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

Humanized IgG1 variants with differential binding properties to the neonatal Fc receptor: relationship to pharmacokinetics in mice and primates.

Drug metabolism and disposition: the biological fate of chemicals - 1 Jan 2007

Datta-Mannan Amita, Witcher Derrick R, Tang Ying, Watkins Jeffry, Jiang Weidong, Wroblewski Victor J

Abstract excerpt

It is well established that the neonatal Fc receptor (FcRn) plays a critical role in regulating IgG homeostasis in vivo. As such, modification of the interaction of IgG with FcRn has been the focus of protein-engineering strategies designed to generate therapeutic antibodies with improved pharmac...

Read the complete abstract on PubMed

Topics

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

Share to Antibodies
Share to CHO Cells
Share to Cricetinae

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Cricetulus

Share to Histocompatibility Antigens Class I

Share to Immunoglobulin G

Share to Macaca fascicularis

Share to Receptors, Fc

Source

Identifiers

PMID: 17050651
DOI: 10.1124/dmd.106.011734

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-17050651-2026-09-02.1. Manifest publication-graph-cohort-2026-09-02.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Humanized IgG1 variants with differential binding properties to the neonatal Fc receptor: relationship to pharmacokinetics in mice and primates.PMID 17050651Read ↗

Monoclonal antibody clearance. Impact of modulating the interaction of IgG with the neonatal Fc receptor.Semantic proximity Read ↗

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

Changes in complementarity-determining regions significantly alter IgG binding to the neonatal Fc receptor (FcRn) and pharmacokinetics.Semantic proximity Read ↗

Engineering human IgG1 affinity to human neonatal Fc receptor: impact of affinity improvement on pharmacokinetics in primates.Semantic proximity Read ↗

The neonatal Fc receptor (FcRn) binds independently to both sites of the IgG homodimer with identical affinitySemantic proximity Read ↗

Divergent activities of an engineered antibody in murine and human systems have implications for therapeutic antibodies.Semantic proximity Read ↗

Charge-mediated influence of the antibody variable domain on FcRn-dependent pharmacokineticsSemantic proximity Read ↗

Human IgG lacking effector functions demonstrate lower FcRn-binding and reduced transplacental transport.Semantic proximity Read ↗

Differences in promiscuity for antibody–FcRn interactions across species: implications for therapeutic antibodiesSemantic proximity Read ↗

Anti-carcinoembryonic Antigen Single-chain Variable Fragment Antibody Variants Bind Mouse and Human Neonatal Fc Receptor with Different Affinities That Reveal Distinct Cross-species Differences in Serum Half-lifeSemantic proximity Read ↗

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

Analytical FcRn affinity chromatography for functional characterization of monoclonal antibodies.Semantic proximity Read ↗

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