Evidence map›Paper›PMID 40103729›Full record

ArticleChemical science2025

A general approach for activity-based protein profiling of oxidoreductases with redox-differentiated diarylhalonium warheads.

Leo Krammer, Barbara Darnhofer, Marko Kljajic, Laura Liesinger, Matthias Schittmayer, Dmytro Neshchadin, Georg Gescheidt, Alexander Kollau, Bernd Mayer, Roland C Fischer and 4 more

Abstract read
In one paragraph

Article in Chemical science, 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. 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.

Leo KrammerInstitute of Organic Chemistry, Graz University of Technology Stremayrgasse 9 8010 Graz Austria breinbauer@tugraz.at.ORCID https://orcid.org/0000-0002-4861-754X
Barbara DarnhoferDiagnostic and Research Institute of Pathology, Medical University of Graz Stiftingtalstraße 6 8036 Graz Austria.
Marko KljajicInstitute of Organic Chemistry, Graz University of Technology Stremayrgasse 9 8010 Graz Austria breinbauer@tugraz.at.
Laura LiesingerInstitute of Chemical Technologies and Analytics, Technische Universität Wien Getreidemarkt 9 1060 Vienna Austria ruth.birner-gruenberger@tuwien.ac.at.
Matthias SchittmayerInstitute of Chemical Technologies and Analytics, Technische Universität Wien Getreidemarkt 9 1060 Vienna Austria ruth.birner-gruenberger@tuwien.ac.at.
Dmytro NeshchadinInstitute of Physical and Theoretical Chemistry, Graz University of Technology Stremayrgasse 9 8010 Graz Austria.ORCID https://orcid.org/0000-0001-8918-1028
Georg GescheidtInstitute of Physical and Theoretical Chemistry, Graz University of Technology Stremayrgasse 9 8010 Graz Austria.ORCID https://orcid.org/0000-0002-6827-4337
Alexander KollauInstitute of Pharmaceutical Sciences, University of Graz Humboldtstraße 46 8010 Graz Austria.
Bernd MayerInstitute of Pharmaceutical Sciences, University of Graz Humboldtstraße 46 8010 Graz Austria.
Roland C FischerInstitute of Inorganic Chemistry, Graz University of Technology Stremayrgasse 9 8010 Graz Austria.ORCID https://orcid.org/0000-0001-9523-5010
Silvia WallnerInstitute of Biochemistry, Graz University of Technology Petersgasse 12 8010 Graz Austria.
Peter MacherouxInstitute of Biochemistry, Graz University of Technology Petersgasse 12 8010 Graz Austria.
Ruth Birner-GruenbergerDiagnostic and Research Institute of Pathology, Medical University of Graz Stiftingtalstraße 6 8036 Graz Austria.ORCID https://orcid.org/0000-0003-3950-0312
Rolf BreinbauerInstitute of Organic Chemistry, Graz University of Technology Stremayrgasse 9 8010 Graz Austria breinbauer@tugraz.at.ORCID https://orcid.org/0000-0001-6009-7359

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Activity-based protein profiling (ABPP) is a unique proteomic tool for measuring the activity of enzymes in their cellular context, which has been well established for enzyme classes exhibiting a characteristic nucleophilic residue (

Identifiers

PMID40103729
PMCPMC11912224

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LicenceCC BY
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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.