Evidence map›Paper›PMID 32877466›Full record

ArticlePloS one2020

A radioligand binding assay for the insulin-like growth factor 2 receptor.

Pavlo Potalitsyn, Irena Selicharová, Kryštof Sršeň, Jelena Radosavljević, Aleš Marek, Kateřina Nováková, Jiří Jiráček, Lenka Žáková

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
1.3field-weighted citation impact, top 19% 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

8 citing papers in PubMed, 12 citations in OpenAlex.

  1. Article
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  8. An Overview of In Vitro Assays ofDiagnostics (Basel, Switzerland) · 2023
    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

8 authors at 2 institutions in 1 country.

Pavlo PotalitsynInstitute of Organic Chemistry and Biochemistry, The Czech Academy of Sciences, Prague, Czech Republic.
Irena SelicharováInstitute of Organic Chemistry and Biochemistry, The Czech Academy of Sciences, Prague, Czech Republic.
Kryštof SršeňInstitute of Organic Chemistry and Biochemistry, The Czech Academy of Sciences, Prague, Czech Republic.
Jelena RadosavljevićInstitute of Organic Chemistry and Biochemistry, The Czech Academy of Sciences, Prague, Czech Republic.
Aleš MarekInstitute of Organic Chemistry and Biochemistry, The Czech Academy of Sciences, Prague, Czech Republic.
Kateřina NovákováInstitute of Organic Chemistry and Biochemistry, The Czech Academy of Sciences, Prague, Czech Republic.
Jiří JiráčekInstitute of Organic Chemistry and Biochemistry, The Czech Academy of Sciences, Prague, Czech Republic.
Lenka ŽákováInstitute of Organic Chemistry and Biochemistry, The Czech Academy of Sciences, Prague, Czech Republic.ORCID 0000-0001-6439-2574
Czech Academy of Sciences, Institute of Organic Chemistry and Biochemistry · CZCharles University · CZ

Funding

Medical Research Council MR/R009066/1
6 · The paper itself

Abstract

Insulin-like growth factors 2 and 1 (IGF2 and IGF1) and insulin are closely related hormones that are responsible for the regulation of metabolic homeostasis, development and growth of the organism. Physiological functions of insulin and IGF1 are relatively well-studied, but information about the role of IGF2 in the body is still sparse. Recent discoveries called attention to emerging functions of IGF2 in the brain, where it could be involved in processes of learning and memory consolidation. It was also proposed that these functions could be mediated by the receptor for IGF2 (IGF2R). Nevertheless, little is known about the mechanism of signal transduction through this receptor. Here we produced His-tagged domain 11 (D11), an IGF2-binding element of IGF2R; we immobilized it on the solid support through a well-defined sandwich, consisting of neutravidin, biotin and synthetic anti-His-tag antibodies. Next, we prepared specifically radiolabeled [125I]-monoiodotyrosyl-Tyr2-IGF2 and optimized a sensitive and robust competitive radioligand binding assay for determination of the nanomolar binding affinities of hormones for D11 of IGF2. The assay will be helpful for the characterization of new IGF2 mutants to study the functions of IGF2R and the development of new compounds for the treatment of neurological disorders.

Indexed as

Binding, CompetitiveCells, CulturedHumansInsulin-Like Growth Factor IInsulin-Like Growth Factor IIIodine RadioisotopesProtein BindingRadioligand AssayReceptor, IGF Type 2Signal TransductionIGF1 protein, humanIGF2 protein, humanIGF2R protein, humanInsulin-Like Growth Factor IInsulin-Like Growth Factor IIIodine-125Iodine RadioisotopesReceptor, IGF Type 2

Identifiers

PMID32877466
PMCPMC7467306
OpenAlexW3081805882

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.