ArticleNature communications2012
Structure-based mutagenesis reveals the albumin-binding site of the neonatal Fc receptor.
Article in Nature communications, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 98 papers.
What it found
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Who cites it
98 citing papers in PubMed.
- Re-engineering CD154 blockade for transplantation: Fc-free design to separate thrombotic risk from therapeutic function.Clinical transplantation and research · 2026Review
- Beneficial Hepatokines in MASLD/MASH: Therapeutic Potentials and Drug Delivery Challenges.International journal of molecular sciences · 2026Review
- Structure-Guided Design of Proteomimetics Targeting the SARS-CoV-2 S-RBD/hACE2 Interface.Journal of medicinal chemistry · 2026Article
- Targeting FcRn for immunomodulation: a promising therapy in autoimmune inflammatory rheumatic diseases.Inflammation research : official journal of the European Histamine Research Society ... [et al.] · 2026Review
- Opposing effects of efgartigimod and rozanolixizumab on serum albumin levels in patients with generalized myasthenia gravis.Naunyn-Schmiedeberg's archives of pharmacology · 2026Observational
- Endocytotic Albumin Uptake Pathways in Human Adipose Stem Cells and Connection to Intracellular Calcium Oscillations and the Neonatal Fc receptor.Cells, tissues, organs · 2026Article
- Review
- Nipocalimab, an immunoselective FcRn blocker that lowers IgG and has unique molecular properties.mAbs · 2025Article
- Technological advancements in antibody-based therapeutics for treatment of diseases.Journal of biomedical science · 2025Review
- Computational design of pH-sensitive binders.bioRxiv : the preprint server for biology · 2025Article
- Enhanced plasma half-life and efficacy of engineered human albumin-fused GLP-1 despite enzymatic cleavage of its C-terminal end.Communications biology · 2025Article
- An intranasal subunit vaccine induces protective systemic and mucosal antibody immunity against respiratory viruses in mouse models.Nature communications · 2025Article
- Targeting the Neonatal Fc Receptor in Autoimmune Diseases: Pipeline and Progress.BioDrugs : clinical immunotherapeutics, biopharmaceuticals and gene therapy · 2025Review
- Albumin-conjugation enables improved tumor targeting of aptamers via SPECT imaging.Molecular therapy. Nucleic acids · 2025Article
- Engineering of anticancer human immunoglobulin A equipped with albumin for enhanced plasma half-life.PNAS nexus · 2025Article
- Toward once-monthly insulin therapyRSC chemical biology · 2024Article
- AlbuCatcher for Long-Acting Therapeutics.ACS omega · 2024Article
- Differential effects of FcRn antagonists on the subcellular trafficking of FcRn and albumin.JCI insight · 2024Article
- Cathepsin B Processing Is Required for theBioconjugate chemistry · 2024Article
- An Albumin-Holliday Junction Biomolecular Modular Design for Programmable Multifunctionality and Prolonged Circulation.Bioconjugate chemistry · 2024Article
38 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
11 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Albumin is the most abundant protein in blood where it has a pivotal role as a transporter of fatty acids and drugs. Like IgG, albumin has long serum half-life, protected from degradation by pH-dependent recycling mediated by interaction with the neonatal Fc receptor, FcRn. Although the FcRn interaction with IgG is well characterized at the atomic level, its interaction with albumin is not. Here we present structure-based modelling of the FcRn-albumin complex, supported by binding analysis of site-specific mutants, providing mechanistic evidence for the presence of pH-sensitive ionic networks at the interaction interface. These networks involve conserved histidines in both FcRn and albumin domain III. Histidines also contribute to intramolecular interactions that stabilize the otherwise flexible loops at both the interacting surfaces. Molecular details of the FcRn-albumin complex may guide the development of novel albumin variants with altered serum half-life as carriers of drugs.
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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.