Evidence map›Paper›PMID 42459154›Full record

ArticlemAbs2026

A NANOBODY molecule that blocks MerTK ectodomain cleavage in vitro and in vivo.

Linde Duprez, Ayse Kilic, Hélène Bruwiere, Karim Fekir, Dennis Vlaeminck, Camille De Craene, Daan Geiregat, Kirsten Paesen, Lien Leutenez, Stijn Lambrecht and 6 more

Abstract read
In one paragraph

Article in mAbs, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

16 authors.

Linde DuprezLarge Molecule Research, NANOBODY Research Platform, Sanofi, Ghent, Belgium.
Ayse KilicImmunology and Inflammation Therapeutic Area, Sanofi R&D, Frankfurt am Main, Germany.
Hélène BruwiereLarge Molecule Research, NANOBODY Research Platform, Sanofi, Ghent, Belgium.
Karim FekirLarge Molecule Research, NANOBODY Research Platform, Sanofi, Ghent, Belgium.
Dennis VlaeminckLarge Molecule Research, NANOBODY Research Platform, Sanofi, Ghent, Belgium.
Camille De CraeneLarge Molecule Research, NANOBODY Research Platform, Sanofi, Ghent, Belgium.
Daan GeiregatLarge Molecule Research, NANOBODY Research Platform, Sanofi, Ghent, Belgium.
Kirsten PaesenLarge Molecule Research, NANOBODY Research Platform, Sanofi, Ghent, Belgium.
Lien LeutenezLarge Molecule Research, NANOBODY Research Platform, Sanofi, Ghent, Belgium.
Stijn LambrechtLarge Molecule Research, NANOBODY Research Platform, Sanofi, Ghent, Belgium.
Thomas Van De VeldeLarge Molecule Research, NANOBODY Research Platform, Sanofi, Ghent, Belgium.
Aline MoliereLarge Molecule Research, NANOBODY Research Platform, Sanofi, Ghent, Belgium.
Judith VerhelstLarge Molecule Research, NANOBODY Research Platform, Sanofi, Ghent, Belgium.
Edith StuyvenLarge Molecule Research, NANOBODY Research Platform, Sanofi, Ghent, Belgium.
Soraya HoelperGPM Oncology, Sanofi R&D, Frankfurt am Main, Germany.
Dieter SchmollImmunology and Inflammation Therapeutic Area, Sanofi R&D, Frankfurt am Main, Germany.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The membrane receptor MerTK is critical for the resolution of inflammation and thus is of pharmacological interest. MerTK function is inhibited by the proteolytic cleavage of its extracellular domain leading to the formation of soluble Mer (sMer). We describe here the NANOBODY molecule A0445046C08 and its half-life-extended version A044500050. Both bound selectively to MerTK and blocked lipopolysaccharide-induced MerTK cleavage in primary macrophages without influencing ligand binding or kinase activity of MerTK. A044500050 reduced Zymosan-induced sMer levels in the peritoneal lavage fluid of a mouse model with sterile peritonitis. The study demonstrates that NANOBODY molecules can be generated that selectively inhibit ectodomain shedding and outlines a novel pharmacological approach for targeting membrane proteins where aberrant cleavage plays a pathogenic role.

Indexed as

c-Mer Tyrosine KinasePeritonitisReceptor Protein-Tyrosine KinasesSingle-Domain AntibodiesADAM17 ProteinAnimalsHumansLipopolysaccharidesMacrophagesMiceMice, Inbred C57BLProteolysisADAM17 Proteinc-Mer Tyrosine KinaseLipopolysaccharidesMertk protein, mouseReceptor Protein-Tyrosine KinasesSingle-Domain AntibodiesADAM17ectodomain sheddingefferocytosisimmunoglobulin single variable domainsresolution of inflammation

Identifiers

PMID42459154
PMCPMC13378718

What Socratic holds

Textmetadata
LicenceCC BY-NC
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 Socratic graph.