Evidence map›Paper›PMID 27648925›Full record

ArticleMolecular therapy. Nucleic acids2016

Targeting Insulin Receptor with a Novel Internalizing Aptamer.

Margherita Iaboni, Raffaela Fontanella, Anna Rienzo, Maria Capuozzo, Silvia Nuzzo, Gianluca Santamaria, Silvia Catuogno, Gerolama Condorelli, Vittorio de Franciscis, Carla Lucia Esposito

Open access · goldAbstract read
In one paragraph

Article in Molecular therapy. Nucleic acids, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
6.0field-weighted citation impact, top 4% 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

22 citing papers in PubMed, 39 citations in OpenAlex.

  1. Review
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  3. Therapeutic Potential of Aptamer-Protein Interactions.ACS pharmacology & translational science · 2022
    Review
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  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Review
  11. Article
  12. Article
  13. Recent Advances in Aptamer Discovery and Applications.Molecules (Basel, Switzerland) · 2019
    Review
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  19. Article
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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

10 authors at 3 institutions in 1 country.

Margherita IaboniDepartment of Molecular Medicine and Medical Biotechnology, "Federico II" University of Naples, Naples, Italy.
Raffaela FontanellaIBB, CNR, Naples, Italy.
Anna RienzoIEOS, CNR, Naples, Italy.
Maria CapuozzoIEOS, CNR, Naples, Italy.
Silvia NuzzoDepartment of Molecular Medicine and Medical Biotechnology, "Federico II" University of Naples, Naples, Italy.
Gianluca SantamariaResearch Center of Advanced Biochemistry and Molecular Biology, Department of Experimental and Clinical Medicine, Magna Graecia University of Catanzaro, Catanzaro, Italy.
Silvia CatuognoIEOS, CNR, Naples, Italy.
Gerolama CondorelliDepartment of Molecular Medicine and Medical Biotechnology, "Federico II" University of Naples, Naples, Italy.
Vittorio de FranciscisIEOS, CNR, Naples, Italy.
Carla Lucia EspositoIEOS, CNR, Naples, Italy.
Institute for Experimental Endocrinology and Oncology · ITUniversity of Naples Federico II · ITMagna Graecia University · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Nucleic acid-based aptamers are emerging as therapeutic antagonists of disease-associated proteins such as receptor tyrosine kinases. They are selected by an in vitro combinatorial chemistry approach, named Systematic Evolution of Ligands by Exponential enrichment (SELEX), and thanks to their small size and unique chemical characteristics, they possess several advantages over antibodies as diagnostics and therapeutics. In addition, aptamers that rapidly internalize into target cells hold as well great potential for their in vivo use as delivery tools of secondary therapeutic agents. Here, we describe a nuclease resistant RNA aptamer, named GL56, which specifically recognizes the insulin receptor (IR). Isolated by a cell-based SELEX method that allows enrichment for internalizing aptamers, GL56 rapidly internalizes into target cells and is able to discriminate IR from the highly homologous insulin-like growth factor receptor 1. Notably, when applied to IR expressing cancer cells, the aptamer inhibits IR dependent signaling. Given the growing interest in the insulin receptor as target for cancer treatment, GL56 reveals a novel molecule with great translational potential as inhibitor and delivery tool for IR-dependent cancers.

Identifiers

PMID27648925
PMCPMC5056995
OpenAlexW2522904083

What OpenQuestion holds

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LicenceCC BY-NC-ND
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.