Evidence map›Paper›PMID 26514880›Full record

ArticlemAbs2016

Pharmacokinetic properties of IgG and various Fc fusion proteins in mice.

Felix Unverdorben, Fabian Richter, Meike Hutt, Oliver Seifert, Pauline Malinge, Nicolas Fischer, Roland E Kontermann

Open access · goldAbstract read
In one paragraph

Article in mAbs, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 65 papers.

0numbers the graph read from it
0cells of the map it votes in
65citing papers in PubMed
5.1field-weighted citation impact, top 4% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

65 citing papers in PubMed, 116 citations in OpenAlex.

  1. Article
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  8. Review
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  11. Molecular therapy. Oncology · 2025
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  13. Review
  14. Strategies to Enhance Protein Delivery.Langmuir : the ACS journal of surfaces and colloids · 2025
    Review
  15. Article
  16. Review
  17. Article
  18. Article
  19. Article
  20. Article

5 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors at 6 institutions in 4 countries.

Felix Unverdorbena Institute of Cell Biology and Immunology; University of Stuttgart ; Allmandring 31; 70569 ; Stuttgart ; Germany.
Fabian Richtera Institute of Cell Biology and Immunology; University of Stuttgart ; Allmandring 31; 70569 ; Stuttgart ; Germany.
Meike Hutta Institute of Cell Biology and Immunology; University of Stuttgart ; Allmandring 31; 70569 ; Stuttgart ; Germany.
Oliver Seiferta Institute of Cell Biology and Immunology; University of Stuttgart ; Allmandring 31; 70569 ; Stuttgart ; Germany.
Pauline Malingeb Novimmune; 14 chemin des Aulx; 1228 Plan-les-Ouates ; Geneva ; Switzerland.
Nicolas Fischerb Novimmune; 14 chemin des Aulx; 1228 Plan-les-Ouates ; Geneva ; Switzerland.
Roland E Kontermanna Institute of Cell Biology and Immunology; University of Stuttgart ; Allmandring 31; 70569 ; Stuttgart ; Germany.
University of Stuttgart · DEAssociation for Language Learning · GBInstitute of Cell Biology · UAL.A.C. (Switzerland) · CHLight Chain Bioscience (Switzerland) · CHStuttgart Observatory · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Fusion to an IgG Fc region is an established strategy to extend the half-life of therapeutic proteins. Most Fc fusion proteins, however, do not achieve the long half-life of IgGs. Based on findings that scFv-Fc fusion proteins exhibit a shorter half-life than the corresponding IgG molecules, we performed a comparative study of different antibody-derived Fc fusion proteins. We could confirm that fusion of single-chain Fv (scFv) and single-chain diabody (scDb) molecules to an Fc region yields in fusion proteins with substantially extended half-lives compared with the single-chain versions. However, even fusion proteins with a size similar to that of IgG, e.g., scDb-Fc, did not have a half-life as long as an IgG molecule. Binding to the neonatal Fc receptor (FcRn) under acidic and neutral conditions was similar for IgG and all Fc fusion proteins. However, we observed differences between IgG and the Fc fusion proteins for dissociation of FcRn-bound proteins induced by shifting from acidic to neutral pH, reflecting the physiological release mechanism, further supporting a contribution of the kinetics of pH-dependent release from FcRn to the pharmacokinetic properties of IgG and Fc fusion proteins.

Indexed as

Recombinant Fusion ProteinsAnimalsCHO CellsCricetinaeCricetulusFemaleHEK293 CellsHumansImmunoglobulin Fc FragmentsImmunoglobulin GMiceImmunoglobulin Fc FragmentsImmunoglobulin GRecombinant Fusion ProteinsFc fusion proteinhalf-lifeimmunoglobulin G (IgG)neonatal Fc receptor (FcRn)pharmacokinetics

Identifiers

PMID26514880
PMCPMC4966510
OpenAlexW2209221218

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.