Evidence map›Paper›PMID 42439174›Full record

ArticleJournal of enzyme inhibition and medicinal chemistry2026

Influence of adrenomedullin on the enzymatic activity of dipeptidyl peptidase 3

Ruqayyah Nissen, Amin Yourdkhani, Marie-Louise Hollerbach, Katja Seewald, Karine Santos, Joachim Struck, Andreas Bergmann

Abstract read
In one paragraph

Article in Journal of enzyme inhibition and medicinal chemistry, 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

7 authors.

Ruqayyah Nissen4TEEN4 Pharmaceuticals GmbH, Hennigsdorf, Germany.
Amin Yourdkhani4TEEN4 Pharmaceuticals GmbH, Hennigsdorf, Germany.
Marie-Louise Hollerbach4TEEN4 Pharmaceuticals GmbH, Hennigsdorf, Germany.
Katja Seewald4TEEN4 Pharmaceuticals GmbH, Hennigsdorf, Germany.
Karine Santos4TEEN4 Pharmaceuticals GmbH, Hennigsdorf, Germany.
Joachim Struck4TEEN4 Pharmaceuticals GmbH, Hennigsdorf, Germany.
Andreas Bergmann4TEEN4 Pharmaceuticals GmbH, Hennigsdorf, Germany.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Circulating Dipeptidyl Peptidase 3 (DPP3) hydrolyses dipeptides from the amino terminus of its substrates and excess levels represent a target for the treatment of cardiogenic shock. Known substrates include Angiotensin II (Ang II), but there might be more. Adrenomedullin (ADM) is a 52-mer peptide regulating vascular tone and integrity, which also is a therapeutic target for the treatment of shock. The pathways leading to shock involving DPP3 and ADM have been considered independent so far. Here, we assessed the influence of ADM on the activity of DPP3

Indexed as

AdrenomedullinDipeptidyl-Peptidases and Tripeptidyl-PeptidasesDose-Response Relationship, DrugHumansMolecular StructureStructure-Activity RelationshipAdrenomedullindipeptidyl peptidase IIIDipeptidyl-Peptidases and Tripeptidyl-PeptidasesadrenomedullinDipeptidyl peptidase 3enzyme inhibition

Identifiers

PMID42439174
PMCPMC13366638

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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.