Evidence map›Paper›PMID 41155491›Full record

ArticleInternational journal of molecular sciences2025

Validating TDP1 as an Inhibition Target for Lipophilic Nucleoside Derivative in Human Cells.

Irina A Chernyshova, Tatyana E Kornienko, Nadezhda S Dyrkheeva, Alexandra L Zakharenko, Arina A Chepanova, Konstantin E Orishchenko, Nikolay N Kurochkin, Mikhail S Drenichev, Olga I Lavrik

Abstract read
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In one paragraph

Article in International journal of molecular sciences, 2025. 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. 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

9 authors.

Irina A ChernyshovaInstitute of Chemical Biology and Fundamental Medicine, Siberian Branch of the Russian Academy of Sciences, 630090 Novosibirsk, Russia.ORCID 0000-0003-1934-5116
Tatyana E KornienkoInstitute of Chemical Biology and Fundamental Medicine, Siberian Branch of the Russian Academy of Sciences, 630090 Novosibirsk, Russia.ORCID 0000-0002-5427-9786
Nadezhda S DyrkheevaInstitute of Chemical Biology and Fundamental Medicine, Siberian Branch of the Russian Academy of Sciences, 630090 Novosibirsk, Russia.ORCID 0000-0002-8360-1041
Alexandra L ZakharenkoInstitute of Chemical Biology and Fundamental Medicine, Siberian Branch of the Russian Academy of Sciences, 630090 Novosibirsk, Russia.
Arina A ChepanovaInstitute of Chemical Biology and Fundamental Medicine, Siberian Branch of the Russian Academy of Sciences, 630090 Novosibirsk, Russia.
Konstantin E OrishchenkoFederal Research Centre Institute of Cytology and Genetics, Siberian Branch of the Russian Academy of Sciences, 630090 Novosibirsk, Russia.ORCID 0000-0001-9718-9038
Nikolay N KurochkinEngelhardt Institute of Molecular Biology, Russian Academy of Sciences, 119991 Moscow, Russia.
Mikhail S DrenichevEngelhardt Institute of Molecular Biology, Russian Academy of Sciences, 119991 Moscow, Russia.ORCID 0000-0001-7624-8801
Olga I LavrikInstitute of Chemical Biology and Fundamental Medicine, Siberian Branch of the Russian Academy of Sciences, 630090 Novosibirsk, Russia.

Funding

This research was funded by the Russian Science Foundation (grants 25-74-30006 and 21-64-00017, preparation of knockout cell lines) and by the Russian state-funded project for ICBFM SB RAS (grant number 125012300658-9, equipment and infrastructure) This research was funded by the Russian Science Foundation (grants 25-74-30006 and 21-64-00017, preparation of knockout cell lines) and by the Russian state-funded project for ICBFM SB RAS (grant number 125012300658-9, equipment and infrastructure)
6 · The paper itself

Abstract

Tyrosyl-DNA phosphodiesterase 1 (TDP1) is an important DNA repair enzyme and its functioning is considered as one of the possible reasons for tumor resistance to topoisomerase 1 (TOP1) poisons such as topotecan. Thus, TDP1 inhibitors in combination with topotecan may improve the effectiveness of anticancer therapy. TDP1 acts somehow in a phospholipase manner, depleting the phosphodiester bond between lipophilic tyrosine residue and 3' end of DNA; therefore, lipophilic molecules bearing aromatic substituents can interact with TDP1 and even possess high inhibitory activity, which is evidenced by data from the literature. Previously, we identified lipophilic nucleoside derivative (compound

Indexed as

NucleosidesPhosphodiesterase InhibitorsPhosphoric Diester HydrolasesA549 CellsAntineoplastic AgentsHEK293 CellsHumansTopoisomerase I InhibitorsTopotecanAntineoplastic AgentsNucleosidesPhosphodiesterase InhibitorsPhosphoric Diester HydrolasesTDP1 protein, humanTopoisomerase I InhibitorsTopotecanDNA repairlipophilic nucleosideTDP1 knockouttopotecanTyrosyl-DNA phosphodiesterase 1 inhibitor

Identifiers

PMID41155491
PMCPMC12565254

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Registered trials

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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.