Evidence map›Paper›PMID 41838040›Full record

ArticleArchiv der Pharmazie2026

Chromones as Nonclassical Inhibitors of Carbonic Anhydrase IX and XII Isoforms: Probing Chromone-Based Derivatives.

Lisa Sequeira, Simona Distinto, Carlos Fernandes, Erica Sanna, Rita Meleddu, Marco Gaspari, Filippo Cottiglia, Alessia Onali, Andrea Angeli, Fernanda Borges and 4 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Archiv der Pharmazie, 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

14 authors.

Lisa SequeiraMedInUP, Department of Biomedicine, Faculty of Medicine, University of Porto, Porto, Portugal.
Simona DistintoDepartment of Life and Environmental Sciences, University of Cagliari, Monserrato, Italy.
Carlos FernandesMedInUP, Department of Biomedicine, Faculty of Medicine, University of Porto, Porto, Portugal.
Erica SannaDepartment of Life and Environmental Sciences, University of Cagliari, Monserrato, Italy.
Rita MeledduDepartment of Life and Environmental Sciences, University of Cagliari, Monserrato, Italy.
Marco GaspariResearch Centre for Advanced Biochemistry and Molecular Biology, Department of Experimental and Clinical Medicine, "Magna Græcia", University of Catanzaro, Catanzaro, Italy.
Filippo CottigliaDepartment of Life and Environmental Sciences, University of Cagliari, Monserrato, Italy.
Alessia OnaliDepartment of Life and Environmental Sciences, University of Cagliari, Monserrato, Italy.
Andrea AngeliDepartment NEUROFARBA, Section of Pharmaceutical Sciences, University of Florence, Florence, Italy.ORCID https://orcid.org/0000-0002-1470-7192
Fernanda BorgesMedInUP, Department of Biomedicine, Faculty of Medicine, University of Porto, Porto, Portugal.ORCID https://orcid.org/0000-0003-1050-2402
Eugenio UriarteDepartment of Organic Chemistry, Faculty of Pharmacy, University of Santiago de Compostela, Santiago de Compostela, Spain.
Stefano AlcaroDepartment of Health Sciences, "Magna Græcia", University of Catanzaro, Catanzaro, Italy.ORCID https://orcid.org/0000-0002-0437-358X
Claudiu T SupuranDepartment NEUROFARBA, Section of Pharmaceutical Sciences, University of Florence, Florence, Italy.ORCID https://orcid.org/0000-0003-4262-0323
Elias MaccioniDepartment of Life and Environmental Sciences, University of Cagliari, Monserrato, Italy.ORCID https://orcid.org/0000-0003-2175-2802

Funding

CeSAR (Centro Servizi d'Ateneo per la Ricerca) of the University of Cagliari, Italy
6 · The paper itself

Abstract

A small library of differently substituted chromones was successfully synthesized and structurally characterized. All compounds were evaluated for their inhibitory potency and selectivity toward human cancer-associated carbonic anhydrase isoforms IX and XII, as well as the off-target isoforms I and II. Compounds 4a, 4g, 4j, and 4k selectively inhibited cancer-associated isoforms IX and XII, with no activity against the off-target isozymes I and II. Among them, compound 4k was the most potent and isozyme-selective inhibitor, with K

Indexed as

Carbonic Anhydrase InhibitorsCarbonic Anhydrase IXCarbonic AnhydrasesChromonesAntigens, NeoplasmCaco-2 CellsDose-Response Relationship, DrugHep G2 CellsHumansIsoenzymesMolecular Docking SimulationMolecular StructureStructure-Activity RelationshipAntigens, NeoplasmCA9 protein, humanCarbonic Anhydrase InhibitorsCarbonic Anhydrase IXCarbonic Anhydrasescarbonic anhydrase XIIChromonesIsoenzymescancercarbonic anhydrasedockingisoform expressionnonclassical inhibitors

Identifiers

PMID41838040
PMCPMC12991041

What OpenQuestion holds

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LicenceCC BY
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.