Evidence map›Paper›PMID 41347713›Full record

ArticleFEBS open bio2026

Anticancer sensitivities and biological characteristics of HCT116 cells resistant to the selective poly(ADP-ribose) glycohydrolase inhibitor.

Kaede Tsuda, Yoko Ogino, Akira Sato

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in FEBS open bio, 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. The role of NADFrontiers in oncology · 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

3 authors.

Kaede TsudaDepartment of Biochemistry and Molecular Biology, Faculty of Pharmaceutical Sciences, Tokyo University of Science, Tokyo, Japan.
Yoko OginoDepartment of Biochemistry and Molecular Biology, Faculty of Pharmaceutical Sciences, Tokyo University of Science, Tokyo, Japan.
Akira SatoDepartment of Biochemistry and Molecular Biology, Faculty of Pharmaceutical Sciences, Tokyo University of Science, Tokyo, Japan.ORCID https://orcid.org/0000-0002-2239-6208

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Poly(ADP-ribose) glycohydrolase (PARG) is a key enzyme involved in poly(ADP-ribose) (PAR) degradation and is considered a potential anticancer target. We previously investigated resistance mechanisms to the PARG inhibitor PDD00017273 in human colorectal cancer HCT116 cells and established an acquired PDD00017273-resistant HCT116R

Indexed as

Antineoplastic AgentsDrug Resistance, NeoplasmEnzyme InhibitorsGlycoside HydrolasesColorectal NeoplasmsHCT116 CellsHumansPoly Adenosine Diphosphate RibosePoly(ADP-ribose) Polymerase InhibitorsAntineoplastic AgentsEnzyme InhibitorsGlycoside HydrolasesPoly Adenosine Diphosphate Ribosepoly ADP-ribose glycohydrolasePoly(ADP-ribose) Polymerase InhibitorsARH3NAMPTPARPARGPARPPDD00017273

Identifiers

PMID41347713
PMCPMC13145335

What OpenQuestion holds

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LicenceCC BY
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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.