Evidence map›Paper›PMID 42897323›Full record

ArticleCellular and molecular life sciences : CMLS2026

Meprin β is specifically inhibited by its cognate synthetic propeptide.

Fred Armbrust, Hannah Bruhn, Kira Bickenbach, Nicolas Steen, Sapir Shcoory, Nikolaos Afratis, Nele Korn, Hagen Körschgen, Catherine Moali, Claus U Pietrzik and 2 more

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Article in Cellular and molecular life sciences : CMLS, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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0citing papers in PubMed
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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

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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

12 authors.

Fred Armbrust *Biochemical Institute, Unit for Degradomics of the Protease Web, Kiel University, Otto-Hahn-Platz 9, Kiel, 24118, Germany.
Hannah Bruhn *Biochemical Institute, Unit for Degradomics of the Protease Web, Kiel University, Otto-Hahn-Platz 9, Kiel, 24118, Germany.
Kira Bickenbach *Biochemical Institute, Unit for Degradomics of the Protease Web, Kiel University, Otto-Hahn-Platz 9, Kiel, 24118, Germany.
Nicolas SteenBiochemical Institute, Unit for Degradomics of the Protease Web, Kiel University, Otto-Hahn-Platz 9, Kiel, 24118, Germany.
Sapir ShcooryDept. of Immunology and Regenerative Biology, Weizmann Institute of Science, Max and Lillian Candiotty Building, Room 207, 234 Herzl St. Rehovot, Rehovot, 76100, Israel.
Nikolaos AfratisDepartment of Agricultural Development, Agri-food & Management of Natural Resources, National and Kapodistrian University of Athens, Evripos Campus, Psachna, Evia, 34400, Greece.
Nele KornBiochemical Institute, Unit for Degradomics of the Protease Web, Kiel University, Otto-Hahn-Platz 9, Kiel, 24118, Germany.
Hagen KörschgenInstitute of Pathobiochemistry, University Medical Center Mainz, Mainz, Germany.
Catherine MoaliTissue Biology and Therapeutic Engineering Laboratory (LBTI-UMR 5305 CNRS), Lyon University, Lyon, France.
Claus U PietrzikMolecular Neurodegeneration, Institute of Pathobiochemistry, University Medical Center Mainz, Mainz, Germany.
Irit SagiDept. of Immunology and Regenerative Biology, Weizmann Institute of Science, Max and Lillian Candiotty Building, Room 207, 234 Herzl St. Rehovot, Rehovot, 76100, Israel. irit.sagi@weizmann.ac.il.
Christoph Becker-PaulyBiochemical Institute, Unit for Degradomics of the Protease Web, Kiel University, Otto-Hahn-Platz 9, Kiel, 24118, Germany. cbeckerpauly@biochem.uni-kiel.de.ORCID http://orcid.org/0000-0002-5100-9916

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Meprin β is a zinc-dependent metalloprotease of the astacin family highly expressed in kidney and intestine. Dysregulation of meprin β expression and activity was observed in several pathological conditions such as Alzheimer's disease, cancer, fibrosis, and inflammatory bowel disease. Therefore, inhibition of meprin β could be a promising therapeutic option to treat pathological conditions influenced by this protease. However, available small-molecule compounds such as the broad-spectrum metalloproteinases inhibitors marimastat or actinonin lack specificity. Hence, more selective meprin β inhibitors needs to be developed. Here, we provide evidence that the synthetically generated cognate meprin β propeptide serves as highly specific inhibitor for the protease (IC

Indexed as

MetalloendopeptidasesPeptidesProtease InhibitorsAnimalsHumansHydroxamic AcidsMiceHydroxamic Acidsmeprin Ameprin BMetalloendopeptidasesPeptidesProtease InhibitorsAlzheimer’s diseaseAmyloid precursor proteinIL-6RInflammationInhibitorLatrophilin-3MetalloproteaseProtease

Identifiers

PMID42897323
PMCPMC13680589

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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.