Evidence map›Paper›PMID 28973461›Full record

ArticleNucleic acids research2017

Coexistence of two main folded G-quadruplexes within a single G-rich domain in the EGFR promoter.

Maria L Greco, Anita Kotar, Riccardo Rigo, Camilla Cristofari, Janez Plavec, Claudia Sissi

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
2.6field-weighted citation impact, top 10% 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

20 citing papers in PubMed, 45 citations in OpenAlex.

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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 3 institutions in 2 countries.

Maria L GrecoDepartment of Pharmaceutical and Pharmacological Sciences, University of Padova, v. Marzolo 5, Padova 35131, Italy.
Anita KotarSlovenian NMR Center, National Institute of Chemistry, Hajdrihova 19, 1000 Ljubljana, Slovenia.
Riccardo RigoDepartment of Pharmaceutical and Pharmacological Sciences, University of Padova, v. Marzolo 5, Padova 35131, Italy.
Camilla CristofariDepartment of Pharmaceutical and Pharmacological Sciences, University of Padova, v. Marzolo 5, Padova 35131, Italy.
Janez PlavecSlovenian NMR Center, National Institute of Chemistry, Hajdrihova 19, 1000 Ljubljana, Slovenia.
Claudia SissiDepartment of Pharmaceutical and Pharmacological Sciences, University of Padova, v. Marzolo 5, Padova 35131, Italy.
University of Padua · ITNational Institute of Chemistry · SIUniversity of Ljubljana · SI

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

EGFR is an oncogene which codifies for a tyrosine kinase receptor that represents an important target for anticancer therapy. Indeed, several human cancers showed an upregulation of the activity of this protein. The promoter of this gene contains some G-rich domains, thus representing a yet unexplored point of intervention to potentially silence this gene. Here, we explore the conformational equilibria of a 30-nt long sequence located at position -272 (EGFR-272). By merging spectroscopic and electrophoretic analysis performed on the wild-type sequence as well as on a wide panel of related mutants, we were able to prove that in potassium ion containing solution this sequence folds into two main G-quadruplex structures, one parallel and one hybrid. They show comparable thermal stabilities and affinities for the metal ion and, indeed, they are always co-present in solution. The folding process is driven by a hairpin occurring in the domain corresponding to the terminal loop which works as an important stabilizing element for both the identified G-quadruplex arrangements.

Indexed as

Genes, erbB-1Promoter Regions, GeneticCircular DichroismDNAElectrophoretic Mobility Shift AssayErbB ReceptorsHumansModels, ChemicalNucleic Acid ConformationPoint MutationPotassium ChlorideSolutionsThermodynamicsDNAEGFR protein, humanErbB ReceptorsPotassium ChlorideSolutions

Identifiers

PMID28973461
PMCPMC5737278
OpenAlexW2741010565

What OpenQuestion holds

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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.