Evidence map›Paper›PMID 26656490›Full record

ArticleNucleic acids research2016

KRAS promoter oligonucleotide with decoy activity dimerizes into a unique topology consisting of two G-quadruplex units.

Peter Podbevšek, Janez Plavec

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.5field-weighted citation impact, top 17% 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

16 citing papers in PubMed, 25 citations in OpenAlex.

  1. Linker dependence ofOrganic & biomolecular chemistry · 2026
    Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Review
  7. Article
  8. Duplex formation in a G-quadruplex bulge.Nucleic acids research · 2020
    Article
  9. Article
  10. Structure and Function of Multimeric G-Quadruplexes.Molecules (Basel, Switzerland) · 2019
    Review
  11. Article
  12. Article
  13. Multimerization rules for G-quadruplexes.Nucleic acids research · 2017
    Article
  14. High-resolution three-dimensional NMR structure of theThe Journal of biological chemistry · 2017
    Article
  15. Article
  16. 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

2 authors at 2 institutions in 1 country.

Peter PodbevšekSlovenian NMR Center, National Institute of Chemistry, Hajdrihova 19, SI-1000 Ljubljana, Slovenia EN-FIST Centre of Excellence, Trg OF 13, SI-1000 Ljubljana, Slovenia.
Janez PlavecSlovenian NMR Center, National Institute of Chemistry, Hajdrihova 19, SI-1000 Ljubljana, Slovenia EN-FIST Centre of Excellence, Trg OF 13, SI-1000 Ljubljana, Slovenia Faculty of Chemistry and Chemical Technology, University of Ljubljana, Ljubljana, Slovenia janez.plavec@ki.si.
EN-FIST Centre of Excellence (Slovenia) · SIUniversity of Ljubljana · SI

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Mutations of the KRAS proto-oncogene are associated with several tumor types, which is why it is being considered as a target for anti-cancer drug development. The human KRAS promoter contains a nuclease hypersensitive element (NHE), which can bind to nuclear proteins and is believed to form G-quadruplex structures. Previous studies showed that a 32-nt oligonucleotide (32R-3n) mimicking the KRAS NHE can reduce gene transcription by sequestering MAZ, a crucial transcription factor. Here we show that 32R-3n has to dimerize in order to fold into a G-quadruplex structure. Individual 5'- and 3'-end G-quadruplex units are formed and both feature a symmetric head-to-head topology with edge-type loops. The MAZ binding sequence is located within the 3'-end unit. Nuclear magnetic resonance data complemented by CD and UV spectra show that nucleotides of the MAZ binding G-rich motif are dynamic and could be available for sequence or structure based recognition. Both stable G-quadruplex structures could protect 5'- and 3'-ends of 32R-3n and enhance its anti-cancer activity. Single stranded genomic KRAS NHE including nucleotides flanking the 32R-3n sequence could favor a different monomeric fold, which remains unknown.

Indexed as

G-QuadruplexesPromoter Regions, GeneticBase PairingBinding SitesCircular DichroismDimerizationDNA-Binding ProteinsMagnetic Resonance SpectroscopyNucleic Acid ConformationNucleotide MotifsProto-Oncogene MasProto-Oncogene Proteins p21(ras)Spectrophotometry, UltravioletTranscription Factorsc-MYC-associated zinc finger proteinDNA-Binding ProteinsKRAS protein, humanMAS1 protein, humanProto-Oncogene MasProto-Oncogene Proteins p21(ras)Transcription Factors

Identifiers

PMID26656490
PMCPMC4737153
OpenAlexW2193393439

What OpenQuestion holds

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LicenceCC BY-NC
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.