Evidence map›Paper›PMID 41767230›Full record

ArticleRSC advances2026

Directed C-H activation of 13α-estrone: a pathway to promising AKR1C inhibitors

Erzsébet Mernyák, Marija Gjorgoška, Masa Sinreih, Aljaž Kotnik, Zala Zanoškar, Ajda Godec, Marko Jukič, Urban Bren, Rebeka Ignácz, Kornél Szőri and 3 more

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Article in RSC advances, 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

13 authors.

Erzsébet MernyákInstitute of Pharmacognosy, University of Szeged Eötvös u. 6 H-6720 Szeged Hungary mernyak.erzsebet@szte.hu.ORCID https://orcid.org/0000-0003-4494-1817
Marija GjorgoškaInstitute of Biochemistry and Molecular Genetics, Faculty of Medicine, University of Ljubljana Vrazov trg 2 1000 Ljubljana Slovenia tea.lanisnik-rizner@mf.uni-lj.si.
Masa SinreihInstitute of Biochemistry and Molecular Genetics, Faculty of Medicine, University of Ljubljana Vrazov trg 2 1000 Ljubljana Slovenia tea.lanisnik-rizner@mf.uni-lj.si.
Aljaž KotnikInstitute of Biochemistry and Molecular Genetics, Faculty of Medicine, University of Ljubljana Vrazov trg 2 1000 Ljubljana Slovenia tea.lanisnik-rizner@mf.uni-lj.si.
Zala ZanoškarInstitute of Biochemistry and Molecular Genetics, Faculty of Medicine, University of Ljubljana Vrazov trg 2 1000 Ljubljana Slovenia tea.lanisnik-rizner@mf.uni-lj.si.
Ajda GodecInstitute of Biochemistry and Molecular Genetics, Faculty of Medicine, University of Ljubljana Vrazov trg 2 1000 Ljubljana Slovenia tea.lanisnik-rizner@mf.uni-lj.si.
Marko JukičLaboratory of Physical Chemistry and Chemical Thermodynamics, Faculty of Chemistry and Chemical Engineering, University of Maribor Smetanova ulica 17 SI-2000 Maribor Slovenia.
Urban BrenLaboratory of Physical Chemistry and Chemical Thermodynamics, Faculty of Chemistry and Chemical Engineering, University of Maribor Smetanova ulica 17 SI-2000 Maribor Slovenia.
Rebeka IgnáczInstitute of Pharmacognosy, University of Szeged Eötvös u. 6 H-6720 Szeged Hungary mernyak.erzsebet@szte.hu.
Kornél SzőriInstitute of Pharmacognosy, University of Szeged Eötvös u. 6 H-6720 Szeged Hungary mernyak.erzsebet@szte.hu.
Zoltán KeleDepartment of Medicinal Chemistry, University of Szeged Dóm tér 8 H-6720 Szeged Hungary.
Attila HunyadiInstitute of Pharmacognosy, University of Szeged Eötvös u. 6 H-6720 Szeged Hungary mernyak.erzsebet@szte.hu.ORCID https://orcid.org/0000-0003-0074-3472
Tea Lanišnik RižnerInstitute of Biochemistry and Molecular Genetics, Faculty of Medicine, University of Ljubljana Vrazov trg 2 1000 Ljubljana Slovenia tea.lanisnik-rizner@mf.uni-lj.si.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The aldo-keto reductase isoenzymes AKR1C1-3 regulate local steroid hormone availability through the interconversion of active and inactive ligands, thereby modulating prereceptor signaling. This regulatory mechanism has been implicated in the progression of hormone-dependent malignancies, highlighting AKR1C enzymes as attractive therapeutic targets for endocrine-related cancers. The AKR1C family is also known to mediate resistance to multiple classes of chemotherapeutic agents through various mechanisms. Inhibition of AKR1C enzymes may therefore potentiate the cytotoxic effects of chemotherapeutic agents. Building on our recent work describing potent A-ring halogenated 13α-estrone-based AKR1C inhibitors, we now report further structural modifications

Identifiers

PMID41767230
PMCPMC12947632

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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.