Evidence map›Paper›PMID 27511871›Full record

ArticleMolecular oncology2016

A ribonucleotide reductase inhibitor with deoxyribonucleoside-reversible cytotoxicity.

Mikael Crona, Paula Codó, Venkateswara Rao Jonna, Anders Hofer, Aristi P Fernandes, Fredrik Tholander

Open access · bronzeAbstract read
In one paragraph

Article in Molecular oncology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
0.6field-weighted citation impact, top 27% 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

14 citing papers in PubMed, 21 citations in OpenAlex.

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  13. Compounds with capacity to quench the tyrosyl radical in Pseudomonas aeruginosa ribonucleotide reductase.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2019
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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

6 authors at 2 institutions in 1 country.

Mikael CronaDepartment of Medicinal Biochemistry and Biophysics, Karolinska Institutet, 171 77, Stockholm, Sweden.
Paula CodóDepartment of Medicinal Biochemistry and Biophysics, Karolinska Institutet, 171 77, Stockholm, Sweden.
Venkateswara Rao JonnaDepartment of Medical Biochemistry and Biophysics, Umeå University, 90187, Umeå, Sweden.
Anders HoferDepartment of Medical Biochemistry and Biophysics, Umeå University, 90187, Umeå, Sweden.
Aristi P FernandesDepartment of Medicinal Biochemistry and Biophysics, Karolinska Institutet, 171 77, Stockholm, Sweden.
Fredrik TholanderDepartment of Medicinal Biochemistry and Biophysics, Karolinska Institutet, 171 77, Stockholm, Sweden. Electronic address: fredrik.tholander@ki.se.
Karolinska Institutet · SEUmeå University · SE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Ribonucleotide Reductase (RNR) is the sole enzyme that catalyzes the reduction of ribonucleotides into deoxyribonucleotides. Even though RNR is a recognized target for antiproliferative molecules, and the main target of the approved drug hydroxyurea, few new leads targeted to this enzyme have been developed. We have evaluated a recently identified set of RNR inhibitors with respect to inhibition of the human enzyme and cellular toxicity. One compound, NSC73735, is particularly interesting; it is specific for leukemia cells and is the first identified compound that hinders oligomerization of the mammalian large RNR subunit. Similar to hydroxyurea, it caused a disruption of the cell cycle distribution of cultured HL-60 cells. In contrast to hydroxyurea, the disruption was reversible, indicating higher specificity. NSC73735 thus defines a potential lead candidate for RNR-targeted anticancer drugs, as well as a chemical probe with better selectivity for RNR inhibition than hydroxyurea.

Indexed as

Biological AssayCell CycleCell DeathCell ProliferationCell SurvivalDeoxyribonucleosidesDose-Response Relationship, DrugEnzyme InhibitorsFlow CytometryGene Expression RegulationHL-60 CellsHumansHydroxyureaProtein Structure, QuaternaryProtein SubunitsRibonucleotide ReductasesDeoxyribonucleosidesEnzyme InhibitorsHydroxyureaProtein SubunitsRibonucleotide ReductasesAntiproliferative compoundsCell cycleCytotoxicityGEMMAInhibitorsNucleotide metabolismOligomeric stateRibonucleotide reductase

Identifiers

PMID27511871
PMCPMC5423217
OpenAlexW2481050409

What OpenQuestion holds

Textmetadata
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.