Evidence map›Paper›PMID 25256921›Full record

ArticleAngewandte Chemie (International ed. in English)2014

Substitution-inert trinuclear platinum complexes efficiently condense/aggregate nucleic acids and inhibit enzymatic activity.

Jaroslav Malina, Nicholas P Farrell, Viktor Brabec

Abstract read
In one paragraph

Article in Angewandte Chemie (International ed. in English), 2014. 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
2.5field-weighted citation impact, top 9% 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, 49 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. On the Biology of Werner's Complex.Angewandte Chemie (International ed. in English) · 2021
    Article
  6. Molecular dynamics simulation of non-covalent interactions between polynuclear platinum(II) complexes and DNA.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2020
    Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. 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

3 authors at 2 institutions in 2 countries.

Jaroslav MalinaInstitute of Biophysics, Academy of Sciences of the Czech Republic, v.v.i. Kralovopolska 135, CZ-61265 Brno (Czech Republic) http://www.ibp.cz/en/departments/molecular-biophysics-and-pharmacology/info-about-the-department.
Nicholas P Farrell
Viktor Brabec
Czech Academy of Sciences, Institute of Biophysics · CZVirginia Commonwealth University · US

Funding

MECHANISTIC STUDIES ON NEW PLATINUM CLINICAL AGENTSR01CA078754 · NCI · VIRGINIA COMMONWEALTH UNIVERSITY · PI FARRELL, NICHOLAS P · 1998 to 2012
$3.6M
NCI NIH HHS R01 CA078754NCI NIH HHS R01 CA-78754
6 · The paper itself

Abstract

The trinuclear platinum complexes (TriplatinNC-A [{Pt(NH3 )3 }2 -μ-{trans-Pt(NH3 )2 (NH2 (CH2 )6 NH2 )2 }](6+) , and TriplatinNC [{trans-Pt(NH3 )2 (NH2 (CH2 )6 NH3 (+) )}2 -μ-{trans-Pt(NH3 )2 (NH2 (CH2 )6 NH2 )2 }](8+) ) are biologically active agents that bind to DNA through noncovalent (hydrogen bonding, electrostatic) interactions. Herein, we show that TriplatinNC condenses DNA with a much higher potency than conventional DNA condensing agents. Both complexes induce aggregation of small transfer RNA molecules, and TriplatinNC in particular completely inhibits DNA transcription at lower concentrations than naturally occurring spermine. Topoisomerase I-mediated relaxation of supercoiled DNA was inhibited by TriplatinNC-A and TriplatinNC at concentrations which were 60 times and 250 times lower than that of spermine. The mechanisms for the biological activity of TriplatinNC-A and TriplatinNC may be associated with their ability to condense/aggregate nucleic acids with consequent inhibitory effects on crucial enzymatic activities.

Indexed as

DNADNA Topoisomerases, Type IMolecular StructureOrganoplatinum CompoundsPlasmidsStructure-Activity RelationshipTopoisomerase I InhibitorsDNADNA Topoisomerases, Type IOrganoplatinum CompoundsTopoisomerase I InhibitorsDNA condensationnucleic acidsplatinumtopoisomerase ItRNA

Identifiers

PMID25256921
PMCPMC4311996
OpenAlexW2125504889

What OpenQuestion holds

Textmetadata
LicenceTDM
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.