Evidence map›Paper›PMID 39985644›Full record

ArticleAMB Express2025

Staphylococcal SplA and SplB serine proteases target ubiquitin(-like) specific proteases.

Felix L Glinka, Ole Schmöker, Abhishek K Singh, Leif Steil, Christian Hentschker, Uwe Völker, Dominique Böttcher, Michael Lammers, Clemens Cammann, Ulrike Seifert and 4 more

Abstract read
In one paragraph

Article in AMB Express, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Frontiers in immunology · 2026
    Article
  2. Article
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

14 authors.

Felix L GlinkaDepartment of Biotechnology & Enzyme Catalysis, Institute of Biochemistry, University of Greifswald, Greifswald, Germany.ORCID http://orcid.org/0000-0003-4795-156X
Ole SchmökerDepartment of Synthetic and Structural Biochemistry, Institute of Biochemistry, University of Greifswald, Greifswald, Germany.ORCID http://orcid.org/0009-0005-4754-8246
Abhishek K SinghFriedrich Loeffler-Institute for Medical Microbiology-Virology, University Medicine Greifswald, Greifswald, Germany.ORCID http://orcid.org/0009-0007-2953-0231
Leif SteilDepartment of Functional Genomics, Interfaculty Institute for Genetics and Functional Genomics, University of Greifswald, Greifswald, Germany.ORCID http://orcid.org/0000-0002-0733-8421
Christian HentschkerDepartment of Functional Genomics, Interfaculty Institute for Genetics and Functional Genomics, University of Greifswald, Greifswald, Germany.
Uwe VölkerDepartment of Functional Genomics, Interfaculty Institute for Genetics and Functional Genomics, University of Greifswald, Greifswald, Germany.ORCID http://orcid.org/0000-0002-5689-3448
Dominique BöttcherDepartment of Biotechnology & Enzyme Catalysis, Institute of Biochemistry, University of Greifswald, Greifswald, Germany.ORCID http://orcid.org/0000-0001-9981-014X
Michael LammersDepartment of Synthetic and Structural Biochemistry, Institute of Biochemistry, University of Greifswald, Greifswald, Germany.ORCID http://orcid.org/0000-0003-4168-4640
Clemens CammannFriedrich Loeffler-Institute for Medical Microbiology-Virology, University Medicine Greifswald, Greifswald, Germany.ORCID http://orcid.org/0009-0008-1699-0607
Ulrike SeifertFriedrich Loeffler-Institute for Medical Microbiology-Virology, University Medicine Greifswald, Greifswald, Germany.ORCID http://orcid.org/0000-0003-1037-3487
Elke KrügerInstitute of Medical Biochemistry and Molecular Biology, University Medicine Greifswald, Greifswald, Germany.ORCID http://orcid.org/0000-0002-2551-242X
Michael NaumannInstitute of Experimental Internal Medicine, Otto Von Guericke University, Magdeburg, Germany.ORCID http://orcid.org/0000-0002-8060-2313
Barbara M BrökerInstitute of Immunology, University Medicine Greifswald, Greifswald, Germany.ORCID http://orcid.org/0000-0002-5020-8542
Uwe T BornscheuerDepartment of Biotechnology & Enzyme Catalysis, Institute of Biochemistry, University of Greifswald, Greifswald, Germany. uwe.bornscheuer@uni-greifswald.de.ORCID http://orcid.org/0000-0003-0685-2696

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Staphylococcus aureus is a Gram-positive opportunistic pathogen that has colonized nearly 30% of the human population and can cause life-threatening infections. S. aureus exports a variety of virulence factors, such as a novel set of extracellular serine protease-like proteins (Spls). Spls are expressed by most clinical isolates of S. aureus, but their pathophysiological substrates and role during the infection are largely unknown. Here we characterized the substrate and cleavage specificity of recombinantly expressed SplA and SplB proteins. We identified a group of ubiquitin or ubiquitin-like modifying enzymes including deubiquitinating enzymes from human as well as from bacterial sources to be so far unknown SplA and SplB substrates. Distinct cleavage sites within these substrates for SplA (YLY

Indexed as

DeubiquitinationProtein degradationSerine protease-likeSplASplBStaphylococcus aureus

Identifiers

PMID39985644
PMCPMC11846797

What OpenQuestion holds

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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.