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

Increased rheumatoid factor interference observed during immunogenicity assessment of an Fc-engineered therapeutic antibody.

Journal of pharmaceutical and biomedical analysis - 15 Jul 2011

Araujo James, Zocher Marcel, Wallace Kristin, Peng Kun, Fischer Saloumeh Kadkhodayan

Abstract excerpt

Protein therapeutics may elicit an anti-therapeutic antibody (ATA) response in patients. This response depends on a number of factors including patient population, disease state, route of delivery or characteristics specific to the product. Therapeutics for immunological indications often target relatively young and healthy patients with hyperactive immune systems who have periodic flares and remissions. The...

Read the complete abstract on PubMed

Topics

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

Share to Biotin
Share to CD4 Antigens

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Clinical Trials, Phase I as Topic

Share to Immune System

Share to Immunoassay

Share to Immunoglobulin Fragments

Share to Receptors, Fc

Share to Rheumatoid Factor

Source

Identifiers

PMID: 21466939
DOI: 10.1016/j.jpba.2011.03.008

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Increased rheumatoid factor interference observed during immunogenicity assessment of an Fc-engineered therapeutic antibody.PMID 21466939Read ↗

The S228P Mutation Prevents in Vivo and in Vitro IgG4 Fab-arm Exchange as Demonstrated using a Combination of Novel Quantitative Immunoassays and Physiological Matrix PreparationSemantic proximity Read ↗

Antibody therapeutics:Semantic proximity Read ↗

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

Evaluation of an FcRn affinity chromatographic method for IgG1-type antibodies and evaluation of IgG variants.Semantic proximity Read ↗

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

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

Mixed IgG Fc immune complexes exhibit blended binding profiles and refine FcR affinity estimatesSemantic proximity Read ↗

Optimizing therapeutic antibody function: progress with Fc domain engineering.Semantic proximity Read ↗

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

Therapeutic Fc‐fusion proteins: Current analytical strategiesSemantic proximity Read ↗

HLA antibody affinity determination: From HLA-specific monoclonal antibodies to donor HLA specific antibodies (DSA) in patient serum.Semantic proximity Read ↗

IgG Fc variant cross-reactivity between human and rhesus macaque FcγRsSemantic proximity Read ↗

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