Evidence map›Paper›PMID 41583563›Full record

ArticleiScience2026

Structural analyses and substrate profiling of PPEP-3 provide new insights into the molecular basis of Pro-Pro endopeptidase specificity.

Bart Claushuis, Fabian Wojtalla, Lisa Papenhagen, Robert A Cordfunke, Arnoud H de Ru, Hans C van Leeuwen, Jeroen Corver, Paul J Hensbergen, Ulrich Baumann

Abstract read
In one paragraph

Article in iScience, 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
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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

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

9 authors.

Bart ClaushuisCenter for Proteomics and Metabolomics, Leiden University Medical Center, Leiden 2333 ZA, the Netherlands.
Fabian WojtallaDepartment of Chemistry, Institute of Biochemistry, University of Cologne, 50674 Cologne, Germany.
Lisa PapenhagenDepartment of Chemistry, Institute of Biochemistry, University of Cologne, 50674 Cologne, Germany.
Robert A CordfunkeDepartment of Immunology, Leiden University Medical Center, Leiden 2333 ZA, the Netherlands.
Arnoud H de RuCenter for Proteomics and Metabolomics, Leiden University Medical Center, Leiden 2333 ZA, the Netherlands.
Hans C van LeeuwenDepartment of CBRN Protection, Netherlands Organization for Applied Scientific Research TNO, Rijswijk 2280 GJ, the Netherlands.
Jeroen CorverLeiden University Center for Infectious Diseases, Leiden University Medical Center, Leiden 2333 ZA, the Netherlands.
Paul J HensbergenCenter for Proteomics and Metabolomics, Leiden University Medical Center, Leiden 2333 ZA, the Netherlands.
Ulrich BaumannDepartment of Chemistry, Institute of Biochemistry, University of Cologne, 50674 Cologne, Germany.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Pro-Pro endopeptidases (PPEPs) are secreted bacterial enzymes that uniquely cleave peptide bonds between adjacent proline residues. Their active site accommodates six substrate residues (P3 to P3'), with interactions at these positions determining specificity. In this study, we investigated the substrate specificity of PPEP-3 from

Indexed as

biochemistrybiological sciencesmethodology in biological sciencesproteomicsstructural biology

Identifiers

PMID41583563
PMCPMC12828418

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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.