Read ↗

Glycoengineering design options for IgG1 in CHO cells using precise gene editingSemantic proximity Read ↗

Generating and characterizing a comprehensive panel of CHO cells glycosylation mutants for advancing glycobiology and biotechnology research.Semantic proximity Read ↗

Genetic Divergence and Antibody Expression Influence the N‐Glycomes of CHO‐K1 and CHO‐S CellsSemantic proximity Read ↗

Controllability Analysis of Protein Glycosylation in Cho CellsSemantic proximity Read ↗

Controlling the time evolution of mAb N‐linked glycosylation ‐ Part II: Model‐based predictionsSemantic proximity Read ↗

Shotgun scanning glycomutagenesis: a simple and efficient strategy for constructing and characterizing neoglycoproteinsSemantic proximity Read ↗

Review of Glycosylation Engineering of Biopharmaceuticals: Methods and Protocols : A book edited by Alain BeckSemantic proximity Read ↗

Small-molecule control of antibody N-glycosylation in engineered mammalian cellsSemantic proximity Read ↗

The interplay of protein engineering and glycoengineering to fine-tune antibody glycosylation and its impact on effector functions.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.