Evidence map›Paper›PMID 26899418›Full record

ArticleScientific reports2016

In silico selection of an aptamer to estrogen receptor alpha using computational docking employing estrogen response elements as aptamer-alike molecules.

Rajesh Ahirwar, Smita Nahar, Shikha Aggarwal, Srinivasan Ramachandran, Souvik Maiti, Pradip Nahar

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
7.0field-weighted citation impact, top 3% 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

40 citing papers in PubMed, 109 citations in OpenAlex.

  1. Article
  2. In silico development of RNA aptamer candidates against thyroid receptor.Journal of computer-aided molecular design · 2025
    Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Aptamers as promising nanotheranostic tools in the COVID-19 pandemic era.Wiley interdisciplinary reviews. Nanomedicine and nanobiotechnology · 2022
    Review
  13. Structure- and Interaction-Based Design of Anti-SARS-CoV-2 Aptamers.Chemistry (Weinheim an der Bergstrasse, Germany) · 2022
    Article
  14. Article
  15. Review
  16. Article
  17. Review
  18. International journal of molecular sciences · 2021
    Article
  19. Artificial Intelligence in Aptamer-Target Binding Prediction.International journal of molecular sciences · 2021
    Review
  20. 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

6 authors at 2 institutions in 1 country.

Rajesh AhirwarAcademy of Scientific and Innovative Research, Delhi, India.
Smita NaharAcademy of Scientific and Innovative Research, Delhi, India.
Shikha AggarwalCSIR- Institute of Genomics and Integrative Biology, Delhi, India.
Srinivasan RamachandranAcademy of Scientific and Innovative Research, Delhi, India.
Souvik MaitiAcademy of Scientific and Innovative Research, Delhi, India.
Pradip NaharAcademy of Scientific and Innovative Research, Delhi, India.
Institute of Genomics and Integrative Biology · INAcademy of Scientific and Innovative Research · IN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Aptamers, the chemical-antibody substitute to conventional antibodies, are primarily discovered through SELEX technology involving multi-round selections and enrichment. Circumventing conventional methodology, here we report an in silico selection of aptamers to estrogen receptor alpha (ERα) using RNA analogs of human estrogen response elements (EREs). The inverted repeat nature of ERE and the ability to form stable hairpins were used as criteria to obtain aptamer-alike sequences. Near-native RNA analogs of selected single stranded EREs were modelled and their likelihood to emerge as ERα aptamer was examined using AutoDock Vina, HADDOCK and PatchDock docking. These in silico predictions were validated by measuring the thermodynamic parameters of ERα -RNA interactions using isothermal titration calorimetry. Based on the in silico and in vitro results, we selected a candidate RNA (ERaptR4; 5'-GGGGUCAAGGUGACCCC-3') having a binding constant (Ka) of 1.02 ± 0.1 × 10(8) M(-1) as an ERα-aptamer. Target-specificity of the selected ERaptR4 aptamer was confirmed through cytochemistry and solid-phase immunoassays. Furthermore, stability analyses identified ERaptR4 resistant to serum and RNase A degradation in presence of ERα. Taken together, an efficient ERα-RNA aptamer is identified using a non-SELEX procedure of aptamer selection. The high-affinity and specificity can be utilized in detection of ERα in breast cancer and related diseases.

Indexed as

SELEX Aptamer TechniqueAptamers, NucleotideBase SequenceBreast NeoplasmsComputational BiologyDNA-Binding ProteinsEstrogen Receptor alphaEstrogensFemaleHumansInverted Repeat SequencesMolecular Docking SimulationProtein BindingResponse ElementsAptamers, NucleotideDNA-Binding ProteinsESR1 protein, humanEstrogen Receptor alphaEstrogens

Identifiers

PMID26899418
PMCPMC4761961
OpenAlexW2286350386

What OpenQuestion holds

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LicenceCC BY
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Registered trials

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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.