Evidence map›Paper›PMID 34227437›Full record

ArticleJournal of enzyme inhibition and medicinal chemistry2021

Synthesis and evaluation of AKR1C inhibitory properties of A-ring halogenated oestrone derivatives.

Maša Sinreih, Rebeka Jójárt, Zoltán Kele, Tomaž Büdefeld, Gábor Paragi, Erzsébet Mernyák, Tea Lanišnik Rižner

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Journal of enzyme inhibition and medicinal chemistry, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.5field-weighted citation impact, top 40% of its field
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

3 citing papers in PubMed, 7 citations in OpenAlex.

  1. Article
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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

7 authors at 3 institutions in 2 countries.

Maša SinreihFaculty of Medicine, Institute of Biochemistry and Molecular Genetics, University of Ljubljana, Ljubljana, Slovenia.
Rebeka JójártDepartment of Organic Chemistry, University of Szeged, Szeged, Hungary.
Zoltán KeleDepartment of Medicinal Chemistry, University of Szeged, Szeged, Hungary.
Tomaž BüdefeldFaculty of Medicine, Institute of Biochemistry and Molecular Genetics, University of Ljubljana, Ljubljana, Slovenia.
Gábor ParagiMTA-SZTE Biomimetic Systems Research Group, University of Szeged, Szeged, Hungary.
Erzsébet MernyákDepartment of Organic Chemistry, University of Szeged, Szeged, Hungary.
Tea Lanišnik RižnerFaculty of Medicine, Institute of Biochemistry and Molecular Genetics, University of Ljubljana, Ljubljana, Slovenia.
University of Ljubljana · SIUniversity of Szeged · HUUniversity of Pecs · HU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Enzymes AKR1C regulate the action of oestrogens, androgens, and progesterone at the pre-receptor level and are also associated with chemo-resistance. The activities of these oestrone halides were investigated on recombinant AKR1C enzymes. The oestrone halides with halogen atoms at both C-2 and C-4 positions (13β-, 13α-methyl-17-keto halogen derivatives) were the most potent inhibitors of AKR1C1. The lowest IC

Indexed as

20-Hydroxysteroid DehydrogenasesDose-Response Relationship, DrugEnzyme InhibitorsEstroneHumansModels, MolecularMolecular StructureStructure-Activity Relationship20-Hydroxysteroid Dehydrogenases3 alpha-beta, 20 beta-hydroxysteroid dehydrogenaseEnzyme InhibitorsEstroneAldo-keto reductasehalogenated oestrone derivativesinhibitionstructure–activity relationships

Identifiers

PMID34227437
PMCPMC8266253
OpenAlexW3179538943

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
Read underepoch 390

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.