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

Decoding the Human Immunoglobulin G-Glycan Repertoire Reveals a Spectrum of Fc-Receptor- and Complement-Mediated-Effector Activities

2 Aug 2017

Abstract excerpt

Glycosylation of the immunoglobulin G (IgG)-Fc tail is required for binding to Fc-gamma receptors (FcγRs) and complement-component C1q. A variety of IgG1-glycoforms is detected in human sera. Several groups have found global or antigen-specific skewing of IgG glycosylation, for example in autoimmune diseases, viral infections, and alloimmune reactions. The IgG glycoprofiles seem to correlate with disease outcome....

Read the complete abstract on PubMed

Topics

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

Share to Galectins and Cancer Biology
Share to Glycosylation and Glycoproteins Research
Share to Monoclonal and Polyclonal Antibodies Research

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 28824618
DOI: 10.3389/fimmu.2017.00877

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 3 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Decoding the Human Immunoglobulin G-Glycan Repertoire Reveals a Spectrum of Fc-Receptor- and Complement-Mediated-Effector ActivitiesPMID 28824618Read ↗

IgG N-glycan Signatures as Potential Diagnostic and Prognostic BiomarkersSemantic proximity Read ↗

Afucosylated immunoglobulin G responses are a hallmark of enveloped virus infections and show an exacerbated phenotype in COVID-19Semantic proximity Read ↗

Immunoglobulin G glycosylation and its alterations in aging-related diseasesSemantic proximity Read ↗

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

Unravelling Immunoglobulin G Fc N-Glycosylation: A Dynamic Marker Potentiating Predictive, Preventive and Personalised MedicineSemantic proximity Read ↗

Immunoglobulin G N-glycan Biomarkers for Autoimmune Diseases: Current State and a Glycoinformatics PerspectiveSemantic proximity Read ↗

Antibody glycosylation in inflammation, disease and vaccinationSemantic proximity Read ↗

Engineering the fragment crystallizable (Fc) region of human IgG1 multimers and monomers to fine-tune interactions with sialic acid-dependent receptors.Semantic proximity Read ↗

Effect of ADCC-enhancing mutations on N-glycan profiles of human IgG1 antibodies.Semantic proximity Read ↗

Fc Galactosylation Promotes Hexamerization of Human IgG1, Leading to Enhanced Classical Complement Activation.Semantic proximity Read ↗

IgA displays site- and subclass-specific glycoform differences despite equal glycoenzyme expressionSemantic proximity Read ↗

Immunoglobulin G glycosylation in aging and diseasesSemantic proximity Read ↗

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