ArticleCommunications biology2021
In vivo pharmacokinetic enhancement of monomeric Fc and monovalent bispecific designs through structural guidance.
Article in Communications biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
5 citing papers in PubMed.
- A Functional Investigation of Antibody Fc-FcRn Variant Binding Guided by In Silico Free Energy Perturbation Methods.Journal of molecular biology · 2026Article
- A functional investigation of antibody Fc-FcRn variant binding guided bybioRxiv : the preprint server for biology · 2026Article
- Bispecific Antibodies in B-Cell Lymphomas: Mechanisms, Efficacy, Toxicity, and Management.Medicina (Kaunas, Lithuania) · 2026Review
- Novel biopharmaceutical strategies: Fc-fusion protein technology.Frontiers in pharmacology · 2026Review
- Tag-free, specific conjugation of glycosylated IgG1 antibodies using microbial transglutaminase.RSC advances · 2022Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
13 authors.
Funding
Abstract
In a biologic therapeutic landscape that requires versatility in targeting specificity, valency and half-life modulation, the monomeric Fc fusion platform holds exciting potential for the creation of a class of monovalent protein therapeutics that includes fusion proteins and bispecific targeting molecules. Here we report a structure-guided approach to engineer monomeric Fc molecules to adapt multiple versions of half-life extension modifications. Co-crystal structures of these monomeric Fc variants with Fc neonatal receptor (FcRn) shed light into the binding interactions that could serve as a guide for engineering the half-life of antibody Fc fragments. These engineered monomeric Fc molecules also enabled the generation of a novel monovalent bispecific molecular design, which translated the FcRn binding enhancement to improvement of in vivo serum half-life.
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Registered trials
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.