Evidence map›Paper›PMID 42471764›Full record

ArticleChemMedChem2026

Sultams as Dual Inhibitors of Human Carbonic Anhydrase and Thioredoxin Reductase.

Aleksandrs Pustenko, Raitis Bobrovs, Venkatesan Saravanan, Kathir Avan, Simone Carradori, Antons Sizovs, Andrea Angeli, Claudiu T Supuran, Raivis Žalubovskis

Abstract read
In one paragraph

Article in ChemMedChem, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. Dual-target carbonic anhydrase inhibitors in cancer therapy: progress, challenges, and opportunities.Medicinal chemistry research : an international journal for rapid communications on design and mechanisms of action of biologically active agents · 2026
    Review
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

9 authors.

Aleksandrs PustenkoLatvian Institute of Organic Synthesis, Riga, Latvia.ORCID https://orcid.org/0000-0003-4930-7372
Raitis BobrovsLatvian Institute of Organic Synthesis, Riga, Latvia.
Venkatesan SaravananDepartment of Pharmaceutical Chemistry, SRM College of Pharmacy, SRM Institute of Science and Technology, Kattankulathur, Chengalpattu, India.
Kathir AvanDepartment of Pharmaceutical Chemistry, SRM College of Pharmacy, SRM Institute of Science and Technology, Kattankulathur, Chengalpattu, India.
Simone CarradoriDepartment of Pharmacy, "G.d'Annunzio" University of Chieti-Pescara, Chieti, Italy.ORCID https://orcid.org/0000-0002-8698-9440
Antons SizovsLatvian Institute of Organic Synthesis, Riga, Latvia.
Andrea AngeliDepartment of Neurofarba, Università degli Studi di Firenze, Florence, Italy.ORCID https://orcid.org/0000-0002-1470-7192
Claudiu T SupuranDepartment of Neurofarba, Università degli Studi di Firenze, Florence, Italy.ORCID https://orcid.org/0000-0003-4262-0323
Raivis ŽalubovskisLatvian Institute of Organic Synthesis, Riga, Latvia.

Funding

Recovery and Resilience Facility (RRF) 41/OSI/PGRecovery and Resilience Facility (RRF) RRF project no. 5.2.1.1.i.0/2/24/I/CFLA/001
6 · The paper itself

Abstract

Cancer remains a leading cause of mortality, often complicated by drug resistance arising from single-target therapies. Dual inhibitors that simultaneously target multiple cancer-related defense mechanisms offer a promising strategy to overcome these limitations. Herein, we report the design, synthesis, and biological evaluation of a series of sultam-based N-acyl derivatives (8a-k and 9a-k) as potential dual inhibitors of thioredoxin reductase (TrxR1) and tumor-associated carbonic anhydrases (CA IX and XII). TrxR1 screening identified a few active compounds, with inhibitory potency strongly influenced by the type and orientation of substituents. CA inhibition assays revealed pronounced selectivity for CA IX/XII, while off-target isoforms CA I and CA II remained unaffected. These findings highlight the potential of sultam derivatives as dual-targeting anticancer agents and provide a foundation for further optimization toward selective, multi-pathway cancer therapy.

Indexed as

Antineoplastic AgentsCarbonic Anhydrase InhibitorsCarbonic AnhydrasesEnzyme InhibitorsThioredoxin-Disulfide ReductaseDose-Response Relationship, DrugHumansMolecular StructureStructure-Activity RelationshipAntineoplastic AgentsCarbonic Anhydrase InhibitorsCarbonic AnhydrasesEnzyme InhibitorsThioredoxin-Disulfide Reductasebiochemistrycancercancer therapycarbonic anhydrasecarbonic anhydrase Ichemistrydrug resistancegene isoformreductasethioredoxin reductase

Identifiers

PMID42471764
PMCPMC13380777

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.