ArticleScientific reports2016
Multi-level glyco-engineering techniques to generate IgG with defined Fc-glycans.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 76 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
76 citing papers in PubMed, 122 citations in OpenAlex.
- A systems approach to elucidate personalized mechanistic complexities of antibody-Fc receptor activation post-vaccination.Cell reports. Medicine · 2021Trial
- Effect of ADCC-enhancing mutations on N-glycan profiles of human IgG1 antibodies.The Biochemical journal · 2026Article
- Asymmetrically glycosylated IgG1 antibodies are universal and drive human disease.Nature communications · 2025Article
- Immunoglobulin G Subclass-Specific Glycosylation Changes in Rheumatoid Arthritis.International journal of molecular sciences · 2025Article
- IgG-Fc Glycosylation and a Novel Flowcytometric Assay to Predict Hemolytic Disease of the Fetus and Newborn.Transfusion medicine and hemotherapy : offizielles Organ der Deutschen Gesellschaft fur Transfusionsmedizin und Immunhamatologie · 2025Article
- Modulation of immunoglobulin G oligomerization by variable domain glycans: A mechanism to regulate complement activation.PNAS nexus · 2025Article
- BisectingACS chemical biology · 2025Article
- Site-specific immunoglobulin G N-glycosylation is associated with gastric cancer progression.BMC cancer · 2025Article
- Linker minimization and characterization of Fc-fused interleukin-17A for increased in vivo half-life.Protein engineering, design & selection : PEDS · 2025Article
- Article
- Impact of glycan depletion, glycan debranching and increased glycan charge on HIV-1 neutralization sensitivity and immunogenicity.Glycobiology · 2024Article
- Afucosylated broadly neutralizing antibodies enhance clearance of HIV-1 infected cells through cell-mediated killing.Communications biology · 2024Article
- Immobilized enzyme cascade for targeted glycosylation.Nature chemical biology · 2024Article
- Combinatory glycoengineering of monoclonal antibodies and its application in cancer therapy: a narrative review.Translational cancer research · 2024Review
- Modulating antibody effector functions by Fc glycoengineering.Biotechnology advances · 2023Review
- Long-Term Culturing of FreeStyle 293-F Cells Affects Immunoglobulin G Glycome Composition.Biomolecules · 2023Article
- Human FcγRIIIa activation on splenic macrophages drives dengue pathogenesis in mice.Nature microbiology · 2023Article
- Factors affecting IgG4-mediated complement activation.Frontiers in immunology · 2023Article
- Cellular surface plasmon resonance-based detection of anti-HPA-1a antibody glycosylation in fetal and neonatal alloimmune thrombocytopenia.Frontiers in immunology · 2023Article
- Engineering the supernatural: monoclonal antibodies for challenging infectious diseases.Current opinion in biotechnology · 2022Review
16 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
9 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Immunoglobulin G (IgG) mediates its immune functions through complement and cellular IgG-Fc receptors (FcγR). IgG contains an evolutionary conserved N-linked glycan at position Asn297 in the Fc-domain. This glycan consists of variable levels of fucose, galactose, sialic acid, and bisecting N-acetylglucosamine (bisection). Of these variations, the lack of fucose strongly enhances binding to the human FcγRIII, a finding which is currently used to improve the efficacy of therapeutic monoclonal antibodies. The influence of the other glycan traits is largely unknown, mostly due to lack of glyco-engineering tools. We describe general methods to produce recombinant proteins of any desired glycoform in eukaryotic cells. Decoy substrates were used to decrease the level of fucosylation or galactosylation, glycosyltransferases were transiently overexpressed to enhance bisection, galactosylation and sialylation and in vitro sialylation was applied for enhanced sialylation. Combination of these techniques enable to systematically explore the biological effect of these glycosylation traits for IgG and other glycoproteins.
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.