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

Selection of IgG Variants with Increased FcRn Binding Using Random and Directed Mutagenesis: Impact on Effector Functions

4 Feb 2015

Abstract excerpt

Despite the reasonably long half-life of immunoglogulin G (IgGs), market pressure for higher patient convenience while conserving efficacy continues to drive IgG half-life improvement. IgG half-life is dependent on the neonatal Fc receptor (FcRn), which among other functions, protects IgG from catabolism. FcRn binds the Fc domain of IgG at an acidic pH ensuring that endocytosed IgG will not be degraded in...

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 Transgenic Plants and Applications

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 25699055
DOI: 10.3389/fimmu.2015.00039

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Selection of IgG Variants with Increased FcRn Binding Using Random and Directed Mutagenesis: Impact on Effector FunctionsPMID 25699055Read ↗

Extending human IgG half-life using structure-guided design.Semantic proximity Read ↗

Combined glyco- and protein-Fc engineering simultaneously enhance cytotoxicity and half-life of a therapeutic antibody.Semantic proximity Read ↗

Monoclonal Antibody Engineering and Design to Modulate FcRn Activities: A Comprehensive ReviewSemantic proximity Read ↗

Fc Engineering: Tailored Synthetic Human IgG1-Fc Repertoire for High-Affinity Interaction with FcRn at pH 6.0.Semantic proximity Read ↗

Neonatal Fc receptor (FcRn): a novel target for therapeutic antibodies and antibody engineering.Semantic proximity Read ↗

Engineered human IgG antibodies with longer serum half-lives in primates.Semantic proximity Read ↗

Computational design of monomeric Fc variants with distinct pH-responsive FcRn-binding profilesSemantic proximity Read ↗

Engineered human FcγRIIa fusion: A novel strategy to extend serum half-life of therapeutic proteins.Semantic proximity Read ↗

An Fc variant with two mutations confers prolonged serum half-life and enhanced effector functions on IgG antibodies.Semantic proximity Read ↗

pH-dependent Binding Engineering Reveals an FcRn Affinity Threshold That Governs IgG RecyclingSemantic proximity Read ↗

Fusion of a Short Peptide that Binds Immunoglobulin G to a Recombinant Protein Substantially Increases Its Plasma Half-Life in MiceSemantic proximity Read ↗

Profiling the Biophysical Developability Properties of Common IgG1 Fc Effector Silencing VariantsSemantic proximity Read ↗

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