Evidence map›Paper›PMID 36128537›Full record

ArticleRSC advances2022

Synthesis of the extracellular domain of GLP-1R by chemical and biotechnological approaches.

János Szolomajer, Pál Stráner, Zoltán Kele, Gábor K Tóth, András Perczel

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in RSC advances, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
0.1field-weighted citation impact, top 57% 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

0 citing papers in PubMed, 1 citations in OpenAlex.

No citing paper in PubMed yet.

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

5 authors at 2 institutions in 1 country.

János SzolomajerDepartment of Medical Chemistry, Albert Szent-Györgyi Medical School, University of Szeged H-6720 Szeged Hungary toth.gabor@med.u-szeged.hu.ORCID https://orcid.org/0000-0003-1458-6156
Pál StránerMTA-ELTE Protein Model. Res. Group and Laboratory of Structural Chemistry and Biology Pázmány P. stny. 1/A 1117 Budapest Hungary perczel@chem.elte.hu.
Zoltán KeleDepartment of Medical Chemistry, Albert Szent-Györgyi Medical School, University of Szeged H-6720 Szeged Hungary toth.gabor@med.u-szeged.hu.
Gábor K TóthDepartment of Medical Chemistry, Albert Szent-Györgyi Medical School, University of Szeged H-6720 Szeged Hungary toth.gabor@med.u-szeged.hu.
András PerczelMTA-ELTE Protein Model. Res. Group and Laboratory of Structural Chemistry and Biology Pázmány P. stny. 1/A 1117 Budapest Hungary perczel@chem.elte.hu.
University of Szeged · HUEötvös Loránd University · HU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The extracellular domain of the glucagon-like peptide-1 receptor, GLP-1R, is responsible for the binding of GLP-1, and a handful of additional agonists (such as exenatide, lixisenatide, and liraglutide) used daily for treating type II diabetes mellitus. Lead discovery and optimization, however, require binding studies, which, in turn, necessitate the total synthesis of GLP-1R, comprising 108 residues. A protein domain of 10-15 kDa size could be obtained either by expression in

Identifiers

PMID36128537
PMCPMC9412715
OpenAlexW4293191590

What OpenQuestion holds

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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.