Evidence map›Paper›PMID 23368812›Full record

ArticleBioscience reports2013

A small organic compound enhances the religation reaction of human topoisomerase I and identifies crucial elements for the religation mechanism.

Barbara Arnò, Andrea Coletta, Cinzia Tesauro, Laura Zuccaro, Paola Fiorani, Sara Lentini, Pierluca Galloni, Valeria Conte, Barbara Floris, Alessandro Desideri

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Bioscience reports, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.1field-weighted citation impact, top 42% 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

3 citing papers in PubMed, 7 citations in OpenAlex.

  1. Review
  2. Article
  3. Topoisomerase IB: a relaxing enzyme for stressed DNA.Cancer drug resistance (Alhambra, Calif.) · 2020
    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

10 authors at 2 institutions in 1 country.

Barbara Arnò*Department of Biology, University of Rome Tor Vergata, Via Della Ricerca Scientifica, Rome 00133, Italy.
Andrea Coletta*Department of Biology, University of Rome Tor Vergata, Via Della Ricerca Scientifica, Rome 00133, Italy.
Cinzia Tesauro*Department of Biology, University of Rome Tor Vergata, Via Della Ricerca Scientifica, Rome 00133, Italy.
Laura Zuccaro*Department of Biology, University of Rome Tor Vergata, Via Della Ricerca Scientifica, Rome 00133, Italy.
Paola Fiorani†Institute of Translational Pharmacology, National Research Council, CNR, Via Del Fosso del Cavaliere 100, 00133 Rome, Italy.
Sara Lentini‡Department of Chemical Sciences and Technology, Via Della Ricerca Scientifica, Rome 00133, Italy.
Pierluca Galloni‡Department of Chemical Sciences and Technology, Via Della Ricerca Scientifica, Rome 00133, Italy.
Valeria Conte‡Department of Chemical Sciences and Technology, Via Della Ricerca Scientifica, Rome 00133, Italy.
Barbara Floris‡Department of Chemical Sciences and Technology, Via Della Ricerca Scientifica, Rome 00133, Italy.
Alessandro Desideri*Department of Biology, University of Rome Tor Vergata, Via Della Ricerca Scientifica, Rome 00133, Italy.
University of Rome Tor Vergata · ITIstituto di Farmacologia Traslazionale · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The different steps of the human Top1 (topoisomerase I) catalytic cycle have been analysed in the presence of a pentacyclic-diquinoid synthetic compound. The experiments indicate that it efficiently inhibits the cleavage step of the enzyme reaction, fitting well into the catalytic site. Surprisingly the compound, when incubated with the binary topoisomerase-DNA cleaved complex, helps the enzyme to remove itself from the cleaved DNA and close the DNA gap, increasing the religation rate. The compound also induces the religation of the stalled enzyme-CPT (camptothecin)-DNA ternary complex. Analysis of the molecule docked over the binary complex, together with its chemical properties, suggests that the religation enhancement is due to the presence on the compound of two oxygen atoms that act as hydrogen acceptors. This property facilitates the deprotonation of the 5' DNA end, suggesting that this is the limiting step in the topoisomerase religation mechanism.

Indexed as

CamptothecinDNADNA Topoisomerases, Type IHumansHydrogenIodoquinolNucleic Acid ConformationOxygenCamptothecinDNADNA Topoisomerases, Type IHydrogenIodoquinolOxygenTOP1 protein, human

Identifiers

PMID23368812
PMCPMC3590572
OpenAlexW2136076752

What OpenQuestion holds

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LicenceCC BY-NC
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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.